Abstract

Current intravital microscopy techniques visualize tauopathy with high-resolution, but have a small field-of-view and depth-of-focus. Herein, we report a transcranial detection of tauopathy over the entire cortex of P301L tauopathy mice using large-field multifocal illumination (LMI) fluorescence microscopy technique and luminescent conjugated oligothiophenes. In vitro assays revealed that fluorescent ligand h-FTAA is optimal for in vivo tau imaging, which was confirmed by observing elevated probe retention in the cortex of P301L mice compared to non-transgenic littermates. Immunohistochemical staining further verified the specificity of h-FTAA to detect tauopathy in P301L mice. The new imaging platform can be leveraged in pre-clinical mechanistic studies of tau spreading and clearance as well as longitudinal monitoring of tau targeting therapeutics.

© 2020 Optical Society of America under the terms of the OSA Open Access Publishing Agreement

1. Introduction

The abnormal deposition of pathological tau fibrils is a characteristic feature of tauopathy related neurodegenerative diseases including Alzheimer’s disease, frontotemporal lobar dementia (FTLD), chronic traumatic encephalopathy, corticobasal degeneration, progressive supranuclear palsy and parkinsonism linked to chromosome 17 [1]. Microtubule associated protein Tau locates intracellularly and is composed of six isoforms classified into 4-repeat (4R) and 3-repeat (3R) species, and the composition of tau isoforms differ among diverse tauopathies [2]. Tau abnormal accumulation in patients with Alzheimer’s disease was found to be closely related to axonal damage, neurodegeneration and cognitive impairment [3–5]. This designates tauopathy an important target for early diagnostic and therapeutic intervention for Alzheimer’s disease, FTLD, and other tauopathy disorders [6]. Tau tracers for positron emission tomography (PET) have been developed recently [5,7–12], while tau imaging has emerged as a useful tool for disease staging, progression prediction, treatment stratification, and monitoring in clinical research setting [4].

Several tau mouse models that recapitulate pathological features of tauopathy have been developed with mutations in the MAPT gene, including P301S [13], P301L (rTg4510 under CaMKII [14], prion [15] and Thy1.2 [16] promotors), and hTau lines [17]. Whole brain high-resolution tau imaging in these disease models provide insights for mechanistic and therapeutic studies [18,19]. At macroscopic level, in vivo imaging of tauopathy was enabled by PET in P301L mouse line using 11C-PBB3 [20–22] or 18F-PI-2620 [10] tau probes. However, the limited resolution of microPET (1 mm) relative to the mouse brain (∼10 mm3) and the need for dedicated and expensive infrastructure for radiolabeling limit usability in preclinical setting. Near-infrared fluorescence imaging using PBB5, PBB3 [20], fluorescently labelled antibodies, and antibody fragments [23] have also been applied for tauopathy detection in animal models. Deep tissue fluorescence imaging is yet affected by severe light scattering and absorption, resulting in limited imaging depth as well as poor spatial resolution and quantification accuracy. At the microscopic scale, two-photon imaging with cranial window using Congo-red derivative FSB [24,25], Thioflavin S [26], and luminescent conjugated oligothiophene (LCO) HS-84 [27] have monitored tauopathy in mouse models with cellular/sub-cellular resolution but restricted (sub-millimeter) field-of-view (FOV).

The aim of the present study is to assess the selectivity and specificity of LCOs [28] for in vivo tauopathy detection in the P301L (Thy1.2) mouse model [16] with large-field multifocal illumination (LMI) fluorescence microscopy attaining 12×12 mm FOV and high spatial resolution (∼6 μm) [29,30].

2. Materials and methods

2.1 LMI fluorescence imaging system and characterization

The LMI fluorescence imaging system is based on a beam-splitting grating and an acousto-optic deflector, which are synchronized with a high speed camera to attain real-time fluorescence microscopy over a 20×20 mm FOV [29,30]. A 473 nm CW laser was used for h-FTAA excitation. The laser beam was first scanned by a two dimensional acousto-optic deflector (AA Opto-Electronic, France) at 900 Hz and then guided into a customized beam-splitting grating (Holoeye GmbH, Germany) to generate 21×21 mini-beam pattern. It is subsequently focused with a scan lens (CLS-SL, Thorlabs) to generate the illumination grid upon the sample. After passing through the dichroic mirror, the emitted fluorescence signals are collected by a Nikon lens (Micro-Nikkor AF-S 60mm f/2.8 G, Nikon) and focused onto the sensor plane of a high-speed camera (pco.dimax S1, PCO AG, Germany). To render one LMI image, the illumination grid is raster scanned over 90×90 positions with ∼7 μm scanning step. After data acquisition, only signals at the excitation foci were extracted and then superimposed to form the high-resolution image.

2.2 In vitro binding of probes to recombinant tau fibrils and mouse brain

Recombinant amyloid-beta Aβ42 and full-length tau were expressed and produced by E.coli as described previously [31,32]. The fluorescence LCO probes h-FTAA, q-FTAA, HS-84 and HS-169 were synthesized as described previously [33,34]. Thioflavin T assays using LCOs (h-FTAA, q-FTAA, HS-84 and HS-169) at 1μM, AOI987 at 10 nM against Aβ42 (80.3 μg/ml) and tau fibrils (379.2 μg/ml) using fluorometer (Fluoromax 4, Horiba scientific, Japan) were performed as described previously [30], with three technical replicates. These experiments were conducted twice.

2.3 Animal model

Two 17 months-old and four 10 months-old mice transgenic for MAPT P301L, overexpressing human 2N/4R tau under neuron-specific Thy1.2 promoter (pR5 line, C57B6.Dg background) [16,35], and four non-transgenic littermates were used (4 and 10 months-of-age), of both gender. Animals were housed in individually ventilated cages inside a temperature-controlled room, under a 12-hour dark/light cycle. Pelleted food (3437PXL15, CARGILL) and water were provided ad-libitum. All experiments were performed in accordance with the Swiss Federal Act on Animal Protection and were approved by the Cantonal Veterinary Office Zurich (permit number: ZH082/18).

2.4 In vivo and ex vivo LMI fluorescence imaging of tauopathy in P301L mice

For in vivo LMI imaging, mice were anesthetized with isoflurane (4% v/v for induction and 1.5% v/v during experiments) in O2:air (1/4) mixture at a flow rate of ∼0.8 l/min. Lidocaine 7 mg/kg and Epinephrine 7 μg/kg were applied subcutaneously. Before scanning, each mouse was positioned onto the imaging stage, with the scalp removed to reduce light scattering while the skull was kept intact. For P301L and non-transgenic littermate mice, an i.v. tail-vein injection of 0.6 mg/kg h-FTAA solution in 0.1 M phosphate buffered saline (PBS, pH 7.4) was administered. LMI imaging and widefield imaging were recorded before and after h-FTAA injection with a time interval of 20 min and terminated at 120 min post-injection.

Seven mice were sacrificed under deep anesthesia (ketamine/xylazine/acepromazine maleate, 75/10/2 mg/kg body weight, i.p. bolus injection) without prior perfusion. The dissected skull, the whole brain and brain slices of 5-mm thickness, prepared using a brain matrix and razor blade, were imaged with LMI and widefield imaging on object holders wrapped with black tape using the aforementioned set-up. To validate the in- and ex vivo signal, the other two P301L and non-transgenic littermate mice were perfused under ketamine/xylazine/acepromazine maleate anesthesia (75/10/2 mg/kg body weight, i.p. bolus injection) with 0.1 M PBS (pH 7.4) and decapitated. The brains were then imaged using LMI imaging, immersion fixed in 4% paraformaldehyde in 0.1 M PBS (pH 7.4) for 1 day and then stored in 0.1 M PBS (pH 7.4) at 4 °C for immunohistochemistry.

2.5 Image reconstruction and data analysis

Reconstruction of the LMI imaging data was performed based on the saved raw data from the CMOS camera. Firstly, local maxima in each scanning frame were identified and the excited fluorescence signals were extracted with their centroids and intensity stored for the subsequent image compounding. Since the illumination grid was well-defined with equal intervals between adjacent spots, this prior information facilitated signal extraction while suppressing noise. Note that the beamsplitting grating was originally designed for the 532 nm wavelength, resulting in a large uniformity error for the zero diffraction order at the 473 nm wavelength. Thus, signal intensity correction was implemented for the central spot before signal superimposition. According to image scanning microscopy theory [36], each scanning image has to be shifted with respect to a common frame before rendering the final high-resolution compounded image. In our case, the extracted signals at the excitation spots were not altered but placed four times further from each other in the final compounded image given the low magnification power and 90×90 raster scanning positions.

For data analysis, fluorescence intensity (F.I.) in five regions-of-interest (ROIs) were drawn for the ex vivo experimental results of both LMI and widefield imaging in P301L mice (Fig. 4(a), (b), red square: ROI, and blue square: bk, background region) for Contrast-to-noise ratio (CNR) analysis according to Eq. (1).

$$CNR = \frac{{({S\_ROI1 - S\_ROI2} )}}{N}$$
where S is F.I. in the two ROIs (red square); and N is the standard deviation from the ROI background (blue square).

2.6 Staining and confocal imaging

LCOs were applied to brain tissue slices from one P301L and one non-transgenic littermate. Horizontal brain sections (5 μm) were stained with h-FTAA, q-FTAA, HS-84, HS-169 (5 μM, dd water), and counterstained using DAPI (Sigma, 1:1000 dilution). Confocal images of brain sections from P301L and non-transgenic littermates were obtained using a Leica SP8 confocal microscope (Leica Microsystems GmbH, Germany) at ScopeM ETH Zurich Hönggerberg core facility. Lambda scan using Leica SP8 was performed on h-FTAA and HS-84 stained brain slices to further determine the fluorescent properties of the dyes. Three ROIs were chosen on the tauopathy deposits stained by dyes.

After ex vivo LMI imaging, brains from P301L mice and non-transgenic littermate mice were removed from the skull and embedded in paraffin following routine procedures for histology and immunohistochemical investigations. Horizontal and sagittal brain sections (5 μm) were made and stained with 5 μM h-FTAA, and anti-phosphorylated antibodies AT-8 (pSer202/pThr205, MN1020, Invitrogen, 1:50) and AT-100 (pThr212/pSer214, MN1060, Invitrogen, 1:50) [35,37], conjugated with Alexa647 Goat polyclonal mouse (Invitrogen, A-21235, 1:100). Sections were counterstained using DAPI (1:1000). The brain sections were imaged at ×20 magnification using Panoramic 250 (3D HISTECH, Hungary) and at ×63 magnification using a Leica SP8 confocal microscope facility for co-localization of h-FTAA and AT-8/AT-100. The images were analyzed using CaseViewer (3D HISTECH, Hungary) and ImageJ (NIH, U.S.A).

2.7 Statistics

An unpaired two-tail student t-test was used (Graphpad Prism) for comparing values between two groups. For the time series, two-way ANOVA was used. All data are present as mean ± standard deviation. Significance was set at *p < 0.05.

3. Results

3.1 In vitro assays revealed that h-TFAA is optimal for in vivo tau imaging

Neurodegenerative diseases are associated not only with the aggregation of tau fibrils, but also with other intra- and extracellular protein aggregates such as Aβ and alpha-synuclein and the ideal probe for tau imaging should be selective for tau fibrils. First, we tested and compared the selectivity of several LCOs and fluorescent probes for their binding to tau fibrils versus Aβ42 fibrils. Fluorescence binding assays were performed in vitro using a panel of probes binding to Aβ42 and full-length (4R/2N) tau fibrils using a fluorescence spectrometer. As expected, Thioflavin-T binds to Aβ42 and tau fibrils, as both proteins have an extensive cross β-pleated sheet conformation [32]. The LCOs h-FTAA, q-FTAA, HS-84, and HS-169 show also binding to Aβ42 and tau fibrils. In contrast, AOI987 designed to target Aβ [38,39], binds to Aβ42 fibrils but not to tau fibrils (Fig. 1), as expected. The LCOs show different spectral characteristics when bound to tau fibrils, the detected emission peaks are for h-FTAA: 549 nm; q-FTAA: 530 nm; HS-84: 504 nm; and HS-169: 654 nm, respectively. Using the same incubation concentration and condition, h-FTAA and HS-84 give higher F.I. to tau fibrils compared to other probes (q-FTAA and HS-169).

 

Fig. 1. Comparison of the selectivity of different fluorescent probes to protein aggregates. Binding of (a) Thioflavin-T, (b) AOI987, and (c-f) LCOs HS-169, HS-84, h-FTAA and q-FTAA to recombinant Aβ42 fibril, and tau fibril.

Download Full Size | PPT Slide | PDF

As tauopathy deposits in human might differ in their structure and conformation from recombinant tau fibrils, we then evaluated the binding of LCOs to tauopathy on mouse brain sections of transgenic animals harboring extensive tau pathology. We choose the P301L line because these animal show an age-dependent accumulation of misfolded hyperphosphorylated tau aggregates in the brain regions (mainly hippocampus, amygdala and cortex), starting at around 7-9 months-of-age [16]. These animals do not show Aβ pathology making them an ideal tool to evaluate the LCOs selectivity towards tau [16].

Mice of 10 months-of-age displayed strong fluorescence signals in the hippocampus and cortex of the P301L mouse when brain sections were incubated with h-FTAA and HS-84 was observed (Figs. 2(b), (c), (f), (g)). In comparison, weaker fluorescence signals were detected in sections stained with HS-169 (Fig. 2(e)) as shown previously [27], and with q-FTAA (Fig. 2(a)). Lambda spectrum mapping using confocal microscopy provides full spectral information from stained brain tissue slices across a range of wavelengths. Results from lambda mapping shows that the major peaks of h-FTAA and HS-84 on P301L brain tau deposits are at 543 nm and 548 nm, respectively (Figs. 2(d), (h)). This demonstrates that h-FTAA has a similar spectral characteristic when bound to tau deposits in brain sections and recombinant tau fibrils, while HS-84 shows a blueshift in recombinant tau fibrils compared to tau deposits binding on brain sections. Taken together the results obtained on recombinant tau fibrils and P301L mouse brain, among all LCOs tested h-FTAA showed in vitro binding to tau fibrils and binding characteristics in brain sections of P301L. h-FTAA showed strong fluorescence emission upon binding in both, which favors its usage for in vivo fluorescence imaging in P301L mice.

 

Fig. 2. Evaluation of the cellular binding of luminescent conjugated oligothiophenes on P301L mouse brain tissue sections. Horizontal cortical brain sections from 10 months-of-age P301L mouse stained with (a) q-FTAA (green)/DAPI (white); (b, c) h-FTAA (green)/DAPI (white) and zoom-in; (e) HS-169 (red)/DAPI (white), and (f, g) HS-84 (green)/DAPI (white) and zoom-in;. Scale bar = 200 μm (a, b, e, f), 10 μm (c, g); (d, h) Lambda spectrum mapping of h-FTAA (c) and HS-84 (g) staining on P301L mouse brain slices showing the peak of binding.

Download Full Size | PPT Slide | PDF

3.2 In vivo LMI imaging with h-FTAA reveals tauopathy in the cortex of P301L mice

The bio-distribution and temporal dynamics of h-FTAA in mouse brain is not known in living tauopathy mouse models. Next we performed non-invasive imaging in P301L and non-transgenic littermate mice of 4-, 10- and 17-months-of-age. Mice were scanned in vivo by LMI and widefield imaging before and after intravenous administration of h-FTAA until 120 minutes post-injection. The h-FTAA uptake signals increased over time over the cerebrum in all groups, indicating that the probe reached the brain (Fig. 3(a)-(c)). F.I. was higher over time in the entire dorsal cortex of P301L compared to non-transgenic littermate mice (p = 0.0257, two-way ANOVA, Fig. 3(d)). Higher normalized F60-120 min/Fpre was observed in P301L compared to non-transgenic littermates (4.6 vs 1.9, t-test, p < 0.0001), indicating retention of probe in vivo in mice with tauopathy.

 

Fig. 3. In vivo large-field multifocal illumination (LMI) imaging of tauopathy. (a-c) In vivo LMI n the brain of P301L mice at 10- and 17 months-of-age, and non-transgenic littermate (NTL) at pre-injection and following i.v. tail vein bolus injection of h-FTAA till120 min post-injection. Fluorescence intensity (F.I.) normalized to pre-injection values; (d) Quantification of Fpost/Fpre) injection over time; NTL, n = 3, P301L n = 4; (e) Higher normalized F60-120 min/Fpre in P301L compare to NTL mice, *** p < 0.001 two-way ANOVA. Scale bar = 200 μm (a-c). (f-g) Corresponding LMI and widefield (WF) imaging and zoom-in views at 80 minutes post-injection in P301L mouse (b).

Download Full Size | PPT Slide | PDF

3.3 Ex vivo LMI imaging confirmed h-FTAA signals in the brain of P301L mice

To confirm the in vivo LMI imaging finding, ex vivo LMI and widefield fluorescence imaging were performed on dissected whole mouse brains and on coronal brain sections at approximately 130 minutes post-injection using the same set-sup. CNR is 18 times higher using LMI imaging (Fig. 4(b)) compared to widefield imaging (Fig. 4(a)) in the ex vivo mouse cerebral cortex (596 vs 163, p < 0.0001) (Fig. 4(m)). The ex vivo LMI imaging revealed fluorescent spots in the cerebral cortex (Figs. 4(b), (c), (g), especially the pyramidal layer Fig. 4(d)), hippocampus (Fig. 4 h) and fluorescent structures in the skull in P301L mice. In non-transgenic littermates no such fluorescent structures were observed after h-FTAA injection. This suggests that h-FTAA binds to tauopathy deposits in vivo after intravenous administration (Figs. 4(i)-(k)), while it is cleared form the normal brain over the imaging period. We quantified signal intensities in different tissue compartments. A four-fold higher levels of F.I. were observed in vivo (p = 0.0047, t-test, Figs. 4(e), (i)) and ex vivo (p = 0.0077, Figs. 4 (g), (k)) in the cerebral cortex in the P301L compared to non-transgenic littermate mice, as well as in the ex vivo skull (p = 0.0108, t-test, Figs. 4(f), (j)). The F.I. in the ex vivo mouse brain and skull were approximately 80% and 57% respectively of that in in vivo mouse head (Fig. 4(n)).

 

Fig. 4. Ex vivo large-field multifocal illumination (LMI) imaging compared to widefield (WF) fluorescence microscopy of tauopathy in P301L mouse brain. (a-b) Ex vivo WF and LMI imaging of one P301L mouse brain (signal ROI (red square), and background region (bk, blue square)); (c-d) Ex vivo LMI and zoom-in showing signal spots in the cortex of P301L mouse brain; Normalized representative LMI imaging in (e-h) 10 months-old P301L and (i-l) age-matched non-transgenic littermate mouse; (e, i) in vivo mouse head at 120 min post-injection, (f, j) ex vivo skull, (g, k) ex vivo whole brain and (h, l) zoomed-in coronal brain slices; (m) Higher contrast-to-noise ratio (CNR) in LMI imaging compared to widefield imaging analyzed using over P301 l mouse ex vivo cortex; (n) Quantification of signals in the brain and in the skull in P301L and non-transgenic littermate mice; * p < 0.05, ** p < 0.01, *** p < 0.001 t-test (m, n).

Download Full Size | PPT Slide | PDF

3.4 Specificity of h-FTAA for detection of tauopathy on brain sections from P301L mice

To validate the in vivo finding and to assess the specificity of h-FTAA binding to tau deposits in mouse brains, we performed immunohistochemistry on horizontal brain tissue sections from P301L mice and non-transgenic littermates using h-FTAA with phosphorylated tau AT-8 and AT-100 antibodies (counterstained with DAPI). P301L mice have only tauopathy deposits, and no Aβ aggregates (which is also positive to h-FTAA) [16,38,40]. In the P301L mouse brain, h-FTAA co-localized with AT-8 positive cells, which binds to sarkosyl-insoluble tau and soluble hyperphosphorylated tau [41] (Figs. 5(a), (b)). In addition, h-FTAA co-labeled neuronal inclusion that were positive for AT-100, which only recognizes sarkosyl-insoluble, but not soluble tau (Fig. 6(c)) [41]. Distribution in the cortex and hippocampus especially CA1 pyramidal neuron, cell bodies, apical dendrites, and in mossy fiber projection, moderate in the dentate gyrus granule cells were observed. No signal was observed on h-FTAA/AT-8 (Figs. 6(d), (e)) and h-FTAA/AT-100 (Figs. 6(f), (g)) stained non-transgenic littermate mouse brain sections, indicating specific targeting of the probe to tau deposits.

 

Fig. 5. Specificity of h-FTAA for tauopathy in P301L mouse brain tissue sections. (a-c) Immunohistochemistry of horizontal brain sections from the cortex and hippocampus of P301L mouse, demonstrating co-localization of AT-8, AT-100 and h-FTAA to tauopathy in P301L mouse brain; (d-g) No specific signals in the cortex and hippocampus of non-transgenic littermate mouse brain are stained by AT-8/ h-FTAA or AT-100/h-FTAA. (a, b, d, e) AT-8 (red), (c, f, g) AT-100 (red), h-FTAA (green), DAPI (white).

Download Full Size | PPT Slide | PDF

4. Discussion

Developing tools for non-invasive detection of tau deposits at high-resolution in animal models of tauopathy is critical for understanding disease mechanism [42] and for translational development of tau-targeted therapies and diagnostics [6,43–45]. Here we demonstrated a novel in vivo transcranial LMI imaging approach to map tau deposits at the entire cortical mantle in P301L mouse model of FTLD tauopathy using h-FTAA that binds with high sensitivity and specificity to tau aggregates.

Thanks to the inherent advantage of laser beam scanning, the proposed LMI imaging method can effectively reject the out-of-focus light, enabling minimally invasive imaging in vivo without employing craniotomy, an essential advantage especially when it comes to longitudinal study of disease progression, such as tauopathy spreading mechanism in the brain [46]. Due to improvement in the spatial resolution of image scanning microscopy, the LMI imaging approach can achieve 6 μm resolution across the entire mouse cortex. Compared to laser scanning confocal microscopy, LMI imaging is a highly parallelized technique employing hundreds of illumination foci, thus enabling fast imaging, which is crucial for mitigating motion artifacts in in vivo studies. In addition, the LMI imaging approach is optimally suited for imaging large objects up to a centimeter scale, which is not attainable with multi-photon microscopy methods that are further hindered by the lack of optimal labels with large absorption cross section and longer absorption/emission wavelengths. Thus, the set-up is ideally suited to detect immunological and vascular events in the mouse brain using dedicated probes [47–49].

Tau imaging has been challenging, due to the structural diversity of tau isoforms, the lack of specificity and off-target binding property of many tau imaging probes [50]. Recently a new family of LCOs were described that detect aggregated proteins such as Aβ and tau fibrils [32]. The LCOs h-FTAA [51], and HS-84 [27] have been used to detect tauopathy in postmortem human brain tissue and in intravital brain imaging of tau deposits in P301L mouse models using two-photon microscopy with a cranial window. Here, we demonstrated the in vivo transcranial imaging of taupathy in a non-invasive manner.

We first compared four LCOs for their suitability for in vivo LMI imaging. All probes have different spectral characteristics, where the emission peak of HS-169 would render the probe most suitable for deep tissue fluorescence imaging with less absorption and scattering compared to other probes with lower emission wavelengths. However, q-FTAA and HS-169 showed low fluorescence upon binding to tau aggregates in in vitro binding assay, while h-FTAA and HS-84 showed bright fluorescence. Moreover, we found that all LCOs did not only bind to tau but also to Aβ42 fibrils. They bind to protein aggregates having an extensive cross β-pleated sheet conformation [31], as many other tau probes such as PBB3, Thioflavin S, Congo Red, and its derivative FSB [30,52–54]. However, compared to dyes such as Thioflavin S and Congo Red, LCOs have a stronger fluorescence emission. The lack of selectivity restricts the use of LCOs in animal models of mixed Aβ and tau pathologies. It has been shown that some LCOs undergo a structural restriction upon protein binding and a shift of the emitted light occurs, dependent on the target protein and its conformation, which would allow discriminating protein deposits based on their spectroscopic signatures ex vivo [32].

We evaluated the binding of LCOs to tauopathy on mouse brain sections of P301L mice. Binding of probes to tau fibrils might be different to probe binding in brain tissue due to the structural diversity of tau aggregates. For example, it was reported recently that HS-169 binds to Aβ and tau fibrils [30], but does not recognize tau deposits in the brain of P301L mice (CaMKII) [27]. We found low fluorescence signals of q-FTAA and HS-169 on brain sections from P301L mice, while sections subjected to HS-84 and h-FTAA had intense and localized fluorescence. Since the lambda spectrum mapping showed a blueshift of HS-84 in tau binding on brain sections compared to h-FTAA, we opted for the use of h-FTAA for in vivo LMI imaging.

We investigated whether the h-FTAA would enter the brain across the blood-brain barrier in amounts sufficient for in vivo brain imaging using LMI. An increase in fluorescence was observed after intravenous administration of probe and uptake of probe to the brain of P301L mice was apparent after excising the brain from the skull. Moreover, we used the high-resolution capability of the LMI system and detected fluorescent circular structures in the excised brain. Tauopathy deposits in P301L (Thy1.2) mice start in entorhinal-hippocampal regions from approximately 7 months-of-age [16], are most pronounced in the cortex, amygdala and hippocampus, moderate in brain stem and striatum, and negligible in the cerebellum. The cortical signals detected by LMI imaging in vivo and ex vivo using h-FTAA are in accordance with immunohistochemical staining results (Figs. 4–6), and with the known tau distribution in the P301L mouse brain [40]. We observed that part of the signals originated for the skull in the tauopathy mouse brain. Due to the wavelength of the probe, hemoglobin may also contribute to the signal.

The skull impairs high-resolution optical imaging of the mouse cortex in vivo due to its strong scattering of the light. Moreover, we observed high signal surrounding the suture and in the skull after probe injection which we cannot currently explain. More studies are needed to elucidate the underpinnings of this phenomenon. It is likely attributed to differences in the vascularization of the bone marrow of the skull [55]. Bone marrow collecting venules have been described to run in parallel with sutures [56]. Circulating probe would give rise to high fluorescence intensities in these venules compared to the surrounding tissue. We did not include the suture signal in our quantification of the in vivo head (Figs. 3(d), (e)). It is unclear whether this phenomenon might be disease/pathology relevant. Using non-invasive fluorescence imaging set up, somatosensory-evoked rapid calcium transients in the GCaMP6f brain (peak excitation: 488 nm, emission: 512 nm) in vivo was detected despite blurred fluorescence images [57]. In the proposed LMI imaging method, the scattering of the excitation light in the surrounding tissue was mitigated by introducing the multifocal illumination. The scattering of the emitted fluorescence signal was reduced during image reconstruction with only the local maxima in the image were extracted and further superimposed in the final reconstructed image. Chronic large cranial window techniques and skull optical clearing solutions were proposed to reduce the skull scattering coefficient [58]. In addition, detection of tau deposits from the brain could be improved by using red shifted tau imaging probes with longer excitation and emission wavelengths. Further studies are needed to clarify the signals within skull in this tauopathy mouse model.

We screened LCOs and assessed the specificity of h-FTAA as a tau probe and whether h-FTAA can detect pathological tau in all tauopathies in brain tissue slices from P301L mouse using immunohistochemistry. We used antibodies that recognize insoluble (AT-100), and filamentous and soluble (AT-8) forms of hyperphosphorylated tau. The h-FTAA localized well both with AT-8 and AT-100 positive cells. In comparison, no probe accumulation was observed in the brain of non-transgenic littermates that were tau negative, suggesting a specificity of the probe in vivo. We observed that h-FTAA were not washed away again with time, potentially suitable for longitudinal imaging of tauopathy deposits in vivo [27]. HS-84 that showed a blue shift probably due to selectivity for in vitro tau fibrils which have an entirely different structure than in vivo murine tau fibrils as demonstrated by the cryogenic electron microscopy structures [59].

In conclusion, we demonstrated LMI fluorescence imaging for tauopathy in P301L mice in vivo. Such platform will provide insight in mechanistic studies of tau spreading [60,61] and clearance [62], as well as in monitoring of tau targeting therapeutics.

Funding

Vontobel-Stiftung; Vetenskapsrådet (2016–00748); European Research Council (ERC-2015-CoG-682379); H2020 Marie Skłodowska-Curie Actions (746430-MSIOAM); Stiftung Synapsis - Alzheimer Forschung Schweiz AFS (2017 CDA-03); ERA-NET NEURON (32NE30_173678/1); Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung (320030_179277).

Disclosures

The authors declare no conflicts of interest

References

1. M. G. Spillantini and M. Goedert, “Tau pathology and neurodegeneration,” Lancet Neurol. 12(6), 609–622 (2013). [CrossRef]  

2. V. M. Lee, M. Goedert, and J. Q. Trojanowski, “Neurodegenerative tauopathies,” Annu. Rev. Neurosci. 24(1), 1121–1159 (2001). [CrossRef]  

3. B. J. Hanseeuw, R. A. Betensky, H. I. L. Jacobs, A. P. Schultz, J. Sepulcre, J. A. Becker, D. M. O. Cosio, M. Farrell, Y. T. Quiroz, E. C. Mormino, R. F. Buckley, K. V. Papp, R. A. Amariglio, I. Dewachter, A. Ivanoiu, W. Huijbers, T. Hedden, G. A. Marshall, J. P. Chhatwal, D. M. Rentz, R. A. Sperling, and K. Johnson, “Association of Amyloid and Tau With Cognition in Preclinical Alzheimer Disease: A Longitudinal Study,” JAMA Neurol. 76(8), 915–924 (2019). [CrossRef]  

4. R. La Joie, A. V. Visani, S. L. Baker, J. A. Brown, V. Bourakova, J. Cha, K. Chaudhary, L. Edwards, L. Iaccarino, M. Janabi, O. H. Lesman-Segev, Z. A. Miller, D. C. Perry, J. P. O’Neil, J. Pham, J. C. Rojas, H. J. Rosen, W. W. Seeley, R. M. Tsai, B. L. Miller, W. J. Jagust, and G. D. Rabinovici, “Prospective longitudinal atrophy in Alzheimer’s disease correlates with the intensity and topography of baseline tau-PET,” Sci. Transl. Med. 12(524), eaau5732 (2020). [CrossRef]  

5. M. Scholl, S. N. Lockhart, D. R. Schonhaut, J. P. O’Neil, M. Janabi, R. Ossenkoppele, S. L. Baker, J. W. Vogel, J. Faria, H. D. Schwimmer, G. D. Rabinovici, and W. J. Jagust, “PET Imaging of Tau Deposition in the Aging Human Brain,” Neuron 89(5), 971–982 (2016). [CrossRef]  

6. E. E. Congdon and E. M. Sigurdsson, “Tau-targeting therapies for Alzheimer disease,” Nat. Rev. Neurol. 14(7), 399–415 (2018). [CrossRef]  

7. M. Ono, N. Sahara, K. Kumata, B. Ji, R. Ni, S. Koga, D. W. Dickson, J. Q. Trojanowski, V. M.-Y. Lee, M. Yoshida, I. Hozumi, Y. Yoshiyama, J. C. v. Swieten, A. Nordberg, T. Suhara, M.-R. Zhang, and M. Higuchi, “Distinct binding of PET ligands PBB3 and AV-1451 to tau fibril strains in neurodegenerative tauopathies,” Brain 140, aww339 (2017). [CrossRef]  

8. K. A. Johnson, A. Schultz, R. A. Betensky, J. A. Becker, J. Sepulcre, D. Rentz, E. Mormino, J. Chhatwal, R. Amariglio, K. Papp, G. Marshall, M. Albers, S. Mauro, L. Pepin, J. Alverio, K. Judge, M. Philiossaint, T. Shoup, D. Yokell, B. Dickerson, T. Gomez-Isla, B. Hyman, N. Vasdev, and R. Sperling, “Tau positron emission tomographic imaging in aging and early Alzheimer disease,” Ann Neurol. 79(1), 110–119 (2016). [CrossRef]  

9. E. D. Hostetler, A. M. Walji, Z. Zeng, P. Miller, I. Bennacef, C. Salinas, B. Connolly, L. Gantert, H. Haley, M. Holahan, M. Purcell, K. Riffel, T. G. Lohith, P. Coleman, A. Soriano, A. Ogawa, S. Xu, X. Zhang, E. Joshi, J. Della Rocca, D. Hesk, D. J. Schenk, and J. L. Evelhoch, ““Preclinical Characterization of 18F-MK-6240, a Promising PET Tracer for In Vivo Quantification of Human Neurofibrillary Tangles,” Journal of nuclear medicine : official publication,” J. Nuclear Medicine 57(10), 1599–1606 (2016). [CrossRef]  

10. H. Kroth, F. Oden, J. Molette, H. Schieferstein, F. Capotosti, A. Mueller, M. Berndt, H. Schmitt-Willich, V. Darmency, E. Gabellieri, C. Boudou, T. Juergens, Y. Varisco, E. Vokali, D. T. Hickman, G. Tamagnan, A. Pfeifer, L. Dinkelborg, A. Muhs, and A. Stephens, “Discovery and preclinical characterization of [(18)F]PI-2620, a next-generation tau PET tracer for the assessment of tau pathology in Alzheimer's disease and other tauopathies,” Eur. J. Nucl. Med. Mol. Imaging 46(10), 2178–2189 (2019). [CrossRef]  

11. A. Mueller, S. Bullich, O. Barret, J. Madonia, M. Berndt, C. Papin, A. Perrotin, N. Koglin, H. Kroth, A. Pfeifer, G. Tamagnan, J. P. Seibyl, K. Marek, S. de Santi, L. M. Dinkelborg, and A. W. Stephens, “Tau PET imaging with (18)F-PI-2620 in patients with Alzheimer's disease and healthy controls: a first-in-human study,” J. Nucl. Med. 61(6), 911–919 (2020). [CrossRef]  

12. S. Sanabria Bohorquez, J. Marik, A. Ogasawara, J. N. Tinianow, H. S. Gill, O. Barret, G. Tamagnan, D. Alagille, G. Ayalon, P. Manser, T. Bengtsson, M. Ward, S. P. Williams, G. A. Kerchner, J. P. Seibyl, K. Marek, and R. M. Weimer, “[(18)F]GTP1 (Genentech Tau Probe 1), a radioligand for detecting neurofibrillary tangle tau pathology in Alzheimer's disease,” Eur. J. Nucl. Med. Mol. Imaging 46(10), 2077–2089 (2019). [CrossRef]  

13. Y. Yoshiyama, M. Higuchi, B. Zhang, S. M. Huang, N. Iwata, T. C. Saido, J. Maeda, T. Suhara, J. Q. Trojanowski, and V. M. Lee, “Synapse loss and microglial activation precede tangles in a P301S tauopathy mouse model,” Neuron 53(3), 337–351 (2007). [CrossRef]  

14. K. SantaCruz, J. Lewis, T. Spires, J. Paulson, L. Kotilinek, M. Ingelsson, A. Guimaraes, M. DeTure, M. Ramsden, E. McGowan, C. Forster, M. Yue, J. Orne, C. Janus, A. Mariash, M. Kuskowski, B. Hyman, M. Hutton, and K. H. Ashe, “Tau Suppression in a Neurodegenerative Mouse Model Improves Memory Function,” Science 309(5733), 476–481 (2005). [CrossRef]  

15. J. Lewis, E. McGowan, J. Rockwood, H. Melrose, P. Nacharaju, M. Van Slegtenhorst, K. Gwinn-Hardy, M. Paul Murphy, M. Baker, X. Yu, K. Duff, J. Hardy, A. Corral, W. L. Lin, S. H. Yen, D. W. Dickson, P. Davies, and M. Hutton, “Neurofibrillary tangles, amyotrophy and progressive motor disturbance in mice expressing mutant (P301L) tau protein,” Nat. Genet. 25(4), 402–405 (2000). [CrossRef]  

16. J. Gotz, F. Chen, J. van Dorpe, and R. M. Nitsch, “Formation of neurofibrillary tangles in P301 l tau transgenic mice induced by Abeta 42 fibrils,” Science 293(5534), 1491–1495 (2001). [CrossRef]  

17. S. Hashimoto, Y. Matsuba, N. Kamano, N. Mihira, N. Sahara, J. Takano, S. I. Muramatsu, T. C. Saido, and T. Saito, “Tau binding protein CAPON induces tau aggregation and neurodegeneration,” Nat. Commun. 10(1), 2394 (2019). [CrossRef]  

18. N. Sahara, M. Shimojo, M. Ono, H. Takuwa, M. Febo, M. Higuchi, and T. Suhara, “In Vivo Tau Imaging for a Diagnostic Platform of Tauopathy Using the rTg4510 Mouse Line,” Front Neurol. 8, 663 (2017). [CrossRef]  

19. P. Marinkovic, S. Blumenstock, P. M. Goltstein, V. Korzhova, F. Peters, A. Knebl, and J. Herms, “In vivo imaging reveals reduced activity of neuronal circuits in a mouse tauopathy model,” Brain 142(4), 1051–1062 (2019). [CrossRef]  

20. M. Maruyama, H. Shimada, T. Suhara, H. Shinotoh, B. Ji, J. Maeda, M. R. Zhang, J. Q. Trojanowski, V. M. Lee, M. Ono, K. Masamoto, H. Takano, N. Sahara, N. Iwata, N. Okamura, S. Furumoto, Y. Kudo, Q. Chang, T. C. Saido, A. Takashima, J. Lewis, M. K. Jang, I. Aoki, H. Ito, and M. Higuchi, “Imaging of tau pathology in a tauopathy mouse model and in Alzheimer patients compared to normal controls,” Neuron 79(6), 1094–1108 (2013). [CrossRef]  

21. R. Ni, B. Ji, M. Ono, N. Sahara, M. R. Zhang, I. Aoki, A. Nordberg, T. Suhara, and M. Higuchi, ““Comparative in-vitro and in-vivo quantifications of pathological tau deposits and their association with neurodegeneration in tauopathy mouse models,” Journal of nuclear medicine : official publication,” J. Nucl. Med. 59(6), 960–966 (2018). [CrossRef]  

22. A. Ishikawa, M. Tokunaga, J. Maeda, T. Minamihisamatsu, M. Shimojo, H. Takuwa, M. Ono, R. Ni, S. Hirano, S. Kuwabara, B. Ji, M. R. Zhang, I. Aoki, T. Suhara, M. Higuchi, and N. Sahara, “In Vivo Visualization of Tau Accumulation, Microglial Activation, and Brain Atrophy in a Mouse Model of Tauopathy rTg4510,” J. Alzheimer’s Dis. 61(3), 1037–1052 (2018). [CrossRef]  

23. S. Krishnaswamy, Y. Lin, W. J. Rajamohamedsait, H. B. Rajamohamedsait, P. Krishnamurthy, and E. M. Sigurdsson, “Antibody-derived in vivo imaging of tau pathology,” J. Neuroscience 34(50), 16835–16850 (2014). [CrossRef]  

24. Q. Wu, Y. Lin, J. Gu, and E. M. Sigurdsson, “Dynamic assessment of tau immunotherapies in the brains of live animals by two-photon imaging,” EBioMedicine 35, 270–278 (2018). [CrossRef]  

25. A. Velasco, G. Fraser, P. Delobel, B. Ghetti, I. Lavenir, and M. Goedert, “Detection of filamentous tau inclusions by the fluorescent Congo red derivative FSB [(trans,trans)-1-fluoro-2,5-bis(3-hydroxycarbonyl-4-hydroxy)styrylbenzene],” FEBS Lett. 582(6), 901–906 (2008). [CrossRef]  

26. A. de Calignon, L. M. Fox, R. Pitstick, G. A. Carlson, B. J. Bacskai, T. L. Spires-Jones, and B. T. Hyman, “Caspase activation precedes and leads to tangles,” Nature 464(7292), 1201–1204 (2010). [CrossRef]  

27. M. Calvo-Rodriguez, S. S. Hou, A. C. Snyder, S. Dujardin, H. Shirani, K. P. R. Nilsson, and B. J. Bacskai, “In vivo detection of tau fibrils and amyloid beta aggregates with luminescent conjugated oligothiophenes and multiphoton microscopy,” Acta Neuropathol. Commun. 7(1), 171 (2019). [CrossRef]  

28. A. Aslund, C. J. Sigurdson, T. Klingstedt, S. Grathwohl, T. Bolmont, D. L. Dickstein, E. Glimsdal, S. Prokop, M. Lindgren, P. Konradsson, D. M. Holtzman, P. R. Hof, F. L. Heppner, S. Gandy, M. Jucker, A. Aguzzi, P. Hammarström, and K. P. Nilsson, “Novel pentameric thiophene derivatives for in vitro and in vivo optical imaging of a plethora of protein aggregates in cerebral amyloidoses,” ACS Chem. Biol. 4(8), 673–684 (2009). [CrossRef]  

29. Z. Chen, B. Mc Larney, J. Rebling, X. L. Deán-Ben, Q. Zhou, S. Gottschalk, and D. Razansky, “High-Speed Large-Field Multifocal Illumination Fluorescence Microscopy,” Laser Photonics Rev. 14, 1900070 (2020). [CrossRef]  

30. R. Ni, Z. Chen, G. Shi, A. Villois, Q. Zhou, P. Arosio, R. M. Nitsch, P. R. Nilsson, J. Klohs, and D. Razansky, “Transcranial in vivo detection of Aβ at single plaque resolution with large-field multifocal illumination fluorescence microscopy,” bioRxiv, 2020.2002.2001.929844 (2020).

31. B. M. Burmann, J. A. Gerez, I. Matecko-Burmann, S. Campioni, P. Kumari, D. Ghosh, A. Mazur, E. E. Aspholm, D. Sulskis, M. Wawrzyniuk, T. Bock, A. Schmidt, S. G. D. Rudiger, R. Riek, and S. Hiller, “Regulation of alpha-synuclein by chaperones in mammalian cells,” Nature 577(7788), 127–132 (2020). [CrossRef]  

32. J. A. Gerez, N. C. Prymaczok, E. Rockenstein, U. S. Herrmann, P. Schwarz, A. Adame, R. I. Enchev, T. Courtheoux, P. J. Boersema, R. Riek, M. Peter, A. Aguzzi, E. Masliah, and P. Picotti, “A cullin-RING ubiquitin ligase targets exogenous alpha-synuclein and inhibits Lewy body-like pathology,” Sci. Transl. Med. 11(495), eaau6722 (2019). [CrossRef]  

33. H. Shirani, M. Linares, C. J. Sigurdson, M. Lindgren, P. Norman, and K. P. Nilsson, “A Palette of Fluorescent Thiophene-Based Ligands for the Identification of Protein Aggregates,” Chem. Eur. J. 21(43), 15133–15137 (2015). [CrossRef]  

34. T. Klingstedt, A. Aslund, R. A. Simon, L. B. Johansson, J. J. Mason, S. Nystrom, P. Hammarstrom, and K. P. Nilsson, “Synthesis of a library of oligothiophenes and their utilization as fluorescent ligands for spectral assignment of protein aggregates,” Org. Biomol. Chem. 9(24), 8356–8370 (2011). [CrossRef]  

35. R. Ni, Y. Zarb, G. A. Kuhn, R. Müller, Y. Yundung, R. M. Nitsch, L. Kulic, A. Keller, and J. Klohs, “Tau deposition is associated with imaging patterns of tissue calcification in the P301L mouse model of human tauopathy,” bioRxiv, 851915 (2019).

36. I. Gregor and J. Enderlein, “Image scanning microscopy,” Curr. Opin. Chem. Biol. 51, 74–83 (2019). [CrossRef]  

37. C. A. Lasagna-Reeves, D. L. Castillo-Carranza, U. Sengupta, J. Sarmiento, J. Troncoso, G. R. Jackson, and R. Kayed, “Identification of oligomers at early stages of tau aggregation in Alzheimer's disease,” FASEB J. 26(5), 1946–1959 (2012). [CrossRef]  

38. R. Ni, X. L. Dean-Ben, D. Kirschenbaum, M. Rudin, Z. Chen, A. Crimi, F. Voigt, P. R. Nilsson, F. Helmchen, R. M. Nitsch, A. Aguzzi, D. Razansky, and J. Klohs, “Whole brain optoacoustic tomography reveals strain-specific regional beta-amyloid densities in Alzheimer`s disease amyloidosis models,” bioRxiv, DOI: 10.1101/2020.1102.1125.964064 (2020).

39. M. Hintersteiner, A. Enz, P. Frey, A. L. Jaton, W. Kinzy, R. Kneuer, U. Neumann, M. Rudin, M. Staufenbiel, M. Stoeckli, K. H. Wiederhold, and H. U. Gremlich, “In vivo detection of amyloid-beta deposits by near-infrared imaging using an oxazine-derivative probe,” Nat. Biotechnol. 23(5), 577–583 (2005). [CrossRef]  

40. J. Gotz, F. Chen, R. Barmettler, and R. M. Nitsch, “Tau filament formation in transgenic mice expressing P301L tau,” J. Biol. Chem. 276(1), 529–534 (2001). [CrossRef]  

41. P. Delobel, I. Lavenir, G. Fraser, E. Ingram, M. Holzer, B. Ghetti, M. G. Spillantini, R. A. Crowther, and M. Goedert, “Analysis of tau phosphorylation and truncation in a mouse model of human tauopathy,” Am. J. Pathology 172(1), 123–131 (2008). [CrossRef]  

42. Z. He, J. D. McBride, H. Xu, L. Changolkar, S. J. Kim, B. Zhang, S. Narasimhan, G. S. Gibbons, J. L. Guo, M. Kozak, G. D. Schellenberg, J. Q. Trojanowski, and V. M. Lee, “Transmission of tauopathy strains is independent of their isoform composition,” Nat. Commun. 11(1), 7 (2020). [CrossRef]  

43. K. M. Schoch, S. L. DeVos, R. L. Miller, S. J. Chun, M. Norrbom, D. F. Wozniak, H. N. Dawson, C. F. Bennett, F. Rigo, and T. M. Miller, “Increased 4R-Tau Induces Pathological Changes in a Human-Tau Mouse Model,” Neuron 90(5), 941–947 (2016). [CrossRef]  

44. B. Dejanovic, M. A. Huntley, A. De Maziere, W. J. Meilandt, T. Wu, K. Srinivasan, Z. Jiang, V. Gandham, B. A. Friedman, H. Ngu, O. Foreman, R. A. D. Carano, B. Chih, J. Klumperman, C. Bakalarski, J. E. Hanson, and M. Sheng, “Changes in the Synaptic Proteome in Tauopathy and Rescue of Tau-Induced Synapse Loss by C1q Antibodies,” Neuron 100(6), 1322–1336.e7 (2018). [CrossRef]  

45. C. H. Lo, C. K. Lim, Z. Ding, S. P. Wickramasinghe, A. R. Braun, K. H. Ashe, E. Rhoades, D. D. Thomas, and J. N. Sachs, “Targeting the ensemble of heterogeneous tau oligomers in cells: A novel small molecule screening platform for tauopathies,” Alzheimer’s & Dementia 15(11), 1489–1502 (2019). [CrossRef]  

46. M. Colin, S. Dujardin, S. Schraen-Maschke, G. Meno-Tetang, C. Duyckaerts, J. P. Courade, and L. Buee, “From the prion-like propagation hypothesis to therapeutic strategies of anti-tau immunotherapy,” Acta Neuropathol. 139(1), 3–25 (2020). [CrossRef]  

47. J. Klohs, N. Baeva, J. Steinbrink, R. Bourayou, C. Boettcher, G. Royl, D. Megow, U. Dirnagl, J. Priller, and A. Wunder, “In vivo near-infrared fluorescence imaging of matrix metalloproteinase activity after cerebral ischemia,” J. Cereb. Blood Flow Metab. 29(7), 1284–1292 (2009). [CrossRef]  

48. R. Ni, M. Vaas, W. Ren, and J. Klohs, “Non-invasive detection of acute cerebral hypoxia and subsequent matrix-metalloproteinase activity in a mouse model of cerebral ischemia using multispectral-optoacoustic-tomography,” Neurophotonics 5(1), 015005 (2018). [CrossRef]  

49. J. Klohs, “An Integrated View on Vascular Dysfunction in Alzheimer’s Disease,” Neurodegenerative Diseases (2020).

50. V. L. Villemagne, V. Dore, S. C. Burnham, C. L. Masters, and C. C. Rowe, “Imaging tau and amyloid-beta proteinopathies in Alzheimer disease and other conditions,” Nat. Rev. Neurol. 14(4), 225–236 (2018). [CrossRef]  

51. B. Wegenast-Braun, A. Skodras, G. Bayraktar, J. Mahler, S. Fritschi, T. Klingstedt, J. Mason, P. Hammarström, K. Nilsson, C. Liebig, and M. Jucker, “Spectral Discrimination of Cerebral Amyloid Lesions after Peripheral Application of Luminescent Conjugated Oligothiophenes,” Am. J. Pathology 181(6), 1953–1960 (2012). [CrossRef]  

52. P. Verwilst, H. S. Kim, S. Kim, C. Kang, and J. S. Kim, “Shedding light on tau protein aggregation: the progress in developing highly selective fluorophores,” Chem. Soc. Rev. 47(7), 2249–2265 (2018). [CrossRef]  

53. P. Füger, J. K. Hefendehl, K. Veeraraghavalu, A.-C. Wendeln, C. Schlosser, U. Obermüller, B. M. Wegenast-Braun, J. J. Neher, P. Martus, S. Kohsaka, M. Thunemann, R. Feil, S. S. Sisodia, A. Skodras, and M. Jucker, “Microglia turnover with aging and in an Alzheimer's model via long-term in vivo single-cell imaging,” Nat. Neurosci. 20(10), 1371–1376 (2017). [CrossRef]  

54. K. V. Kuchibhotla, S. Wegmann, K. J. Kopeikina, J. Hawkes, N. Rudinskiy, M. L. Andermann, T. L. Spires-Jones, B. J. Bacskai, and B. T. Hyman, “Neurofibrillary tangle-bearing neurons are functionally integrated in cortical circuits in vivo,” Proc. Natl. Acad. Sci. 111(1), 510–514 (2014). [CrossRef]  

55. F. Lassailly, K. Foster, L. Lopez-Onieva, E. Currie, and D. Bonnet, “Multimodal imaging reveals structural and functional heterogeneity in different bone marrow compartments: functional implications on hematopoietic stem cells,” Blood 122(10), 1730–1740 (2013). [CrossRef]  

56. I. B. Mazo, J.-C. Gutierrez-Ramos, P. S. Frenette, R. O. Hynes, D. D. Wagner, and U. H. von Andrian, “Hematopoietic Progenitor Cell Rolling in Bone Marrow Microvessels: Parallel Contributions by Endothelial Selectins and Vascular Cell Adhesion Molecule 1,” J. Exp. Med. 188(3), 465–474 (1998). [CrossRef]  

57. S. Gottschalk, O. Degtyaruk, B. Mc Larney, J. Rebling, M. A. Hutter, X. L. Deán-Ben, S. Shoham, and D. Razansky, “Rapid volumetric optoacoustic imaging of neural dynamics across the mouse brain,” Nat. Biomed. Eng. 3(5), 392–401 (2019). [CrossRef]  

58. Y. Zhang, C. Zhang, X. Zhong, and D. Zhu, “Quantitative evaluation of SOCS-induced optical clearing efficiency of skull,” Quant. Imaging Med. Surg. 5, 136–142 (2015). [CrossRef]  

59. A. W. P. Fitzpatrick, B. Falcon, S. He, A. G. Murzin, G. Murshudov, H. J. Garringer, R. A. Crowther, B. Ghetti, M. Goedert, and S. H. W. Scheres, “Cryo-EM structures of tau filaments from Alzheimer's disease,” Nature 547(7662), 185–190 (2017). [CrossRef]  

60. S. K. Kaufman, D. W. Sanders, T. L. Thomas, A. J. Ruchinskas, J. Vaquer-Alicea, A. M. Sharma, T. M. Miller, and M. I. Diamond, “Tau Prion Strains Dictate Patterns of Cell Pathology, Progression Rate, and Regional Vulnerability In Vivo,” Neuron 92(4), 796–812 (2016). [CrossRef]  

61. E. J. Kim, J. L. Hwang, S. E. Gaus, A. L. Nana, J. Deng, J. A. Brown, S. Spina, M. J. Lee, E. M. Ramos, L. T. Grinberg, J. H. Kramer, A. L. Boxer, M. L. Gorno-Tempini, H. J. Rosen, B. L. Miller, and W. W. Seeley, “Evidence of corticofugal tau spreading in patients with frontotemporal dementia,” Acta Neuropathol. 139(1), 27–43 (2020). [CrossRef]  

62. T. K. Patel, L. Habimana-Griffin, X. Gao, B. Xu, S. Achilefu, K. Alitalo, C. A. McKee, P. W. Sheehan, E. S. Musiek, C. Xiong, D. Coble, and D. M. Holtzman, “Dural lymphatics regulate clearance of extracellular tau from the CNS,” Mol. Neurodegener. 14(1), 11 (2019). [CrossRef]  

References

  • View by:
  • Article Order
  • |
  • Year
  • |
  • Author
  • |
  • Publication
  1. M. G. Spillantini and M. Goedert, “Tau pathology and neurodegeneration,” Lancet Neurol. 12(6), 609–622 (2013).
    [Crossref]
  2. V. M. Lee, M. Goedert, and J. Q. Trojanowski, “Neurodegenerative tauopathies,” Annu. Rev. Neurosci. 24(1), 1121–1159 (2001).
    [Crossref]
  3. B. J. Hanseeuw, R. A. Betensky, H. I. L. Jacobs, A. P. Schultz, J. Sepulcre, J. A. Becker, D. M. O. Cosio, M. Farrell, Y. T. Quiroz, E. C. Mormino, R. F. Buckley, K. V. Papp, R. A. Amariglio, I. Dewachter, A. Ivanoiu, W. Huijbers, T. Hedden, G. A. Marshall, J. P. Chhatwal, D. M. Rentz, R. A. Sperling, and K. Johnson, “Association of Amyloid and Tau With Cognition in Preclinical Alzheimer Disease: A Longitudinal Study,” JAMA Neurol. 76(8), 915–924 (2019).
    [Crossref]
  4. R. La Joie, A. V. Visani, S. L. Baker, J. A. Brown, V. Bourakova, J. Cha, K. Chaudhary, L. Edwards, L. Iaccarino, M. Janabi, O. H. Lesman-Segev, Z. A. Miller, D. C. Perry, J. P. O’Neil, J. Pham, J. C. Rojas, H. J. Rosen, W. W. Seeley, R. M. Tsai, B. L. Miller, W. J. Jagust, and G. D. Rabinovici, “Prospective longitudinal atrophy in Alzheimer’s disease correlates with the intensity and topography of baseline tau-PET,” Sci. Transl. Med. 12(524), eaau5732 (2020).
    [Crossref]
  5. M. Scholl, S. N. Lockhart, D. R. Schonhaut, J. P. O’Neil, M. Janabi, R. Ossenkoppele, S. L. Baker, J. W. Vogel, J. Faria, H. D. Schwimmer, G. D. Rabinovici, and W. J. Jagust, “PET Imaging of Tau Deposition in the Aging Human Brain,” Neuron 89(5), 971–982 (2016).
    [Crossref]
  6. E. E. Congdon and E. M. Sigurdsson, “Tau-targeting therapies for Alzheimer disease,” Nat. Rev. Neurol. 14(7), 399–415 (2018).
    [Crossref]
  7. M. Ono, N. Sahara, K. Kumata, B. Ji, R. Ni, S. Koga, D. W. Dickson, J. Q. Trojanowski, V. M.-Y. Lee, M. Yoshida, I. Hozumi, Y. Yoshiyama, J. C. v. Swieten, A. Nordberg, T. Suhara, M.-R. Zhang, and M. Higuchi, “Distinct binding of PET ligands PBB3 and AV-1451 to tau fibril strains in neurodegenerative tauopathies,” Brain 140, aww339 (2017).
    [Crossref]
  8. K. A. Johnson, A. Schultz, R. A. Betensky, J. A. Becker, J. Sepulcre, D. Rentz, E. Mormino, J. Chhatwal, R. Amariglio, K. Papp, G. Marshall, M. Albers, S. Mauro, L. Pepin, J. Alverio, K. Judge, M. Philiossaint, T. Shoup, D. Yokell, B. Dickerson, T. Gomez-Isla, B. Hyman, N. Vasdev, and R. Sperling, “Tau positron emission tomographic imaging in aging and early Alzheimer disease,” Ann Neurol. 79(1), 110–119 (2016).
    [Crossref]
  9. E. D. Hostetler, A. M. Walji, Z. Zeng, P. Miller, I. Bennacef, C. Salinas, B. Connolly, L. Gantert, H. Haley, M. Holahan, M. Purcell, K. Riffel, T. G. Lohith, P. Coleman, A. Soriano, A. Ogawa, S. Xu, X. Zhang, E. Joshi, J. Della Rocca, D. Hesk, D. J. Schenk, and J. L. Evelhoch, ““Preclinical Characterization of 18F-MK-6240, a Promising PET Tracer for In Vivo Quantification of Human Neurofibrillary Tangles,” Journal of nuclear medicine : official publication,” J. Nuclear Medicine 57(10), 1599–1606 (2016).
    [Crossref]
  10. H. Kroth, F. Oden, J. Molette, H. Schieferstein, F. Capotosti, A. Mueller, M. Berndt, H. Schmitt-Willich, V. Darmency, E. Gabellieri, C. Boudou, T. Juergens, Y. Varisco, E. Vokali, D. T. Hickman, G. Tamagnan, A. Pfeifer, L. Dinkelborg, A. Muhs, and A. Stephens, “Discovery and preclinical characterization of [(18)F]PI-2620, a next-generation tau PET tracer for the assessment of tau pathology in Alzheimer's disease and other tauopathies,” Eur. J. Nucl. Med. Mol. Imaging 46(10), 2178–2189 (2019).
    [Crossref]
  11. A. Mueller, S. Bullich, O. Barret, J. Madonia, M. Berndt, C. Papin, A. Perrotin, N. Koglin, H. Kroth, A. Pfeifer, G. Tamagnan, J. P. Seibyl, K. Marek, S. de Santi, L. M. Dinkelborg, and A. W. Stephens, “Tau PET imaging with (18)F-PI-2620 in patients with Alzheimer's disease and healthy controls: a first-in-human study,” J. Nucl. Med. 61(6), 911–919 (2020).
    [Crossref]
  12. S. Sanabria Bohorquez, J. Marik, A. Ogasawara, J. N. Tinianow, H. S. Gill, O. Barret, G. Tamagnan, D. Alagille, G. Ayalon, P. Manser, T. Bengtsson, M. Ward, S. P. Williams, G. A. Kerchner, J. P. Seibyl, K. Marek, and R. M. Weimer, “[(18)F]GTP1 (Genentech Tau Probe 1), a radioligand for detecting neurofibrillary tangle tau pathology in Alzheimer's disease,” Eur. J. Nucl. Med. Mol. Imaging 46(10), 2077–2089 (2019).
    [Crossref]
  13. Y. Yoshiyama, M. Higuchi, B. Zhang, S. M. Huang, N. Iwata, T. C. Saido, J. Maeda, T. Suhara, J. Q. Trojanowski, and V. M. Lee, “Synapse loss and microglial activation precede tangles in a P301S tauopathy mouse model,” Neuron 53(3), 337–351 (2007).
    [Crossref]
  14. K. SantaCruz, J. Lewis, T. Spires, J. Paulson, L. Kotilinek, M. Ingelsson, A. Guimaraes, M. DeTure, M. Ramsden, E. McGowan, C. Forster, M. Yue, J. Orne, C. Janus, A. Mariash, M. Kuskowski, B. Hyman, M. Hutton, and K. H. Ashe, “Tau Suppression in a Neurodegenerative Mouse Model Improves Memory Function,” Science 309(5733), 476–481 (2005).
    [Crossref]
  15. J. Lewis, E. McGowan, J. Rockwood, H. Melrose, P. Nacharaju, M. Van Slegtenhorst, K. Gwinn-Hardy, M. Paul Murphy, M. Baker, X. Yu, K. Duff, J. Hardy, A. Corral, W. L. Lin, S. H. Yen, D. W. Dickson, P. Davies, and M. Hutton, “Neurofibrillary tangles, amyotrophy and progressive motor disturbance in mice expressing mutant (P301L) tau protein,” Nat. Genet. 25(4), 402–405 (2000).
    [Crossref]
  16. J. Gotz, F. Chen, J. van Dorpe, and R. M. Nitsch, “Formation of neurofibrillary tangles in P301 l tau transgenic mice induced by Abeta 42 fibrils,” Science 293(5534), 1491–1495 (2001).
    [Crossref]
  17. S. Hashimoto, Y. Matsuba, N. Kamano, N. Mihira, N. Sahara, J. Takano, S. I. Muramatsu, T. C. Saido, and T. Saito, “Tau binding protein CAPON induces tau aggregation and neurodegeneration,” Nat. Commun. 10(1), 2394 (2019).
    [Crossref]
  18. N. Sahara, M. Shimojo, M. Ono, H. Takuwa, M. Febo, M. Higuchi, and T. Suhara, “In Vivo Tau Imaging for a Diagnostic Platform of Tauopathy Using the rTg4510 Mouse Line,” Front Neurol. 8, 663 (2017).
    [Crossref]
  19. P. Marinkovic, S. Blumenstock, P. M. Goltstein, V. Korzhova, F. Peters, A. Knebl, and J. Herms, “In vivo imaging reveals reduced activity of neuronal circuits in a mouse tauopathy model,” Brain 142(4), 1051–1062 (2019).
    [Crossref]
  20. M. Maruyama, H. Shimada, T. Suhara, H. Shinotoh, B. Ji, J. Maeda, M. R. Zhang, J. Q. Trojanowski, V. M. Lee, M. Ono, K. Masamoto, H. Takano, N. Sahara, N. Iwata, N. Okamura, S. Furumoto, Y. Kudo, Q. Chang, T. C. Saido, A. Takashima, J. Lewis, M. K. Jang, I. Aoki, H. Ito, and M. Higuchi, “Imaging of tau pathology in a tauopathy mouse model and in Alzheimer patients compared to normal controls,” Neuron 79(6), 1094–1108 (2013).
    [Crossref]
  21. R. Ni, B. Ji, M. Ono, N. Sahara, M. R. Zhang, I. Aoki, A. Nordberg, T. Suhara, and M. Higuchi, ““Comparative in-vitro and in-vivo quantifications of pathological tau deposits and their association with neurodegeneration in tauopathy mouse models,” Journal of nuclear medicine : official publication,” J. Nucl. Med. 59(6), 960–966 (2018).
    [Crossref]
  22. A. Ishikawa, M. Tokunaga, J. Maeda, T. Minamihisamatsu, M. Shimojo, H. Takuwa, M. Ono, R. Ni, S. Hirano, S. Kuwabara, B. Ji, M. R. Zhang, I. Aoki, T. Suhara, M. Higuchi, and N. Sahara, “In Vivo Visualization of Tau Accumulation, Microglial Activation, and Brain Atrophy in a Mouse Model of Tauopathy rTg4510,” J. Alzheimer’s Dis. 61(3), 1037–1052 (2018).
    [Crossref]
  23. S. Krishnaswamy, Y. Lin, W. J. Rajamohamedsait, H. B. Rajamohamedsait, P. Krishnamurthy, and E. M. Sigurdsson, “Antibody-derived in vivo imaging of tau pathology,” J. Neuroscience 34(50), 16835–16850 (2014).
    [Crossref]
  24. Q. Wu, Y. Lin, J. Gu, and E. M. Sigurdsson, “Dynamic assessment of tau immunotherapies in the brains of live animals by two-photon imaging,” EBioMedicine 35, 270–278 (2018).
    [Crossref]
  25. A. Velasco, G. Fraser, P. Delobel, B. Ghetti, I. Lavenir, and M. Goedert, “Detection of filamentous tau inclusions by the fluorescent Congo red derivative FSB [(trans,trans)-1-fluoro-2,5-bis(3-hydroxycarbonyl-4-hydroxy)styrylbenzene],” FEBS Lett. 582(6), 901–906 (2008).
    [Crossref]
  26. A. de Calignon, L. M. Fox, R. Pitstick, G. A. Carlson, B. J. Bacskai, T. L. Spires-Jones, and B. T. Hyman, “Caspase activation precedes and leads to tangles,” Nature 464(7292), 1201–1204 (2010).
    [Crossref]
  27. M. Calvo-Rodriguez, S. S. Hou, A. C. Snyder, S. Dujardin, H. Shirani, K. P. R. Nilsson, and B. J. Bacskai, “In vivo detection of tau fibrils and amyloid beta aggregates with luminescent conjugated oligothiophenes and multiphoton microscopy,” Acta Neuropathol. Commun. 7(1), 171 (2019).
    [Crossref]
  28. A. Aslund, C. J. Sigurdson, T. Klingstedt, S. Grathwohl, T. Bolmont, D. L. Dickstein, E. Glimsdal, S. Prokop, M. Lindgren, P. Konradsson, D. M. Holtzman, P. R. Hof, F. L. Heppner, S. Gandy, M. Jucker, A. Aguzzi, P. Hammarström, and K. P. Nilsson, “Novel pentameric thiophene derivatives for in vitro and in vivo optical imaging of a plethora of protein aggregates in cerebral amyloidoses,” ACS Chem. Biol. 4(8), 673–684 (2009).
    [Crossref]
  29. Z. Chen, B. Mc Larney, J. Rebling, X. L. Deán-Ben, Q. Zhou, S. Gottschalk, and D. Razansky, “High-Speed Large-Field Multifocal Illumination Fluorescence Microscopy,” Laser Photonics Rev. 14, 1900070 (2020).
    [Crossref]
  30. R. Ni, Z. Chen, G. Shi, A. Villois, Q. Zhou, P. Arosio, R. M. Nitsch, P. R. Nilsson, J. Klohs, and D. Razansky, “Transcranial in vivo detection of Aβ at single plaque resolution with large-field multifocal illumination fluorescence microscopy,” bioRxiv, 2020.2002.2001.929844 (2020).
  31. B. M. Burmann, J. A. Gerez, I. Matecko-Burmann, S. Campioni, P. Kumari, D. Ghosh, A. Mazur, E. E. Aspholm, D. Sulskis, M. Wawrzyniuk, T. Bock, A. Schmidt, S. G. D. Rudiger, R. Riek, and S. Hiller, “Regulation of alpha-synuclein by chaperones in mammalian cells,” Nature 577(7788), 127–132 (2020).
    [Crossref]
  32. J. A. Gerez, N. C. Prymaczok, E. Rockenstein, U. S. Herrmann, P. Schwarz, A. Adame, R. I. Enchev, T. Courtheoux, P. J. Boersema, R. Riek, M. Peter, A. Aguzzi, E. Masliah, and P. Picotti, “A cullin-RING ubiquitin ligase targets exogenous alpha-synuclein and inhibits Lewy body-like pathology,” Sci. Transl. Med. 11(495), eaau6722 (2019).
    [Crossref]
  33. H. Shirani, M. Linares, C. J. Sigurdson, M. Lindgren, P. Norman, and K. P. Nilsson, “A Palette of Fluorescent Thiophene-Based Ligands for the Identification of Protein Aggregates,” Chem. Eur. J. 21(43), 15133–15137 (2015).
    [Crossref]
  34. T. Klingstedt, A. Aslund, R. A. Simon, L. B. Johansson, J. J. Mason, S. Nystrom, P. Hammarstrom, and K. P. Nilsson, “Synthesis of a library of oligothiophenes and their utilization as fluorescent ligands for spectral assignment of protein aggregates,” Org. Biomol. Chem. 9(24), 8356–8370 (2011).
    [Crossref]
  35. R. Ni, Y. Zarb, G. A. Kuhn, R. Müller, Y. Yundung, R. M. Nitsch, L. Kulic, A. Keller, and J. Klohs, “Tau deposition is associated with imaging patterns of tissue calcification in the P301L mouse model of human tauopathy,” bioRxiv, 851915 (2019).
  36. I. Gregor and J. Enderlein, “Image scanning microscopy,” Curr. Opin. Chem. Biol. 51, 74–83 (2019).
    [Crossref]
  37. C. A. Lasagna-Reeves, D. L. Castillo-Carranza, U. Sengupta, J. Sarmiento, J. Troncoso, G. R. Jackson, and R. Kayed, “Identification of oligomers at early stages of tau aggregation in Alzheimer's disease,” FASEB J. 26(5), 1946–1959 (2012).
    [Crossref]
  38. R. Ni, X. L. Dean-Ben, D. Kirschenbaum, M. Rudin, Z. Chen, A. Crimi, F. Voigt, P. R. Nilsson, F. Helmchen, R. M. Nitsch, A. Aguzzi, D. Razansky, and J. Klohs, “Whole brain optoacoustic tomography reveals strain-specific regional beta-amyloid densities in Alzheimer`s disease amyloidosis models,” bioRxiv, DOI: 10.1101/2020.1102.1125.964064 (2020).
  39. M. Hintersteiner, A. Enz, P. Frey, A. L. Jaton, W. Kinzy, R. Kneuer, U. Neumann, M. Rudin, M. Staufenbiel, M. Stoeckli, K. H. Wiederhold, and H. U. Gremlich, “In vivo detection of amyloid-beta deposits by near-infrared imaging using an oxazine-derivative probe,” Nat. Biotechnol. 23(5), 577–583 (2005).
    [Crossref]
  40. J. Gotz, F. Chen, R. Barmettler, and R. M. Nitsch, “Tau filament formation in transgenic mice expressing P301L tau,” J. Biol. Chem. 276(1), 529–534 (2001).
    [Crossref]
  41. P. Delobel, I. Lavenir, G. Fraser, E. Ingram, M. Holzer, B. Ghetti, M. G. Spillantini, R. A. Crowther, and M. Goedert, “Analysis of tau phosphorylation and truncation in a mouse model of human tauopathy,” Am. J. Pathology 172(1), 123–131 (2008).
    [Crossref]
  42. Z. He, J. D. McBride, H. Xu, L. Changolkar, S. J. Kim, B. Zhang, S. Narasimhan, G. S. Gibbons, J. L. Guo, M. Kozak, G. D. Schellenberg, J. Q. Trojanowski, and V. M. Lee, “Transmission of tauopathy strains is independent of their isoform composition,” Nat. Commun. 11(1), 7 (2020).
    [Crossref]
  43. K. M. Schoch, S. L. DeVos, R. L. Miller, S. J. Chun, M. Norrbom, D. F. Wozniak, H. N. Dawson, C. F. Bennett, F. Rigo, and T. M. Miller, “Increased 4R-Tau Induces Pathological Changes in a Human-Tau Mouse Model,” Neuron 90(5), 941–947 (2016).
    [Crossref]
  44. B. Dejanovic, M. A. Huntley, A. De Maziere, W. J. Meilandt, T. Wu, K. Srinivasan, Z. Jiang, V. Gandham, B. A. Friedman, H. Ngu, O. Foreman, R. A. D. Carano, B. Chih, J. Klumperman, C. Bakalarski, J. E. Hanson, and M. Sheng, “Changes in the Synaptic Proteome in Tauopathy and Rescue of Tau-Induced Synapse Loss by C1q Antibodies,” Neuron 100(6), 1322–1336.e7 (2018).
    [Crossref]
  45. C. H. Lo, C. K. Lim, Z. Ding, S. P. Wickramasinghe, A. R. Braun, K. H. Ashe, E. Rhoades, D. D. Thomas, and J. N. Sachs, “Targeting the ensemble of heterogeneous tau oligomers in cells: A novel small molecule screening platform for tauopathies,” Alzheimer’s & Dementia 15(11), 1489–1502 (2019).
    [Crossref]
  46. M. Colin, S. Dujardin, S. Schraen-Maschke, G. Meno-Tetang, C. Duyckaerts, J. P. Courade, and L. Buee, “From the prion-like propagation hypothesis to therapeutic strategies of anti-tau immunotherapy,” Acta Neuropathol. 139(1), 3–25 (2020).
    [Crossref]
  47. J. Klohs, N. Baeva, J. Steinbrink, R. Bourayou, C. Boettcher, G. Royl, D. Megow, U. Dirnagl, J. Priller, and A. Wunder, “In vivo near-infrared fluorescence imaging of matrix metalloproteinase activity after cerebral ischemia,” J. Cereb. Blood Flow Metab. 29(7), 1284–1292 (2009).
    [Crossref]
  48. R. Ni, M. Vaas, W. Ren, and J. Klohs, “Non-invasive detection of acute cerebral hypoxia and subsequent matrix-metalloproteinase activity in a mouse model of cerebral ischemia using multispectral-optoacoustic-tomography,” Neurophotonics 5(1), 015005 (2018).
    [Crossref]
  49. J. Klohs, “An Integrated View on Vascular Dysfunction in Alzheimer’s Disease,” Neurodegenerative Diseases (2020).
  50. V. L. Villemagne, V. Dore, S. C. Burnham, C. L. Masters, and C. C. Rowe, “Imaging tau and amyloid-beta proteinopathies in Alzheimer disease and other conditions,” Nat. Rev. Neurol. 14(4), 225–236 (2018).
    [Crossref]
  51. B. Wegenast-Braun, A. Skodras, G. Bayraktar, J. Mahler, S. Fritschi, T. Klingstedt, J. Mason, P. Hammarström, K. Nilsson, C. Liebig, and M. Jucker, “Spectral Discrimination of Cerebral Amyloid Lesions after Peripheral Application of Luminescent Conjugated Oligothiophenes,” Am. J. Pathology 181(6), 1953–1960 (2012).
    [Crossref]
  52. P. Verwilst, H. S. Kim, S. Kim, C. Kang, and J. S. Kim, “Shedding light on tau protein aggregation: the progress in developing highly selective fluorophores,” Chem. Soc. Rev. 47(7), 2249–2265 (2018).
    [Crossref]
  53. P. Füger, J. K. Hefendehl, K. Veeraraghavalu, A.-C. Wendeln, C. Schlosser, U. Obermüller, B. M. Wegenast-Braun, J. J. Neher, P. Martus, S. Kohsaka, M. Thunemann, R. Feil, S. S. Sisodia, A. Skodras, and M. Jucker, “Microglia turnover with aging and in an Alzheimer's model via long-term in vivo single-cell imaging,” Nat. Neurosci. 20(10), 1371–1376 (2017).
    [Crossref]
  54. K. V. Kuchibhotla, S. Wegmann, K. J. Kopeikina, J. Hawkes, N. Rudinskiy, M. L. Andermann, T. L. Spires-Jones, B. J. Bacskai, and B. T. Hyman, “Neurofibrillary tangle-bearing neurons are functionally integrated in cortical circuits in vivo,” Proc. Natl. Acad. Sci. 111(1), 510–514 (2014).
    [Crossref]
  55. F. Lassailly, K. Foster, L. Lopez-Onieva, E. Currie, and D. Bonnet, “Multimodal imaging reveals structural and functional heterogeneity in different bone marrow compartments: functional implications on hematopoietic stem cells,” Blood 122(10), 1730–1740 (2013).
    [Crossref]
  56. I. B. Mazo, J.-C. Gutierrez-Ramos, P. S. Frenette, R. O. Hynes, D. D. Wagner, and U. H. von Andrian, “Hematopoietic Progenitor Cell Rolling in Bone Marrow Microvessels: Parallel Contributions by Endothelial Selectins and Vascular Cell Adhesion Molecule 1,” J. Exp. Med. 188(3), 465–474 (1998).
    [Crossref]
  57. S. Gottschalk, O. Degtyaruk, B. Mc Larney, J. Rebling, M. A. Hutter, X. L. Deán-Ben, S. Shoham, and D. Razansky, “Rapid volumetric optoacoustic imaging of neural dynamics across the mouse brain,” Nat. Biomed. Eng. 3(5), 392–401 (2019).
    [Crossref]
  58. Y. Zhang, C. Zhang, X. Zhong, and D. Zhu, “Quantitative evaluation of SOCS-induced optical clearing efficiency of skull,” Quant. Imaging Med. Surg. 5, 136–142 (2015).
    [Crossref]
  59. A. W. P. Fitzpatrick, B. Falcon, S. He, A. G. Murzin, G. Murshudov, H. J. Garringer, R. A. Crowther, B. Ghetti, M. Goedert, and S. H. W. Scheres, “Cryo-EM structures of tau filaments from Alzheimer's disease,” Nature 547(7662), 185–190 (2017).
    [Crossref]
  60. S. K. Kaufman, D. W. Sanders, T. L. Thomas, A. J. Ruchinskas, J. Vaquer-Alicea, A. M. Sharma, T. M. Miller, and M. I. Diamond, “Tau Prion Strains Dictate Patterns of Cell Pathology, Progression Rate, and Regional Vulnerability In Vivo,” Neuron 92(4), 796–812 (2016).
    [Crossref]
  61. E. J. Kim, J. L. Hwang, S. E. Gaus, A. L. Nana, J. Deng, J. A. Brown, S. Spina, M. J. Lee, E. M. Ramos, L. T. Grinberg, J. H. Kramer, A. L. Boxer, M. L. Gorno-Tempini, H. J. Rosen, B. L. Miller, and W. W. Seeley, “Evidence of corticofugal tau spreading in patients with frontotemporal dementia,” Acta Neuropathol. 139(1), 27–43 (2020).
    [Crossref]
  62. T. K. Patel, L. Habimana-Griffin, X. Gao, B. Xu, S. Achilefu, K. Alitalo, C. A. McKee, P. W. Sheehan, E. S. Musiek, C. Xiong, D. Coble, and D. M. Holtzman, “Dural lymphatics regulate clearance of extracellular tau from the CNS,” Mol. Neurodegener. 14(1), 11 (2019).
    [Crossref]

2020 (7)

R. La Joie, A. V. Visani, S. L. Baker, J. A. Brown, V. Bourakova, J. Cha, K. Chaudhary, L. Edwards, L. Iaccarino, M. Janabi, O. H. Lesman-Segev, Z. A. Miller, D. C. Perry, J. P. O’Neil, J. Pham, J. C. Rojas, H. J. Rosen, W. W. Seeley, R. M. Tsai, B. L. Miller, W. J. Jagust, and G. D. Rabinovici, “Prospective longitudinal atrophy in Alzheimer’s disease correlates with the intensity and topography of baseline tau-PET,” Sci. Transl. Med. 12(524), eaau5732 (2020).
[Crossref]

A. Mueller, S. Bullich, O. Barret, J. Madonia, M. Berndt, C. Papin, A. Perrotin, N. Koglin, H. Kroth, A. Pfeifer, G. Tamagnan, J. P. Seibyl, K. Marek, S. de Santi, L. M. Dinkelborg, and A. W. Stephens, “Tau PET imaging with (18)F-PI-2620 in patients with Alzheimer's disease and healthy controls: a first-in-human study,” J. Nucl. Med. 61(6), 911–919 (2020).
[Crossref]

Z. Chen, B. Mc Larney, J. Rebling, X. L. Deán-Ben, Q. Zhou, S. Gottschalk, and D. Razansky, “High-Speed Large-Field Multifocal Illumination Fluorescence Microscopy,” Laser Photonics Rev. 14, 1900070 (2020).
[Crossref]

B. M. Burmann, J. A. Gerez, I. Matecko-Burmann, S. Campioni, P. Kumari, D. Ghosh, A. Mazur, E. E. Aspholm, D. Sulskis, M. Wawrzyniuk, T. Bock, A. Schmidt, S. G. D. Rudiger, R. Riek, and S. Hiller, “Regulation of alpha-synuclein by chaperones in mammalian cells,” Nature 577(7788), 127–132 (2020).
[Crossref]

Z. He, J. D. McBride, H. Xu, L. Changolkar, S. J. Kim, B. Zhang, S. Narasimhan, G. S. Gibbons, J. L. Guo, M. Kozak, G. D. Schellenberg, J. Q. Trojanowski, and V. M. Lee, “Transmission of tauopathy strains is independent of their isoform composition,” Nat. Commun. 11(1), 7 (2020).
[Crossref]

M. Colin, S. Dujardin, S. Schraen-Maschke, G. Meno-Tetang, C. Duyckaerts, J. P. Courade, and L. Buee, “From the prion-like propagation hypothesis to therapeutic strategies of anti-tau immunotherapy,” Acta Neuropathol. 139(1), 3–25 (2020).
[Crossref]

E. J. Kim, J. L. Hwang, S. E. Gaus, A. L. Nana, J. Deng, J. A. Brown, S. Spina, M. J. Lee, E. M. Ramos, L. T. Grinberg, J. H. Kramer, A. L. Boxer, M. L. Gorno-Tempini, H. J. Rosen, B. L. Miller, and W. W. Seeley, “Evidence of corticofugal tau spreading in patients with frontotemporal dementia,” Acta Neuropathol. 139(1), 27–43 (2020).
[Crossref]

2019 (11)

T. K. Patel, L. Habimana-Griffin, X. Gao, B. Xu, S. Achilefu, K. Alitalo, C. A. McKee, P. W. Sheehan, E. S. Musiek, C. Xiong, D. Coble, and D. M. Holtzman, “Dural lymphatics regulate clearance of extracellular tau from the CNS,” Mol. Neurodegener. 14(1), 11 (2019).
[Crossref]

C. H. Lo, C. K. Lim, Z. Ding, S. P. Wickramasinghe, A. R. Braun, K. H. Ashe, E. Rhoades, D. D. Thomas, and J. N. Sachs, “Targeting the ensemble of heterogeneous tau oligomers in cells: A novel small molecule screening platform for tauopathies,” Alzheimer’s & Dementia 15(11), 1489–1502 (2019).
[Crossref]

M. Calvo-Rodriguez, S. S. Hou, A. C. Snyder, S. Dujardin, H. Shirani, K. P. R. Nilsson, and B. J. Bacskai, “In vivo detection of tau fibrils and amyloid beta aggregates with luminescent conjugated oligothiophenes and multiphoton microscopy,” Acta Neuropathol. Commun. 7(1), 171 (2019).
[Crossref]

S. Gottschalk, O. Degtyaruk, B. Mc Larney, J. Rebling, M. A. Hutter, X. L. Deán-Ben, S. Shoham, and D. Razansky, “Rapid volumetric optoacoustic imaging of neural dynamics across the mouse brain,” Nat. Biomed. Eng. 3(5), 392–401 (2019).
[Crossref]

J. A. Gerez, N. C. Prymaczok, E. Rockenstein, U. S. Herrmann, P. Schwarz, A. Adame, R. I. Enchev, T. Courtheoux, P. J. Boersema, R. Riek, M. Peter, A. Aguzzi, E. Masliah, and P. Picotti, “A cullin-RING ubiquitin ligase targets exogenous alpha-synuclein and inhibits Lewy body-like pathology,” Sci. Transl. Med. 11(495), eaau6722 (2019).
[Crossref]

I. Gregor and J. Enderlein, “Image scanning microscopy,” Curr. Opin. Chem. Biol. 51, 74–83 (2019).
[Crossref]

P. Marinkovic, S. Blumenstock, P. M. Goltstein, V. Korzhova, F. Peters, A. Knebl, and J. Herms, “In vivo imaging reveals reduced activity of neuronal circuits in a mouse tauopathy model,” Brain 142(4), 1051–1062 (2019).
[Crossref]

S. Sanabria Bohorquez, J. Marik, A. Ogasawara, J. N. Tinianow, H. S. Gill, O. Barret, G. Tamagnan, D. Alagille, G. Ayalon, P. Manser, T. Bengtsson, M. Ward, S. P. Williams, G. A. Kerchner, J. P. Seibyl, K. Marek, and R. M. Weimer, “[(18)F]GTP1 (Genentech Tau Probe 1), a radioligand for detecting neurofibrillary tangle tau pathology in Alzheimer's disease,” Eur. J. Nucl. Med. Mol. Imaging 46(10), 2077–2089 (2019).
[Crossref]

B. J. Hanseeuw, R. A. Betensky, H. I. L. Jacobs, A. P. Schultz, J. Sepulcre, J. A. Becker, D. M. O. Cosio, M. Farrell, Y. T. Quiroz, E. C. Mormino, R. F. Buckley, K. V. Papp, R. A. Amariglio, I. Dewachter, A. Ivanoiu, W. Huijbers, T. Hedden, G. A. Marshall, J. P. Chhatwal, D. M. Rentz, R. A. Sperling, and K. Johnson, “Association of Amyloid and Tau With Cognition in Preclinical Alzheimer Disease: A Longitudinal Study,” JAMA Neurol. 76(8), 915–924 (2019).
[Crossref]

H. Kroth, F. Oden, J. Molette, H. Schieferstein, F. Capotosti, A. Mueller, M. Berndt, H. Schmitt-Willich, V. Darmency, E. Gabellieri, C. Boudou, T. Juergens, Y. Varisco, E. Vokali, D. T. Hickman, G. Tamagnan, A. Pfeifer, L. Dinkelborg, A. Muhs, and A. Stephens, “Discovery and preclinical characterization of [(18)F]PI-2620, a next-generation tau PET tracer for the assessment of tau pathology in Alzheimer's disease and other tauopathies,” Eur. J. Nucl. Med. Mol. Imaging 46(10), 2178–2189 (2019).
[Crossref]

S. Hashimoto, Y. Matsuba, N. Kamano, N. Mihira, N. Sahara, J. Takano, S. I. Muramatsu, T. C. Saido, and T. Saito, “Tau binding protein CAPON induces tau aggregation and neurodegeneration,” Nat. Commun. 10(1), 2394 (2019).
[Crossref]

2018 (8)

E. E. Congdon and E. M. Sigurdsson, “Tau-targeting therapies for Alzheimer disease,” Nat. Rev. Neurol. 14(7), 399–415 (2018).
[Crossref]

R. Ni, B. Ji, M. Ono, N. Sahara, M. R. Zhang, I. Aoki, A. Nordberg, T. Suhara, and M. Higuchi, ““Comparative in-vitro and in-vivo quantifications of pathological tau deposits and their association with neurodegeneration in tauopathy mouse models,” Journal of nuclear medicine : official publication,” J. Nucl. Med. 59(6), 960–966 (2018).
[Crossref]

A. Ishikawa, M. Tokunaga, J. Maeda, T. Minamihisamatsu, M. Shimojo, H. Takuwa, M. Ono, R. Ni, S. Hirano, S. Kuwabara, B. Ji, M. R. Zhang, I. Aoki, T. Suhara, M. Higuchi, and N. Sahara, “In Vivo Visualization of Tau Accumulation, Microglial Activation, and Brain Atrophy in a Mouse Model of Tauopathy rTg4510,” J. Alzheimer’s Dis. 61(3), 1037–1052 (2018).
[Crossref]

Q. Wu, Y. Lin, J. Gu, and E. M. Sigurdsson, “Dynamic assessment of tau immunotherapies in the brains of live animals by two-photon imaging,” EBioMedicine 35, 270–278 (2018).
[Crossref]

R. Ni, M. Vaas, W. Ren, and J. Klohs, “Non-invasive detection of acute cerebral hypoxia and subsequent matrix-metalloproteinase activity in a mouse model of cerebral ischemia using multispectral-optoacoustic-tomography,” Neurophotonics 5(1), 015005 (2018).
[Crossref]

V. L. Villemagne, V. Dore, S. C. Burnham, C. L. Masters, and C. C. Rowe, “Imaging tau and amyloid-beta proteinopathies in Alzheimer disease and other conditions,” Nat. Rev. Neurol. 14(4), 225–236 (2018).
[Crossref]

P. Verwilst, H. S. Kim, S. Kim, C. Kang, and J. S. Kim, “Shedding light on tau protein aggregation: the progress in developing highly selective fluorophores,” Chem. Soc. Rev. 47(7), 2249–2265 (2018).
[Crossref]

B. Dejanovic, M. A. Huntley, A. De Maziere, W. J. Meilandt, T. Wu, K. Srinivasan, Z. Jiang, V. Gandham, B. A. Friedman, H. Ngu, O. Foreman, R. A. D. Carano, B. Chih, J. Klumperman, C. Bakalarski, J. E. Hanson, and M. Sheng, “Changes in the Synaptic Proteome in Tauopathy and Rescue of Tau-Induced Synapse Loss by C1q Antibodies,” Neuron 100(6), 1322–1336.e7 (2018).
[Crossref]

2017 (4)

P. Füger, J. K. Hefendehl, K. Veeraraghavalu, A.-C. Wendeln, C. Schlosser, U. Obermüller, B. M. Wegenast-Braun, J. J. Neher, P. Martus, S. Kohsaka, M. Thunemann, R. Feil, S. S. Sisodia, A. Skodras, and M. Jucker, “Microglia turnover with aging and in an Alzheimer's model via long-term in vivo single-cell imaging,” Nat. Neurosci. 20(10), 1371–1376 (2017).
[Crossref]

A. W. P. Fitzpatrick, B. Falcon, S. He, A. G. Murzin, G. Murshudov, H. J. Garringer, R. A. Crowther, B. Ghetti, M. Goedert, and S. H. W. Scheres, “Cryo-EM structures of tau filaments from Alzheimer's disease,” Nature 547(7662), 185–190 (2017).
[Crossref]

M. Ono, N. Sahara, K. Kumata, B. Ji, R. Ni, S. Koga, D. W. Dickson, J. Q. Trojanowski, V. M.-Y. Lee, M. Yoshida, I. Hozumi, Y. Yoshiyama, J. C. v. Swieten, A. Nordberg, T. Suhara, M.-R. Zhang, and M. Higuchi, “Distinct binding of PET ligands PBB3 and AV-1451 to tau fibril strains in neurodegenerative tauopathies,” Brain 140, aww339 (2017).
[Crossref]

N. Sahara, M. Shimojo, M. Ono, H. Takuwa, M. Febo, M. Higuchi, and T. Suhara, “In Vivo Tau Imaging for a Diagnostic Platform of Tauopathy Using the rTg4510 Mouse Line,” Front Neurol. 8, 663 (2017).
[Crossref]

2016 (5)

K. A. Johnson, A. Schultz, R. A. Betensky, J. A. Becker, J. Sepulcre, D. Rentz, E. Mormino, J. Chhatwal, R. Amariglio, K. Papp, G. Marshall, M. Albers, S. Mauro, L. Pepin, J. Alverio, K. Judge, M. Philiossaint, T. Shoup, D. Yokell, B. Dickerson, T. Gomez-Isla, B. Hyman, N. Vasdev, and R. Sperling, “Tau positron emission tomographic imaging in aging and early Alzheimer disease,” Ann Neurol. 79(1), 110–119 (2016).
[Crossref]

E. D. Hostetler, A. M. Walji, Z. Zeng, P. Miller, I. Bennacef, C. Salinas, B. Connolly, L. Gantert, H. Haley, M. Holahan, M. Purcell, K. Riffel, T. G. Lohith, P. Coleman, A. Soriano, A. Ogawa, S. Xu, X. Zhang, E. Joshi, J. Della Rocca, D. Hesk, D. J. Schenk, and J. L. Evelhoch, ““Preclinical Characterization of 18F-MK-6240, a Promising PET Tracer for In Vivo Quantification of Human Neurofibrillary Tangles,” Journal of nuclear medicine : official publication,” J. Nuclear Medicine 57(10), 1599–1606 (2016).
[Crossref]

M. Scholl, S. N. Lockhart, D. R. Schonhaut, J. P. O’Neil, M. Janabi, R. Ossenkoppele, S. L. Baker, J. W. Vogel, J. Faria, H. D. Schwimmer, G. D. Rabinovici, and W. J. Jagust, “PET Imaging of Tau Deposition in the Aging Human Brain,” Neuron 89(5), 971–982 (2016).
[Crossref]

S. K. Kaufman, D. W. Sanders, T. L. Thomas, A. J. Ruchinskas, J. Vaquer-Alicea, A. M. Sharma, T. M. Miller, and M. I. Diamond, “Tau Prion Strains Dictate Patterns of Cell Pathology, Progression Rate, and Regional Vulnerability In Vivo,” Neuron 92(4), 796–812 (2016).
[Crossref]

K. M. Schoch, S. L. DeVos, R. L. Miller, S. J. Chun, M. Norrbom, D. F. Wozniak, H. N. Dawson, C. F. Bennett, F. Rigo, and T. M. Miller, “Increased 4R-Tau Induces Pathological Changes in a Human-Tau Mouse Model,” Neuron 90(5), 941–947 (2016).
[Crossref]

2015 (2)

Y. Zhang, C. Zhang, X. Zhong, and D. Zhu, “Quantitative evaluation of SOCS-induced optical clearing efficiency of skull,” Quant. Imaging Med. Surg. 5, 136–142 (2015).
[Crossref]

H. Shirani, M. Linares, C. J. Sigurdson, M. Lindgren, P. Norman, and K. P. Nilsson, “A Palette of Fluorescent Thiophene-Based Ligands for the Identification of Protein Aggregates,” Chem. Eur. J. 21(43), 15133–15137 (2015).
[Crossref]

2014 (2)

S. Krishnaswamy, Y. Lin, W. J. Rajamohamedsait, H. B. Rajamohamedsait, P. Krishnamurthy, and E. M. Sigurdsson, “Antibody-derived in vivo imaging of tau pathology,” J. Neuroscience 34(50), 16835–16850 (2014).
[Crossref]

K. V. Kuchibhotla, S. Wegmann, K. J. Kopeikina, J. Hawkes, N. Rudinskiy, M. L. Andermann, T. L. Spires-Jones, B. J. Bacskai, and B. T. Hyman, “Neurofibrillary tangle-bearing neurons are functionally integrated in cortical circuits in vivo,” Proc. Natl. Acad. Sci. 111(1), 510–514 (2014).
[Crossref]

2013 (3)

F. Lassailly, K. Foster, L. Lopez-Onieva, E. Currie, and D. Bonnet, “Multimodal imaging reveals structural and functional heterogeneity in different bone marrow compartments: functional implications on hematopoietic stem cells,” Blood 122(10), 1730–1740 (2013).
[Crossref]

M. Maruyama, H. Shimada, T. Suhara, H. Shinotoh, B. Ji, J. Maeda, M. R. Zhang, J. Q. Trojanowski, V. M. Lee, M. Ono, K. Masamoto, H. Takano, N. Sahara, N. Iwata, N. Okamura, S. Furumoto, Y. Kudo, Q. Chang, T. C. Saido, A. Takashima, J. Lewis, M. K. Jang, I. Aoki, H. Ito, and M. Higuchi, “Imaging of tau pathology in a tauopathy mouse model and in Alzheimer patients compared to normal controls,” Neuron 79(6), 1094–1108 (2013).
[Crossref]

M. G. Spillantini and M. Goedert, “Tau pathology and neurodegeneration,” Lancet Neurol. 12(6), 609–622 (2013).
[Crossref]

2012 (2)

C. A. Lasagna-Reeves, D. L. Castillo-Carranza, U. Sengupta, J. Sarmiento, J. Troncoso, G. R. Jackson, and R. Kayed, “Identification of oligomers at early stages of tau aggregation in Alzheimer's disease,” FASEB J. 26(5), 1946–1959 (2012).
[Crossref]

B. Wegenast-Braun, A. Skodras, G. Bayraktar, J. Mahler, S. Fritschi, T. Klingstedt, J. Mason, P. Hammarström, K. Nilsson, C. Liebig, and M. Jucker, “Spectral Discrimination of Cerebral Amyloid Lesions after Peripheral Application of Luminescent Conjugated Oligothiophenes,” Am. J. Pathology 181(6), 1953–1960 (2012).
[Crossref]

2011 (1)

T. Klingstedt, A. Aslund, R. A. Simon, L. B. Johansson, J. J. Mason, S. Nystrom, P. Hammarstrom, and K. P. Nilsson, “Synthesis of a library of oligothiophenes and their utilization as fluorescent ligands for spectral assignment of protein aggregates,” Org. Biomol. Chem. 9(24), 8356–8370 (2011).
[Crossref]

2010 (1)

A. de Calignon, L. M. Fox, R. Pitstick, G. A. Carlson, B. J. Bacskai, T. L. Spires-Jones, and B. T. Hyman, “Caspase activation precedes and leads to tangles,” Nature 464(7292), 1201–1204 (2010).
[Crossref]

2009 (2)

A. Aslund, C. J. Sigurdson, T. Klingstedt, S. Grathwohl, T. Bolmont, D. L. Dickstein, E. Glimsdal, S. Prokop, M. Lindgren, P. Konradsson, D. M. Holtzman, P. R. Hof, F. L. Heppner, S. Gandy, M. Jucker, A. Aguzzi, P. Hammarström, and K. P. Nilsson, “Novel pentameric thiophene derivatives for in vitro and in vivo optical imaging of a plethora of protein aggregates in cerebral amyloidoses,” ACS Chem. Biol. 4(8), 673–684 (2009).
[Crossref]

J. Klohs, N. Baeva, J. Steinbrink, R. Bourayou, C. Boettcher, G. Royl, D. Megow, U. Dirnagl, J. Priller, and A. Wunder, “In vivo near-infrared fluorescence imaging of matrix metalloproteinase activity after cerebral ischemia,” J. Cereb. Blood Flow Metab. 29(7), 1284–1292 (2009).
[Crossref]

2008 (2)

P. Delobel, I. Lavenir, G. Fraser, E. Ingram, M. Holzer, B. Ghetti, M. G. Spillantini, R. A. Crowther, and M. Goedert, “Analysis of tau phosphorylation and truncation in a mouse model of human tauopathy,” Am. J. Pathology 172(1), 123–131 (2008).
[Crossref]

A. Velasco, G. Fraser, P. Delobel, B. Ghetti, I. Lavenir, and M. Goedert, “Detection of filamentous tau inclusions by the fluorescent Congo red derivative FSB [(trans,trans)-1-fluoro-2,5-bis(3-hydroxycarbonyl-4-hydroxy)styrylbenzene],” FEBS Lett. 582(6), 901–906 (2008).
[Crossref]

2007 (1)

Y. Yoshiyama, M. Higuchi, B. Zhang, S. M. Huang, N. Iwata, T. C. Saido, J. Maeda, T. Suhara, J. Q. Trojanowski, and V. M. Lee, “Synapse loss and microglial activation precede tangles in a P301S tauopathy mouse model,” Neuron 53(3), 337–351 (2007).
[Crossref]

2005 (2)

K. SantaCruz, J. Lewis, T. Spires, J. Paulson, L. Kotilinek, M. Ingelsson, A. Guimaraes, M. DeTure, M. Ramsden, E. McGowan, C. Forster, M. Yue, J. Orne, C. Janus, A. Mariash, M. Kuskowski, B. Hyman, M. Hutton, and K. H. Ashe, “Tau Suppression in a Neurodegenerative Mouse Model Improves Memory Function,” Science 309(5733), 476–481 (2005).
[Crossref]

M. Hintersteiner, A. Enz, P. Frey, A. L. Jaton, W. Kinzy, R. Kneuer, U. Neumann, M. Rudin, M. Staufenbiel, M. Stoeckli, K. H. Wiederhold, and H. U. Gremlich, “In vivo detection of amyloid-beta deposits by near-infrared imaging using an oxazine-derivative probe,” Nat. Biotechnol. 23(5), 577–583 (2005).
[Crossref]

2001 (3)

J. Gotz, F. Chen, R. Barmettler, and R. M. Nitsch, “Tau filament formation in transgenic mice expressing P301L tau,” J. Biol. Chem. 276(1), 529–534 (2001).
[Crossref]

J. Gotz, F. Chen, J. van Dorpe, and R. M. Nitsch, “Formation of neurofibrillary tangles in P301 l tau transgenic mice induced by Abeta 42 fibrils,” Science 293(5534), 1491–1495 (2001).
[Crossref]

V. M. Lee, M. Goedert, and J. Q. Trojanowski, “Neurodegenerative tauopathies,” Annu. Rev. Neurosci. 24(1), 1121–1159 (2001).
[Crossref]

2000 (1)

J. Lewis, E. McGowan, J. Rockwood, H. Melrose, P. Nacharaju, M. Van Slegtenhorst, K. Gwinn-Hardy, M. Paul Murphy, M. Baker, X. Yu, K. Duff, J. Hardy, A. Corral, W. L. Lin, S. H. Yen, D. W. Dickson, P. Davies, and M. Hutton, “Neurofibrillary tangles, amyotrophy and progressive motor disturbance in mice expressing mutant (P301L) tau protein,” Nat. Genet. 25(4), 402–405 (2000).
[Crossref]

1998 (1)

I. B. Mazo, J.-C. Gutierrez-Ramos, P. S. Frenette, R. O. Hynes, D. D. Wagner, and U. H. von Andrian, “Hematopoietic Progenitor Cell Rolling in Bone Marrow Microvessels: Parallel Contributions by Endothelial Selectins and Vascular Cell Adhesion Molecule 1,” J. Exp. Med. 188(3), 465–474 (1998).
[Crossref]

Achilefu, S.

T. K. Patel, L. Habimana-Griffin, X. Gao, B. Xu, S. Achilefu, K. Alitalo, C. A. McKee, P. W. Sheehan, E. S. Musiek, C. Xiong, D. Coble, and D. M. Holtzman, “Dural lymphatics regulate clearance of extracellular tau from the CNS,” Mol. Neurodegener. 14(1), 11 (2019).
[Crossref]

Adame, A.

J. A. Gerez, N. C. Prymaczok, E. Rockenstein, U. S. Herrmann, P. Schwarz, A. Adame, R. I. Enchev, T. Courtheoux, P. J. Boersema, R. Riek, M. Peter, A. Aguzzi, E. Masliah, and P. Picotti, “A cullin-RING ubiquitin ligase targets exogenous alpha-synuclein and inhibits Lewy body-like pathology,” Sci. Transl. Med. 11(495), eaau6722 (2019).
[Crossref]

Aguzzi, A.

J. A. Gerez, N. C. Prymaczok, E. Rockenstein, U. S. Herrmann, P. Schwarz, A. Adame, R. I. Enchev, T. Courtheoux, P. J. Boersema, R. Riek, M. Peter, A. Aguzzi, E. Masliah, and P. Picotti, “A cullin-RING ubiquitin ligase targets exogenous alpha-synuclein and inhibits Lewy body-like pathology,” Sci. Transl. Med. 11(495), eaau6722 (2019).
[Crossref]

A. Aslund, C. J. Sigurdson, T. Klingstedt, S. Grathwohl, T. Bolmont, D. L. Dickstein, E. Glimsdal, S. Prokop, M. Lindgren, P. Konradsson, D. M. Holtzman, P. R. Hof, F. L. Heppner, S. Gandy, M. Jucker, A. Aguzzi, P. Hammarström, and K. P. Nilsson, “Novel pentameric thiophene derivatives for in vitro and in vivo optical imaging of a plethora of protein aggregates in cerebral amyloidoses,” ACS Chem. Biol. 4(8), 673–684 (2009).
[Crossref]

R. Ni, X. L. Dean-Ben, D. Kirschenbaum, M. Rudin, Z. Chen, A. Crimi, F. Voigt, P. R. Nilsson, F. Helmchen, R. M. Nitsch, A. Aguzzi, D. Razansky, and J. Klohs, “Whole brain optoacoustic tomography reveals strain-specific regional beta-amyloid densities in Alzheimer`s disease amyloidosis models,” bioRxiv, DOI: 10.1101/2020.1102.1125.964064 (2020).

Alagille, D.

S. Sanabria Bohorquez, J. Marik, A. Ogasawara, J. N. Tinianow, H. S. Gill, O. Barret, G. Tamagnan, D. Alagille, G. Ayalon, P. Manser, T. Bengtsson, M. Ward, S. P. Williams, G. A. Kerchner, J. P. Seibyl, K. Marek, and R. M. Weimer, “[(18)F]GTP1 (Genentech Tau Probe 1), a radioligand for detecting neurofibrillary tangle tau pathology in Alzheimer's disease,” Eur. J. Nucl. Med. Mol. Imaging 46(10), 2077–2089 (2019).
[Crossref]

Albers, M.

K. A. Johnson, A. Schultz, R. A. Betensky, J. A. Becker, J. Sepulcre, D. Rentz, E. Mormino, J. Chhatwal, R. Amariglio, K. Papp, G. Marshall, M. Albers, S. Mauro, L. Pepin, J. Alverio, K. Judge, M. Philiossaint, T. Shoup, D. Yokell, B. Dickerson, T. Gomez-Isla, B. Hyman, N. Vasdev, and R. Sperling, “Tau positron emission tomographic imaging in aging and early Alzheimer disease,” Ann Neurol. 79(1), 110–119 (2016).
[Crossref]

Alitalo, K.

T. K. Patel, L. Habimana-Griffin, X. Gao, B. Xu, S. Achilefu, K. Alitalo, C. A. McKee, P. W. Sheehan, E. S. Musiek, C. Xiong, D. Coble, and D. M. Holtzman, “Dural lymphatics regulate clearance of extracellular tau from the CNS,” Mol. Neurodegener. 14(1), 11 (2019).
[Crossref]

Alverio, J.

K. A. Johnson, A. Schultz, R. A. Betensky, J. A. Becker, J. Sepulcre, D. Rentz, E. Mormino, J. Chhatwal, R. Amariglio, K. Papp, G. Marshall, M. Albers, S. Mauro, L. Pepin, J. Alverio, K. Judge, M. Philiossaint, T. Shoup, D. Yokell, B. Dickerson, T. Gomez-Isla, B. Hyman, N. Vasdev, and R. Sperling, “Tau positron emission tomographic imaging in aging and early Alzheimer disease,” Ann Neurol. 79(1), 110–119 (2016).
[Crossref]

Amariglio, R.

K. A. Johnson, A. Schultz, R. A. Betensky, J. A. Becker, J. Sepulcre, D. Rentz, E. Mormino, J. Chhatwal, R. Amariglio, K. Papp, G. Marshall, M. Albers, S. Mauro, L. Pepin, J. Alverio, K. Judge, M. Philiossaint, T. Shoup, D. Yokell, B. Dickerson, T. Gomez-Isla, B. Hyman, N. Vasdev, and R. Sperling, “Tau positron emission tomographic imaging in aging and early Alzheimer disease,” Ann Neurol. 79(1), 110–119 (2016).
[Crossref]

Amariglio, R. A.

B. J. Hanseeuw, R. A. Betensky, H. I. L. Jacobs, A. P. Schultz, J. Sepulcre, J. A. Becker, D. M. O. Cosio, M. Farrell, Y. T. Quiroz, E. C. Mormino, R. F. Buckley, K. V. Papp, R. A. Amariglio, I. Dewachter, A. Ivanoiu, W. Huijbers, T. Hedden, G. A. Marshall, J. P. Chhatwal, D. M. Rentz, R. A. Sperling, and K. Johnson, “Association of Amyloid and Tau With Cognition in Preclinical Alzheimer Disease: A Longitudinal Study,” JAMA Neurol. 76(8), 915–924 (2019).
[Crossref]

Andermann, M. L.

K. V. Kuchibhotla, S. Wegmann, K. J. Kopeikina, J. Hawkes, N. Rudinskiy, M. L. Andermann, T. L. Spires-Jones, B. J. Bacskai, and B. T. Hyman, “Neurofibrillary tangle-bearing neurons are functionally integrated in cortical circuits in vivo,” Proc. Natl. Acad. Sci. 111(1), 510–514 (2014).
[Crossref]

Aoki, I.

R. Ni, B. Ji, M. Ono, N. Sahara, M. R. Zhang, I. Aoki, A. Nordberg, T. Suhara, and M. Higuchi, ““Comparative in-vitro and in-vivo quantifications of pathological tau deposits and their association with neurodegeneration in tauopathy mouse models,” Journal of nuclear medicine : official publication,” J. Nucl. Med. 59(6), 960–966 (2018).
[Crossref]

A. Ishikawa, M. Tokunaga, J. Maeda, T. Minamihisamatsu, M. Shimojo, H. Takuwa, M. Ono, R. Ni, S. Hirano, S. Kuwabara, B. Ji, M. R. Zhang, I. Aoki, T. Suhara, M. Higuchi, and N. Sahara, “In Vivo Visualization of Tau Accumulation, Microglial Activation, and Brain Atrophy in a Mouse Model of Tauopathy rTg4510,” J. Alzheimer’s Dis. 61(3), 1037–1052 (2018).
[Crossref]

M. Maruyama, H. Shimada, T. Suhara, H. Shinotoh, B. Ji, J. Maeda, M. R. Zhang, J. Q. Trojanowski, V. M. Lee, M. Ono, K. Masamoto, H. Takano, N. Sahara, N. Iwata, N. Okamura, S. Furumoto, Y. Kudo, Q. Chang, T. C. Saido, A. Takashima, J. Lewis, M. K. Jang, I. Aoki, H. Ito, and M. Higuchi, “Imaging of tau pathology in a tauopathy mouse model and in Alzheimer patients compared to normal controls,” Neuron 79(6), 1094–1108 (2013).
[Crossref]

Arosio, P.

R. Ni, Z. Chen, G. Shi, A. Villois, Q. Zhou, P. Arosio, R. M. Nitsch, P. R. Nilsson, J. Klohs, and D. Razansky, “Transcranial in vivo detection of Aβ at single plaque resolution with large-field multifocal illumination fluorescence microscopy,” bioRxiv, 2020.2002.2001.929844 (2020).

Ashe, K. H.

C. H. Lo, C. K. Lim, Z. Ding, S. P. Wickramasinghe, A. R. Braun, K. H. Ashe, E. Rhoades, D. D. Thomas, and J. N. Sachs, “Targeting the ensemble of heterogeneous tau oligomers in cells: A novel small molecule screening platform for tauopathies,” Alzheimer’s & Dementia 15(11), 1489–1502 (2019).
[Crossref]

K. SantaCruz, J. Lewis, T. Spires, J. Paulson, L. Kotilinek, M. Ingelsson, A. Guimaraes, M. DeTure, M. Ramsden, E. McGowan, C. Forster, M. Yue, J. Orne, C. Janus, A. Mariash, M. Kuskowski, B. Hyman, M. Hutton, and K. H. Ashe, “Tau Suppression in a Neurodegenerative Mouse Model Improves Memory Function,” Science 309(5733), 476–481 (2005).
[Crossref]

Aslund, A.

T. Klingstedt, A. Aslund, R. A. Simon, L. B. Johansson, J. J. Mason, S. Nystrom, P. Hammarstrom, and K. P. Nilsson, “Synthesis of a library of oligothiophenes and their utilization as fluorescent ligands for spectral assignment of protein aggregates,” Org. Biomol. Chem. 9(24), 8356–8370 (2011).
[Crossref]

A. Aslund, C. J. Sigurdson, T. Klingstedt, S. Grathwohl, T. Bolmont, D. L. Dickstein, E. Glimsdal, S. Prokop, M. Lindgren, P. Konradsson, D. M. Holtzman, P. R. Hof, F. L. Heppner, S. Gandy, M. Jucker, A. Aguzzi, P. Hammarström, and K. P. Nilsson, “Novel pentameric thiophene derivatives for in vitro and in vivo optical imaging of a plethora of protein aggregates in cerebral amyloidoses,” ACS Chem. Biol. 4(8), 673–684 (2009).
[Crossref]

Aspholm, E. E.

B. M. Burmann, J. A. Gerez, I. Matecko-Burmann, S. Campioni, P. Kumari, D. Ghosh, A. Mazur, E. E. Aspholm, D. Sulskis, M. Wawrzyniuk, T. Bock, A. Schmidt, S. G. D. Rudiger, R. Riek, and S. Hiller, “Regulation of alpha-synuclein by chaperones in mammalian cells,” Nature 577(7788), 127–132 (2020).
[Crossref]

Ayalon, G.

S. Sanabria Bohorquez, J. Marik, A. Ogasawara, J. N. Tinianow, H. S. Gill, O. Barret, G. Tamagnan, D. Alagille, G. Ayalon, P. Manser, T. Bengtsson, M. Ward, S. P. Williams, G. A. Kerchner, J. P. Seibyl, K. Marek, and R. M. Weimer, “[(18)F]GTP1 (Genentech Tau Probe 1), a radioligand for detecting neurofibrillary tangle tau pathology in Alzheimer's disease,” Eur. J. Nucl. Med. Mol. Imaging 46(10), 2077–2089 (2019).
[Crossref]

Bacskai, B. J.

M. Calvo-Rodriguez, S. S. Hou, A. C. Snyder, S. Dujardin, H. Shirani, K. P. R. Nilsson, and B. J. Bacskai, “In vivo detection of tau fibrils and amyloid beta aggregates with luminescent conjugated oligothiophenes and multiphoton microscopy,” Acta Neuropathol. Commun. 7(1), 171 (2019).
[Crossref]

K. V. Kuchibhotla, S. Wegmann, K. J. Kopeikina, J. Hawkes, N. Rudinskiy, M. L. Andermann, T. L. Spires-Jones, B. J. Bacskai, and B. T. Hyman, “Neurofibrillary tangle-bearing neurons are functionally integrated in cortical circuits in vivo,” Proc. Natl. Acad. Sci. 111(1), 510–514 (2014).
[Crossref]

A. de Calignon, L. M. Fox, R. Pitstick, G. A. Carlson, B. J. Bacskai, T. L. Spires-Jones, and B. T. Hyman, “Caspase activation precedes and leads to tangles,” Nature 464(7292), 1201–1204 (2010).
[Crossref]

Baeva, N.

J. Klohs, N. Baeva, J. Steinbrink, R. Bourayou, C. Boettcher, G. Royl, D. Megow, U. Dirnagl, J. Priller, and A. Wunder, “In vivo near-infrared fluorescence imaging of matrix metalloproteinase activity after cerebral ischemia,” J. Cereb. Blood Flow Metab. 29(7), 1284–1292 (2009).
[Crossref]

Bakalarski, C.

B. Dejanovic, M. A. Huntley, A. De Maziere, W. J. Meilandt, T. Wu, K. Srinivasan, Z. Jiang, V. Gandham, B. A. Friedman, H. Ngu, O. Foreman, R. A. D. Carano, B. Chih, J. Klumperman, C. Bakalarski, J. E. Hanson, and M. Sheng, “Changes in the Synaptic Proteome in Tauopathy and Rescue of Tau-Induced Synapse Loss by C1q Antibodies,” Neuron 100(6), 1322–1336.e7 (2018).
[Crossref]

Baker, M.

J. Lewis, E. McGowan, J. Rockwood, H. Melrose, P. Nacharaju, M. Van Slegtenhorst, K. Gwinn-Hardy, M. Paul Murphy, M. Baker, X. Yu, K. Duff, J. Hardy, A. Corral, W. L. Lin, S. H. Yen, D. W. Dickson, P. Davies, and M. Hutton, “Neurofibrillary tangles, amyotrophy and progressive motor disturbance in mice expressing mutant (P301L) tau protein,” Nat. Genet. 25(4), 402–405 (2000).
[Crossref]

Baker, S. L.

R. La Joie, A. V. Visani, S. L. Baker, J. A. Brown, V. Bourakova, J. Cha, K. Chaudhary, L. Edwards, L. Iaccarino, M. Janabi, O. H. Lesman-Segev, Z. A. Miller, D. C. Perry, J. P. O’Neil, J. Pham, J. C. Rojas, H. J. Rosen, W. W. Seeley, R. M. Tsai, B. L. Miller, W. J. Jagust, and G. D. Rabinovici, “Prospective longitudinal atrophy in Alzheimer’s disease correlates with the intensity and topography of baseline tau-PET,” Sci. Transl. Med. 12(524), eaau5732 (2020).
[Crossref]

M. Scholl, S. N. Lockhart, D. R. Schonhaut, J. P. O’Neil, M. Janabi, R. Ossenkoppele, S. L. Baker, J. W. Vogel, J. Faria, H. D. Schwimmer, G. D. Rabinovici, and W. J. Jagust, “PET Imaging of Tau Deposition in the Aging Human Brain,” Neuron 89(5), 971–982 (2016).
[Crossref]

Barmettler, R.

J. Gotz, F. Chen, R. Barmettler, and R. M. Nitsch, “Tau filament formation in transgenic mice expressing P301L tau,” J. Biol. Chem. 276(1), 529–534 (2001).
[Crossref]

Barret, O.

A. Mueller, S. Bullich, O. Barret, J. Madonia, M. Berndt, C. Papin, A. Perrotin, N. Koglin, H. Kroth, A. Pfeifer, G. Tamagnan, J. P. Seibyl, K. Marek, S. de Santi, L. M. Dinkelborg, and A. W. Stephens, “Tau PET imaging with (18)F-PI-2620 in patients with Alzheimer's disease and healthy controls: a first-in-human study,” J. Nucl. Med. 61(6), 911–919 (2020).
[Crossref]

S. Sanabria Bohorquez, J. Marik, A. Ogasawara, J. N. Tinianow, H. S. Gill, O. Barret, G. Tamagnan, D. Alagille, G. Ayalon, P. Manser, T. Bengtsson, M. Ward, S. P. Williams, G. A. Kerchner, J. P. Seibyl, K. Marek, and R. M. Weimer, “[(18)F]GTP1 (Genentech Tau Probe 1), a radioligand for detecting neurofibrillary tangle tau pathology in Alzheimer's disease,” Eur. J. Nucl. Med. Mol. Imaging 46(10), 2077–2089 (2019).
[Crossref]

Bayraktar, G.

B. Wegenast-Braun, A. Skodras, G. Bayraktar, J. Mahler, S. Fritschi, T. Klingstedt, J. Mason, P. Hammarström, K. Nilsson, C. Liebig, and M. Jucker, “Spectral Discrimination of Cerebral Amyloid Lesions after Peripheral Application of Luminescent Conjugated Oligothiophenes,” Am. J. Pathology 181(6), 1953–1960 (2012).
[Crossref]

Becker, J. A.

B. J. Hanseeuw, R. A. Betensky, H. I. L. Jacobs, A. P. Schultz, J. Sepulcre, J. A. Becker, D. M. O. Cosio, M. Farrell, Y. T. Quiroz, E. C. Mormino, R. F. Buckley, K. V. Papp, R. A. Amariglio, I. Dewachter, A. Ivanoiu, W. Huijbers, T. Hedden, G. A. Marshall, J. P. Chhatwal, D. M. Rentz, R. A. Sperling, and K. Johnson, “Association of Amyloid and Tau With Cognition in Preclinical Alzheimer Disease: A Longitudinal Study,” JAMA Neurol. 76(8), 915–924 (2019).
[Crossref]

K. A. Johnson, A. Schultz, R. A. Betensky, J. A. Becker, J. Sepulcre, D. Rentz, E. Mormino, J. Chhatwal, R. Amariglio, K. Papp, G. Marshall, M. Albers, S. Mauro, L. Pepin, J. Alverio, K. Judge, M. Philiossaint, T. Shoup, D. Yokell, B. Dickerson, T. Gomez-Isla, B. Hyman, N. Vasdev, and R. Sperling, “Tau positron emission tomographic imaging in aging and early Alzheimer disease,” Ann Neurol. 79(1), 110–119 (2016).
[Crossref]

Bengtsson, T.

S. Sanabria Bohorquez, J. Marik, A. Ogasawara, J. N. Tinianow, H. S. Gill, O. Barret, G. Tamagnan, D. Alagille, G. Ayalon, P. Manser, T. Bengtsson, M. Ward, S. P. Williams, G. A. Kerchner, J. P. Seibyl, K. Marek, and R. M. Weimer, “[(18)F]GTP1 (Genentech Tau Probe 1), a radioligand for detecting neurofibrillary tangle tau pathology in Alzheimer's disease,” Eur. J. Nucl. Med. Mol. Imaging 46(10), 2077–2089 (2019).
[Crossref]

Bennacef, I.

E. D. Hostetler, A. M. Walji, Z. Zeng, P. Miller, I. Bennacef, C. Salinas, B. Connolly, L. Gantert, H. Haley, M. Holahan, M. Purcell, K. Riffel, T. G. Lohith, P. Coleman, A. Soriano, A. Ogawa, S. Xu, X. Zhang, E. Joshi, J. Della Rocca, D. Hesk, D. J. Schenk, and J. L. Evelhoch, ““Preclinical Characterization of 18F-MK-6240, a Promising PET Tracer for In Vivo Quantification of Human Neurofibrillary Tangles,” Journal of nuclear medicine : official publication,” J. Nuclear Medicine 57(10), 1599–1606 (2016).
[Crossref]

Bennett, C. F.

K. M. Schoch, S. L. DeVos, R. L. Miller, S. J. Chun, M. Norrbom, D. F. Wozniak, H. N. Dawson, C. F. Bennett, F. Rigo, and T. M. Miller, “Increased 4R-Tau Induces Pathological Changes in a Human-Tau Mouse Model,” Neuron 90(5), 941–947 (2016).
[Crossref]

Berndt, M.

A. Mueller, S. Bullich, O. Barret, J. Madonia, M. Berndt, C. Papin, A. Perrotin, N. Koglin, H. Kroth, A. Pfeifer, G. Tamagnan, J. P. Seibyl, K. Marek, S. de Santi, L. M. Dinkelborg, and A. W. Stephens, “Tau PET imaging with (18)F-PI-2620 in patients with Alzheimer's disease and healthy controls: a first-in-human study,” J. Nucl. Med. 61(6), 911–919 (2020).
[Crossref]

H. Kroth, F. Oden, J. Molette, H. Schieferstein, F. Capotosti, A. Mueller, M. Berndt, H. Schmitt-Willich, V. Darmency, E. Gabellieri, C. Boudou, T. Juergens, Y. Varisco, E. Vokali, D. T. Hickman, G. Tamagnan, A. Pfeifer, L. Dinkelborg, A. Muhs, and A. Stephens, “Discovery and preclinical characterization of [(18)F]PI-2620, a next-generation tau PET tracer for the assessment of tau pathology in Alzheimer's disease and other tauopathies,” Eur. J. Nucl. Med. Mol. Imaging 46(10), 2178–2189 (2019).
[Crossref]

Betensky, R. A.

B. J. Hanseeuw, R. A. Betensky, H. I. L. Jacobs, A. P. Schultz, J. Sepulcre, J. A. Becker, D. M. O. Cosio, M. Farrell, Y. T. Quiroz, E. C. Mormino, R. F. Buckley, K. V. Papp, R. A. Amariglio, I. Dewachter, A. Ivanoiu, W. Huijbers, T. Hedden, G. A. Marshall, J. P. Chhatwal, D. M. Rentz, R. A. Sperling, and K. Johnson, “Association of Amyloid and Tau With Cognition in Preclinical Alzheimer Disease: A Longitudinal Study,” JAMA Neurol. 76(8), 915–924 (2019).
[Crossref]

K. A. Johnson, A. Schultz, R. A. Betensky, J. A. Becker, J. Sepulcre, D. Rentz, E. Mormino, J. Chhatwal, R. Amariglio, K. Papp, G. Marshall, M. Albers, S. Mauro, L. Pepin, J. Alverio, K. Judge, M. Philiossaint, T. Shoup, D. Yokell, B. Dickerson, T. Gomez-Isla, B. Hyman, N. Vasdev, and R. Sperling, “Tau positron emission tomographic imaging in aging and early Alzheimer disease,” Ann Neurol. 79(1), 110–119 (2016).
[Crossref]

Blumenstock, S.

P. Marinkovic, S. Blumenstock, P. M. Goltstein, V. Korzhova, F. Peters, A. Knebl, and J. Herms, “In vivo imaging reveals reduced activity of neuronal circuits in a mouse tauopathy model,” Brain 142(4), 1051–1062 (2019).
[Crossref]

Bock, T.

B. M. Burmann, J. A. Gerez, I. Matecko-Burmann, S. Campioni, P. Kumari, D. Ghosh, A. Mazur, E. E. Aspholm, D. Sulskis, M. Wawrzyniuk, T. Bock, A. Schmidt, S. G. D. Rudiger, R. Riek, and S. Hiller, “Regulation of alpha-synuclein by chaperones in mammalian cells,” Nature 577(7788), 127–132 (2020).
[Crossref]

Boersema, P. J.

J. A. Gerez, N. C. Prymaczok, E. Rockenstein, U. S. Herrmann, P. Schwarz, A. Adame, R. I. Enchev, T. Courtheoux, P. J. Boersema, R. Riek, M. Peter, A. Aguzzi, E. Masliah, and P. Picotti, “A cullin-RING ubiquitin ligase targets exogenous alpha-synuclein and inhibits Lewy body-like pathology,” Sci. Transl. Med. 11(495), eaau6722 (2019).
[Crossref]

Boettcher, C.

J. Klohs, N. Baeva, J. Steinbrink, R. Bourayou, C. Boettcher, G. Royl, D. Megow, U. Dirnagl, J. Priller, and A. Wunder, “In vivo near-infrared fluorescence imaging of matrix metalloproteinase activity after cerebral ischemia,” J. Cereb. Blood Flow Metab. 29(7), 1284–1292 (2009).
[Crossref]

Bolmont, T.

A. Aslund, C. J. Sigurdson, T. Klingstedt, S. Grathwohl, T. Bolmont, D. L. Dickstein, E. Glimsdal, S. Prokop, M. Lindgren, P. Konradsson, D. M. Holtzman, P. R. Hof, F. L. Heppner, S. Gandy, M. Jucker, A. Aguzzi, P. Hammarström, and K. P. Nilsson, “Novel pentameric thiophene derivatives for in vitro and in vivo optical imaging of a plethora of protein aggregates in cerebral amyloidoses,” ACS Chem. Biol. 4(8), 673–684 (2009).
[Crossref]

Bonnet, D.

F. Lassailly, K. Foster, L. Lopez-Onieva, E. Currie, and D. Bonnet, “Multimodal imaging reveals structural and functional heterogeneity in different bone marrow compartments: functional implications on hematopoietic stem cells,” Blood 122(10), 1730–1740 (2013).
[Crossref]

Boudou, C.

H. Kroth, F. Oden, J. Molette, H. Schieferstein, F. Capotosti, A. Mueller, M. Berndt, H. Schmitt-Willich, V. Darmency, E. Gabellieri, C. Boudou, T. Juergens, Y. Varisco, E. Vokali, D. T. Hickman, G. Tamagnan, A. Pfeifer, L. Dinkelborg, A. Muhs, and A. Stephens, “Discovery and preclinical characterization of [(18)F]PI-2620, a next-generation tau PET tracer for the assessment of tau pathology in Alzheimer's disease and other tauopathies,” Eur. J. Nucl. Med. Mol. Imaging 46(10), 2178–2189 (2019).
[Crossref]

Bourakova, V.

R. La Joie, A. V. Visani, S. L. Baker, J. A. Brown, V. Bourakova, J. Cha, K. Chaudhary, L. Edwards, L. Iaccarino, M. Janabi, O. H. Lesman-Segev, Z. A. Miller, D. C. Perry, J. P. O’Neil, J. Pham, J. C. Rojas, H. J. Rosen, W. W. Seeley, R. M. Tsai, B. L. Miller, W. J. Jagust, and G. D. Rabinovici, “Prospective longitudinal atrophy in Alzheimer’s disease correlates with the intensity and topography of baseline tau-PET,” Sci. Transl. Med. 12(524), eaau5732 (2020).
[Crossref]

Bourayou, R.

J. Klohs, N. Baeva, J. Steinbrink, R. Bourayou, C. Boettcher, G. Royl, D. Megow, U. Dirnagl, J. Priller, and A. Wunder, “In vivo near-infrared fluorescence imaging of matrix metalloproteinase activity after cerebral ischemia,” J. Cereb. Blood Flow Metab. 29(7), 1284–1292 (2009).
[Crossref]

Boxer, A. L.

E. J. Kim, J. L. Hwang, S. E. Gaus, A. L. Nana, J. Deng, J. A. Brown, S. Spina, M. J. Lee, E. M. Ramos, L. T. Grinberg, J. H. Kramer, A. L. Boxer, M. L. Gorno-Tempini, H. J. Rosen, B. L. Miller, and W. W. Seeley, “Evidence of corticofugal tau spreading in patients with frontotemporal dementia,” Acta Neuropathol. 139(1), 27–43 (2020).
[Crossref]

Braun, A. R.

C. H. Lo, C. K. Lim, Z. Ding, S. P. Wickramasinghe, A. R. Braun, K. H. Ashe, E. Rhoades, D. D. Thomas, and J. N. Sachs, “Targeting the ensemble of heterogeneous tau oligomers in cells: A novel small molecule screening platform for tauopathies,” Alzheimer’s & Dementia 15(11), 1489–1502 (2019).
[Crossref]

Brown, J. A.

R. La Joie, A. V. Visani, S. L. Baker, J. A. Brown, V. Bourakova, J. Cha, K. Chaudhary, L. Edwards, L. Iaccarino, M. Janabi, O. H. Lesman-Segev, Z. A. Miller, D. C. Perry, J. P. O’Neil, J. Pham, J. C. Rojas, H. J. Rosen, W. W. Seeley, R. M. Tsai, B. L. Miller, W. J. Jagust, and G. D. Rabinovici, “Prospective longitudinal atrophy in Alzheimer’s disease correlates with the intensity and topography of baseline tau-PET,” Sci. Transl. Med. 12(524), eaau5732 (2020).
[Crossref]

E. J. Kim, J. L. Hwang, S. E. Gaus, A. L. Nana, J. Deng, J. A. Brown, S. Spina, M. J. Lee, E. M. Ramos, L. T. Grinberg, J. H. Kramer, A. L. Boxer, M. L. Gorno-Tempini, H. J. Rosen, B. L. Miller, and W. W. Seeley, “Evidence of corticofugal tau spreading in patients with frontotemporal dementia,” Acta Neuropathol. 139(1), 27–43 (2020).
[Crossref]

Buckley, R. F.

B. J. Hanseeuw, R. A. Betensky, H. I. L. Jacobs, A. P. Schultz, J. Sepulcre, J. A. Becker, D. M. O. Cosio, M. Farrell, Y. T. Quiroz, E. C. Mormino, R. F. Buckley, K. V. Papp, R. A. Amariglio, I. Dewachter, A. Ivanoiu, W. Huijbers, T. Hedden, G. A. Marshall, J. P. Chhatwal, D. M. Rentz, R. A. Sperling, and K. Johnson, “Association of Amyloid and Tau With Cognition in Preclinical Alzheimer Disease: A Longitudinal Study,” JAMA Neurol. 76(8), 915–924 (2019).
[Crossref]

Buee, L.

M. Colin, S. Dujardin, S. Schraen-Maschke, G. Meno-Tetang, C. Duyckaerts, J. P. Courade, and L. Buee, “From the prion-like propagation hypothesis to therapeutic strategies of anti-tau immunotherapy,” Acta Neuropathol. 139(1), 3–25 (2020).
[Crossref]

Bullich, S.

A. Mueller, S. Bullich, O. Barret, J. Madonia, M. Berndt, C. Papin, A. Perrotin, N. Koglin, H. Kroth, A. Pfeifer, G. Tamagnan, J. P. Seibyl, K. Marek, S. de Santi, L. M. Dinkelborg, and A. W. Stephens, “Tau PET imaging with (18)F-PI-2620 in patients with Alzheimer's disease and healthy controls: a first-in-human study,” J. Nucl. Med. 61(6), 911–919 (2020).
[Crossref]

Burmann, B. M.

B. M. Burmann, J. A. Gerez, I. Matecko-Burmann, S. Campioni, P. Kumari, D. Ghosh, A. Mazur, E. E. Aspholm, D. Sulskis, M. Wawrzyniuk, T. Bock, A. Schmidt, S. G. D. Rudiger, R. Riek, and S. Hiller, “Regulation of alpha-synuclein by chaperones in mammalian cells,” Nature 577(7788), 127–132 (2020).
[Crossref]

Burnham, S. C.

V. L. Villemagne, V. Dore, S. C. Burnham, C. L. Masters, and C. C. Rowe, “Imaging tau and amyloid-beta proteinopathies in Alzheimer disease and other conditions,” Nat. Rev. Neurol. 14(4), 225–236 (2018).
[Crossref]

Calvo-Rodriguez, M.

M. Calvo-Rodriguez, S. S. Hou, A. C. Snyder, S. Dujardin, H. Shirani, K. P. R. Nilsson, and B. J. Bacskai, “In vivo detection of tau fibrils and amyloid beta aggregates with luminescent conjugated oligothiophenes and multiphoton microscopy,” Acta Neuropathol. Commun. 7(1), 171 (2019).
[Crossref]

Campioni, S.

B. M. Burmann, J. A. Gerez, I. Matecko-Burmann, S. Campioni, P. Kumari, D. Ghosh, A. Mazur, E. E. Aspholm, D. Sulskis, M. Wawrzyniuk, T. Bock, A. Schmidt, S. G. D. Rudiger, R. Riek, and S. Hiller, “Regulation of alpha-synuclein by chaperones in mammalian cells,” Nature 577(7788), 127–132 (2020).
[Crossref]

Capotosti, F.

H. Kroth, F. Oden, J. Molette, H. Schieferstein, F. Capotosti, A. Mueller, M. Berndt, H. Schmitt-Willich, V. Darmency, E. Gabellieri, C. Boudou, T. Juergens, Y. Varisco, E. Vokali, D. T. Hickman, G. Tamagnan, A. Pfeifer, L. Dinkelborg, A. Muhs, and A. Stephens, “Discovery and preclinical characterization of [(18)F]PI-2620, a next-generation tau PET tracer for the assessment of tau pathology in Alzheimer's disease and other tauopathies,” Eur. J. Nucl. Med. Mol. Imaging 46(10), 2178–2189 (2019).
[Crossref]

Carano, R. A. D.

B. Dejanovic, M. A. Huntley, A. De Maziere, W. J. Meilandt, T. Wu, K. Srinivasan, Z. Jiang, V. Gandham, B. A. Friedman, H. Ngu, O. Foreman, R. A. D. Carano, B. Chih, J. Klumperman, C. Bakalarski, J. E. Hanson, and M. Sheng, “Changes in the Synaptic Proteome in Tauopathy and Rescue of Tau-Induced Synapse Loss by C1q Antibodies,” Neuron 100(6), 1322–1336.e7 (2018).
[Crossref]

Carlson, G. A.

A. de Calignon, L. M. Fox, R. Pitstick, G. A. Carlson, B. J. Bacskai, T. L. Spires-Jones, and B. T. Hyman, “Caspase activation precedes and leads to tangles,” Nature 464(7292), 1201–1204 (2010).
[Crossref]

Castillo-Carranza, D. L.

C. A. Lasagna-Reeves, D. L. Castillo-Carranza, U. Sengupta, J. Sarmiento, J. Troncoso, G. R. Jackson, and R. Kayed, “Identification of oligomers at early stages of tau aggregation in Alzheimer's disease,” FASEB J. 26(5), 1946–1959 (2012).
[Crossref]

Cha, J.

R. La Joie, A. V. Visani, S. L. Baker, J. A. Brown, V. Bourakova, J. Cha, K. Chaudhary, L. Edwards, L. Iaccarino, M. Janabi, O. H. Lesman-Segev, Z. A. Miller, D. C. Perry, J. P. O’Neil, J. Pham, J. C. Rojas, H. J. Rosen, W. W. Seeley, R. M. Tsai, B. L. Miller, W. J. Jagust, and G. D. Rabinovici, “Prospective longitudinal atrophy in Alzheimer’s disease correlates with the intensity and topography of baseline tau-PET,” Sci. Transl. Med. 12(524), eaau5732 (2020).
[Crossref]

Chang, Q.

M. Maruyama, H. Shimada, T. Suhara, H. Shinotoh, B. Ji, J. Maeda, M. R. Zhang, J. Q. Trojanowski, V. M. Lee, M. Ono, K. Masamoto, H. Takano, N. Sahara, N. Iwata, N. Okamura, S. Furumoto, Y. Kudo, Q. Chang, T. C. Saido, A. Takashima, J. Lewis, M. K. Jang, I. Aoki, H. Ito, and M. Higuchi, “Imaging of tau pathology in a tauopathy mouse model and in Alzheimer patients compared to normal controls,” Neuron 79(6), 1094–1108 (2013).
[Crossref]

Changolkar, L.

Z. He, J. D. McBride, H. Xu, L. Changolkar, S. J. Kim, B. Zhang, S. Narasimhan, G. S. Gibbons, J. L. Guo, M. Kozak, G. D. Schellenberg, J. Q. Trojanowski, and V. M. Lee, “Transmission of tauopathy strains is independent of their isoform composition,” Nat. Commun. 11(1), 7 (2020).
[Crossref]

Chaudhary, K.

R. La Joie, A. V. Visani, S. L. Baker, J. A. Brown, V. Bourakova, J. Cha, K. Chaudhary, L. Edwards, L. Iaccarino, M. Janabi, O. H. Lesman-Segev, Z. A. Miller, D. C. Perry, J. P. O’Neil, J. Pham, J. C. Rojas, H. J. Rosen, W. W. Seeley, R. M. Tsai, B. L. Miller, W. J. Jagust, and G. D. Rabinovici, “Prospective longitudinal atrophy in Alzheimer’s disease correlates with the intensity and topography of baseline tau-PET,” Sci. Transl. Med. 12(524), eaau5732 (2020).
[Crossref]

Chen, F.

J. Gotz, F. Chen, J. van Dorpe, and R. M. Nitsch, “Formation of neurofibrillary tangles in P301 l tau transgenic mice induced by Abeta 42 fibrils,” Science 293(5534), 1491–1495 (2001).
[Crossref]

J. Gotz, F. Chen, R. Barmettler, and R. M. Nitsch, “Tau filament formation in transgenic mice expressing P301L tau,” J. Biol. Chem. 276(1), 529–534 (2001).
[Crossref]

Chen, Z.

Z. Chen, B. Mc Larney, J. Rebling, X. L. Deán-Ben, Q. Zhou, S. Gottschalk, and D. Razansky, “High-Speed Large-Field Multifocal Illumination Fluorescence Microscopy,” Laser Photonics Rev. 14, 1900070 (2020).
[Crossref]

R. Ni, Z. Chen, G. Shi, A. Villois, Q. Zhou, P. Arosio, R. M. Nitsch, P. R. Nilsson, J. Klohs, and D. Razansky, “Transcranial in vivo detection of Aβ at single plaque resolution with large-field multifocal illumination fluorescence microscopy,” bioRxiv, 2020.2002.2001.929844 (2020).

R. Ni, X. L. Dean-Ben, D. Kirschenbaum, M. Rudin, Z. Chen, A. Crimi, F. Voigt, P. R. Nilsson, F. Helmchen, R. M. Nitsch, A. Aguzzi, D. Razansky, and J. Klohs, “Whole brain optoacoustic tomography reveals strain-specific regional beta-amyloid densities in Alzheimer`s disease amyloidosis models,” bioRxiv, DOI: 10.1101/2020.1102.1125.964064 (2020).

Chhatwal, J.

K. A. Johnson, A. Schultz, R. A. Betensky, J. A. Becker, J. Sepulcre, D. Rentz, E. Mormino, J. Chhatwal, R. Amariglio, K. Papp, G. Marshall, M. Albers, S. Mauro, L. Pepin, J. Alverio, K. Judge, M. Philiossaint, T. Shoup, D. Yokell, B. Dickerson, T. Gomez-Isla, B. Hyman, N. Vasdev, and R. Sperling, “Tau positron emission tomographic imaging in aging and early Alzheimer disease,” Ann Neurol. 79(1), 110–119 (2016).
[Crossref]

Chhatwal, J. P.

B. J. Hanseeuw, R. A. Betensky, H. I. L. Jacobs, A. P. Schultz, J. Sepulcre, J. A. Becker, D. M. O. Cosio, M. Farrell, Y. T. Quiroz, E. C. Mormino, R. F. Buckley, K. V. Papp, R. A. Amariglio, I. Dewachter, A. Ivanoiu, W. Huijbers, T. Hedden, G. A. Marshall, J. P. Chhatwal, D. M. Rentz, R. A. Sperling, and K. Johnson, “Association of Amyloid and Tau With Cognition in Preclinical Alzheimer Disease: A Longitudinal Study,” JAMA Neurol. 76(8), 915–924 (2019).
[Crossref]

Chih, B.

B. Dejanovic, M. A. Huntley, A. De Maziere, W. J. Meilandt, T. Wu, K. Srinivasan, Z. Jiang, V. Gandham, B. A. Friedman, H. Ngu, O. Foreman, R. A. D. Carano, B. Chih, J. Klumperman, C. Bakalarski, J. E. Hanson, and M. Sheng, “Changes in the Synaptic Proteome in Tauopathy and Rescue of Tau-Induced Synapse Loss by C1q Antibodies,” Neuron 100(6), 1322–1336.e7 (2018).
[Crossref]

Chun, S. J.

K. M. Schoch, S. L. DeVos, R. L. Miller, S. J. Chun, M. Norrbom, D. F. Wozniak, H. N. Dawson, C. F. Bennett, F. Rigo, and T. M. Miller, “Increased 4R-Tau Induces Pathological Changes in a Human-Tau Mouse Model,” Neuron 90(5), 941–947 (2016).
[Crossref]

Coble, D.

T. K. Patel, L. Habimana-Griffin, X. Gao, B. Xu, S. Achilefu, K. Alitalo, C. A. McKee, P. W. Sheehan, E. S. Musiek, C. Xiong, D. Coble, and D. M. Holtzman, “Dural lymphatics regulate clearance of extracellular tau from the CNS,” Mol. Neurodegener. 14(1), 11 (2019).
[Crossref]

Coleman, P.

E. D. Hostetler, A. M. Walji, Z. Zeng, P. Miller, I. Bennacef, C. Salinas, B. Connolly, L. Gantert, H. Haley, M. Holahan, M. Purcell, K. Riffel, T. G. Lohith, P. Coleman, A. Soriano, A. Ogawa, S. Xu, X. Zhang, E. Joshi, J. Della Rocca, D. Hesk, D. J. Schenk, and J. L. Evelhoch, ““Preclinical Characterization of 18F-MK-6240, a Promising PET Tracer for In Vivo Quantification of Human Neurofibrillary Tangles,” Journal of nuclear medicine : official publication,” J. Nuclear Medicine 57(10), 1599–1606 (2016).
[Crossref]

Colin, M.

M. Colin, S. Dujardin, S. Schraen-Maschke, G. Meno-Tetang, C. Duyckaerts, J. P. Courade, and L. Buee, “From the prion-like propagation hypothesis to therapeutic strategies of anti-tau immunotherapy,” Acta Neuropathol. 139(1), 3–25 (2020).
[Crossref]

Congdon, E. E.

E. E. Congdon and E. M. Sigurdsson, “Tau-targeting therapies for Alzheimer disease,” Nat. Rev. Neurol. 14(7), 399–415 (2018).
[Crossref]

Connolly, B.

E. D. Hostetler, A. M. Walji, Z. Zeng, P. Miller, I. Bennacef, C. Salinas, B. Connolly, L. Gantert, H. Haley, M. Holahan, M. Purcell, K. Riffel, T. G. Lohith, P. Coleman, A. Soriano, A. Ogawa, S. Xu, X. Zhang, E. Joshi, J. Della Rocca, D. Hesk, D. J. Schenk, and J. L. Evelhoch, ““Preclinical Characterization of 18F-MK-6240, a Promising PET Tracer for In Vivo Quantification of Human Neurofibrillary Tangles,” Journal of nuclear medicine : official publication,” J. Nuclear Medicine 57(10), 1599–1606 (2016).
[Crossref]

Corral, A.

J. Lewis, E. McGowan, J. Rockwood, H. Melrose, P. Nacharaju, M. Van Slegtenhorst, K. Gwinn-Hardy, M. Paul Murphy, M. Baker, X. Yu, K. Duff, J. Hardy, A. Corral, W. L. Lin, S. H. Yen, D. W. Dickson, P. Davies, and M. Hutton, “Neurofibrillary tangles, amyotrophy and progressive motor disturbance in mice expressing mutant (P301L) tau protein,” Nat. Genet. 25(4), 402–405 (2000).
[Crossref]

Cosio, D. M. O.

B. J. Hanseeuw, R. A. Betensky, H. I. L. Jacobs, A. P. Schultz, J. Sepulcre, J. A. Becker, D. M. O. Cosio, M. Farrell, Y. T. Quiroz, E. C. Mormino, R. F. Buckley, K. V. Papp, R. A. Amariglio, I. Dewachter, A. Ivanoiu, W. Huijbers, T. Hedden, G. A. Marshall, J. P. Chhatwal, D. M. Rentz, R. A. Sperling, and K. Johnson, “Association of Amyloid and Tau With Cognition in Preclinical Alzheimer Disease: A Longitudinal Study,” JAMA Neurol. 76(8), 915–924 (2019).
[Crossref]

Courade, J. P.

M. Colin, S. Dujardin, S. Schraen-Maschke, G. Meno-Tetang, C. Duyckaerts, J. P. Courade, and L. Buee, “From the prion-like propagation hypothesis to therapeutic strategies of anti-tau immunotherapy,” Acta Neuropathol. 139(1), 3–25 (2020).
[Crossref]

Courtheoux, T.

J. A. Gerez, N. C. Prymaczok, E. Rockenstein, U. S. Herrmann, P. Schwarz, A. Adame, R. I. Enchev, T. Courtheoux, P. J. Boersema, R. Riek, M. Peter, A. Aguzzi, E. Masliah, and P. Picotti, “A cullin-RING ubiquitin ligase targets exogenous alpha-synuclein and inhibits Lewy body-like pathology,” Sci. Transl. Med. 11(495), eaau6722 (2019).
[Crossref]

Crimi, A.

R. Ni, X. L. Dean-Ben, D. Kirschenbaum, M. Rudin, Z. Chen, A. Crimi, F. Voigt, P. R. Nilsson, F. Helmchen, R. M. Nitsch, A. Aguzzi, D. Razansky, and J. Klohs, “Whole brain optoacoustic tomography reveals strain-specific regional beta-amyloid densities in Alzheimer`s disease amyloidosis models,” bioRxiv, DOI: 10.1101/2020.1102.1125.964064 (2020).

Crowther, R. A.

A. W. P. Fitzpatrick, B. Falcon, S. He, A. G. Murzin, G. Murshudov, H. J. Garringer, R. A. Crowther, B. Ghetti, M. Goedert, and S. H. W. Scheres, “Cryo-EM structures of tau filaments from Alzheimer's disease,” Nature 547(7662), 185–190 (2017).
[Crossref]

P. Delobel, I. Lavenir, G. Fraser, E. Ingram, M. Holzer, B. Ghetti, M. G. Spillantini, R. A. Crowther, and M. Goedert, “Analysis of tau phosphorylation and truncation in a mouse model of human tauopathy,” Am. J. Pathology 172(1), 123–131 (2008).
[Crossref]

Currie, E.

F. Lassailly, K. Foster, L. Lopez-Onieva, E. Currie, and D. Bonnet, “Multimodal imaging reveals structural and functional heterogeneity in different bone marrow compartments: functional implications on hematopoietic stem cells,” Blood 122(10), 1730–1740 (2013).
[Crossref]

Darmency, V.

H. Kroth, F. Oden, J. Molette, H. Schieferstein, F. Capotosti, A. Mueller, M. Berndt, H. Schmitt-Willich, V. Darmency, E. Gabellieri, C. Boudou, T. Juergens, Y. Varisco, E. Vokali, D. T. Hickman, G. Tamagnan, A. Pfeifer, L. Dinkelborg, A. Muhs, and A. Stephens, “Discovery and preclinical characterization of [(18)F]PI-2620, a next-generation tau PET tracer for the assessment of tau pathology in Alzheimer's disease and other tauopathies,” Eur. J. Nucl. Med. Mol. Imaging 46(10), 2178–2189 (2019).
[Crossref]

Davies, P.

J. Lewis, E. McGowan, J. Rockwood, H. Melrose, P. Nacharaju, M. Van Slegtenhorst, K. Gwinn-Hardy, M. Paul Murphy, M. Baker, X. Yu, K. Duff, J. Hardy, A. Corral, W. L. Lin, S. H. Yen, D. W. Dickson, P. Davies, and M. Hutton, “Neurofibrillary tangles, amyotrophy and progressive motor disturbance in mice expressing mutant (P301L) tau protein,” Nat. Genet. 25(4), 402–405 (2000).
[Crossref]

Dawson, H. N.

K. M. Schoch, S. L. DeVos, R. L. Miller, S. J. Chun, M. Norrbom, D. F. Wozniak, H. N. Dawson, C. F. Bennett, F. Rigo, and T. M. Miller, “Increased 4R-Tau Induces Pathological Changes in a Human-Tau Mouse Model,” Neuron 90(5), 941–947 (2016).
[Crossref]

de Calignon, A.

A. de Calignon, L. M. Fox, R. Pitstick, G. A. Carlson, B. J. Bacskai, T. L. Spires-Jones, and B. T. Hyman, “Caspase activation precedes and leads to tangles,” Nature 464(7292), 1201–1204 (2010).
[Crossref]

De Maziere, A.

B. Dejanovic, M. A. Huntley, A. De Maziere, W. J. Meilandt, T. Wu, K. Srinivasan, Z. Jiang, V. Gandham, B. A. Friedman, H. Ngu, O. Foreman, R. A. D. Carano, B. Chih, J. Klumperman, C. Bakalarski, J. E. Hanson, and M. Sheng, “Changes in the Synaptic Proteome in Tauopathy and Rescue of Tau-Induced Synapse Loss by C1q Antibodies,” Neuron 100(6), 1322–1336.e7 (2018).
[Crossref]

de Santi, S.

A. Mueller, S. Bullich, O. Barret, J. Madonia, M. Berndt, C. Papin, A. Perrotin, N. Koglin, H. Kroth, A. Pfeifer, G. Tamagnan, J. P. Seibyl, K. Marek, S. de Santi, L. M. Dinkelborg, and A. W. Stephens, “Tau PET imaging with (18)F-PI-2620 in patients with Alzheimer's disease and healthy controls: a first-in-human study,” J. Nucl. Med. 61(6), 911–919 (2020).
[Crossref]

Dean-Ben, X. L.

R. Ni, X. L. Dean-Ben, D. Kirschenbaum, M. Rudin, Z. Chen, A. Crimi, F. Voigt, P. R. Nilsson, F. Helmchen, R. M. Nitsch, A. Aguzzi, D. Razansky, and J. Klohs, “Whole brain optoacoustic tomography reveals strain-specific regional beta-amyloid densities in Alzheimer`s disease amyloidosis models,” bioRxiv, DOI: 10.1101/2020.1102.1125.964064 (2020).

Deán-Ben, X. L.

Z. Chen, B. Mc Larney, J. Rebling, X. L. Deán-Ben, Q. Zhou, S. Gottschalk, and D. Razansky, “High-Speed Large-Field Multifocal Illumination Fluorescence Microscopy,” Laser Photonics Rev. 14, 1900070 (2020).
[Crossref]

S. Gottschalk, O. Degtyaruk, B. Mc Larney, J. Rebling, M. A. Hutter, X. L. Deán-Ben, S. Shoham, and D. Razansky, “Rapid volumetric optoacoustic imaging of neural dynamics across the mouse brain,” Nat. Biomed. Eng. 3(5), 392–401 (2019).
[Crossref]

Degtyaruk, O.

S. Gottschalk, O. Degtyaruk, B. Mc Larney, J. Rebling, M. A. Hutter, X. L. Deán-Ben, S. Shoham, and D. Razansky, “Rapid volumetric optoacoustic imaging of neural dynamics across the mouse brain,” Nat. Biomed. Eng. 3(5), 392–401 (2019).
[Crossref]

Dejanovic, B.

B. Dejanovic, M. A. Huntley, A. De Maziere, W. J. Meilandt, T. Wu, K. Srinivasan, Z. Jiang, V. Gandham, B. A. Friedman, H. Ngu, O. Foreman, R. A. D. Carano, B. Chih, J. Klumperman, C. Bakalarski, J. E. Hanson, and M. Sheng, “Changes in the Synaptic Proteome in Tauopathy and Rescue of Tau-Induced Synapse Loss by C1q Antibodies,” Neuron 100(6), 1322–1336.e7 (2018).
[Crossref]

Della Rocca, J.

E. D. Hostetler, A. M. Walji, Z. Zeng, P. Miller, I. Bennacef, C. Salinas, B. Connolly, L. Gantert, H. Haley, M. Holahan, M. Purcell, K. Riffel, T. G. Lohith, P. Coleman, A. Soriano, A. Ogawa, S. Xu, X. Zhang, E. Joshi, J. Della Rocca, D. Hesk, D. J. Schenk, and J. L. Evelhoch, ““Preclinical Characterization of 18F-MK-6240, a Promising PET Tracer for In Vivo Quantification of Human Neurofibrillary Tangles,” Journal of nuclear medicine : official publication,” J. Nuclear Medicine 57(10), 1599–1606 (2016).
[Crossref]

Delobel, P.

P. Delobel, I. Lavenir, G. Fraser, E. Ingram, M. Holzer, B. Ghetti, M. G. Spillantini, R. A. Crowther, and M. Goedert, “Analysis of tau phosphorylation and truncation in a mouse model of human tauopathy,” Am. J. Pathology 172(1), 123–131 (2008).
[Crossref]

A. Velasco, G. Fraser, P. Delobel, B. Ghetti, I. Lavenir, and M. Goedert, “Detection of filamentous tau inclusions by the fluorescent Congo red derivative FSB [(trans,trans)-1-fluoro-2,5-bis(3-hydroxycarbonyl-4-hydroxy)styrylbenzene],” FEBS Lett. 582(6), 901–906 (2008).
[Crossref]

Deng, J.

E. J. Kim, J. L. Hwang, S. E. Gaus, A. L. Nana, J. Deng, J. A. Brown, S. Spina, M. J. Lee, E. M. Ramos, L. T. Grinberg, J. H. Kramer, A. L. Boxer, M. L. Gorno-Tempini, H. J. Rosen, B. L. Miller, and W. W. Seeley, “Evidence of corticofugal tau spreading in patients with frontotemporal dementia,” Acta Neuropathol. 139(1), 27–43 (2020).
[Crossref]

DeTure, M.

K. SantaCruz, J. Lewis, T. Spires, J. Paulson, L. Kotilinek, M. Ingelsson, A. Guimaraes, M. DeTure, M. Ramsden, E. McGowan, C. Forster, M. Yue, J. Orne, C. Janus, A. Mariash, M. Kuskowski, B. Hyman, M. Hutton, and K. H. Ashe, “Tau Suppression in a Neurodegenerative Mouse Model Improves Memory Function,” Science 309(5733), 476–481 (2005).
[Crossref]

DeVos, S. L.

K. M. Schoch, S. L. DeVos, R. L. Miller, S. J. Chun, M. Norrbom, D. F. Wozniak, H. N. Dawson, C. F. Bennett, F. Rigo, and T. M. Miller, “Increased 4R-Tau Induces Pathological Changes in a Human-Tau Mouse Model,” Neuron 90(5), 941–947 (2016).
[Crossref]

Dewachter, I.

B. J. Hanseeuw, R. A. Betensky, H. I. L. Jacobs, A. P. Schultz, J. Sepulcre, J. A. Becker, D. M. O. Cosio, M. Farrell, Y. T. Quiroz, E. C. Mormino, R. F. Buckley, K. V. Papp, R. A. Amariglio, I. Dewachter, A. Ivanoiu, W. Huijbers, T. Hedden, G. A. Marshall, J. P. Chhatwal, D. M. Rentz, R. A. Sperling, and K. Johnson, “Association of Amyloid and Tau With Cognition in Preclinical Alzheimer Disease: A Longitudinal Study,” JAMA Neurol. 76(8), 915–924 (2019).
[Crossref]

Diamond, M. I.

S. K. Kaufman, D. W. Sanders, T. L. Thomas, A. J. Ruchinskas, J. Vaquer-Alicea, A. M. Sharma, T. M. Miller, and M. I. Diamond, “Tau Prion Strains Dictate Patterns of Cell Pathology, Progression Rate, and Regional Vulnerability In Vivo,” Neuron 92(4), 796–812 (2016).
[Crossref]

Dickerson, B.

K. A. Johnson, A. Schultz, R. A. Betensky, J. A. Becker, J. Sepulcre, D. Rentz, E. Mormino, J. Chhatwal, R. Amariglio, K. Papp, G. Marshall, M. Albers, S. Mauro, L. Pepin, J. Alverio, K. Judge, M. Philiossaint, T. Shoup, D. Yokell, B. Dickerson, T. Gomez-Isla, B. Hyman, N. Vasdev, and R. Sperling, “Tau positron emission tomographic imaging in aging and early Alzheimer disease,” Ann Neurol. 79(1), 110–119 (2016).
[Crossref]

Dickson, D. W.

M. Ono, N. Sahara, K. Kumata, B. Ji, R. Ni, S. Koga, D. W. Dickson, J. Q. Trojanowski, V. M.-Y. Lee, M. Yoshida, I. Hozumi, Y. Yoshiyama, J. C. v. Swieten, A. Nordberg, T. Suhara, M.-R. Zhang, and M. Higuchi, “Distinct binding of PET ligands PBB3 and AV-1451 to tau fibril strains in neurodegenerative tauopathies,” Brain 140, aww339 (2017).
[Crossref]

J. Lewis, E. McGowan, J. Rockwood, H. Melrose, P. Nacharaju, M. Van Slegtenhorst, K. Gwinn-Hardy, M. Paul Murphy, M. Baker, X. Yu, K. Duff, J. Hardy, A. Corral, W. L. Lin, S. H. Yen, D. W. Dickson, P. Davies, and M. Hutton, “Neurofibrillary tangles, amyotrophy and progressive motor disturbance in mice expressing mutant (P301L) tau protein,” Nat. Genet. 25(4), 402–405 (2000).
[Crossref]

Dickstein, D. L.

A. Aslund, C. J. Sigurdson, T. Klingstedt, S. Grathwohl, T. Bolmont, D. L. Dickstein, E. Glimsdal, S. Prokop, M. Lindgren, P. Konradsson, D. M. Holtzman, P. R. Hof, F. L. Heppner, S. Gandy, M. Jucker, A. Aguzzi, P. Hammarström, and K. P. Nilsson, “Novel pentameric thiophene derivatives for in vitro and in vivo optical imaging of a plethora of protein aggregates in cerebral amyloidoses,” ACS Chem. Biol. 4(8), 673–684 (2009).
[Crossref]

Ding, Z.

C. H. Lo, C. K. Lim, Z. Ding, S. P. Wickramasinghe, A. R. Braun, K. H. Ashe, E. Rhoades, D. D. Thomas, and J. N. Sachs, “Targeting the ensemble of heterogeneous tau oligomers in cells: A novel small molecule screening platform for tauopathies,” Alzheimer’s & Dementia 15(11), 1489–1502 (2019).
[Crossref]

Dinkelborg, L.

H. Kroth, F. Oden, J. Molette, H. Schieferstein, F. Capotosti, A. Mueller, M. Berndt, H. Schmitt-Willich, V. Darmency, E. Gabellieri, C. Boudou, T. Juergens, Y. Varisco, E. Vokali, D. T. Hickman, G. Tamagnan, A. Pfeifer, L. Dinkelborg, A. Muhs, and A. Stephens, “Discovery and preclinical characterization of [(18)F]PI-2620, a next-generation tau PET tracer for the assessment of tau pathology in Alzheimer's disease and other tauopathies,” Eur. J. Nucl. Med. Mol. Imaging 46(10), 2178–2189 (2019).
[Crossref]

Dinkelborg, L. M.

A. Mueller, S. Bullich, O. Barret, J. Madonia, M. Berndt, C. Papin, A. Perrotin, N. Koglin, H. Kroth, A. Pfeifer, G. Tamagnan, J. P. Seibyl, K. Marek, S. de Santi, L. M. Dinkelborg, and A. W. Stephens, “Tau PET imaging with (18)F-PI-2620 in patients with Alzheimer's disease and healthy controls: a first-in-human study,” J. Nucl. Med. 61(6), 911–919 (2020).
[Crossref]

Dirnagl, U.

J. Klohs, N. Baeva, J. Steinbrink, R. Bourayou, C. Boettcher, G. Royl, D. Megow, U. Dirnagl, J. Priller, and A. Wunder, “In vivo near-infrared fluorescence imaging of matrix metalloproteinase activity after cerebral ischemia,” J. Cereb. Blood Flow Metab. 29(7), 1284–1292 (2009).
[Crossref]

Dore, V.

V. L. Villemagne, V. Dore, S. C. Burnham, C. L. Masters, and C. C. Rowe, “Imaging tau and amyloid-beta proteinopathies in Alzheimer disease and other conditions,” Nat. Rev. Neurol. 14(4), 225–236 (2018).
[Crossref]

Duff, K.

J. Lewis, E. McGowan, J. Rockwood, H. Melrose, P. Nacharaju, M. Van Slegtenhorst, K. Gwinn-Hardy, M. Paul Murphy, M. Baker, X. Yu, K. Duff, J. Hardy, A. Corral, W. L. Lin, S. H. Yen, D. W. Dickson, P. Davies, and M. Hutton, “Neurofibrillary tangles, amyotrophy and progressive motor disturbance in mice expressing mutant (P301L) tau protein,” Nat. Genet. 25(4), 402–405 (2000).
[Crossref]

Dujardin, S.

M. Colin, S. Dujardin, S. Schraen-Maschke, G. Meno-Tetang, C. Duyckaerts, J. P. Courade, and L. Buee, “From the prion-like propagation hypothesis to therapeutic strategies of anti-tau immunotherapy,” Acta Neuropathol. 139(1), 3–25 (2020).
[Crossref]

M. Calvo-Rodriguez, S. S. Hou, A. C. Snyder, S. Dujardin, H. Shirani, K. P. R. Nilsson, and B. J. Bacskai, “In vivo detection of tau fibrils and amyloid beta aggregates with luminescent conjugated oligothiophenes and multiphoton microscopy,” Acta Neuropathol. Commun. 7(1), 171 (2019).
[Crossref]

Duyckaerts, C.

M. Colin, S. Dujardin, S. Schraen-Maschke, G. Meno-Tetang, C. Duyckaerts, J. P. Courade, and L. Buee, “From the prion-like propagation hypothesis to therapeutic strategies of anti-tau immunotherapy,” Acta Neuropathol. 139(1), 3–25 (2020).
[Crossref]

Edwards, L.

R. La Joie, A. V. Visani, S. L. Baker, J. A. Brown, V. Bourakova, J. Cha, K. Chaudhary, L. Edwards, L. Iaccarino, M. Janabi, O. H. Lesman-Segev, Z. A. Miller, D. C. Perry, J. P. O’Neil, J. Pham, J. C. Rojas, H. J. Rosen, W. W. Seeley, R. M. Tsai, B. L. Miller, W. J. Jagust, and G. D. Rabinovici, “Prospective longitudinal atrophy in Alzheimer’s disease correlates with the intensity and topography of baseline tau-PET,” Sci. Transl. Med. 12(524), eaau5732 (2020).
[Crossref]

Enchev, R. I.

J. A. Gerez, N. C. Prymaczok, E. Rockenstein, U. S. Herrmann, P. Schwarz, A. Adame, R. I. Enchev, T. Courtheoux, P. J. Boersema, R. Riek, M. Peter, A. Aguzzi, E. Masliah, and P. Picotti, “A cullin-RING ubiquitin ligase targets exogenous alpha-synuclein and inhibits Lewy body-like pathology,” Sci. Transl. Med. 11(495), eaau6722 (2019).
[Crossref]

Enderlein, J.

I. Gregor and J. Enderlein, “Image scanning microscopy,” Curr. Opin. Chem. Biol. 51, 74–83 (2019).
[Crossref]

Enz, A.

M. Hintersteiner, A. Enz, P. Frey, A. L. Jaton, W. Kinzy, R. Kneuer, U. Neumann, M. Rudin, M. Staufenbiel, M. Stoeckli, K. H. Wiederhold, and H. U. Gremlich, “In vivo detection of amyloid-beta deposits by near-infrared imaging using an oxazine-derivative probe,” Nat. Biotechnol. 23(5), 577–583 (2005).
[Crossref]

Evelhoch, J. L.

E. D. Hostetler, A. M. Walji, Z. Zeng, P. Miller, I. Bennacef, C. Salinas, B. Connolly, L. Gantert, H. Haley, M. Holahan, M. Purcell, K. Riffel, T. G. Lohith, P. Coleman, A. Soriano, A. Ogawa, S. Xu, X. Zhang, E. Joshi, J. Della Rocca, D. Hesk, D. J. Schenk, and J. L. Evelhoch, ““Preclinical Characterization of 18F-MK-6240, a Promising PET Tracer for In Vivo Quantification of Human Neurofibrillary Tangles,” Journal of nuclear medicine : official publication,” J. Nuclear Medicine 57(10), 1599–1606 (2016).
[Crossref]

Falcon, B.

A. W. P. Fitzpatrick, B. Falcon, S. He, A. G. Murzin, G. Murshudov, H. J. Garringer, R. A. Crowther, B. Ghetti, M. Goedert, and S. H. W. Scheres, “Cryo-EM structures of tau filaments from Alzheimer's disease,” Nature 547(7662), 185–190 (2017).
[Crossref]

Faria, J.

M. Scholl, S. N. Lockhart, D. R. Schonhaut, J. P. O’Neil, M. Janabi, R. Ossenkoppele, S. L. Baker, J. W. Vogel, J. Faria, H. D. Schwimmer, G. D. Rabinovici, and W. J. Jagust, “PET Imaging of Tau Deposition in the Aging Human Brain,” Neuron 89(5), 971–982 (2016).
[Crossref]

Farrell, M.

B. J. Hanseeuw, R. A. Betensky, H. I. L. Jacobs, A. P. Schultz, J. Sepulcre, J. A. Becker, D. M. O. Cosio, M. Farrell, Y. T. Quiroz, E. C. Mormino, R. F. Buckley, K. V. Papp, R. A. Amariglio, I. Dewachter, A. Ivanoiu, W. Huijbers, T. Hedden, G. A. Marshall, J. P. Chhatwal, D. M. Rentz, R. A. Sperling, and K. Johnson, “Association of Amyloid and Tau With Cognition in Preclinical Alzheimer Disease: A Longitudinal Study,” JAMA Neurol. 76(8), 915–924 (2019).
[Crossref]

Febo, M.

N. Sahara, M. Shimojo, M. Ono, H. Takuwa, M. Febo, M. Higuchi, and T. Suhara, “In Vivo Tau Imaging for a Diagnostic Platform of Tauopathy Using the rTg4510 Mouse Line,” Front Neurol. 8, 663 (2017).
[Crossref]

Feil, R.

P. Füger, J. K. Hefendehl, K. Veeraraghavalu, A.-C. Wendeln, C. Schlosser, U. Obermüller, B. M. Wegenast-Braun, J. J. Neher, P. Martus, S. Kohsaka, M. Thunemann, R. Feil, S. S. Sisodia, A. Skodras, and M. Jucker, “Microglia turnover with aging and in an Alzheimer's model via long-term in vivo single-cell imaging,” Nat. Neurosci. 20(10), 1371–1376 (2017).
[Crossref]

Fitzpatrick, A. W. P.

A. W. P. Fitzpatrick, B. Falcon, S. He, A. G. Murzin, G. Murshudov, H. J. Garringer, R. A. Crowther, B. Ghetti, M. Goedert, and S. H. W. Scheres, “Cryo-EM structures of tau filaments from Alzheimer's disease,” Nature 547(7662), 185–190 (2017).
[Crossref]

Foreman, O.

B. Dejanovic, M. A. Huntley, A. De Maziere, W. J. Meilandt, T. Wu, K. Srinivasan, Z. Jiang, V. Gandham, B. A. Friedman, H. Ngu, O. Foreman, R. A. D. Carano, B. Chih, J. Klumperman, C. Bakalarski, J. E. Hanson, and M. Sheng, “Changes in the Synaptic Proteome in Tauopathy and Rescue of Tau-Induced Synapse Loss by C1q Antibodies,” Neuron 100(6), 1322–1336.e7 (2018).
[Crossref]

Forster, C.

K. SantaCruz, J. Lewis, T. Spires, J. Paulson, L. Kotilinek, M. Ingelsson, A. Guimaraes, M. DeTure, M. Ramsden, E. McGowan, C. Forster, M. Yue, J. Orne, C. Janus, A. Mariash, M. Kuskowski, B. Hyman, M. Hutton, and K. H. Ashe, “Tau Suppression in a Neurodegenerative Mouse Model Improves Memory Function,” Science 309(5733), 476–481 (2005).
[Crossref]

Foster, K.

F. Lassailly, K. Foster, L. Lopez-Onieva, E. Currie, and D. Bonnet, “Multimodal imaging reveals structural and functional heterogeneity in different bone marrow compartments: functional implications on hematopoietic stem cells,” Blood 122(10), 1730–1740 (2013).
[Crossref]

Fox, L. M.

A. de Calignon, L. M. Fox, R. Pitstick, G. A. Carlson, B. J. Bacskai, T. L. Spires-Jones, and B. T. Hyman, “Caspase activation precedes and leads to tangles,” Nature 464(7292), 1201–1204 (2010).
[Crossref]

Fraser, G.

A. Velasco, G. Fraser, P. Delobel, B. Ghetti, I. Lavenir, and M. Goedert, “Detection of filamentous tau inclusions by the fluorescent Congo red derivative FSB [(trans,trans)-1-fluoro-2,5-bis(3-hydroxycarbonyl-4-hydroxy)styrylbenzene],” FEBS Lett. 582(6), 901–906 (2008).
[Crossref]

P. Delobel, I. Lavenir, G. Fraser, E. Ingram, M. Holzer, B. Ghetti, M. G. Spillantini, R. A. Crowther, and M. Goedert, “Analysis of tau phosphorylation and truncation in a mouse model of human tauopathy,” Am. J. Pathology 172(1), 123–131 (2008).
[Crossref]

Frenette, P. S.

I. B. Mazo, J.-C. Gutierrez-Ramos, P. S. Frenette, R. O. Hynes, D. D. Wagner, and U. H. von Andrian, “Hematopoietic Progenitor Cell Rolling in Bone Marrow Microvessels: Parallel Contributions by Endothelial Selectins and Vascular Cell Adhesion Molecule 1,” J. Exp. Med. 188(3), 465–474 (1998).
[Crossref]

Frey, P.

M. Hintersteiner, A. Enz, P. Frey, A. L. Jaton, W. Kinzy, R. Kneuer, U. Neumann, M. Rudin, M. Staufenbiel, M. Stoeckli, K. H. Wiederhold, and H. U. Gremlich, “In vivo detection of amyloid-beta deposits by near-infrared imaging using an oxazine-derivative probe,” Nat. Biotechnol. 23(5), 577–583 (2005).
[Crossref]

Friedman, B. A.

B. Dejanovic, M. A. Huntley, A. De Maziere, W. J. Meilandt, T. Wu, K. Srinivasan, Z. Jiang, V. Gandham, B. A. Friedman, H. Ngu, O. Foreman, R. A. D. Carano, B. Chih, J. Klumperman, C. Bakalarski, J. E. Hanson, and M. Sheng, “Changes in the Synaptic Proteome in Tauopathy and Rescue of Tau-Induced Synapse Loss by C1q Antibodies,” Neuron 100(6), 1322–1336.e7 (2018).
[Crossref]

Fritschi, S.

B. Wegenast-Braun, A. Skodras, G. Bayraktar, J. Mahler, S. Fritschi, T. Klingstedt, J. Mason, P. Hammarström, K. Nilsson, C. Liebig, and M. Jucker, “Spectral Discrimination of Cerebral Amyloid Lesions after Peripheral Application of Luminescent Conjugated Oligothiophenes,” Am. J. Pathology 181(6), 1953–1960 (2012).
[Crossref]

Füger, P.

P. Füger, J. K. Hefendehl, K. Veeraraghavalu, A.-C. Wendeln, C. Schlosser, U. Obermüller, B. M. Wegenast-Braun, J. J. Neher, P. Martus, S. Kohsaka, M. Thunemann, R. Feil, S. S. Sisodia, A. Skodras, and M. Jucker, “Microglia turnover with aging and in an Alzheimer's model via long-term in vivo single-cell imaging,” Nat. Neurosci. 20(10), 1371–1376 (2017).
[Crossref]

Furumoto, S.

M. Maruyama, H. Shimada, T. Suhara, H. Shinotoh, B. Ji, J. Maeda, M. R. Zhang, J. Q. Trojanowski, V. M. Lee, M. Ono, K. Masamoto, H. Takano, N. Sahara, N. Iwata, N. Okamura, S. Furumoto, Y. Kudo, Q. Chang, T. C. Saido, A. Takashima, J. Lewis, M. K. Jang, I. Aoki, H. Ito, and M. Higuchi, “Imaging of tau pathology in a tauopathy mouse model and in Alzheimer patients compared to normal controls,” Neuron 79(6), 1094–1108 (2013).
[Crossref]

Gabellieri, E.

H. Kroth, F. Oden, J. Molette, H. Schieferstein, F. Capotosti, A. Mueller, M. Berndt, H. Schmitt-Willich, V. Darmency, E. Gabellieri, C. Boudou, T. Juergens, Y. Varisco, E. Vokali, D. T. Hickman, G. Tamagnan, A. Pfeifer, L. Dinkelborg, A. Muhs, and A. Stephens, “Discovery and preclinical characterization of [(18)F]PI-2620, a next-generation tau PET tracer for the assessment of tau pathology in Alzheimer's disease and other tauopathies,” Eur. J. Nucl. Med. Mol. Imaging 46(10), 2178–2189 (2019).
[Crossref]

Gandham, V.

B. Dejanovic, M. A. Huntley, A. De Maziere, W. J. Meilandt, T. Wu, K. Srinivasan, Z. Jiang, V. Gandham, B. A. Friedman, H. Ngu, O. Foreman, R. A. D. Carano, B. Chih, J. Klumperman, C. Bakalarski, J. E. Hanson, and M. Sheng, “Changes in the Synaptic Proteome in Tauopathy and Rescue of Tau-Induced Synapse Loss by C1q Antibodies,” Neuron 100(6), 1322–1336.e7 (2018).
[Crossref]

Gandy, S.

A. Aslund, C. J. Sigurdson, T. Klingstedt, S. Grathwohl, T. Bolmont, D. L. Dickstein, E. Glimsdal, S. Prokop, M. Lindgren, P. Konradsson, D. M. Holtzman, P. R. Hof, F. L. Heppner, S. Gandy, M. Jucker, A. Aguzzi, P. Hammarström, and K. P. Nilsson, “Novel pentameric thiophene derivatives for in vitro and in vivo optical imaging of a plethora of protein aggregates in cerebral amyloidoses,” ACS Chem. Biol. 4(8), 673–684 (2009).
[Crossref]

Gantert, L.

E. D. Hostetler, A. M. Walji, Z. Zeng, P. Miller, I. Bennacef, C. Salinas, B. Connolly, L. Gantert, H. Haley, M. Holahan, M. Purcell, K. Riffel, T. G. Lohith, P. Coleman, A. Soriano, A. Ogawa, S. Xu, X. Zhang, E. Joshi, J. Della Rocca, D. Hesk, D. J. Schenk, and J. L. Evelhoch, ““Preclinical Characterization of 18F-MK-6240, a Promising PET Tracer for In Vivo Quantification of Human Neurofibrillary Tangles,” Journal of nuclear medicine : official publication,” J. Nuclear Medicine 57(10), 1599–1606 (2016).
[Crossref]

Gao, X.

T. K. Patel, L. Habimana-Griffin, X. Gao, B. Xu, S. Achilefu, K. Alitalo, C. A. McKee, P. W. Sheehan, E. S. Musiek, C. Xiong, D. Coble, and D. M. Holtzman, “Dural lymphatics regulate clearance of extracellular tau from the CNS,” Mol. Neurodegener. 14(1), 11 (2019).
[Crossref]

Garringer, H. J.

A. W. P. Fitzpatrick, B. Falcon, S. He, A. G. Murzin, G. Murshudov, H. J. Garringer, R. A. Crowther, B. Ghetti, M. Goedert, and S. H. W. Scheres, “Cryo-EM structures of tau filaments from Alzheimer's disease,” Nature 547(7662), 185–190 (2017).
[Crossref]

Gaus, S. E.

E. J. Kim, J. L. Hwang, S. E. Gaus, A. L. Nana, J. Deng, J. A. Brown, S. Spina, M. J. Lee, E. M. Ramos, L. T. Grinberg, J. H. Kramer, A. L. Boxer, M. L. Gorno-Tempini, H. J. Rosen, B. L. Miller, and W. W. Seeley, “Evidence of corticofugal tau spreading in patients with frontotemporal dementia,” Acta Neuropathol. 139(1), 27–43 (2020).
[Crossref]

Gerez, J. A.

B. M. Burmann, J. A. Gerez, I. Matecko-Burmann, S. Campioni, P. Kumari, D. Ghosh, A. Mazur, E. E. Aspholm, D. Sulskis, M. Wawrzyniuk, T. Bock, A. Schmidt, S. G. D. Rudiger, R. Riek, and S. Hiller, “Regulation of alpha-synuclein by chaperones in mammalian cells,” Nature 577(7788), 127–132 (2020).
[Crossref]

J. A. Gerez, N. C. Prymaczok, E. Rockenstein, U. S. Herrmann, P. Schwarz, A. Adame, R. I. Enchev, T. Courtheoux, P. J. Boersema, R. Riek, M. Peter, A. Aguzzi, E. Masliah, and P. Picotti, “A cullin-RING ubiquitin ligase targets exogenous alpha-synuclein and inhibits Lewy body-like pathology,” Sci. Transl. Med. 11(495), eaau6722 (2019).
[Crossref]

Ghetti, B.

A. W. P. Fitzpatrick, B. Falcon, S. He, A. G. Murzin, G. Murshudov, H. J. Garringer, R. A. Crowther, B. Ghetti, M. Goedert, and S. H. W. Scheres, “Cryo-EM structures of tau filaments from Alzheimer's disease,” Nature 547(7662), 185–190 (2017).
[Crossref]

A. Velasco, G. Fraser, P. Delobel, B. Ghetti, I. Lavenir, and M. Goedert, “Detection of filamentous tau inclusions by the fluorescent Congo red derivative FSB [(trans,trans)-1-fluoro-2,5-bis(3-hydroxycarbonyl-4-hydroxy)styrylbenzene],” FEBS Lett. 582(6), 901–906 (2008).
[Crossref]

P. Delobel, I. Lavenir, G. Fraser, E. Ingram, M. Holzer, B. Ghetti, M. G. Spillantini, R. A. Crowther, and M. Goedert, “Analysis of tau phosphorylation and truncation in a mouse model of human tauopathy,” Am. J. Pathology 172(1), 123–131 (2008).
[Crossref]

Ghosh, D.

B. M. Burmann, J. A. Gerez, I. Matecko-Burmann, S. Campioni, P. Kumari, D. Ghosh, A. Mazur, E. E. Aspholm, D. Sulskis, M. Wawrzyniuk, T. Bock, A. Schmidt, S. G. D. Rudiger, R. Riek, and S. Hiller, “Regulation of alpha-synuclein by chaperones in mammalian cells,” Nature 577(7788), 127–132 (2020).
[Crossref]

Gibbons, G. S.

Z. He, J. D. McBride, H. Xu, L. Changolkar, S. J. Kim, B. Zhang, S. Narasimhan, G. S. Gibbons, J. L. Guo, M. Kozak, G. D. Schellenberg, J. Q. Trojanowski, and V. M. Lee, “Transmission of tauopathy strains is independent of their isoform composition,” Nat. Commun. 11(1), 7 (2020).
[Crossref]

Gill, H. S.

S. Sanabria Bohorquez, J. Marik, A. Ogasawara, J. N. Tinianow, H. S. Gill, O. Barret, G. Tamagnan, D. Alagille, G. Ayalon, P. Manser, T. Bengtsson, M. Ward, S. P. Williams, G. A. Kerchner, J. P. Seibyl, K. Marek, and R. M. Weimer, “[(18)F]GTP1 (Genentech Tau Probe 1), a radioligand for detecting neurofibrillary tangle tau pathology in Alzheimer's disease,” Eur. J. Nucl. Med. Mol. Imaging 46(10), 2077–2089 (2019).
[Crossref]

Glimsdal, E.

A. Aslund, C. J. Sigurdson, T. Klingstedt, S. Grathwohl, T. Bolmont, D. L. Dickstein, E. Glimsdal, S. Prokop, M. Lindgren, P. Konradsson, D. M. Holtzman, P. R. Hof, F. L. Heppner, S. Gandy, M. Jucker, A. Aguzzi, P. Hammarström, and K. P. Nilsson, “Novel pentameric thiophene derivatives for in vitro and in vivo optical imaging of a plethora of protein aggregates in cerebral amyloidoses,” ACS Chem. Biol. 4(8), 673–684 (2009).
[Crossref]

Goedert, M.

A. W. P. Fitzpatrick, B. Falcon, S. He, A. G. Murzin, G. Murshudov, H. J. Garringer, R. A. Crowther, B. Ghetti, M. Goedert, and S. H. W. Scheres, “Cryo-EM structures of tau filaments from Alzheimer's disease,” Nature 547(7662), 185–190 (2017).
[Crossref]

M. G. Spillantini and M. Goedert, “Tau pathology and neurodegeneration,” Lancet Neurol. 12(6), 609–622 (2013).
[Crossref]

A. Velasco, G. Fraser, P. Delobel, B. Ghetti, I. Lavenir, and M. Goedert, “Detection of filamentous tau inclusions by the fluorescent Congo red derivative FSB [(trans,trans)-1-fluoro-2,5-bis(3-hydroxycarbonyl-4-hydroxy)styrylbenzene],” FEBS Lett. 582(6), 901–906 (2008).
[Crossref]

P. Delobel, I. Lavenir, G. Fraser, E. Ingram, M. Holzer, B. Ghetti, M. G. Spillantini, R. A. Crowther, and M. Goedert, “Analysis of tau phosphorylation and truncation in a mouse model of human tauopathy,” Am. J. Pathology 172(1), 123–131 (2008).
[Crossref]

V. M. Lee, M. Goedert, and J. Q. Trojanowski, “Neurodegenerative tauopathies,” Annu. Rev. Neurosci. 24(1), 1121–1159 (2001).
[Crossref]

Goltstein, P. M.

P. Marinkovic, S. Blumenstock, P. M. Goltstein, V. Korzhova, F. Peters, A. Knebl, and J. Herms, “In vivo imaging reveals reduced activity of neuronal circuits in a mouse tauopathy model,” Brain 142(4), 1051–1062 (2019).
[Crossref]

Gomez-Isla, T.

K. A. Johnson, A. Schultz, R. A. Betensky, J. A. Becker, J. Sepulcre, D. Rentz, E. Mormino, J. Chhatwal, R. Amariglio, K. Papp, G. Marshall, M. Albers, S. Mauro, L. Pepin, J. Alverio, K. Judge, M. Philiossaint, T. Shoup, D. Yokell, B. Dickerson, T. Gomez-Isla, B. Hyman, N. Vasdev, and R. Sperling, “Tau positron emission tomographic imaging in aging and early Alzheimer disease,” Ann Neurol. 79(1), 110–119 (2016).
[Crossref]

Gorno-Tempini, M. L.

E. J. Kim, J. L. Hwang, S. E. Gaus, A. L. Nana, J. Deng, J. A. Brown, S. Spina, M. J. Lee, E. M. Ramos, L. T. Grinberg, J. H. Kramer, A. L. Boxer, M. L. Gorno-Tempini, H. J. Rosen, B. L. Miller, and W. W. Seeley, “Evidence of corticofugal tau spreading in patients with frontotemporal dementia,” Acta Neuropathol. 139(1), 27–43 (2020).
[Crossref]

Gottschalk, S.

Z. Chen, B. Mc Larney, J. Rebling, X. L. Deán-Ben, Q. Zhou, S. Gottschalk, and D. Razansky, “High-Speed Large-Field Multifocal Illumination Fluorescence Microscopy,” Laser Photonics Rev. 14, 1900070 (2020).
[Crossref]

S. Gottschalk, O. Degtyaruk, B. Mc Larney, J. Rebling, M. A. Hutter, X. L. Deán-Ben, S. Shoham, and D. Razansky, “Rapid volumetric optoacoustic imaging of neural dynamics across the mouse brain,” Nat. Biomed. Eng. 3(5), 392–401 (2019).
[Crossref]

Gotz, J.

J. Gotz, F. Chen, R. Barmettler, and R. M. Nitsch, “Tau filament formation in transgenic mice expressing P301L tau,” J. Biol. Chem. 276(1), 529–534 (2001).
[Crossref]

J. Gotz, F. Chen, J. van Dorpe, and R. M. Nitsch, “Formation of neurofibrillary tangles in P301 l tau transgenic mice induced by Abeta 42 fibrils,” Science 293(5534), 1491–1495 (2001).
[Crossref]

Grathwohl, S.

A. Aslund, C. J. Sigurdson, T. Klingstedt, S. Grathwohl, T. Bolmont, D. L. Dickstein, E. Glimsdal, S. Prokop, M. Lindgren, P. Konradsson, D. M. Holtzman, P. R. Hof, F. L. Heppner, S. Gandy, M. Jucker, A. Aguzzi, P. Hammarström, and K. P. Nilsson, “Novel pentameric thiophene derivatives for in vitro and in vivo optical imaging of a plethora of protein aggregates in cerebral amyloidoses,” ACS Chem. Biol. 4(8), 673–684 (2009).
[Crossref]

Gregor, I.

I. Gregor and J. Enderlein, “Image scanning microscopy,” Curr. Opin. Chem. Biol. 51, 74–83 (2019).
[Crossref]

Gremlich, H. U.

M. Hintersteiner, A. Enz, P. Frey, A. L. Jaton, W. Kinzy, R. Kneuer, U. Neumann, M. Rudin, M. Staufenbiel, M. Stoeckli, K. H. Wiederhold, and H. U. Gremlich, “In vivo detection of amyloid-beta deposits by near-infrared imaging using an oxazine-derivative probe,” Nat. Biotechnol. 23(5), 577–583 (2005).
[Crossref]

Grinberg, L. T.

E. J. Kim, J. L. Hwang, S. E. Gaus, A. L. Nana, J. Deng, J. A. Brown, S. Spina, M. J. Lee, E. M. Ramos, L. T. Grinberg, J. H. Kramer, A. L. Boxer, M. L. Gorno-Tempini, H. J. Rosen, B. L. Miller, and W. W. Seeley, “Evidence of corticofugal tau spreading in patients with frontotemporal dementia,” Acta Neuropathol. 139(1), 27–43 (2020).
[Crossref]

Gu, J.

Q. Wu, Y. Lin, J. Gu, and E. M. Sigurdsson, “Dynamic assessment of tau immunotherapies in the brains of live animals by two-photon imaging,” EBioMedicine 35, 270–278 (2018).
[Crossref]

Guimaraes, A.

K. SantaCruz, J. Lewis, T. Spires, J. Paulson, L. Kotilinek, M. Ingelsson, A. Guimaraes, M. DeTure, M. Ramsden, E. McGowan, C. Forster, M. Yue, J. Orne, C. Janus, A. Mariash, M. Kuskowski, B. Hyman, M. Hutton, and K. H. Ashe, “Tau Suppression in a Neurodegenerative Mouse Model Improves Memory Function,” Science 309(5733), 476–481 (2005).
[Crossref]

Guo, J. L.

Z. He, J. D. McBride, H. Xu, L. Changolkar, S. J. Kim, B. Zhang, S. Narasimhan, G. S. Gibbons, J. L. Guo, M. Kozak, G. D. Schellenberg, J. Q. Trojanowski, and V. M. Lee, “Transmission of tauopathy strains is independent of their isoform composition,” Nat. Commun. 11(1), 7 (2020).
[Crossref]

Gutierrez-Ramos, J.-C.

I. B. Mazo, J.-C. Gutierrez-Ramos, P. S. Frenette, R. O. Hynes, D. D. Wagner, and U. H. von Andrian, “Hematopoietic Progenitor Cell Rolling in Bone Marrow Microvessels: Parallel Contributions by Endothelial Selectins and Vascular Cell Adhesion Molecule 1,” J. Exp. Med. 188(3), 465–474 (1998).
[Crossref]

Gwinn-Hardy, K.

J. Lewis, E. McGowan, J. Rockwood, H. Melrose, P. Nacharaju, M. Van Slegtenhorst, K. Gwinn-Hardy, M. Paul Murphy, M. Baker, X. Yu, K. Duff, J. Hardy, A. Corral, W. L. Lin, S. H. Yen, D. W. Dickson, P. Davies, and M. Hutton, “Neurofibrillary tangles, amyotrophy and progressive motor disturbance in mice expressing mutant (P301L) tau protein,” Nat. Genet. 25(4), 402–405 (2000).
[Crossref]

Habimana-Griffin, L.

T. K. Patel, L. Habimana-Griffin, X. Gao, B. Xu, S. Achilefu, K. Alitalo, C. A. McKee, P. W. Sheehan, E. S. Musiek, C. Xiong, D. Coble, and D. M. Holtzman, “Dural lymphatics regulate clearance of extracellular tau from the CNS,” Mol. Neurodegener. 14(1), 11 (2019).
[Crossref]

Haley, H.

E. D. Hostetler, A. M. Walji, Z. Zeng, P. Miller, I. Bennacef, C. Salinas, B. Connolly, L. Gantert, H. Haley, M. Holahan, M. Purcell, K. Riffel, T. G. Lohith, P. Coleman, A. Soriano, A. Ogawa, S. Xu, X. Zhang, E. Joshi, J. Della Rocca, D. Hesk, D. J. Schenk, and J. L. Evelhoch, ““Preclinical Characterization of 18F-MK-6240, a Promising PET Tracer for In Vivo Quantification of Human Neurofibrillary Tangles,” Journal of nuclear medicine : official publication,” J. Nuclear Medicine 57(10), 1599–1606 (2016).
[Crossref]

Hammarstrom, P.

T. Klingstedt, A. Aslund, R. A. Simon, L. B. Johansson, J. J. Mason, S. Nystrom, P. Hammarstrom, and K. P. Nilsson, “Synthesis of a library of oligothiophenes and their utilization as fluorescent ligands for spectral assignment of protein aggregates,” Org. Biomol. Chem. 9(24), 8356–8370 (2011).
[Crossref]

Hammarström, P.

B. Wegenast-Braun, A. Skodras, G. Bayraktar, J. Mahler, S. Fritschi, T. Klingstedt, J. Mason, P. Hammarström, K. Nilsson, C. Liebig, and M. Jucker, “Spectral Discrimination of Cerebral Amyloid Lesions after Peripheral Application of Luminescent Conjugated Oligothiophenes,” Am. J. Pathology 181(6), 1953–1960 (2012).
[Crossref]

A. Aslund, C. J. Sigurdson, T. Klingstedt, S. Grathwohl, T. Bolmont, D. L. Dickstein, E. Glimsdal, S. Prokop, M. Lindgren, P. Konradsson, D. M. Holtzman, P. R. Hof, F. L. Heppner, S. Gandy, M. Jucker, A. Aguzzi, P. Hammarström, and K. P. Nilsson, “Novel pentameric thiophene derivatives for in vitro and in vivo optical imaging of a plethora of protein aggregates in cerebral amyloidoses,” ACS Chem. Biol. 4(8), 673–684 (2009).
[Crossref]

Hanseeuw, B. J.

B. J. Hanseeuw, R. A. Betensky, H. I. L. Jacobs, A. P. Schultz, J. Sepulcre, J. A. Becker, D. M. O. Cosio, M. Farrell, Y. T. Quiroz, E. C. Mormino, R. F. Buckley, K. V. Papp, R. A. Amariglio, I. Dewachter, A. Ivanoiu, W. Huijbers, T. Hedden, G. A. Marshall, J. P. Chhatwal, D. M. Rentz, R. A. Sperling, and K. Johnson, “Association of Amyloid and Tau With Cognition in Preclinical Alzheimer Disease: A Longitudinal Study,” JAMA Neurol. 76(8), 915–924 (2019).
[Crossref]

Hanson, J. E.

B. Dejanovic, M. A. Huntley, A. De Maziere, W. J. Meilandt, T. Wu, K. Srinivasan, Z. Jiang, V. Gandham, B. A. Friedman, H. Ngu, O. Foreman, R. A. D. Carano, B. Chih, J. Klumperman, C. Bakalarski, J. E. Hanson, and M. Sheng, “Changes in the Synaptic Proteome in Tauopathy and Rescue of Tau-Induced Synapse Loss by C1q Antibodies,” Neuron 100(6), 1322–1336.e7 (2018).
[Crossref]

Hardy, J.

J. Lewis, E. McGowan, J. Rockwood, H. Melrose, P. Nacharaju, M. Van Slegtenhorst, K. Gwinn-Hardy, M. Paul Murphy, M. Baker, X. Yu, K. Duff, J. Hardy, A. Corral, W. L. Lin, S. H. Yen, D. W. Dickson, P. Davies, and M. Hutton, “Neurofibrillary tangles, amyotrophy and progressive motor disturbance in mice expressing mutant (P301L) tau protein,” Nat. Genet. 25(4), 402–405 (2000).
[Crossref]

Hashimoto, S.

S. Hashimoto, Y. Matsuba, N. Kamano, N. Mihira, N. Sahara, J. Takano, S. I. Muramatsu, T. C. Saido, and T. Saito, “Tau binding protein CAPON induces tau aggregation and neurodegeneration,” Nat. Commun. 10(1), 2394 (2019).
[Crossref]

Hawkes, J.

K. V. Kuchibhotla, S. Wegmann, K. J. Kopeikina, J. Hawkes, N. Rudinskiy, M. L. Andermann, T. L. Spires-Jones, B. J. Bacskai, and B. T. Hyman, “Neurofibrillary tangle-bearing neurons are functionally integrated in cortical circuits in vivo,” Proc. Natl. Acad. Sci. 111(1), 510–514 (2014).
[Crossref]

He, S.

A. W. P. Fitzpatrick, B. Falcon, S. He, A. G. Murzin, G. Murshudov, H. J. Garringer, R. A. Crowther, B. Ghetti, M. Goedert, and S. H. W. Scheres, “Cryo-EM structures of tau filaments from Alzheimer's disease,” Nature 547(7662), 185–190 (2017).
[Crossref]

He, Z.

Z. He, J. D. McBride, H. Xu, L. Changolkar, S. J. Kim, B. Zhang, S. Narasimhan, G. S. Gibbons, J. L. Guo, M. Kozak, G. D. Schellenberg, J. Q. Trojanowski, and V. M. Lee, “Transmission of tauopathy strains is independent of their isoform composition,” Nat. Commun. 11(1), 7 (2020).
[Crossref]

Hedden, T.

B. J. Hanseeuw, R. A. Betensky, H. I. L. Jacobs, A. P. Schultz, J. Sepulcre, J. A. Becker, D. M. O. Cosio, M. Farrell, Y. T. Quiroz, E. C. Mormino, R. F. Buckley, K. V. Papp, R. A. Amariglio, I. Dewachter, A. Ivanoiu, W. Huijbers, T. Hedden, G. A. Marshall, J. P. Chhatwal, D. M. Rentz, R. A. Sperling, and K. Johnson, “Association of Amyloid and Tau With Cognition in Preclinical Alzheimer Disease: A Longitudinal Study,” JAMA Neurol. 76(8), 915–924 (2019).
[Crossref]

Hefendehl, J. K.

P. Füger, J. K. Hefendehl, K. Veeraraghavalu, A.-C. Wendeln, C. Schlosser, U. Obermüller, B. M. Wegenast-Braun, J. J. Neher, P. Martus, S. Kohsaka, M. Thunemann, R. Feil, S. S. Sisodia, A. Skodras, and M. Jucker, “Microglia turnover with aging and in an Alzheimer's model via long-term in vivo single-cell imaging,” Nat. Neurosci. 20(10), 1371–1376 (2017).
[Crossref]

Helmchen, F.

R. Ni, X. L. Dean-Ben, D. Kirschenbaum, M. Rudin, Z. Chen, A. Crimi, F. Voigt, P. R. Nilsson, F. Helmchen, R. M. Nitsch, A. Aguzzi, D. Razansky, and J. Klohs, “Whole brain optoacoustic tomography reveals strain-specific regional beta-amyloid densities in Alzheimer`s disease amyloidosis models,” bioRxiv, DOI: 10.1101/2020.1102.1125.964064 (2020).

Heppner, F. L.

A. Aslund, C. J. Sigurdson, T. Klingstedt, S. Grathwohl, T. Bolmont, D. L. Dickstein, E. Glimsdal, S. Prokop, M. Lindgren, P. Konradsson, D. M. Holtzman, P. R. Hof, F. L. Heppner, S. Gandy, M. Jucker, A. Aguzzi, P. Hammarström, and K. P. Nilsson, “Novel pentameric thiophene derivatives for in vitro and in vivo optical imaging of a plethora of protein aggregates in cerebral amyloidoses,” ACS Chem. Biol. 4(8), 673–684 (2009).
[Crossref]

Herms, J.

P. Marinkovic, S. Blumenstock, P. M. Goltstein, V. Korzhova, F. Peters, A. Knebl, and J. Herms, “In vivo imaging reveals reduced activity of neuronal circuits in a mouse tauopathy model,” Brain 142(4), 1051–1062 (2019).
[Crossref]

Herrmann, U. S.

J. A. Gerez, N. C. Prymaczok, E. Rockenstein, U. S. Herrmann, P. Schwarz, A. Adame, R. I. Enchev, T. Courtheoux, P. J. Boersema, R. Riek, M. Peter, A. Aguzzi, E. Masliah, and P. Picotti, “A cullin-RING ubiquitin ligase targets exogenous alpha-synuclein and inhibits Lewy body-like pathology,” Sci. Transl. Med. 11(495), eaau6722 (2019).
[Crossref]

Hesk, D.

E. D. Hostetler, A. M. Walji, Z. Zeng, P. Miller, I. Bennacef, C. Salinas, B. Connolly, L. Gantert, H. Haley, M. Holahan, M. Purcell, K. Riffel, T. G. Lohith, P. Coleman, A. Soriano, A. Ogawa, S. Xu, X. Zhang, E. Joshi, J. Della Rocca, D. Hesk, D. J. Schenk, and J. L. Evelhoch, ““Preclinical Characterization of 18F-MK-6240, a Promising PET Tracer for In Vivo Quantification of Human Neurofibrillary Tangles,” Journal of nuclear medicine : official publication,” J. Nuclear Medicine 57(10), 1599–1606 (2016).
[Crossref]

Hickman, D. T.

H. Kroth, F. Oden, J. Molette, H. Schieferstein, F. Capotosti, A. Mueller, M. Berndt, H. Schmitt-Willich, V. Darmency, E. Gabellieri, C. Boudou, T. Juergens, Y. Varisco, E. Vokali, D. T. Hickman, G. Tamagnan, A. Pfeifer, L. Dinkelborg, A. Muhs, and A. Stephens, “Discovery and preclinical characterization of [(18)F]PI-2620, a next-generation tau PET tracer for the assessment of tau pathology in Alzheimer's disease and other tauopathies,” Eur. J. Nucl. Med. Mol. Imaging 46(10), 2178–2189 (2019).
[Crossref]

Higuchi, M.

R. Ni, B. Ji, M. Ono, N. Sahara, M. R. Zhang, I. Aoki, A. Nordberg, T. Suhara, and M. Higuchi, ““Comparative in-vitro and in-vivo quantifications of pathological tau deposits and their association with neurodegeneration in tauopathy mouse models,” Journal of nuclear medicine : official publication,” J. Nucl. Med. 59(6), 960–966 (2018).
[Crossref]

A. Ishikawa, M. Tokunaga, J. Maeda, T. Minamihisamatsu, M. Shimojo, H. Takuwa, M. Ono, R. Ni, S. Hirano, S. Kuwabara, B. Ji, M. R. Zhang, I. Aoki, T. Suhara, M. Higuchi, and N. Sahara, “In Vivo Visualization of Tau Accumulation, Microglial Activation, and Brain Atrophy in a Mouse Model of Tauopathy rTg4510,” J. Alzheimer’s Dis. 61(3), 1037–1052 (2018).
[Crossref]

N. Sahara, M. Shimojo, M. Ono, H. Takuwa, M. Febo, M. Higuchi, and T. Suhara, “In Vivo Tau Imaging for a Diagnostic Platform of Tauopathy Using the rTg4510 Mouse Line,” Front Neurol. 8, 663 (2017).
[Crossref]

M. Ono, N. Sahara, K. Kumata, B. Ji, R. Ni, S. Koga, D. W. Dickson, J. Q. Trojanowski, V. M.-Y. Lee, M. Yoshida, I. Hozumi, Y. Yoshiyama, J. C. v. Swieten, A. Nordberg, T. Suhara, M.-R. Zhang, and M. Higuchi, “Distinct binding of PET ligands PBB3 and AV-1451 to tau fibril strains in neurodegenerative tauopathies,” Brain 140, aww339 (2017).
[Crossref]

M. Maruyama, H. Shimada, T. Suhara, H. Shinotoh, B. Ji, J. Maeda, M. R. Zhang, J. Q. Trojanowski, V. M. Lee, M. Ono, K. Masamoto, H. Takano, N. Sahara, N. Iwata, N. Okamura, S. Furumoto, Y. Kudo, Q. Chang, T. C. Saido, A. Takashima, J. Lewis, M. K. Jang, I. Aoki, H. Ito, and M. Higuchi, “Imaging of tau pathology in a tauopathy mouse model and in Alzheimer patients compared to normal controls,” Neuron 79(6), 1094–1108 (2013).
[Crossref]

Y. Yoshiyama, M. Higuchi, B. Zhang, S. M. Huang, N. Iwata, T. C. Saido, J. Maeda, T. Suhara, J. Q. Trojanowski, and V. M. Lee, “Synapse loss and microglial activation precede tangles in a P301S tauopathy mouse model,” Neuron 53(3), 337–351 (2007).
[Crossref]

Hiller, S.

B. M. Burmann, J. A. Gerez, I. Matecko-Burmann, S. Campioni, P. Kumari, D. Ghosh, A. Mazur, E. E. Aspholm, D. Sulskis, M. Wawrzyniuk, T. Bock, A. Schmidt, S. G. D. Rudiger, R. Riek, and S. Hiller, “Regulation of alpha-synuclein by chaperones in mammalian cells,” Nature 577(7788), 127–132 (2020).
[Crossref]

Hintersteiner, M.

M. Hintersteiner, A. Enz, P. Frey, A. L. Jaton, W. Kinzy, R. Kneuer, U. Neumann, M. Rudin, M. Staufenbiel, M. Stoeckli, K. H. Wiederhold, and H. U. Gremlich, “In vivo detection of amyloid-beta deposits by near-infrared imaging using an oxazine-derivative probe,” Nat. Biotechnol. 23(5), 577–583 (2005).
[Crossref]

Hirano, S.

A. Ishikawa, M. Tokunaga, J. Maeda, T. Minamihisamatsu, M. Shimojo, H. Takuwa, M. Ono, R. Ni, S. Hirano, S. Kuwabara, B. Ji, M. R. Zhang, I. Aoki, T. Suhara, M. Higuchi, and N. Sahara, “In Vivo Visualization of Tau Accumulation, Microglial Activation, and Brain Atrophy in a Mouse Model of Tauopathy rTg4510,” J. Alzheimer’s Dis. 61(3), 1037–1052 (2018).
[Crossref]

Hof, P. R.

A. Aslund, C. J. Sigurdson, T. Klingstedt, S. Grathwohl, T. Bolmont, D. L. Dickstein, E. Glimsdal, S. Prokop, M. Lindgren, P. Konradsson, D. M. Holtzman, P. R. Hof, F. L. Heppner, S. Gandy, M. Jucker, A. Aguzzi, P. Hammarström, and K. P. Nilsson, “Novel pentameric thiophene derivatives for in vitro and in vivo optical imaging of a plethora of protein aggregates in cerebral amyloidoses,” ACS Chem. Biol. 4(8), 673–684 (2009).
[Crossref]

Holahan, M.

E. D. Hostetler, A. M. Walji, Z. Zeng, P. Miller, I. Bennacef, C. Salinas, B. Connolly, L. Gantert, H. Haley, M. Holahan, M. Purcell, K. Riffel, T. G. Lohith, P. Coleman, A. Soriano, A. Ogawa, S. Xu, X. Zhang, E. Joshi, J. Della Rocca, D. Hesk, D. J. Schenk, and J. L. Evelhoch, ““Preclinical Characterization of 18F-MK-6240, a Promising PET Tracer for In Vivo Quantification of Human Neurofibrillary Tangles,” Journal of nuclear medicine : official publication,” J. Nuclear Medicine 57(10), 1599–1606 (2016).
[Crossref]

Holtzman, D. M.

T. K. Patel, L. Habimana-Griffin, X. Gao, B. Xu, S. Achilefu, K. Alitalo, C. A. McKee, P. W. Sheehan, E. S. Musiek, C. Xiong, D. Coble, and D. M. Holtzman, “Dural lymphatics regulate clearance of extracellular tau from the CNS,” Mol. Neurodegener. 14(1), 11 (2019).
[Crossref]

A. Aslund, C. J. Sigurdson, T. Klingstedt, S. Grathwohl, T. Bolmont, D. L. Dickstein, E. Glimsdal, S. Prokop, M. Lindgren, P. Konradsson, D. M. Holtzman, P. R. Hof, F. L. Heppner, S. Gandy, M. Jucker, A. Aguzzi, P. Hammarström, and K. P. Nilsson, “Novel pentameric thiophene derivatives for in vitro and in vivo optical imaging of a plethora of protein aggregates in cerebral amyloidoses,” ACS Chem. Biol. 4(8), 673–684 (2009).
[Crossref]

Holzer, M.

P. Delobel, I. Lavenir, G. Fraser, E. Ingram, M. Holzer, B. Ghetti, M. G. Spillantini, R. A. Crowther, and M. Goedert, “Analysis of tau phosphorylation and truncation in a mouse model of human tauopathy,” Am. J. Pathology 172(1), 123–131 (2008).
[Crossref]

Hostetler, E. D.

E. D. Hostetler, A. M. Walji, Z. Zeng, P. Miller, I. Bennacef, C. Salinas, B. Connolly, L. Gantert, H. Haley, M. Holahan, M. Purcell, K. Riffel, T. G. Lohith, P. Coleman, A. Soriano, A. Ogawa, S. Xu, X. Zhang, E. Joshi, J. Della Rocca, D. Hesk, D. J. Schenk, and J. L. Evelhoch, ““Preclinical Characterization of 18F-MK-6240, a Promising PET Tracer for In Vivo Quantification of Human Neurofibrillary Tangles,” Journal of nuclear medicine : official publication,” J. Nuclear Medicine 57(10), 1599–1606 (2016).
[Crossref]

Hou, S. S.

M. Calvo-Rodriguez, S. S. Hou, A. C. Snyder, S. Dujardin, H. Shirani, K. P. R. Nilsson, and B. J. Bacskai, “In vivo detection of tau fibrils and amyloid beta aggregates with luminescent conjugated oligothiophenes and multiphoton microscopy,” Acta Neuropathol. Commun. 7(1), 171 (2019).
[Crossref]

Hozumi, I.

M. Ono, N. Sahara, K. Kumata, B. Ji, R. Ni, S. Koga, D. W. Dickson, J. Q. Trojanowski, V. M.-Y. Lee, M. Yoshida, I. Hozumi, Y. Yoshiyama, J. C. v. Swieten, A. Nordberg, T. Suhara, M.-R. Zhang, and M. Higuchi, “Distinct binding of PET ligands PBB3 and AV-1451 to tau fibril strains in neurodegenerative tauopathies,” Brain 140, aww339 (2017).
[Crossref]

Huang, S. M.

Y. Yoshiyama, M. Higuchi, B. Zhang, S. M. Huang, N. Iwata, T. C. Saido, J. Maeda, T. Suhara, J. Q. Trojanowski, and V. M. Lee, “Synapse loss and microglial activation precede tangles in a P301S tauopathy mouse model,” Neuron 53(3), 337–351 (2007).
[Crossref]

Huijbers, W.

B. J. Hanseeuw, R. A. Betensky, H. I. L. Jacobs, A. P. Schultz, J. Sepulcre, J. A. Becker, D. M. O. Cosio, M. Farrell, Y. T. Quiroz, E. C. Mormino, R. F. Buckley, K. V. Papp, R. A. Amariglio, I. Dewachter, A. Ivanoiu, W. Huijbers, T. Hedden, G. A. Marshall, J. P. Chhatwal, D. M. Rentz, R. A. Sperling, and K. Johnson, “Association of Amyloid and Tau With Cognition in Preclinical Alzheimer Disease: A Longitudinal Study,” JAMA Neurol. 76(8), 915–924 (2019).
[Crossref]

Huntley, M. A.

B. Dejanovic, M. A. Huntley, A. De Maziere, W. J. Meilandt, T. Wu, K. Srinivasan, Z. Jiang, V. Gandham, B. A. Friedman, H. Ngu, O. Foreman, R. A. D. Carano, B. Chih, J. Klumperman, C. Bakalarski, J. E. Hanson, and M. Sheng, “Changes in the Synaptic Proteome in Tauopathy and Rescue of Tau-Induced Synapse Loss by C1q Antibodies,” Neuron 100(6), 1322–1336.e7 (2018).
[Crossref]

Hutter, M. A.

S. Gottschalk, O. Degtyaruk, B. Mc Larney, J. Rebling, M. A. Hutter, X. L. Deán-Ben, S. Shoham, and D. Razansky, “Rapid volumetric optoacoustic imaging of neural dynamics across the mouse brain,” Nat. Biomed. Eng. 3(5), 392–401 (2019).
[Crossref]

Hutton, M.

K. SantaCruz, J. Lewis, T. Spires, J. Paulson, L. Kotilinek, M. Ingelsson, A. Guimaraes, M. DeTure, M. Ramsden, E. McGowan, C. Forster, M. Yue, J. Orne, C. Janus, A. Mariash, M. Kuskowski, B. Hyman, M. Hutton, and K. H. Ashe, “Tau Suppression in a Neurodegenerative Mouse Model Improves Memory Function,” Science 309(5733), 476–481 (2005).
[Crossref]

J. Lewis, E. McGowan, J. Rockwood, H. Melrose, P. Nacharaju, M. Van Slegtenhorst, K. Gwinn-Hardy, M. Paul Murphy, M. Baker, X. Yu, K. Duff, J. Hardy, A. Corral, W. L. Lin, S. H. Yen, D. W. Dickson, P. Davies, and M. Hutton, “Neurofibrillary tangles, amyotrophy and progressive motor disturbance in mice expressing mutant (P301L) tau protein,” Nat. Genet. 25(4), 402–405 (2000).
[Crossref]

Hwang, J. L.

E. J. Kim, J. L. Hwang, S. E. Gaus, A. L. Nana, J. Deng, J. A. Brown, S. Spina, M. J. Lee, E. M. Ramos, L. T. Grinberg, J. H. Kramer, A. L. Boxer, M. L. Gorno-Tempini, H. J. Rosen, B. L. Miller, and W. W. Seeley, “Evidence of corticofugal tau spreading in patients with frontotemporal dementia,” Acta Neuropathol. 139(1), 27–43 (2020).
[Crossref]

Hyman, B.

K. A. Johnson, A. Schultz, R. A. Betensky, J. A. Becker, J. Sepulcre, D. Rentz, E. Mormino, J. Chhatwal, R. Amariglio, K. Papp, G. Marshall, M. Albers, S. Mauro, L. Pepin, J. Alverio, K. Judge, M. Philiossaint, T. Shoup, D. Yokell, B. Dickerson, T. Gomez-Isla, B. Hyman, N. Vasdev, and R. Sperling, “Tau positron emission tomographic imaging in aging and early Alzheimer disease,” Ann Neurol. 79(1), 110–119 (2016).
[Crossref]

K. SantaCruz, J. Lewis, T. Spires, J. Paulson, L. Kotilinek, M. Ingelsson, A. Guimaraes, M. DeTure, M. Ramsden, E. McGowan, C. Forster, M. Yue, J. Orne, C. Janus, A. Mariash, M. Kuskowski, B. Hyman, M. Hutton, and K. H. Ashe, “Tau Suppression in a Neurodegenerative Mouse Model Improves Memory Function,” Science 309(5733), 476–481 (2005).
[Crossref]

Hyman, B. T.

K. V. Kuchibhotla, S. Wegmann, K. J. Kopeikina, J. Hawkes, N. Rudinskiy, M. L. Andermann, T. L. Spires-Jones, B. J. Bacskai, and B. T. Hyman, “Neurofibrillary tangle-bearing neurons are functionally integrated in cortical circuits in vivo,” Proc. Natl. Acad. Sci. 111(1), 510–514 (2014).
[Crossref]

A. de Calignon, L. M. Fox, R. Pitstick, G. A. Carlson, B. J. Bacskai, T. L. Spires-Jones, and B. T. Hyman, “Caspase activation precedes and leads to tangles,” Nature 464(7292), 1201–1204 (2010).
[Crossref]

Hynes, R. O.

I. B. Mazo, J.-C. Gutierrez-Ramos, P. S. Frenette, R. O. Hynes, D. D. Wagner, and U. H. von Andrian, “Hematopoietic Progenitor Cell Rolling in Bone Marrow Microvessels: Parallel Contributions by Endothelial Selectins and Vascular Cell Adhesion Molecule 1,” J. Exp. Med. 188(3), 465–474 (1998).
[Crossref]

Iaccarino, L.

R. La Joie, A. V. Visani, S. L. Baker, J. A. Brown, V. Bourakova, J. Cha, K. Chaudhary, L. Edwards, L. Iaccarino, M. Janabi, O. H. Lesman-Segev, Z. A. Miller, D. C. Perry, J. P. O’Neil, J. Pham, J. C. Rojas, H. J. Rosen, W. W. Seeley, R. M. Tsai, B. L. Miller, W. J. Jagust, and G. D. Rabinovici, “Prospective longitudinal atrophy in Alzheimer’s disease correlates with the intensity and topography of baseline tau-PET,” Sci. Transl. Med. 12(524), eaau5732 (2020).
[Crossref]

Ingelsson, M.

K. SantaCruz, J. Lewis, T. Spires, J. Paulson, L. Kotilinek, M. Ingelsson, A. Guimaraes, M. DeTure, M. Ramsden, E. McGowan, C. Forster, M. Yue, J. Orne, C. Janus, A. Mariash, M. Kuskowski, B. Hyman, M. Hutton, and K. H. Ashe, “Tau Suppression in a Neurodegenerative Mouse Model Improves Memory Function,” Science 309(5733), 476–481 (2005).
[Crossref]

Ingram, E.

P. Delobel, I. Lavenir, G. Fraser, E. Ingram, M. Holzer, B. Ghetti, M. G. Spillantini, R. A. Crowther, and M. Goedert, “Analysis of tau phosphorylation and truncation in a mouse model of human tauopathy,” Am. J. Pathology 172(1), 123–131 (2008).
[Crossref]

Ishikawa, A.

A. Ishikawa, M. Tokunaga, J. Maeda, T. Minamihisamatsu, M. Shimojo, H. Takuwa, M. Ono, R. Ni, S. Hirano, S. Kuwabara, B. Ji, M. R. Zhang, I. Aoki, T. Suhara, M. Higuchi, and N. Sahara, “In Vivo Visualization of Tau Accumulation, Microglial Activation, and Brain Atrophy in a Mouse Model of Tauopathy rTg4510,” J. Alzheimer’s Dis. 61(3), 1037–1052 (2018).
[Crossref]

Ito, H.

M. Maruyama, H. Shimada, T. Suhara, H. Shinotoh, B. Ji, J. Maeda, M. R. Zhang, J. Q. Trojanowski, V. M. Lee, M. Ono, K. Masamoto, H. Takano, N. Sahara, N. Iwata, N. Okamura, S. Furumoto, Y. Kudo, Q. Chang, T. C. Saido, A. Takashima, J. Lewis, M. K. Jang, I. Aoki, H. Ito, and M. Higuchi, “Imaging of tau pathology in a tauopathy mouse model and in Alzheimer patients compared to normal controls,” Neuron 79(6), 1094–1108 (2013).
[Crossref]

Ivanoiu, A.

B. J. Hanseeuw, R. A. Betensky, H. I. L. Jacobs, A. P. Schultz, J. Sepulcre, J. A. Becker, D. M. O. Cosio, M. Farrell, Y. T. Quiroz, E. C. Mormino, R. F. Buckley, K. V. Papp, R. A. Amariglio, I. Dewachter, A. Ivanoiu, W. Huijbers, T. Hedden, G. A. Marshall, J. P. Chhatwal, D. M. Rentz, R. A. Sperling, and K. Johnson, “Association of Amyloid and Tau With Cognition in Preclinical Alzheimer Disease: A Longitudinal Study,” JAMA Neurol. 76(8), 915–924 (2019).
[Crossref]

Iwata, N.

M. Maruyama, H. Shimada, T. Suhara, H. Shinotoh, B. Ji, J. Maeda, M. R. Zhang, J. Q. Trojanowski, V. M. Lee, M. Ono, K. Masamoto, H. Takano, N. Sahara, N. Iwata, N. Okamura, S. Furumoto, Y. Kudo, Q. Chang, T. C. Saido, A. Takashima, J. Lewis, M. K. Jang, I. Aoki, H. Ito, and M. Higuchi, “Imaging of tau pathology in a tauopathy mouse model and in Alzheimer patients compared to normal controls,” Neuron 79(6), 1094–1108 (2013).
[Crossref]

Y. Yoshiyama, M. Higuchi, B. Zhang, S. M. Huang, N. Iwata, T. C. Saido, J. Maeda, T. Suhara, J. Q. Trojanowski, and V. M. Lee, “Synapse loss and microglial activation precede tangles in a P301S tauopathy mouse model,” Neuron 53(3), 337–351 (2007).
[Crossref]

Jackson, G. R.

C. A. Lasagna-Reeves, D. L. Castillo-Carranza, U. Sengupta, J. Sarmiento, J. Troncoso, G. R. Jackson, and R. Kayed, “Identification of oligomers at early stages of tau aggregation in Alzheimer's disease,” FASEB J. 26(5), 1946–1959 (2012).
[Crossref]

Jacobs, H. I. L.

B. J. Hanseeuw, R. A. Betensky, H. I. L. Jacobs, A. P. Schultz, J. Sepulcre, J. A. Becker, D. M. O. Cosio, M. Farrell, Y. T. Quiroz, E. C. Mormino, R. F. Buckley, K. V. Papp, R. A. Amariglio, I. Dewachter, A. Ivanoiu, W. Huijbers, T. Hedden, G. A. Marshall, J. P. Chhatwal, D. M. Rentz, R. A. Sperling, and K. Johnson, “Association of Amyloid and Tau With Cognition in Preclinical Alzheimer Disease: A Longitudinal Study,” JAMA Neurol. 76(8), 915–924 (2019).
[Crossref]

Jagust, W. J.

R. La Joie, A. V. Visani, S. L. Baker, J. A. Brown, V. Bourakova, J. Cha, K. Chaudhary, L. Edwards, L. Iaccarino, M. Janabi, O. H. Lesman-Segev, Z. A. Miller, D. C. Perry, J. P. O’Neil, J. Pham, J. C. Rojas, H. J. Rosen, W. W. Seeley, R. M. Tsai, B. L. Miller, W. J. Jagust, and G. D. Rabinovici, “Prospective longitudinal atrophy in Alzheimer’s disease correlates with the intensity and topography of baseline tau-PET,” Sci. Transl. Med. 12(524), eaau5732 (2020).
[Crossref]

M. Scholl, S. N. Lockhart, D. R. Schonhaut, J. P. O’Neil, M. Janabi, R. Ossenkoppele, S. L. Baker, J. W. Vogel, J. Faria, H. D. Schwimmer, G. D. Rabinovici, and W. J. Jagust, “PET Imaging of Tau Deposition in the Aging Human Brain,” Neuron 89(5), 971–982 (2016).
[Crossref]

Janabi, M.

R. La Joie, A. V. Visani, S. L. Baker, J. A. Brown, V. Bourakova, J. Cha, K. Chaudhary, L. Edwards, L. Iaccarino, M. Janabi, O. H. Lesman-Segev, Z. A. Miller, D. C. Perry, J. P. O’Neil, J. Pham, J. C. Rojas, H. J. Rosen, W. W. Seeley, R. M. Tsai, B. L. Miller, W. J. Jagust, and G. D. Rabinovici, “Prospective longitudinal atrophy in Alzheimer’s disease correlates with the intensity and topography of baseline tau-PET,” Sci. Transl. Med. 12(524), eaau5732 (2020).
[Crossref]

M. Scholl, S. N. Lockhart, D. R. Schonhaut, J. P. O’Neil, M. Janabi, R. Ossenkoppele, S. L. Baker, J. W. Vogel, J. Faria, H. D. Schwimmer, G. D. Rabinovici, and W. J. Jagust, “PET Imaging of Tau Deposition in the Aging Human Brain,” Neuron 89(5), 971–982 (2016).
[Crossref]

Jang, M. K.

M. Maruyama, H. Shimada, T. Suhara, H. Shinotoh, B. Ji, J. Maeda, M. R. Zhang, J. Q. Trojanowski, V. M. Lee, M. Ono, K. Masamoto, H. Takano, N. Sahara, N. Iwata, N. Okamura, S. Furumoto, Y. Kudo, Q. Chang, T. C. Saido, A. Takashima, J. Lewis, M. K. Jang, I. Aoki, H. Ito, and M. Higuchi, “Imaging of tau pathology in a tauopathy mouse model and in Alzheimer patients compared to normal controls,” Neuron 79(6), 1094–1108 (2013).
[Crossref]

Janus, C.

K. SantaCruz, J. Lewis, T. Spires, J. Paulson, L. Kotilinek, M. Ingelsson, A. Guimaraes, M. DeTure, M. Ramsden, E. McGowan, C. Forster, M. Yue, J. Orne, C. Janus, A. Mariash, M. Kuskowski, B. Hyman, M. Hutton, and K. H. Ashe, “Tau Suppression in a Neurodegenerative Mouse Model Improves Memory Function,” Science 309(5733), 476–481 (2005).
[Crossref]

Jaton, A. L.

M. Hintersteiner, A. Enz, P. Frey, A. L. Jaton, W. Kinzy, R. Kneuer, U. Neumann, M. Rudin, M. Staufenbiel, M. Stoeckli, K. H. Wiederhold, and H. U. Gremlich, “In vivo detection of amyloid-beta deposits by near-infrared imaging using an oxazine-derivative probe,” Nat. Biotechnol. 23(5), 577–583 (2005).
[Crossref]

Ji, B.

A. Ishikawa, M. Tokunaga, J. Maeda, T. Minamihisamatsu, M. Shimojo, H. Takuwa, M. Ono, R. Ni, S. Hirano, S. Kuwabara, B. Ji, M. R. Zhang, I. Aoki, T. Suhara, M. Higuchi, and N. Sahara, “In Vivo Visualization of Tau Accumulation, Microglial Activation, and Brain Atrophy in a Mouse Model of Tauopathy rTg4510,” J. Alzheimer’s Dis. 61(3), 1037–1052 (2018).
[Crossref]

R. Ni, B. Ji, M. Ono, N. Sahara, M. R. Zhang, I. Aoki, A. Nordberg, T. Suhara, and M. Higuchi, ““Comparative in-vitro and in-vivo quantifications of pathological tau deposits and their association with neurodegeneration in tauopathy mouse models,” Journal of nuclear medicine : official publication,” J. Nucl. Med. 59(6), 960–966 (2018).
[Crossref]

M. Ono, N. Sahara, K. Kumata, B. Ji, R. Ni, S. Koga, D. W. Dickson, J. Q. Trojanowski, V. M.-Y. Lee, M. Yoshida, I. Hozumi, Y. Yoshiyama, J. C. v. Swieten, A. Nordberg, T. Suhara, M.-R. Zhang, and M. Higuchi, “Distinct binding of PET ligands PBB3 and AV-1451 to tau fibril strains in neurodegenerative tauopathies,” Brain 140, aww339 (2017).
[Crossref]

M. Maruyama, H. Shimada, T. Suhara, H. Shinotoh, B. Ji, J. Maeda, M. R. Zhang, J. Q. Trojanowski, V. M. Lee, M. Ono, K. Masamoto, H. Takano, N. Sahara, N. Iwata, N. Okamura, S. Furumoto, Y. Kudo, Q. Chang, T. C. Saido, A. Takashima, J. Lewis, M. K. Jang, I. Aoki, H. Ito, and M. Higuchi, “Imaging of tau pathology in a tauopathy mouse model and in Alzheimer patients compared to normal controls,” Neuron 79(6), 1094–1108 (2013).
[Crossref]

Jiang, Z.

B. Dejanovic, M. A. Huntley, A. De Maziere, W. J. Meilandt, T. Wu, K. Srinivasan, Z. Jiang, V. Gandham, B. A. Friedman, H. Ngu, O. Foreman, R. A. D. Carano, B. Chih, J. Klumperman, C. Bakalarski, J. E. Hanson, and M. Sheng, “Changes in the Synaptic Proteome in Tauopathy and Rescue of Tau-Induced Synapse Loss by C1q Antibodies,” Neuron 100(6), 1322–1336.e7 (2018).
[Crossref]

Johansson, L. B.

T. Klingstedt, A. Aslund, R. A. Simon, L. B. Johansson, J. J. Mason, S. Nystrom, P. Hammarstrom, and K. P. Nilsson, “Synthesis of a library of oligothiophenes and their utilization as fluorescent ligands for spectral assignment of protein aggregates,” Org. Biomol. Chem. 9(24), 8356–8370 (2011).
[Crossref]

Johnson, K.

B. J. Hanseeuw, R. A. Betensky, H. I. L. Jacobs, A. P. Schultz, J. Sepulcre, J. A. Becker, D. M. O. Cosio, M. Farrell, Y. T. Quiroz, E. C. Mormino, R. F. Buckley, K. V. Papp, R. A. Amariglio, I. Dewachter, A. Ivanoiu, W. Huijbers, T. Hedden, G. A. Marshall, J. P. Chhatwal, D. M. Rentz, R. A. Sperling, and K. Johnson, “Association of Amyloid and Tau With Cognition in Preclinical Alzheimer Disease: A Longitudinal Study,” JAMA Neurol. 76(8), 915–924 (2019).
[Crossref]

Johnson, K. A.

K. A. Johnson, A. Schultz, R. A. Betensky, J. A. Becker, J. Sepulcre, D. Rentz, E. Mormino, J. Chhatwal, R. Amariglio, K. Papp, G. Marshall, M. Albers, S. Mauro, L. Pepin, J. Alverio, K. Judge, M. Philiossaint, T. Shoup, D. Yokell, B. Dickerson, T. Gomez-Isla, B. Hyman, N. Vasdev, and R. Sperling, “Tau positron emission tomographic imaging in aging and early Alzheimer disease,” Ann Neurol. 79(1), 110–119 (2016).
[Crossref]

Joshi, E.

E. D. Hostetler, A. M. Walji, Z. Zeng, P. Miller, I. Bennacef, C. Salinas, B. Connolly, L. Gantert, H. Haley, M. Holahan, M. Purcell, K. Riffel, T. G. Lohith, P. Coleman, A. Soriano, A. Ogawa, S. Xu, X. Zhang, E. Joshi, J. Della Rocca, D. Hesk, D. J. Schenk, and J. L. Evelhoch, ““Preclinical Characterization of 18F-MK-6240, a Promising PET Tracer for In Vivo Quantification of Human Neurofibrillary Tangles,” Journal of nuclear medicine : official publication,” J. Nuclear Medicine 57(10), 1599–1606 (2016).
[Crossref]

Jucker, M.

P. Füger, J. K. Hefendehl, K. Veeraraghavalu, A.-C. Wendeln, C. Schlosser, U. Obermüller, B. M. Wegenast-Braun, J. J. Neher, P. Martus, S. Kohsaka, M. Thunemann, R. Feil, S. S. Sisodia, A. Skodras, and M. Jucker, “Microglia turnover with aging and in an Alzheimer's model via long-term in vivo single-cell imaging,” Nat. Neurosci. 20(10), 1371–1376 (2017).
[Crossref]

B. Wegenast-Braun, A. Skodras, G. Bayraktar, J. Mahler, S. Fritschi, T. Klingstedt, J. Mason, P. Hammarström, K. Nilsson, C. Liebig, and M. Jucker, “Spectral Discrimination of Cerebral Amyloid Lesions after Peripheral Application of Luminescent Conjugated Oligothiophenes,” Am. J. Pathology 181(6), 1953–1960 (2012).
[Crossref]

A. Aslund, C. J. Sigurdson, T. Klingstedt, S. Grathwohl, T. Bolmont, D. L. Dickstein, E. Glimsdal, S. Prokop, M. Lindgren, P. Konradsson, D. M. Holtzman, P. R. Hof, F. L. Heppner, S. Gandy, M. Jucker, A. Aguzzi, P. Hammarström, and K. P. Nilsson, “Novel pentameric thiophene derivatives for in vitro and in vivo optical imaging of a plethora of protein aggregates in cerebral amyloidoses,” ACS Chem. Biol. 4(8), 673–684 (2009).
[Crossref]

Judge, K.

K. A. Johnson, A. Schultz, R. A. Betensky, J. A. Becker, J. Sepulcre, D. Rentz, E. Mormino, J. Chhatwal, R. Amariglio, K. Papp, G. Marshall, M. Albers, S. Mauro, L. Pepin, J. Alverio, K. Judge, M. Philiossaint, T. Shoup, D. Yokell, B. Dickerson, T. Gomez-Isla, B. Hyman, N. Vasdev, and R. Sperling, “Tau positron emission tomographic imaging in aging and early Alzheimer disease,” Ann Neurol. 79(1), 110–119 (2016).
[Crossref]

Juergens, T.

H. Kroth, F. Oden, J. Molette, H. Schieferstein, F. Capotosti, A. Mueller, M. Berndt, H. Schmitt-Willich, V. Darmency, E. Gabellieri, C. Boudou, T. Juergens, Y. Varisco, E. Vokali, D. T. Hickman, G. Tamagnan, A. Pfeifer, L. Dinkelborg, A. Muhs, and A. Stephens, “Discovery and preclinical characterization of [(18)F]PI-2620, a next-generation tau PET tracer for the assessment of tau pathology in Alzheimer's disease and other tauopathies,” Eur. J. Nucl. Med. Mol. Imaging 46(10), 2178–2189 (2019).
[Crossref]

Kamano, N.

S. Hashimoto, Y. Matsuba, N. Kamano, N. Mihira, N. Sahara, J. Takano, S. I. Muramatsu, T. C. Saido, and T. Saito, “Tau binding protein CAPON induces tau aggregation and neurodegeneration,” Nat. Commun. 10(1), 2394 (2019).
[Crossref]

Kang, C.

P. Verwilst, H. S. Kim, S. Kim, C. Kang, and J. S. Kim, “Shedding light on tau protein aggregation: the progress in developing highly selective fluorophores,” Chem. Soc. Rev. 47(7), 2249–2265 (2018).
[Crossref]

Kaufman, S. K.

S. K. Kaufman, D. W. Sanders, T. L. Thomas, A. J. Ruchinskas, J. Vaquer-Alicea, A. M. Sharma, T. M. Miller, and M. I. Diamond, “Tau Prion Strains Dictate Patterns of Cell Pathology, Progression Rate, and Regional Vulnerability In Vivo,” Neuron 92(4), 796–812 (2016).
[Crossref]

Kayed, R.

C. A. Lasagna-Reeves, D. L. Castillo-Carranza, U. Sengupta, J. Sarmiento, J. Troncoso, G. R. Jackson, and R. Kayed, “Identification of oligomers at early stages of tau aggregation in Alzheimer's disease,” FASEB J. 26(5), 1946–1959 (2012).
[Crossref]

Keller, A.

R. Ni, Y. Zarb, G. A. Kuhn, R. Müller, Y. Yundung, R. M. Nitsch, L. Kulic, A. Keller, and J. Klohs, “Tau deposition is associated with imaging patterns of tissue calcification in the P301L mouse model of human tauopathy,” bioRxiv, 851915 (2019).

Kerchner, G. A.

S. Sanabria Bohorquez, J. Marik, A. Ogasawara, J. N. Tinianow, H. S. Gill, O. Barret, G. Tamagnan, D. Alagille, G. Ayalon, P. Manser, T. Bengtsson, M. Ward, S. P. Williams, G. A. Kerchner, J. P. Seibyl, K. Marek, and R. M. Weimer, “[(18)F]GTP1 (Genentech Tau Probe 1), a radioligand for detecting neurofibrillary tangle tau pathology in Alzheimer's disease,” Eur. J. Nucl. Med. Mol. Imaging 46(10), 2077–2089 (2019).
[Crossref]

Kim, E. J.

E. J. Kim, J. L. Hwang, S. E. Gaus, A. L. Nana, J. Deng, J. A. Brown, S. Spina, M. J. Lee, E. M. Ramos, L. T. Grinberg, J. H. Kramer, A. L. Boxer, M. L. Gorno-Tempini, H. J. Rosen, B. L. Miller, and W. W. Seeley, “Evidence of corticofugal tau spreading in patients with frontotemporal dementia,” Acta Neuropathol. 139(1), 27–43 (2020).
[Crossref]

Kim, H. S.

P. Verwilst, H. S. Kim, S. Kim, C. Kang, and J. S. Kim, “Shedding light on tau protein aggregation: the progress in developing highly selective fluorophores,” Chem. Soc. Rev. 47(7), 2249–2265 (2018).
[Crossref]

Kim, J. S.

P. Verwilst, H. S. Kim, S. Kim, C. Kang, and J. S. Kim, “Shedding light on tau protein aggregation: the progress in developing highly selective fluorophores,” Chem. Soc. Rev. 47(7), 2249–2265 (2018).
[Crossref]

Kim, S.

P. Verwilst, H. S. Kim, S. Kim, C. Kang, and J. S. Kim, “Shedding light on tau protein aggregation: the progress in developing highly selective fluorophores,” Chem. Soc. Rev. 47(7), 2249–2265 (2018).
[Crossref]

Kim, S. J.

Z. He, J. D. McBride, H. Xu, L. Changolkar, S. J. Kim, B. Zhang, S. Narasimhan, G. S. Gibbons, J. L. Guo, M. Kozak, G. D. Schellenberg, J. Q. Trojanowski, and V. M. Lee, “Transmission of tauopathy strains is independent of their isoform composition,” Nat. Commun. 11(1), 7 (2020).
[Crossref]

Kinzy, W.

M. Hintersteiner, A. Enz, P. Frey, A. L. Jaton, W. Kinzy, R. Kneuer, U. Neumann, M. Rudin, M. Staufenbiel, M. Stoeckli, K. H. Wiederhold, and H. U. Gremlich, “In vivo detection of amyloid-beta deposits by near-infrared imaging using an oxazine-derivative probe,” Nat. Biotechnol. 23(5), 577–583 (2005).
[Crossref]

Kirschenbaum, D.

R. Ni, X. L. Dean-Ben, D. Kirschenbaum, M. Rudin, Z. Chen, A. Crimi, F. Voigt, P. R. Nilsson, F. Helmchen, R. M. Nitsch, A. Aguzzi, D. Razansky, and J. Klohs, “Whole brain optoacoustic tomography reveals strain-specific regional beta-amyloid densities in Alzheimer`s disease amyloidosis models,” bioRxiv, DOI: 10.1101/2020.1102.1125.964064 (2020).

Klingstedt, T.

B. Wegenast-Braun, A. Skodras, G. Bayraktar, J. Mahler, S. Fritschi, T. Klingstedt, J. Mason, P. Hammarström, K. Nilsson, C. Liebig, and M. Jucker, “Spectral Discrimination of Cerebral Amyloid Lesions after Peripheral Application of Luminescent Conjugated Oligothiophenes,” Am. J. Pathology 181(6), 1953–1960 (2012).
[Crossref]

T. Klingstedt, A. Aslund, R. A. Simon, L. B. Johansson, J. J. Mason, S. Nystrom, P. Hammarstrom, and K. P. Nilsson, “Synthesis of a library of oligothiophenes and their utilization as fluorescent ligands for spectral assignment of protein aggregates,” Org. Biomol. Chem. 9(24), 8356–8370 (2011).
[Crossref]

A. Aslund, C. J. Sigurdson, T. Klingstedt, S. Grathwohl, T. Bolmont, D. L. Dickstein, E. Glimsdal, S. Prokop, M. Lindgren, P. Konradsson, D. M. Holtzman, P. R. Hof, F. L. Heppner, S. Gandy, M. Jucker, A. Aguzzi, P. Hammarström, and K. P. Nilsson, “Novel pentameric thiophene derivatives for in vitro and in vivo optical imaging of a plethora of protein aggregates in cerebral amyloidoses,” ACS Chem. Biol. 4(8), 673–684 (2009).
[Crossref]

Klohs, J.

R. Ni, M. Vaas, W. Ren, and J. Klohs, “Non-invasive detection of acute cerebral hypoxia and subsequent matrix-metalloproteinase activity in a mouse model of cerebral ischemia using multispectral-optoacoustic-tomography,” Neurophotonics 5(1), 015005 (2018).
[Crossref]

J. Klohs, N. Baeva, J. Steinbrink, R. Bourayou, C. Boettcher, G. Royl, D. Megow, U. Dirnagl, J. Priller, and A. Wunder, “In vivo near-infrared fluorescence imaging of matrix metalloproteinase activity after cerebral ischemia,” J. Cereb. Blood Flow Metab. 29(7), 1284–1292 (2009).
[Crossref]

J. Klohs, “An Integrated View on Vascular Dysfunction in Alzheimer’s Disease,” Neurodegenerative Diseases (2020).

R. Ni, X. L. Dean-Ben, D. Kirschenbaum, M. Rudin, Z. Chen, A. Crimi, F. Voigt, P. R. Nilsson, F. Helmchen, R. M. Nitsch, A. Aguzzi, D. Razansky, and J. Klohs, “Whole brain optoacoustic tomography reveals strain-specific regional beta-amyloid densities in Alzheimer`s disease amyloidosis models,” bioRxiv, DOI: 10.1101/2020.1102.1125.964064 (2020).

R. Ni, Y. Zarb, G. A. Kuhn, R. Müller, Y. Yundung, R. M. Nitsch, L. Kulic, A. Keller, and J. Klohs, “Tau deposition is associated with imaging patterns of tissue calcification in the P301L mouse model of human tauopathy,” bioRxiv, 851915 (2019).

R. Ni, Z. Chen, G. Shi, A. Villois, Q. Zhou, P. Arosio, R. M. Nitsch, P. R. Nilsson, J. Klohs, and D. Razansky, “Transcranial in vivo detection of Aβ at single plaque resolution with large-field multifocal illumination fluorescence microscopy,” bioRxiv, 2020.2002.2001.929844 (2020).

Klumperman, J.

B. Dejanovic, M. A. Huntley, A. De Maziere, W. J. Meilandt, T. Wu, K. Srinivasan, Z. Jiang, V. Gandham, B. A. Friedman, H. Ngu, O. Foreman, R. A. D. Carano, B. Chih, J. Klumperman, C. Bakalarski, J. E. Hanson, and M. Sheng, “Changes in the Synaptic Proteome in Tauopathy and Rescue of Tau-Induced Synapse Loss by C1q Antibodies,” Neuron 100(6), 1322–1336.e7 (2018).
[Crossref]

Knebl, A.

P. Marinkovic, S. Blumenstock, P. M. Goltstein, V. Korzhova, F. Peters, A. Knebl, and J. Herms, “In vivo imaging reveals reduced activity of neuronal circuits in a mouse tauopathy model,” Brain 142(4), 1051–1062 (2019).
[Crossref]

Kneuer, R.

M. Hintersteiner, A. Enz, P. Frey, A. L. Jaton, W. Kinzy, R. Kneuer, U. Neumann, M. Rudin, M. Staufenbiel, M. Stoeckli, K. H. Wiederhold, and H. U. Gremlich, “In vivo detection of amyloid-beta deposits by near-infrared imaging using an oxazine-derivative probe,” Nat. Biotechnol. 23(5), 577–583 (2005).
[Crossref]

Koga, S.

M. Ono, N. Sahara, K. Kumata, B. Ji, R. Ni, S. Koga, D. W. Dickson, J. Q. Trojanowski, V. M.-Y. Lee, M. Yoshida, I. Hozumi, Y. Yoshiyama, J. C. v. Swieten, A. Nordberg, T. Suhara, M.-R. Zhang, and M. Higuchi, “Distinct binding of PET ligands PBB3 and AV-1451 to tau fibril strains in neurodegenerative tauopathies,” Brain 140, aww339 (2017).
[Crossref]

Koglin, N.

A. Mueller, S. Bullich, O. Barret, J. Madonia, M. Berndt, C. Papin, A. Perrotin, N. Koglin, H. Kroth, A. Pfeifer, G. Tamagnan, J. P. Seibyl, K. Marek, S. de Santi, L. M. Dinkelborg, and A. W. Stephens, “Tau PET imaging with (18)F-PI-2620 in patients with Alzheimer's disease and healthy controls: a first-in-human study,” J. Nucl. Med. 61(6), 911–919 (2020).
[Crossref]

Kohsaka, S.

P. Füger, J. K. Hefendehl, K. Veeraraghavalu, A.-C. Wendeln, C. Schlosser, U. Obermüller, B. M. Wegenast-Braun, J. J. Neher, P. Martus, S. Kohsaka, M. Thunemann, R. Feil, S. S. Sisodia, A. Skodras, and M. Jucker, “Microglia turnover with aging and in an Alzheimer's model via long-term in vivo single-cell imaging,” Nat. Neurosci. 20(10), 1371–1376 (2017).
[Crossref]

Konradsson, P.

A. Aslund, C. J. Sigurdson, T. Klingstedt, S. Grathwohl, T. Bolmont, D. L. Dickstein, E. Glimsdal, S. Prokop, M. Lindgren, P. Konradsson, D. M. Holtzman, P. R. Hof, F. L. Heppner, S. Gandy, M. Jucker, A. Aguzzi, P. Hammarström, and K. P. Nilsson, “Novel pentameric thiophene derivatives for in vitro and in vivo optical imaging of a plethora of protein aggregates in cerebral amyloidoses,” ACS Chem. Biol. 4(8), 673–684 (2009).
[Crossref]

Kopeikina, K. J.

K. V. Kuchibhotla, S. Wegmann, K. J. Kopeikina, J. Hawkes, N. Rudinskiy, M. L. Andermann, T. L. Spires-Jones, B. J. Bacskai, and B. T. Hyman, “Neurofibrillary tangle-bearing neurons are functionally integrated in cortical circuits in vivo,” Proc. Natl. Acad. Sci. 111(1), 510–514 (2014).
[Crossref]

Korzhova, V.

P. Marinkovic, S. Blumenstock, P. M. Goltstein, V. Korzhova, F. Peters, A. Knebl, and J. Herms, “In vivo imaging reveals reduced activity of neuronal circuits in a mouse tauopathy model,” Brain 142(4), 1051–1062 (2019).
[Crossref]

Kotilinek, L.

K. SantaCruz, J. Lewis, T. Spires, J. Paulson, L. Kotilinek, M. Ingelsson, A. Guimaraes, M. DeTure, M. Ramsden, E. McGowan, C. Forster, M. Yue, J. Orne, C. Janus, A. Mariash, M. Kuskowski, B. Hyman, M. Hutton, and K. H. Ashe, “Tau Suppression in a Neurodegenerative Mouse Model Improves Memory Function,” Science 309(5733), 476–481 (2005).
[Crossref]

Kozak, M.

Z. He, J. D. McBride, H. Xu, L. Changolkar, S. J. Kim, B. Zhang, S. Narasimhan, G. S. Gibbons, J. L. Guo, M. Kozak, G. D. Schellenberg, J. Q. Trojanowski, and V. M. Lee, “Transmission of tauopathy strains is independent of their isoform composition,” Nat. Commun. 11(1), 7 (2020).
[Crossref]

Kramer, J. H.

E. J. Kim, J. L. Hwang, S. E. Gaus, A. L. Nana, J. Deng, J. A. Brown, S. Spina, M. J. Lee, E. M. Ramos, L. T. Grinberg, J. H. Kramer, A. L. Boxer, M. L. Gorno-Tempini, H. J. Rosen, B. L. Miller, and W. W. Seeley, “Evidence of corticofugal tau spreading in patients with frontotemporal dementia,” Acta Neuropathol. 139(1), 27–43 (2020).
[Crossref]

Krishnamurthy, P.

S. Krishnaswamy, Y. Lin, W. J. Rajamohamedsait, H. B. Rajamohamedsait, P. Krishnamurthy, and E. M. Sigurdsson, “Antibody-derived in vivo imaging of tau pathology,” J. Neuroscience 34(50), 16835–16850 (2014).
[Crossref]

Krishnaswamy, S.

S. Krishnaswamy, Y. Lin, W. J. Rajamohamedsait, H. B. Rajamohamedsait, P. Krishnamurthy, and E. M. Sigurdsson, “Antibody-derived in vivo imaging of tau pathology,” J. Neuroscience 34(50), 16835–16850 (2014).
[Crossref]

Kroth, H.

A. Mueller, S. Bullich, O. Barret, J. Madonia, M. Berndt, C. Papin, A. Perrotin, N. Koglin, H. Kroth, A. Pfeifer, G. Tamagnan, J. P. Seibyl, K. Marek, S. de Santi, L. M. Dinkelborg, and A. W. Stephens, “Tau PET imaging with (18)F-PI-2620 in patients with Alzheimer's disease and healthy controls: a first-in-human study,” J. Nucl. Med. 61(6), 911–919 (2020).
[Crossref]

H. Kroth, F. Oden, J. Molette, H. Schieferstein, F. Capotosti, A. Mueller, M. Berndt, H. Schmitt-Willich, V. Darmency, E. Gabellieri, C. Boudou, T. Juergens, Y. Varisco, E. Vokali, D. T. Hickman, G. Tamagnan, A. Pfeifer, L. Dinkelborg, A. Muhs, and A. Stephens, “Discovery and preclinical characterization of [(18)F]PI-2620, a next-generation tau PET tracer for the assessment of tau pathology in Alzheimer's disease and other tauopathies,” Eur. J. Nucl. Med. Mol. Imaging 46(10), 2178–2189 (2019).
[Crossref]

Kuchibhotla, K. V.

K. V. Kuchibhotla, S. Wegmann, K. J. Kopeikina, J. Hawkes, N. Rudinskiy, M. L. Andermann, T. L. Spires-Jones, B. J. Bacskai, and B. T. Hyman, “Neurofibrillary tangle-bearing neurons are functionally integrated in cortical circuits in vivo,” Proc. Natl. Acad. Sci. 111(1), 510–514 (2014).
[Crossref]

Kudo, Y.

M. Maruyama, H. Shimada, T. Suhara, H. Shinotoh, B. Ji, J. Maeda, M. R. Zhang, J. Q. Trojanowski, V. M. Lee, M. Ono, K. Masamoto, H. Takano, N. Sahara, N. Iwata, N. Okamura, S. Furumoto, Y. Kudo, Q. Chang, T. C. Saido, A. Takashima, J. Lewis, M. K. Jang, I. Aoki, H. Ito, and M. Higuchi, “Imaging of tau pathology in a tauopathy mouse model and in Alzheimer patients compared to normal controls,” Neuron 79(6), 1094–1108 (2013).
[Crossref]

Kuhn, G. A.

R. Ni, Y. Zarb, G. A. Kuhn, R. Müller, Y. Yundung, R. M. Nitsch, L. Kulic, A. Keller, and J. Klohs, “Tau deposition is associated with imaging patterns of tissue calcification in the P301L mouse model of human tauopathy,” bioRxiv, 851915 (2019).

Kulic, L.

R. Ni, Y. Zarb, G. A. Kuhn, R. Müller, Y. Yundung, R. M. Nitsch, L. Kulic, A. Keller, and J. Klohs, “Tau deposition is associated with imaging patterns of tissue calcification in the P301L mouse model of human tauopathy,” bioRxiv, 851915 (2019).

Kumari, P.

B. M. Burmann, J. A. Gerez, I. Matecko-Burmann, S. Campioni, P. Kumari, D. Ghosh, A. Mazur, E. E. Aspholm, D. Sulskis, M. Wawrzyniuk, T. Bock, A. Schmidt, S. G. D. Rudiger, R. Riek, and S. Hiller, “Regulation of alpha-synuclein by chaperones in mammalian cells,” Nature 577(7788), 127–132 (2020).
[Crossref]

Kumata, K.

M. Ono, N. Sahara, K. Kumata, B. Ji, R. Ni, S. Koga, D. W. Dickson, J. Q. Trojanowski, V. M.-Y. Lee, M. Yoshida, I. Hozumi, Y. Yoshiyama, J. C. v. Swieten, A. Nordberg, T. Suhara, M.-R. Zhang, and M. Higuchi, “Distinct binding of PET ligands PBB3 and AV-1451 to tau fibril strains in neurodegenerative tauopathies,” Brain 140, aww339 (2017).
[Crossref]

Kuskowski, M.

K. SantaCruz, J. Lewis, T. Spires, J. Paulson, L. Kotilinek, M. Ingelsson, A. Guimaraes, M. DeTure, M. Ramsden, E. McGowan, C. Forster, M. Yue, J. Orne, C. Janus, A. Mariash, M. Kuskowski, B. Hyman, M. Hutton, and K. H. Ashe, “Tau Suppression in a Neurodegenerative Mouse Model Improves Memory Function,” Science 309(5733), 476–481 (2005).
[Crossref]

Kuwabara, S.

A. Ishikawa, M. Tokunaga, J. Maeda, T. Minamihisamatsu, M. Shimojo, H. Takuwa, M. Ono, R. Ni, S. Hirano, S. Kuwabara, B. Ji, M. R. Zhang, I. Aoki, T. Suhara, M. Higuchi, and N. Sahara, “In Vivo Visualization of Tau Accumulation, Microglial Activation, and Brain Atrophy in a Mouse Model of Tauopathy rTg4510,” J. Alzheimer’s Dis. 61(3), 1037–1052 (2018).
[Crossref]

La Joie, R.

R. La Joie, A. V. Visani, S. L. Baker, J. A. Brown, V. Bourakova, J. Cha, K. Chaudhary, L. Edwards, L. Iaccarino, M. Janabi, O. H. Lesman-Segev, Z. A. Miller, D. C. Perry, J. P. O’Neil, J. Pham, J. C. Rojas, H. J. Rosen, W. W. Seeley, R. M. Tsai, B. L. Miller, W. J. Jagust, and G. D. Rabinovici, “Prospective longitudinal atrophy in Alzheimer’s disease correlates with the intensity and topography of baseline tau-PET,” Sci. Transl. Med. 12(524), eaau5732 (2020).
[Crossref]

Lasagna-Reeves, C. A.

C. A. Lasagna-Reeves, D. L. Castillo-Carranza, U. Sengupta, J. Sarmiento, J. Troncoso, G. R. Jackson, and R. Kayed, “Identification of oligomers at early stages of tau aggregation in Alzheimer's disease,” FASEB J. 26(5), 1946–1959 (2012).
[Crossref]

Lassailly, F.

F. Lassailly, K. Foster, L. Lopez-Onieva, E. Currie, and D. Bonnet, “Multimodal imaging reveals structural and functional heterogeneity in different bone marrow compartments: functional implications on hematopoietic stem cells,” Blood 122(10), 1730–1740 (2013).
[Crossref]

Lavenir, I.

A. Velasco, G. Fraser, P. Delobel, B. Ghetti, I. Lavenir, and M. Goedert, “Detection of filamentous tau inclusions by the fluorescent Congo red derivative FSB [(trans,trans)-1-fluoro-2,5-bis(3-hydroxycarbonyl-4-hydroxy)styrylbenzene],” FEBS Lett. 582(6), 901–906 (2008).
[Crossref]

P. Delobel, I. Lavenir, G. Fraser, E. Ingram, M. Holzer, B. Ghetti, M. G. Spillantini, R. A. Crowther, and M. Goedert, “Analysis of tau phosphorylation and truncation in a mouse model of human tauopathy,” Am. J. Pathology 172(1), 123–131 (2008).
[Crossref]

Lee, M. J.

E. J. Kim, J. L. Hwang, S. E. Gaus, A. L. Nana, J. Deng, J. A. Brown, S. Spina, M. J. Lee, E. M. Ramos, L. T. Grinberg, J. H. Kramer, A. L. Boxer, M. L. Gorno-Tempini, H. J. Rosen, B. L. Miller, and W. W. Seeley, “Evidence of corticofugal tau spreading in patients with frontotemporal dementia,” Acta Neuropathol. 139(1), 27–43 (2020).
[Crossref]

Lee, V. M.

Z. He, J. D. McBride, H. Xu, L. Changolkar, S. J. Kim, B. Zhang, S. Narasimhan, G. S. Gibbons, J. L. Guo, M. Kozak, G. D. Schellenberg, J. Q. Trojanowski, and V. M. Lee, “Transmission of tauopathy strains is independent of their isoform composition,” Nat. Commun. 11(1), 7 (2020).
[Crossref]

M. Maruyama, H. Shimada, T. Suhara, H. Shinotoh, B. Ji, J. Maeda, M. R. Zhang, J. Q. Trojanowski, V. M. Lee, M. Ono, K. Masamoto, H. Takano, N. Sahara, N. Iwata, N. Okamura, S. Furumoto, Y. Kudo, Q. Chang, T. C. Saido, A. Takashima, J. Lewis, M. K. Jang, I. Aoki, H. Ito, and M. Higuchi, “Imaging of tau pathology in a tauopathy mouse model and in Alzheimer patients compared to normal controls,” Neuron 79(6), 1094–1108 (2013).
[Crossref]

Y. Yoshiyama, M. Higuchi, B. Zhang, S. M. Huang, N. Iwata, T. C. Saido, J. Maeda, T. Suhara, J. Q. Trojanowski, and V. M. Lee, “Synapse loss and microglial activation precede tangles in a P301S tauopathy mouse model,” Neuron 53(3), 337–351 (2007).
[Crossref]

V. M. Lee, M. Goedert, and J. Q. Trojanowski, “Neurodegenerative tauopathies,” Annu. Rev. Neurosci. 24(1), 1121–1159 (2001).
[Crossref]

Lee, V. M.-Y.

M. Ono, N. Sahara, K. Kumata, B. Ji, R. Ni, S. Koga, D. W. Dickson, J. Q. Trojanowski, V. M.-Y. Lee, M. Yoshida, I. Hozumi, Y. Yoshiyama, J. C. v. Swieten, A. Nordberg, T. Suhara, M.-R. Zhang, and M. Higuchi, “Distinct binding of PET ligands PBB3 and AV-1451 to tau fibril strains in neurodegenerative tauopathies,” Brain 140, aww339 (2017).
[Crossref]

Lesman-Segev, O. H.

R. La Joie, A. V. Visani, S. L. Baker, J. A. Brown, V. Bourakova, J. Cha, K. Chaudhary, L. Edwards, L. Iaccarino, M. Janabi, O. H. Lesman-Segev, Z. A. Miller, D. C. Perry, J. P. O’Neil, J. Pham, J. C. Rojas, H. J. Rosen, W. W. Seeley, R. M. Tsai, B. L. Miller, W. J. Jagust, and G. D. Rabinovici, “Prospective longitudinal atrophy in Alzheimer’s disease correlates with the intensity and topography of baseline tau-PET,” Sci. Transl. Med. 12(524), eaau5732 (2020).
[Crossref]

Lewis, J.

M. Maruyama, H. Shimada, T. Suhara, H. Shinotoh, B. Ji, J. Maeda, M. R. Zhang, J. Q. Trojanowski, V. M. Lee, M. Ono, K. Masamoto, H. Takano, N. Sahara, N. Iwata, N. Okamura, S. Furumoto, Y. Kudo, Q. Chang, T. C. Saido, A. Takashima, J. Lewis, M. K. Jang, I. Aoki, H. Ito, and M. Higuchi, “Imaging of tau pathology in a tauopathy mouse model and in Alzheimer patients compared to normal controls,” Neuron 79(6), 1094–1108 (2013).
[Crossref]

K. SantaCruz, J. Lewis, T. Spires, J. Paulson, L. Kotilinek, M. Ingelsson, A. Guimaraes, M. DeTure, M. Ramsden, E. McGowan, C. Forster, M. Yue, J. Orne, C. Janus, A. Mariash, M. Kuskowski, B. Hyman, M. Hutton, and K. H. Ashe, “Tau Suppression in a Neurodegenerative Mouse Model Improves Memory Function,” Science 309(5733), 476–481 (2005).
[Crossref]

J. Lewis, E. McGowan, J. Rockwood, H. Melrose, P. Nacharaju, M. Van Slegtenhorst, K. Gwinn-Hardy, M. Paul Murphy, M. Baker, X. Yu, K. Duff, J. Hardy, A. Corral, W. L. Lin, S. H. Yen, D. W. Dickson, P. Davies, and M. Hutton, “Neurofibrillary tangles, amyotrophy and progressive motor disturbance in mice expressing mutant (P301L) tau protein,” Nat. Genet. 25(4), 402–405 (2000).
[Crossref]

Liebig, C.

B. Wegenast-Braun, A. Skodras, G. Bayraktar, J. Mahler, S. Fritschi, T. Klingstedt, J. Mason, P. Hammarström, K. Nilsson, C. Liebig, and M. Jucker, “Spectral Discrimination of Cerebral Amyloid Lesions after Peripheral Application of Luminescent Conjugated Oligothiophenes,” Am. J. Pathology 181(6), 1953–1960 (2012).
[Crossref]

Lim, C. K.

C. H. Lo, C. K. Lim, Z. Ding, S. P. Wickramasinghe, A. R. Braun, K. H. Ashe, E. Rhoades, D. D. Thomas, and J. N. Sachs, “Targeting the ensemble of heterogeneous tau oligomers in cells: A novel small molecule screening platform for tauopathies,” Alzheimer’s & Dementia 15(11), 1489–1502 (2019).
[Crossref]

Lin, W. L.

J. Lewis, E. McGowan, J. Rockwood, H. Melrose, P. Nacharaju, M. Van Slegtenhorst, K. Gwinn-Hardy, M. Paul Murphy, M. Baker, X. Yu, K. Duff, J. Hardy, A. Corral, W. L. Lin, S. H. Yen, D. W. Dickson, P. Davies, and M. Hutton, “Neurofibrillary tangles, amyotrophy and progressive motor disturbance in mice expressing mutant (P301L) tau protein,” Nat. Genet. 25(4), 402–405 (2000).
[Crossref]

Lin, Y.

Q. Wu, Y. Lin, J. Gu, and E. M. Sigurdsson, “Dynamic assessment of tau immunotherapies in the brains of live animals by two-photon imaging,” EBioMedicine 35, 270–278 (2018).
[Crossref]

S. Krishnaswamy, Y. Lin, W. J. Rajamohamedsait, H. B. Rajamohamedsait, P. Krishnamurthy, and E. M. Sigurdsson, “Antibody-derived in vivo imaging of tau pathology,” J. Neuroscience 34(50), 16835–16850 (2014).
[Crossref]

Linares, M.

H. Shirani, M. Linares, C. J. Sigurdson, M. Lindgren, P. Norman, and K. P. Nilsson, “A Palette of Fluorescent Thiophene-Based Ligands for the Identification of Protein Aggregates,” Chem. Eur. J. 21(43), 15133–15137 (2015).
[Crossref]

Lindgren, M.

H. Shirani, M. Linares, C. J. Sigurdson, M. Lindgren, P. Norman, and K. P. Nilsson, “A Palette of Fluorescent Thiophene-Based Ligands for the Identification of Protein Aggregates,” Chem. Eur. J. 21(43), 15133–15137 (2015).
[Crossref]

A. Aslund, C. J. Sigurdson, T. Klingstedt, S. Grathwohl, T. Bolmont, D. L. Dickstein, E. Glimsdal, S. Prokop, M. Lindgren, P. Konradsson, D. M. Holtzman, P. R. Hof, F. L. Heppner, S. Gandy, M. Jucker, A. Aguzzi, P. Hammarström, and K. P. Nilsson, “Novel pentameric thiophene derivatives for in vitro and in vivo optical imaging of a plethora of protein aggregates in cerebral amyloidoses,” ACS Chem. Biol. 4(8), 673–684 (2009).
[Crossref]

Lo, C. H.

C. H. Lo, C. K. Lim, Z. Ding, S. P. Wickramasinghe, A. R. Braun, K. H. Ashe, E. Rhoades, D. D. Thomas, and J. N. Sachs, “Targeting the ensemble of heterogeneous tau oligomers in cells: A novel small molecule screening platform for tauopathies,” Alzheimer’s & Dementia 15(11), 1489–1502 (2019).
[Crossref]

Lockhart, S. N.

M. Scholl, S. N. Lockhart, D. R. Schonhaut, J. P. O’Neil, M. Janabi, R. Ossenkoppele, S. L. Baker, J. W. Vogel, J. Faria, H. D. Schwimmer, G. D. Rabinovici, and W. J. Jagust, “PET Imaging of Tau Deposition in the Aging Human Brain,” Neuron 89(5), 971–982 (2016).
[Crossref]

Lohith, T. G.

E. D. Hostetler, A. M. Walji, Z. Zeng, P. Miller, I. Bennacef, C. Salinas, B. Connolly, L. Gantert, H. Haley, M. Holahan, M. Purcell, K. Riffel, T. G. Lohith, P. Coleman, A. Soriano, A. Ogawa, S. Xu, X. Zhang, E. Joshi, J. Della Rocca, D. Hesk, D. J. Schenk, and J. L. Evelhoch, ““Preclinical Characterization of 18F-MK-6240, a Promising PET Tracer for In Vivo Quantification of Human Neurofibrillary Tangles,” Journal of nuclear medicine : official publication,” J. Nuclear Medicine 57(10), 1599–1606 (2016).
[Crossref]

Lopez-Onieva, L.

F. Lassailly, K. Foster, L. Lopez-Onieva, E. Currie, and D. Bonnet, “Multimodal imaging reveals structural and functional heterogeneity in different bone marrow compartments: functional implications on hematopoietic stem cells,” Blood 122(10), 1730–1740 (2013).
[Crossref]

Madonia, J.

A. Mueller, S. Bullich, O. Barret, J. Madonia, M. Berndt, C. Papin, A. Perrotin, N. Koglin, H. Kroth, A. Pfeifer, G. Tamagnan, J. P. Seibyl, K. Marek, S. de Santi, L. M. Dinkelborg, and A. W. Stephens, “Tau PET imaging with (18)F-PI-2620 in patients with Alzheimer's disease and healthy controls: a first-in-human study,” J. Nucl. Med. 61(6), 911–919 (2020).
[Crossref]

Maeda, J.

A. Ishikawa, M. Tokunaga, J. Maeda, T. Minamihisamatsu, M. Shimojo, H. Takuwa, M. Ono, R. Ni, S. Hirano, S. Kuwabara, B. Ji, M. R. Zhang, I. Aoki, T. Suhara, M. Higuchi, and N. Sahara, “In Vivo Visualization of Tau Accumulation, Microglial Activation, and Brain Atrophy in a Mouse Model of Tauopathy rTg4510,” J. Alzheimer’s Dis. 61(3), 1037–1052 (2018).
[Crossref]

M. Maruyama, H. Shimada, T. Suhara, H. Shinotoh, B. Ji, J. Maeda, M. R. Zhang, J. Q. Trojanowski, V. M. Lee, M. Ono, K. Masamoto, H. Takano, N. Sahara, N. Iwata, N. Okamura, S. Furumoto, Y. Kudo, Q. Chang, T. C. Saido, A. Takashima, J. Lewis, M. K. Jang, I. Aoki, H. Ito, and M. Higuchi, “Imaging of tau pathology in a tauopathy mouse model and in Alzheimer patients compared to normal controls,” Neuron 79(6), 1094–1108 (2013).
[Crossref]

Y. Yoshiyama, M. Higuchi, B. Zhang, S. M. Huang, N. Iwata, T. C. Saido, J. Maeda, T. Suhara, J. Q. Trojanowski, and V. M. Lee, “Synapse loss and microglial activation precede tangles in a P301S tauopathy mouse model,” Neuron 53(3), 337–351 (2007).
[Crossref]

Mahler, J.

B. Wegenast-Braun, A. Skodras, G. Bayraktar, J. Mahler, S. Fritschi, T. Klingstedt, J. Mason, P. Hammarström, K. Nilsson, C. Liebig, and M. Jucker, “Spectral Discrimination of Cerebral Amyloid Lesions after Peripheral Application of Luminescent Conjugated Oligothiophenes,” Am. J. Pathology 181(6), 1953–1960 (2012).
[Crossref]

Manser, P.

S. Sanabria Bohorquez, J. Marik, A. Ogasawara, J. N. Tinianow, H. S. Gill, O. Barret, G. Tamagnan, D. Alagille, G. Ayalon, P. Manser, T. Bengtsson, M. Ward, S. P. Williams, G. A. Kerchner, J. P. Seibyl, K. Marek, and R. M. Weimer, “[(18)F]GTP1 (Genentech Tau Probe 1), a radioligand for detecting neurofibrillary tangle tau pathology in Alzheimer's disease,” Eur. J. Nucl. Med. Mol. Imaging 46(10), 2077–2089 (2019).
[Crossref]

Marek, K.

A. Mueller, S. Bullich, O. Barret, J. Madonia, M. Berndt, C. Papin, A. Perrotin, N. Koglin, H. Kroth, A. Pfeifer, G. Tamagnan, J. P. Seibyl, K. Marek, S. de Santi, L. M. Dinkelborg, and A. W. Stephens, “Tau PET imaging with (18)F-PI-2620 in patients with Alzheimer's disease and healthy controls: a first-in-human study,” J. Nucl. Med. 61(6), 911–919 (2020).
[Crossref]

S. Sanabria Bohorquez, J. Marik, A. Ogasawara, J. N. Tinianow, H. S. Gill, O. Barret, G. Tamagnan, D. Alagille, G. Ayalon, P. Manser, T. Bengtsson, M. Ward, S. P. Williams, G. A. Kerchner, J. P. Seibyl, K. Marek, and R. M. Weimer, “[(18)F]GTP1 (Genentech Tau Probe 1), a radioligand for detecting neurofibrillary tangle tau pathology in Alzheimer's disease,” Eur. J. Nucl. Med. Mol. Imaging 46(10), 2077–2089 (2019).
[Crossref]

Mariash, A.

K. SantaCruz, J. Lewis, T. Spires, J. Paulson, L. Kotilinek, M. Ingelsson, A. Guimaraes, M. DeTure, M. Ramsden, E. McGowan, C. Forster, M. Yue, J. Orne, C. Janus, A. Mariash, M. Kuskowski, B. Hyman, M. Hutton, and K. H. Ashe, “Tau Suppression in a Neurodegenerative Mouse Model Improves Memory Function,” Science 309(5733), 476–481 (2005).
[Crossref]

Marik, J.

S. Sanabria Bohorquez, J. Marik, A. Ogasawara, J. N. Tinianow, H. S. Gill, O. Barret, G. Tamagnan, D. Alagille, G. Ayalon, P. Manser, T. Bengtsson, M. Ward, S. P. Williams, G. A. Kerchner, J. P. Seibyl, K. Marek, and R. M. Weimer, “[(18)F]GTP1 (Genentech Tau Probe 1), a radioligand for detecting neurofibrillary tangle tau pathology in Alzheimer's disease,” Eur. J. Nucl. Med. Mol. Imaging 46(10), 2077–2089 (2019).
[Crossref]

Marinkovic, P.

P. Marinkovic, S. Blumenstock, P. M. Goltstein, V. Korzhova, F. Peters, A. Knebl, and J. Herms, “In vivo imaging reveals reduced activity of neuronal circuits in a mouse tauopathy model,” Brain 142(4), 1051–1062 (2019).
[Crossref]

Marshall, G.

K. A. Johnson, A. Schultz, R. A. Betensky, J. A. Becker, J. Sepulcre, D. Rentz, E. Mormino, J. Chhatwal, R. Amariglio, K. Papp, G. Marshall, M. Albers, S. Mauro, L. Pepin, J. Alverio, K. Judge, M. Philiossaint, T. Shoup, D. Yokell, B. Dickerson, T. Gomez-Isla, B. Hyman, N. Vasdev, and R. Sperling, “Tau positron emission tomographic imaging in aging and early Alzheimer disease,” Ann Neurol. 79(1), 110–119 (2016).
[Crossref]

Marshall, G. A.

B. J. Hanseeuw, R. A. Betensky, H. I. L. Jacobs, A. P. Schultz, J. Sepulcre, J. A. Becker, D. M. O. Cosio, M. Farrell, Y. T. Quiroz, E. C. Mormino, R. F. Buckley, K. V. Papp, R. A. Amariglio, I. Dewachter, A. Ivanoiu, W. Huijbers, T. Hedden, G. A. Marshall, J. P. Chhatwal, D. M. Rentz, R. A. Sperling, and K. Johnson, “Association of Amyloid and Tau With Cognition in Preclinical Alzheimer Disease: A Longitudinal Study,” JAMA Neurol. 76(8), 915–924 (2019).
[Crossref]

Martus, P.

P. Füger, J. K. Hefendehl, K. Veeraraghavalu, A.-C. Wendeln, C. Schlosser, U. Obermüller, B. M. Wegenast-Braun, J. J. Neher, P. Martus, S. Kohsaka, M. Thunemann, R. Feil, S. S. Sisodia, A. Skodras, and M. Jucker, “Microglia turnover with aging and in an Alzheimer's model via long-term in vivo single-cell imaging,” Nat. Neurosci. 20(10), 1371–1376 (2017).
[Crossref]

Maruyama, M.

M. Maruyama, H. Shimada, T. Suhara, H. Shinotoh, B. Ji, J. Maeda, M. R. Zhang, J. Q. Trojanowski, V. M. Lee, M. Ono, K. Masamoto, H. Takano, N. Sahara, N. Iwata, N. Okamura, S. Furumoto, Y. Kudo, Q. Chang, T. C. Saido, A. Takashima, J. Lewis, M. K. Jang, I. Aoki, H. Ito, and M. Higuchi, “Imaging of tau pathology in a tauopathy mouse model and in Alzheimer patients compared to normal controls,” Neuron 79(6), 1094–1108 (2013).
[Crossref]

Masamoto, K.

M. Maruyama, H. Shimada, T. Suhara, H. Shinotoh, B. Ji, J. Maeda, M. R. Zhang, J. Q. Trojanowski, V. M. Lee, M. Ono, K. Masamoto, H. Takano, N. Sahara, N. Iwata, N. Okamura, S. Furumoto, Y. Kudo, Q. Chang, T. C. Saido, A. Takashima, J. Lewis, M. K. Jang, I. Aoki, H. Ito, and M. Higuchi, “Imaging of tau pathology in a tauopathy mouse model and in Alzheimer patients compared to normal controls,” Neuron 79(6), 1094–1108 (2013).
[Crossref]

Masliah, E.

J. A. Gerez, N. C. Prymaczok, E. Rockenstein, U. S. Herrmann, P. Schwarz, A. Adame, R. I. Enchev, T. Courtheoux, P. J. Boersema, R. Riek, M. Peter, A. Aguzzi, E. Masliah, and P. Picotti, “A cullin-RING ubiquitin ligase targets exogenous alpha-synuclein and inhibits Lewy body-like pathology,” Sci. Transl. Med. 11(495), eaau6722 (2019).
[Crossref]

Mason, J.

B. Wegenast-Braun, A. Skodras, G. Bayraktar, J. Mahler, S. Fritschi, T. Klingstedt, J. Mason, P. Hammarström, K. Nilsson, C. Liebig, and M. Jucker, “Spectral Discrimination of Cerebral Amyloid Lesions after Peripheral Application of Luminescent Conjugated Oligothiophenes,” Am. J. Pathology 181(6), 1953–1960 (2012).
[Crossref]

Mason, J. J.

T. Klingstedt, A. Aslund, R. A. Simon, L. B. Johansson, J. J. Mason, S. Nystrom, P. Hammarstrom, and K. P. Nilsson, “Synthesis of a library of oligothiophenes and their utilization as fluorescent ligands for spectral assignment of protein aggregates,” Org. Biomol. Chem. 9(24), 8356–8370 (2011).
[Crossref]

Masters, C. L.

V. L. Villemagne, V. Dore, S. C. Burnham, C. L. Masters, and C. C. Rowe, “Imaging tau and amyloid-beta proteinopathies in Alzheimer disease and other conditions,” Nat. Rev. Neurol. 14(4), 225–236 (2018).
[Crossref]

Matecko-Burmann, I.

B. M. Burmann, J. A. Gerez, I. Matecko-Burmann, S. Campioni, P. Kumari, D. Ghosh, A. Mazur, E. E. Aspholm, D. Sulskis, M. Wawrzyniuk, T. Bock, A. Schmidt, S. G. D. Rudiger, R. Riek, and S. Hiller, “Regulation of alpha-synuclein by chaperones in mammalian cells,” Nature 577(7788), 127–132 (2020).
[Crossref]

Matsuba, Y.

S. Hashimoto, Y. Matsuba, N. Kamano, N. Mihira, N. Sahara, J. Takano, S. I. Muramatsu, T. C. Saido, and T. Saito, “Tau binding protein CAPON induces tau aggregation and neurodegeneration,” Nat. Commun. 10(1), 2394 (2019).
[Crossref]

Mauro, S.

K. A. Johnson, A. Schultz, R. A. Betensky, J. A. Becker, J. Sepulcre, D. Rentz, E. Mormino, J. Chhatwal, R. Amariglio, K. Papp, G. Marshall, M. Albers, S. Mauro, L. Pepin, J. Alverio, K. Judge, M. Philiossaint, T. Shoup, D. Yokell, B. Dickerson, T. Gomez-Isla, B. Hyman, N. Vasdev, and R. Sperling, “Tau positron emission tomographic imaging in aging and early Alzheimer disease,” Ann Neurol. 79(1), 110–119 (2016).
[Crossref]

Mazo, I. B.

I. B. Mazo, J.-C. Gutierrez-Ramos, P. S. Frenette, R. O. Hynes, D. D. Wagner, and U. H. von Andrian, “Hematopoietic Progenitor Cell Rolling in Bone Marrow Microvessels: Parallel Contributions by Endothelial Selectins and Vascular Cell Adhesion Molecule 1,” J. Exp. Med. 188(3), 465–474 (1998).
[Crossref]

Mazur, A.

B. M. Burmann, J. A. Gerez, I. Matecko-Burmann, S. Campioni, P. Kumari, D. Ghosh, A. Mazur, E. E. Aspholm, D. Sulskis, M. Wawrzyniuk, T. Bock, A. Schmidt, S. G. D. Rudiger, R. Riek, and S. Hiller, “Regulation of alpha-synuclein by chaperones in mammalian cells,” Nature 577(7788), 127–132 (2020).
[Crossref]

Mc Larney, B.

Z. Chen, B. Mc Larney, J. Rebling, X. L. Deán-Ben, Q. Zhou, S. Gottschalk, and D. Razansky, “High-Speed Large-Field Multifocal Illumination Fluorescence Microscopy,” Laser Photonics Rev. 14, 1900070 (2020).
[Crossref]

S. Gottschalk, O. Degtyaruk, B. Mc Larney, J. Rebling, M. A. Hutter, X. L. Deán-Ben, S. Shoham, and D. Razansky, “Rapid volumetric optoacoustic imaging of neural dynamics across the mouse brain,” Nat. Biomed. Eng. 3(5), 392–401 (2019).
[Crossref]

McBride, J. D.

Z. He, J. D. McBride, H. Xu, L. Changolkar, S. J. Kim, B. Zhang, S. Narasimhan, G. S. Gibbons, J. L. Guo, M. Kozak, G. D. Schellenberg, J. Q. Trojanowski, and V. M. Lee, “Transmission of tauopathy strains is independent of their isoform composition,” Nat. Commun. 11(1), 7 (2020).
[Crossref]

McGowan, E.

K. SantaCruz, J. Lewis, T. Spires, J. Paulson, L. Kotilinek, M. Ingelsson, A. Guimaraes, M. DeTure, M. Ramsden, E. McGowan, C. Forster, M. Yue, J. Orne, C. Janus, A. Mariash, M. Kuskowski, B. Hyman, M. Hutton, and K. H. Ashe, “Tau Suppression in a Neurodegenerative Mouse Model Improves Memory Function,” Science 309(5733), 476–481 (2005).
[Crossref]

J. Lewis, E. McGowan, J. Rockwood, H. Melrose, P. Nacharaju, M. Van Slegtenhorst, K. Gwinn-Hardy, M. Paul Murphy, M. Baker, X. Yu, K. Duff, J. Hardy, A. Corral, W. L. Lin, S. H. Yen, D. W. Dickson, P. Davies, and M. Hutton, “Neurofibrillary tangles, amyotrophy and progressive motor disturbance in mice expressing mutant (P301L) tau protein,” Nat. Genet. 25(4), 402–405 (2000).
[Crossref]

McKee, C. A.

T. K. Patel, L. Habimana-Griffin, X. Gao, B. Xu, S. Achilefu, K. Alitalo, C. A. McKee, P. W. Sheehan, E. S. Musiek, C. Xiong, D. Coble, and D. M. Holtzman, “Dural lymphatics regulate clearance of extracellular tau from the CNS,” Mol. Neurodegener. 14(1), 11 (2019).
[Crossref]

Megow, D.

J. Klohs, N. Baeva, J. Steinbrink, R. Bourayou, C. Boettcher, G. Royl, D. Megow, U. Dirnagl, J. Priller, and A. Wunder, “In vivo near-infrared fluorescence imaging of matrix metalloproteinase activity after cerebral ischemia,” J. Cereb. Blood Flow Metab. 29(7), 1284–1292 (2009).
[Crossref]

Meilandt, W. J.

B. Dejanovic, M. A. Huntley, A. De Maziere, W. J. Meilandt, T. Wu, K. Srinivasan, Z. Jiang, V. Gandham, B. A. Friedman, H. Ngu, O. Foreman, R. A. D. Carano, B. Chih, J. Klumperman, C. Bakalarski, J. E. Hanson, and M. Sheng, “Changes in the Synaptic Proteome in Tauopathy and Rescue of Tau-Induced Synapse Loss by C1q Antibodies,” Neuron 100(6), 1322–1336.e7 (2018).
[Crossref]

Melrose, H.

J. Lewis, E. McGowan, J. Rockwood, H. Melrose, P. Nacharaju, M. Van Slegtenhorst, K. Gwinn-Hardy, M. Paul Murphy, M. Baker, X. Yu, K. Duff, J. Hardy, A. Corral, W. L. Lin, S. H. Yen, D. W. Dickson, P. Davies, and M. Hutton, “Neurofibrillary tangles, amyotrophy and progressive motor disturbance in mice expressing mutant (P301L) tau protein,” Nat. Genet. 25(4), 402–405 (2000).
[Crossref]

Meno-Tetang, G.

M. Colin, S. Dujardin, S. Schraen-Maschke, G. Meno-Tetang, C. Duyckaerts, J. P. Courade, and L. Buee, “From the prion-like propagation hypothesis to therapeutic strategies of anti-tau immunotherapy,” Acta Neuropathol. 139(1), 3–25 (2020).
[Crossref]

Mihira, N.

S. Hashimoto, Y. Matsuba, N. Kamano, N. Mihira, N. Sahara, J. Takano, S. I. Muramatsu, T. C. Saido, and T. Saito, “Tau binding protein CAPON induces tau aggregation and neurodegeneration,” Nat. Commun. 10(1), 2394 (2019).
[Crossref]

Miller, B. L.

R. La Joie, A. V. Visani, S. L. Baker, J. A. Brown, V. Bourakova, J. Cha, K. Chaudhary, L. Edwards, L. Iaccarino, M. Janabi, O. H. Lesman-Segev, Z. A. Miller, D. C. Perry, J. P. O’Neil, J. Pham, J. C. Rojas, H. J. Rosen, W. W. Seeley, R. M. Tsai, B. L. Miller, W. J. Jagust, and G. D. Rabinovici, “Prospective longitudinal atrophy in Alzheimer’s disease correlates with the intensity and topography of baseline tau-PET,” Sci. Transl. Med. 12(524), eaau5732 (2020).
[Crossref]

E. J. Kim, J. L. Hwang, S. E. Gaus, A. L. Nana, J. Deng, J. A. Brown, S. Spina, M. J. Lee, E. M. Ramos, L. T. Grinberg, J. H. Kramer, A. L. Boxer, M. L. Gorno-Tempini, H. J. Rosen, B. L. Miller, and W. W. Seeley, “Evidence of corticofugal tau spreading in patients with frontotemporal dementia,” Acta Neuropathol. 139(1), 27–43 (2020).
[Crossref]

Miller, P.

E. D. Hostetler, A. M. Walji, Z. Zeng, P. Miller, I. Bennacef, C. Salinas, B. Connolly, L. Gantert, H. Haley, M. Holahan, M. Purcell, K. Riffel, T. G. Lohith, P. Coleman, A. Soriano, A. Ogawa, S. Xu, X. Zhang, E. Joshi, J. Della Rocca, D. Hesk, D. J. Schenk, and J. L. Evelhoch, ““Preclinical Characterization of 18F-MK-6240, a Promising PET Tracer for In Vivo Quantification of Human Neurofibrillary Tangles,” Journal of nuclear medicine : official publication,” J. Nuclear Medicine 57(10), 1599–1606 (2016).
[Crossref]

Miller, R. L.

K. M. Schoch, S. L. DeVos, R. L. Miller, S. J. Chun, M. Norrbom, D. F. Wozniak, H. N. Dawson, C. F. Bennett, F. Rigo, and T. M. Miller, “Increased 4R-Tau Induces Pathological Changes in a Human-Tau Mouse Model,” Neuron 90(5), 941–947 (2016).
[Crossref]

Miller, T. M.

K. M. Schoch, S. L. DeVos, R. L. Miller, S. J. Chun, M. Norrbom, D. F. Wozniak, H. N. Dawson, C. F. Bennett, F. Rigo, and T. M. Miller, “Increased 4R-Tau Induces Pathological Changes in a Human-Tau Mouse Model,” Neuron 90(5), 941–947 (2016).
[Crossref]

S. K. Kaufman, D. W. Sanders, T. L. Thomas, A. J. Ruchinskas, J. Vaquer-Alicea, A. M. Sharma, T. M. Miller, and M. I. Diamond, “Tau Prion Strains Dictate Patterns of Cell Pathology, Progression Rate, and Regional Vulnerability In Vivo,” Neuron 92(4), 796–812 (2016).
[Crossref]

Miller, Z. A.

R. La Joie, A. V. Visani, S. L. Baker, J. A. Brown, V. Bourakova, J. Cha, K. Chaudhary, L. Edwards, L. Iaccarino, M. Janabi, O. H. Lesman-Segev, Z. A. Miller, D. C. Perry, J. P. O’Neil, J. Pham, J. C. Rojas, H. J. Rosen, W. W. Seeley, R. M. Tsai, B. L. Miller, W. J. Jagust, and G. D. Rabinovici, “Prospective longitudinal atrophy in Alzheimer’s disease correlates with the intensity and topography of baseline tau-PET,” Sci. Transl. Med. 12(524), eaau5732 (2020).
[Crossref]

Minamihisamatsu, T.

A. Ishikawa, M. Tokunaga, J. Maeda, T. Minamihisamatsu, M. Shimojo, H. Takuwa, M. Ono, R. Ni, S. Hirano, S. Kuwabara, B. Ji, M. R. Zhang, I. Aoki, T. Suhara, M. Higuchi, and N. Sahara, “In Vivo Visualization of Tau Accumulation, Microglial Activation, and Brain Atrophy in a Mouse Model of Tauopathy rTg4510,” J. Alzheimer’s Dis. 61(3), 1037–1052 (2018).
[Crossref]

Molette, J.

H. Kroth, F. Oden, J. Molette, H. Schieferstein, F. Capotosti, A. Mueller, M. Berndt, H. Schmitt-Willich, V. Darmency, E. Gabellieri, C. Boudou, T. Juergens, Y. Varisco, E. Vokali, D. T. Hickman, G. Tamagnan, A. Pfeifer, L. Dinkelborg, A. Muhs, and A. Stephens, “Discovery and preclinical characterization of [(18)F]PI-2620, a next-generation tau PET tracer for the assessment of tau pathology in Alzheimer's disease and other tauopathies,” Eur. J. Nucl. Med. Mol. Imaging 46(10), 2178–2189 (2019).
[Crossref]

Mormino, E.

K. A. Johnson, A. Schultz, R. A. Betensky, J. A. Becker, J. Sepulcre, D. Rentz, E. Mormino, J. Chhatwal, R. Amariglio, K. Papp, G. Marshall, M. Albers, S. Mauro, L. Pepin, J. Alverio, K. Judge, M. Philiossaint, T. Shoup, D. Yokell, B. Dickerson, T. Gomez-Isla, B. Hyman, N. Vasdev, and R. Sperling, “Tau positron emission tomographic imaging in aging and early Alzheimer disease,” Ann Neurol. 79(1), 110–119 (2016).
[Crossref]

Mormino, E. C.

B. J. Hanseeuw, R. A. Betensky, H. I. L. Jacobs, A. P. Schultz, J. Sepulcre, J. A. Becker, D. M. O. Cosio, M. Farrell, Y. T. Quiroz, E. C. Mormino, R. F. Buckley, K. V. Papp, R. A. Amariglio, I. Dewachter, A. Ivanoiu, W. Huijbers, T. Hedden, G. A. Marshall, J. P. Chhatwal, D. M. Rentz, R. A. Sperling, and K. Johnson, “Association of Amyloid and Tau With Cognition in Preclinical Alzheimer Disease: A Longitudinal Study,” JAMA Neurol. 76(8), 915–924 (2019).
[Crossref]

Mueller, A.

A. Mueller, S. Bullich, O. Barret, J. Madonia, M. Berndt, C. Papin, A. Perrotin, N. Koglin, H. Kroth, A. Pfeifer, G. Tamagnan, J. P. Seibyl, K. Marek, S. de Santi, L. M. Dinkelborg, and A. W. Stephens, “Tau PET imaging with (18)F-PI-2620 in patients with Alzheimer's disease and healthy controls: a first-in-human study,” J. Nucl. Med. 61(6), 911–919 (2020).
[Crossref]

H. Kroth, F. Oden, J. Molette, H. Schieferstein, F. Capotosti, A. Mueller, M. Berndt, H. Schmitt-Willich, V. Darmency, E. Gabellieri, C. Boudou, T. Juergens, Y. Varisco, E. Vokali, D. T. Hickman, G. Tamagnan, A. Pfeifer, L. Dinkelborg, A. Muhs, and A. Stephens, “Discovery and preclinical characterization of [(18)F]PI-2620, a next-generation tau PET tracer for the assessment of tau pathology in Alzheimer's disease and other tauopathies,” Eur. J. Nucl. Med. Mol. Imaging 46(10), 2178–2189 (2019).
[Crossref]

Muhs, A.

H. Kroth, F. Oden, J. Molette, H. Schieferstein, F. Capotosti, A. Mueller, M. Berndt, H. Schmitt-Willich, V. Darmency, E. Gabellieri, C. Boudou, T. Juergens, Y. Varisco, E. Vokali, D. T. Hickman, G. Tamagnan, A. Pfeifer, L. Dinkelborg, A. Muhs, and A. Stephens, “Discovery and preclinical characterization of [(18)F]PI-2620, a next-generation tau PET tracer for the assessment of tau pathology in Alzheimer's disease and other tauopathies,” Eur. J. Nucl. Med. Mol. Imaging 46(10), 2178–2189 (2019).
[Crossref]

Müller, R.

R. Ni, Y. Zarb, G. A. Kuhn, R. Müller, Y. Yundung, R. M. Nitsch, L. Kulic, A. Keller, and J. Klohs, “Tau deposition is associated with imaging patterns of tissue calcification in the P301L mouse model of human tauopathy,” bioRxiv, 851915 (2019).

Muramatsu, S. I.

S. Hashimoto, Y. Matsuba, N. Kamano, N. Mihira, N. Sahara, J. Takano, S. I. Muramatsu, T. C. Saido, and T. Saito, “Tau binding protein CAPON induces tau aggregation and neurodegeneration,” Nat. Commun. 10(1), 2394 (2019).
[Crossref]

Murshudov, G.

A. W. P. Fitzpatrick, B. Falcon, S. He, A. G. Murzin, G. Murshudov, H. J. Garringer, R. A. Crowther, B. Ghetti, M. Goedert, and S. H. W. Scheres, “Cryo-EM structures of tau filaments from Alzheimer's disease,” Nature 547(7662), 185–190 (2017).
[Crossref]

Murzin, A. G.

A. W. P. Fitzpatrick, B. Falcon, S. He, A. G. Murzin, G. Murshudov, H. J. Garringer, R. A. Crowther, B. Ghetti, M. Goedert, and S. H. W. Scheres, “Cryo-EM structures of tau filaments from Alzheimer's disease,” Nature 547(7662), 185–190 (2017).
[Crossref]

Musiek, E. S.

T. K. Patel, L. Habimana-Griffin, X. Gao, B. Xu, S. Achilefu, K. Alitalo, C. A. McKee, P. W. Sheehan, E. S. Musiek, C. Xiong, D. Coble, and D. M. Holtzman, “Dural lymphatics regulate clearance of extracellular tau from the CNS,” Mol. Neurodegener. 14(1), 11 (2019).
[Crossref]

Nacharaju, P.

J. Lewis, E. McGowan, J. Rockwood, H. Melrose, P. Nacharaju, M. Van Slegtenhorst, K. Gwinn-Hardy, M. Paul Murphy, M. Baker, X. Yu, K. Duff, J. Hardy, A. Corral, W. L. Lin, S. H. Yen, D. W. Dickson, P. Davies, and M. Hutton, “Neurofibrillary tangles, amyotrophy and progressive motor disturbance in mice expressing mutant (P301L) tau protein,” Nat. Genet. 25(4), 402–405 (2000).
[Crossref]

Nana, A. L.

E. J. Kim, J. L. Hwang, S. E. Gaus, A. L. Nana, J. Deng, J. A. Brown, S. Spina, M. J. Lee, E. M. Ramos, L. T. Grinberg, J. H. Kramer, A. L. Boxer, M. L. Gorno-Tempini, H. J. Rosen, B. L. Miller, and W. W. Seeley, “Evidence of corticofugal tau spreading in patients with frontotemporal dementia,” Acta Neuropathol. 139(1), 27–43 (2020).
[Crossref]

Narasimhan, S.

Z. He, J. D. McBride, H. Xu, L. Changolkar, S. J. Kim, B. Zhang, S. Narasimhan, G. S. Gibbons, J. L. Guo, M. Kozak, G. D. Schellenberg, J. Q. Trojanowski, and V. M. Lee, “Transmission of tauopathy strains is independent of their isoform composition,” Nat. Commun. 11(1), 7 (2020).
[Crossref]

Neher, J. J.

P. Füger, J. K. Hefendehl, K. Veeraraghavalu, A.-C. Wendeln, C. Schlosser, U. Obermüller, B. M. Wegenast-Braun, J. J. Neher, P. Martus, S. Kohsaka, M. Thunemann, R. Feil, S. S. Sisodia, A. Skodras, and M. Jucker, “Microglia turnover with aging and in an Alzheimer's model via long-term in vivo single-cell imaging,” Nat. Neurosci. 20(10), 1371–1376 (2017).
[Crossref]

Neumann, U.

M. Hintersteiner, A. Enz, P. Frey, A. L. Jaton, W. Kinzy, R. Kneuer, U. Neumann, M. Rudin, M. Staufenbiel, M. Stoeckli, K. H. Wiederhold, and H. U. Gremlich, “In vivo detection of amyloid-beta deposits by near-infrared imaging using an oxazine-derivative probe,” Nat. Biotechnol. 23(5), 577–583 (2005).
[Crossref]

Ngu, H.

B. Dejanovic, M. A. Huntley, A. De Maziere, W. J. Meilandt, T. Wu, K. Srinivasan, Z. Jiang, V. Gandham, B. A. Friedman, H. Ngu, O. Foreman, R. A. D. Carano, B. Chih, J. Klumperman, C. Bakalarski, J. E. Hanson, and M. Sheng, “Changes in the Synaptic Proteome in Tauopathy and Rescue of Tau-Induced Synapse Loss by C1q Antibodies,” Neuron 100(6), 1322–1336.e7 (2018).
[Crossref]

Ni, R.

R. Ni, M. Vaas, W. Ren, and J. Klohs, “Non-invasive detection of acute cerebral hypoxia and subsequent matrix-metalloproteinase activity in a mouse model of cerebral ischemia using multispectral-optoacoustic-tomography,” Neurophotonics 5(1), 015005 (2018).
[Crossref]

A. Ishikawa, M. Tokunaga, J. Maeda, T. Minamihisamatsu, M. Shimojo, H. Takuwa, M. Ono, R. Ni, S. Hirano, S. Kuwabara, B. Ji, M. R. Zhang, I. Aoki, T. Suhara, M. Higuchi, and N. Sahara, “In Vivo Visualization of Tau Accumulation, Microglial Activation, and Brain Atrophy in a Mouse Model of Tauopathy rTg4510,” J. Alzheimer’s Dis. 61(3), 1037–1052 (2018).
[Crossref]

R. Ni, B. Ji, M. Ono, N. Sahara, M. R. Zhang, I. Aoki, A. Nordberg, T. Suhara, and M. Higuchi, ““Comparative in-vitro and in-vivo quantifications of pathological tau deposits and their association with neurodegeneration in tauopathy mouse models,” Journal of nuclear medicine : official publication,” J. Nucl. Med. 59(6), 960–966 (2018).
[Crossref]

M. Ono, N. Sahara, K. Kumata, B. Ji, R. Ni, S. Koga, D. W. Dickson, J. Q. Trojanowski, V. M.-Y. Lee, M. Yoshida, I. Hozumi, Y. Yoshiyama, J. C. v. Swieten, A. Nordberg, T. Suhara, M.-R. Zhang, and M. Higuchi, “Distinct binding of PET ligands PBB3 and AV-1451 to tau fibril strains in neurodegenerative tauopathies,” Brain 140, aww339 (2017).
[Crossref]

R. Ni, X. L. Dean-Ben, D. Kirschenbaum, M. Rudin, Z. Chen, A. Crimi, F. Voigt, P. R. Nilsson, F. Helmchen, R. M. Nitsch, A. Aguzzi, D. Razansky, and J. Klohs, “Whole brain optoacoustic tomography reveals strain-specific regional beta-amyloid densities in Alzheimer`s disease amyloidosis models,” bioRxiv, DOI: 10.1101/2020.1102.1125.964064 (2020).

R. Ni, Y. Zarb, G. A. Kuhn, R. Müller, Y. Yundung, R. M. Nitsch, L. Kulic, A. Keller, and J. Klohs, “Tau deposition is associated with imaging patterns of tissue calcification in the P301L mouse model of human tauopathy,” bioRxiv, 851915 (2019).

R. Ni, Z. Chen, G. Shi, A. Villois, Q. Zhou, P. Arosio, R. M. Nitsch, P. R. Nilsson, J. Klohs, and D. Razansky, “Transcranial in vivo detection of Aβ at single plaque resolution with large-field multifocal illumination fluorescence microscopy,” bioRxiv, 2020.2002.2001.929844 (2020).

Nilsson, K.

B. Wegenast-Braun, A. Skodras, G. Bayraktar, J. Mahler, S. Fritschi, T. Klingstedt, J. Mason, P. Hammarström, K. Nilsson, C. Liebig, and M. Jucker, “Spectral Discrimination of Cerebral Amyloid Lesions after Peripheral Application of Luminescent Conjugated Oligothiophenes,” Am. J. Pathology 181(6), 1953–1960 (2012).
[Crossref]

Nilsson, K. P.

H. Shirani, M. Linares, C. J. Sigurdson, M. Lindgren, P. Norman, and K. P. Nilsson, “A Palette of Fluorescent Thiophene-Based Ligands for the Identification of Protein Aggregates,” Chem. Eur. J. 21(43), 15133–15137 (2015).
[Crossref]

T. Klingstedt, A. Aslund, R. A. Simon, L. B. Johansson, J. J. Mason, S. Nystrom, P. Hammarstrom, and K. P. Nilsson, “Synthesis of a library of oligothiophenes and their utilization as fluorescent ligands for spectral assignment of protein aggregates,” Org. Biomol. Chem. 9(24), 8356–8370 (2011).
[Crossref]

A. Aslund, C. J. Sigurdson, T. Klingstedt, S. Grathwohl, T. Bolmont, D. L. Dickstein, E. Glimsdal, S. Prokop, M. Lindgren, P. Konradsson, D. M. Holtzman, P. R. Hof, F. L. Heppner, S. Gandy, M. Jucker, A. Aguzzi, P. Hammarström, and K. P. Nilsson, “Novel pentameric thiophene derivatives for in vitro and in vivo optical imaging of a plethora of protein aggregates in cerebral amyloidoses,” ACS Chem. Biol. 4(8), 673–684 (2009).
[Crossref]

Nilsson, K. P. R.

M. Calvo-Rodriguez, S. S. Hou, A. C. Snyder, S. Dujardin, H. Shirani, K. P. R. Nilsson, and B. J. Bacskai, “In vivo detection of tau fibrils and amyloid beta aggregates with luminescent conjugated oligothiophenes and multiphoton microscopy,” Acta Neuropathol. Commun. 7(1), 171 (2019).
[Crossref]

Nilsson, P. R.

R. Ni, Z. Chen, G. Shi, A. Villois, Q. Zhou, P. Arosio, R. M. Nitsch, P. R. Nilsson, J. Klohs, and D. Razansky, “Transcranial in vivo detection of Aβ at single plaque resolution with large-field multifocal illumination fluorescence microscopy,” bioRxiv, 2020.2002.2001.929844 (2020).

R. Ni, X. L. Dean-Ben, D. Kirschenbaum, M. Rudin, Z. Chen, A. Crimi, F. Voigt, P. R. Nilsson, F. Helmchen, R. M. Nitsch, A. Aguzzi, D. Razansky, and J. Klohs, “Whole brain optoacoustic tomography reveals strain-specific regional beta-amyloid densities in Alzheimer`s disease amyloidosis models,” bioRxiv, DOI: 10.1101/2020.1102.1125.964064 (2020).

Nitsch, R. M.

J. Gotz, F. Chen, R. Barmettler, and R. M. Nitsch, “Tau filament formation in transgenic mice expressing P301L tau,” J. Biol. Chem. 276(1), 529–534 (2001).
[Crossref]

J. Gotz, F. Chen, J. van Dorpe, and R. M. Nitsch, “Formation of neurofibrillary tangles in P301 l tau transgenic mice induced by Abeta 42 fibrils,” Science 293(5534), 1491–1495 (2001).
[Crossref]

R. Ni, X. L. Dean-Ben, D. Kirschenbaum, M. Rudin, Z. Chen, A. Crimi, F. Voigt, P. R. Nilsson, F. Helmchen, R. M. Nitsch, A. Aguzzi, D. Razansky, and J. Klohs, “Whole brain optoacoustic tomography reveals strain-specific regional beta-amyloid densities in Alzheimer`s disease amyloidosis models,” bioRxiv, DOI: 10.1101/2020.1102.1125.964064 (2020).

R. Ni, Z. Chen, G. Shi, A. Villois, Q. Zhou, P. Arosio, R. M. Nitsch, P. R. Nilsson, J. Klohs, and D. Razansky, “Transcranial in vivo detection of Aβ at single plaque resolution with large-field multifocal illumination fluorescence microscopy,” bioRxiv, 2020.2002.2001.929844 (2020).

R. Ni, Y. Zarb, G. A. Kuhn, R. Müller, Y. Yundung, R. M. Nitsch, L. Kulic, A. Keller, and J. Klohs, “Tau deposition is associated with imaging patterns of tissue calcification in the P301L mouse model of human tauopathy,” bioRxiv, 851915 (2019).

Nordberg, A.

R. Ni, B. Ji, M. Ono, N. Sahara, M. R. Zhang, I. Aoki, A. Nordberg, T. Suhara, and M. Higuchi, ““Comparative in-vitro and in-vivo quantifications of pathological tau deposits and their association with neurodegeneration in tauopathy mouse models,” Journal of nuclear medicine : official publication,” J. Nucl. Med. 59(6), 960–966 (2018).
[Crossref]

M. Ono, N. Sahara, K. Kumata, B. Ji, R. Ni, S. Koga, D. W. Dickson, J. Q. Trojanowski, V. M.-Y. Lee, M. Yoshida, I. Hozumi, Y. Yoshiyama, J. C. v. Swieten, A. Nordberg, T. Suhara, M.-R. Zhang, and M. Higuchi, “Distinct binding of PET ligands PBB3 and AV-1451 to tau fibril strains in neurodegenerative tauopathies,” Brain 140, aww339 (2017).
[Crossref]

Norman, P.

H. Shirani, M. Linares, C. J. Sigurdson, M. Lindgren, P. Norman, and K. P. Nilsson, “A Palette of Fluorescent Thiophene-Based Ligands for the Identification of Protein Aggregates,” Chem. Eur. J. 21(43), 15133–15137 (2015).
[Crossref]

Norrbom, M.

K. M. Schoch, S. L. DeVos, R. L. Miller, S. J. Chun, M. Norrbom, D. F. Wozniak, H. N. Dawson, C. F. Bennett, F. Rigo, and T. M. Miller, “Increased 4R-Tau Induces Pathological Changes in a Human-Tau Mouse Model,” Neuron 90(5), 941–947 (2016).
[Crossref]

Nystrom, S.

T. Klingstedt, A. Aslund, R. A. Simon, L. B. Johansson, J. J. Mason, S. Nystrom, P. Hammarstrom, and K. P. Nilsson, “Synthesis of a library of oligothiophenes and their utilization as fluorescent ligands for spectral assignment of protein aggregates,” Org. Biomol. Chem. 9(24), 8356–8370 (2011).
[Crossref]

O’Neil, J. P.

R. La Joie, A. V. Visani, S. L. Baker, J. A. Brown, V. Bourakova, J. Cha, K. Chaudhary, L. Edwards, L. Iaccarino, M. Janabi, O. H. Lesman-Segev, Z. A. Miller, D. C. Perry, J. P. O’Neil, J. Pham, J. C. Rojas, H. J. Rosen, W. W. Seeley, R. M. Tsai, B. L. Miller, W. J. Jagust, and G. D. Rabinovici, “Prospective longitudinal atrophy in Alzheimer’s disease correlates with the intensity and topography of baseline tau-PET,” Sci. Transl. Med. 12(524), eaau5732 (2020).
[Crossref]

M. Scholl, S. N. Lockhart, D. R. Schonhaut, J. P. O’Neil, M. Janabi, R. Ossenkoppele, S. L. Baker, J. W. Vogel, J. Faria, H. D. Schwimmer, G. D. Rabinovici, and W. J. Jagust, “PET Imaging of Tau Deposition in the Aging Human Brain,” Neuron 89(5), 971–982 (2016).
[Crossref]

Obermüller, U.

P. Füger, J. K. Hefendehl, K. Veeraraghavalu, A.-C. Wendeln, C. Schlosser, U. Obermüller, B. M. Wegenast-Braun, J. J. Neher, P. Martus, S. Kohsaka, M. Thunemann, R. Feil, S. S. Sisodia, A. Skodras, and M. Jucker, “Microglia turnover with aging and in an Alzheimer's model via long-term in vivo single-cell imaging,” Nat. Neurosci. 20(10), 1371–1376 (2017).
[Crossref]

Oden, F.

H. Kroth, F. Oden, J. Molette, H. Schieferstein, F. Capotosti, A. Mueller, M. Berndt, H. Schmitt-Willich, V. Darmency, E. Gabellieri, C. Boudou, T. Juergens, Y. Varisco, E. Vokali, D. T. Hickman, G. Tamagnan, A. Pfeifer, L. Dinkelborg, A. Muhs, and A. Stephens, “Discovery and preclinical characterization of [(18)F]PI-2620, a next-generation tau PET tracer for the assessment of tau pathology in Alzheimer's disease and other tauopathies,” Eur. J. Nucl. Med. Mol. Imaging 46(10), 2178–2189 (2019).
[Crossref]

Ogasawara, A.

S. Sanabria Bohorquez, J. Marik, A. Ogasawara, J. N. Tinianow, H. S. Gill, O. Barret, G. Tamagnan, D. Alagille, G. Ayalon, P. Manser, T. Bengtsson, M. Ward, S. P. Williams, G. A. Kerchner, J. P. Seibyl, K. Marek, and R. M. Weimer, “[(18)F]GTP1 (Genentech Tau Probe 1), a radioligand for detecting neurofibrillary tangle tau pathology in Alzheimer's disease,” Eur. J. Nucl. Med. Mol. Imaging 46(10), 2077–2089 (2019).
[Crossref]

Ogawa, A.

E. D. Hostetler, A. M. Walji, Z. Zeng, P. Miller, I. Bennacef, C. Salinas, B. Connolly, L. Gantert, H. Haley, M. Holahan, M. Purcell, K. Riffel, T. G. Lohith, P. Coleman, A. Soriano, A. Ogawa, S. Xu, X. Zhang, E. Joshi, J. Della Rocca, D. Hesk, D. J. Schenk, and J. L. Evelhoch, ““Preclinical Characterization of 18F-MK-6240, a Promising PET Tracer for In Vivo Quantification of Human Neurofibrillary Tangles,” Journal of nuclear medicine : official publication,” J. Nuclear Medicine 57(10), 1599–1606 (2016).
[Crossref]

Okamura, N.

M. Maruyama, H. Shimada, T. Suhara, H. Shinotoh, B. Ji, J. Maeda, M. R. Zhang, J. Q. Trojanowski, V. M. Lee, M. Ono, K. Masamoto, H. Takano, N. Sahara, N. Iwata, N. Okamura, S. Furumoto, Y. Kudo, Q. Chang, T. C. Saido, A. Takashima, J. Lewis, M. K. Jang, I. Aoki, H. Ito, and M. Higuchi, “Imaging of tau pathology in a tauopathy mouse model and in Alzheimer patients compared to normal controls,” Neuron 79(6), 1094–1108 (2013).
[Crossref]

Ono, M.

R. Ni, B. Ji, M. Ono, N. Sahara, M. R. Zhang, I. Aoki, A. Nordberg, T. Suhara, and M. Higuchi, ““Comparative in-vitro and in-vivo quantifications of pathological tau deposits and their association with neurodegeneration in tauopathy mouse models,” Journal of nuclear medicine : official publication,” J. Nucl. Med. 59(6), 960–966 (2018).
[Crossref]

A. Ishikawa, M. Tokunaga, J. Maeda, T. Minamihisamatsu, M. Shimojo, H. Takuwa, M. Ono, R. Ni, S. Hirano, S. Kuwabara, B. Ji, M. R. Zhang, I. Aoki, T. Suhara, M. Higuchi, and N. Sahara, “In Vivo Visualization of Tau Accumulation, Microglial Activation, and Brain Atrophy in a Mouse Model of Tauopathy rTg4510,” J. Alzheimer’s Dis. 61(3), 1037–1052 (2018).
[Crossref]

N. Sahara, M. Shimojo, M. Ono, H. Takuwa, M. Febo, M. Higuchi, and T. Suhara, “In Vivo Tau Imaging for a Diagnostic Platform of Tauopathy Using the rTg4510 Mouse Line,” Front Neurol. 8, 663 (2017).
[Crossref]

M. Ono, N. Sahara, K. Kumata, B. Ji, R. Ni, S. Koga, D. W. Dickson, J. Q. Trojanowski, V. M.-Y. Lee, M. Yoshida, I. Hozumi, Y. Yoshiyama, J. C. v. Swieten, A. Nordberg, T. Suhara, M.-R. Zhang, and M. Higuchi, “Distinct binding of PET ligands PBB3 and AV-1451 to tau fibril strains in neurodegenerative tauopathies,” Brain 140, aww339 (2017).
[Crossref]

M. Maruyama, H. Shimada, T. Suhara, H. Shinotoh, B. Ji, J. Maeda, M. R. Zhang, J. Q. Trojanowski, V. M. Lee, M. Ono, K. Masamoto, H. Takano, N. Sahara, N. Iwata, N. Okamura, S. Furumoto, Y. Kudo, Q. Chang, T. C. Saido, A. Takashima, J. Lewis, M. K. Jang, I. Aoki, H. Ito, and M. Higuchi, “Imaging of tau pathology in a tauopathy mouse model and in Alzheimer patients compared to normal controls,” Neuron 79(6), 1094–1108 (2013).
[Crossref]

Orne, J.

K. SantaCruz, J. Lewis, T. Spires, J. Paulson, L. Kotilinek, M. Ingelsson, A. Guimaraes, M. DeTure, M. Ramsden, E. McGowan, C. Forster, M. Yue, J. Orne, C. Janus, A. Mariash, M. Kuskowski, B. Hyman, M. Hutton, and K. H. Ashe, “Tau Suppression in a Neurodegenerative Mouse Model Improves Memory Function,” Science 309(5733), 476–481 (2005).
[Crossref]

Ossenkoppele, R.

M. Scholl, S. N. Lockhart, D. R. Schonhaut, J. P. O’Neil, M. Janabi, R. Ossenkoppele, S. L. Baker, J. W. Vogel, J. Faria, H. D. Schwimmer, G. D. Rabinovici, and W. J. Jagust, “PET Imaging of Tau Deposition in the Aging Human Brain,” Neuron 89(5), 971–982 (2016).
[Crossref]

Papin, C.

A. Mueller, S. Bullich, O. Barret, J. Madonia, M. Berndt, C. Papin, A. Perrotin, N. Koglin, H. Kroth, A. Pfeifer, G. Tamagnan, J. P. Seibyl, K. Marek, S. de Santi, L. M. Dinkelborg, and A. W. Stephens, “Tau PET imaging with (18)F-PI-2620 in patients with Alzheimer's disease and healthy controls: a first-in-human study,” J. Nucl. Med. 61(6), 911–919 (2020).
[Crossref]

Papp, K.

K. A. Johnson, A. Schultz, R. A. Betensky, J. A. Becker, J. Sepulcre, D. Rentz, E. Mormino, J. Chhatwal, R. Amariglio, K. Papp, G. Marshall, M. Albers, S. Mauro, L. Pepin, J. Alverio, K. Judge, M. Philiossaint, T. Shoup, D. Yokell, B. Dickerson, T. Gomez-Isla, B. Hyman, N. Vasdev, and R. Sperling, “Tau positron emission tomographic imaging in aging and early Alzheimer disease,” Ann Neurol. 79(1), 110–119 (2016).
[Crossref]

Papp, K. V.

B. J. Hanseeuw, R. A. Betensky, H. I. L. Jacobs, A. P. Schultz, J. Sepulcre, J. A. Becker, D. M. O. Cosio, M. Farrell, Y. T. Quiroz, E. C. Mormino, R. F. Buckley, K. V. Papp, R. A. Amariglio, I. Dewachter, A. Ivanoiu, W. Huijbers, T. Hedden, G. A. Marshall, J. P. Chhatwal, D. M. Rentz, R. A. Sperling, and K. Johnson, “Association of Amyloid and Tau With Cognition in Preclinical Alzheimer Disease: A Longitudinal Study,” JAMA Neurol. 76(8), 915–924 (2019).
[Crossref]

Patel, T. K.

T. K. Patel, L. Habimana-Griffin, X. Gao, B. Xu, S. Achilefu, K. Alitalo, C. A. McKee, P. W. Sheehan, E. S. Musiek, C. Xiong, D. Coble, and D. M. Holtzman, “Dural lymphatics regulate clearance of extracellular tau from the CNS,” Mol. Neurodegener. 14(1), 11 (2019).
[Crossref]

Paul Murphy, M.

J. Lewis, E. McGowan, J. Rockwood, H. Melrose, P. Nacharaju, M. Van Slegtenhorst, K. Gwinn-Hardy, M. Paul Murphy, M. Baker, X. Yu, K. Duff, J. Hardy, A. Corral, W. L. Lin, S. H. Yen, D. W. Dickson, P. Davies, and M. Hutton, “Neurofibrillary tangles, amyotrophy and progressive motor disturbance in mice expressing mutant (P301L) tau protein,” Nat. Genet. 25(4), 402–405 (2000).
[Crossref]

Paulson, J.

K. SantaCruz, J. Lewis, T. Spires, J. Paulson, L. Kotilinek, M. Ingelsson, A. Guimaraes, M. DeTure, M. Ramsden, E. McGowan, C. Forster, M. Yue, J. Orne, C. Janus, A. Mariash, M. Kuskowski, B. Hyman, M. Hutton, and K. H. Ashe, “Tau Suppression in a Neurodegenerative Mouse Model Improves Memory Function,” Science 309(5733), 476–481 (2005).
[Crossref]

Pepin, L.

K. A. Johnson, A. Schultz, R. A. Betensky, J. A. Becker, J. Sepulcre, D. Rentz, E. Mormino, J. Chhatwal, R. Amariglio, K. Papp, G. Marshall, M. Albers, S. Mauro, L. Pepin, J. Alverio, K. Judge, M. Philiossaint, T. Shoup, D. Yokell, B. Dickerson, T. Gomez-Isla, B. Hyman, N. Vasdev, and R. Sperling, “Tau positron emission tomographic imaging in aging and early Alzheimer disease,” Ann Neurol. 79(1), 110–119 (2016).
[Crossref]

Perrotin, A.

A. Mueller, S. Bullich, O. Barret, J. Madonia, M. Berndt, C. Papin, A. Perrotin, N. Koglin, H. Kroth, A. Pfeifer, G. Tamagnan, J. P. Seibyl, K. Marek, S. de Santi, L. M. Dinkelborg, and A. W. Stephens, “Tau PET imaging with (18)F-PI-2620 in patients with Alzheimer's disease and healthy controls: a first-in-human study,” J. Nucl. Med. 61(6), 911–919 (2020).
[Crossref]

Perry, D. C.

R. La Joie, A. V. Visani, S. L. Baker, J. A. Brown, V. Bourakova, J. Cha, K. Chaudhary, L. Edwards, L. Iaccarino, M. Janabi, O. H. Lesman-Segev, Z. A. Miller, D. C. Perry, J. P. O’Neil, J. Pham, J. C. Rojas, H. J. Rosen, W. W. Seeley, R. M. Tsai, B. L. Miller, W. J. Jagust, and G. D. Rabinovici, “Prospective longitudinal atrophy in Alzheimer’s disease correlates with the intensity and topography of baseline tau-PET,” Sci. Transl. Med. 12(524), eaau5732 (2020).
[Crossref]

Peter, M.

J. A. Gerez, N. C. Prymaczok, E. Rockenstein, U. S. Herrmann, P. Schwarz, A. Adame, R. I. Enchev, T. Courtheoux, P. J. Boersema, R. Riek, M. Peter, A. Aguzzi, E. Masliah, and P. Picotti, “A cullin-RING ubiquitin ligase targets exogenous alpha-synuclein and inhibits Lewy body-like pathology,” Sci. Transl. Med. 11(495), eaau6722 (2019).
[Crossref]

Peters, F.

P. Marinkovic, S. Blumenstock, P. M. Goltstein, V. Korzhova, F. Peters, A. Knebl, and J. Herms, “In vivo imaging reveals reduced activity of neuronal circuits in a mouse tauopathy model,” Brain 142(4), 1051–1062 (2019).
[Crossref]

Pfeifer, A.

A. Mueller, S. Bullich, O. Barret, J. Madonia, M. Berndt, C. Papin, A. Perrotin, N. Koglin, H. Kroth, A. Pfeifer, G. Tamagnan, J. P. Seibyl, K. Marek, S. de Santi, L. M. Dinkelborg, and A. W. Stephens, “Tau PET imaging with (18)F-PI-2620 in patients with Alzheimer's disease and healthy controls: a first-in-human study,” J. Nucl. Med. 61(6), 911–919 (2020).
[Crossref]

H. Kroth, F. Oden, J. Molette, H. Schieferstein, F. Capotosti, A. Mueller, M. Berndt, H. Schmitt-Willich, V. Darmency, E. Gabellieri, C. Boudou, T. Juergens, Y. Varisco, E. Vokali, D. T. Hickman, G. Tamagnan, A. Pfeifer, L. Dinkelborg, A. Muhs, and A. Stephens, “Discovery and preclinical characterization of [(18)F]PI-2620, a next-generation tau PET tracer for the assessment of tau pathology in Alzheimer's disease and other tauopathies,” Eur. J. Nucl. Med. Mol. Imaging 46(10), 2178–2189 (2019).
[Crossref]

Pham, J.

R. La Joie, A. V. Visani, S. L. Baker, J. A. Brown, V. Bourakova, J. Cha, K. Chaudhary, L. Edwards, L. Iaccarino, M. Janabi, O. H. Lesman-Segev, Z. A. Miller, D. C. Perry, J. P. O’Neil, J. Pham, J. C. Rojas, H. J. Rosen, W. W. Seeley, R. M. Tsai, B. L. Miller, W. J. Jagust, and G. D. Rabinovici, “Prospective longitudinal atrophy in Alzheimer’s disease correlates with the intensity and topography of baseline tau-PET,” Sci. Transl. Med. 12(524), eaau5732 (2020).
[Crossref]

Philiossaint, M.

K. A. Johnson, A. Schultz, R. A. Betensky, J. A. Becker, J. Sepulcre, D. Rentz, E. Mormino, J. Chhatwal, R. Amariglio, K. Papp, G. Marshall, M. Albers, S. Mauro, L. Pepin, J. Alverio, K. Judge, M. Philiossaint, T. Shoup, D. Yokell, B. Dickerson, T. Gomez-Isla, B. Hyman, N. Vasdev, and R. Sperling, “Tau positron emission tomographic imaging in aging and early Alzheimer disease,” Ann Neurol. 79(1), 110–119 (2016).
[Crossref]

Picotti, P.

J. A. Gerez, N. C. Prymaczok, E. Rockenstein, U. S. Herrmann, P. Schwarz, A. Adame, R. I. Enchev, T. Courtheoux, P. J. Boersema, R. Riek, M. Peter, A. Aguzzi, E. Masliah, and P. Picotti, “A cullin-RING ubiquitin ligase targets exogenous alpha-synuclein and inhibits Lewy body-like pathology,” Sci. Transl. Med. 11(495), eaau6722 (2019).
[Crossref]

Pitstick, R.

A. de Calignon, L. M. Fox, R. Pitstick, G. A. Carlson, B. J. Bacskai, T. L. Spires-Jones, and B. T. Hyman, “Caspase activation precedes and leads to tangles,” Nature 464(7292), 1201–1204 (2010).
[Crossref]

Priller, J.

J. Klohs, N. Baeva, J. Steinbrink, R. Bourayou, C. Boettcher, G. Royl, D. Megow, U. Dirnagl, J. Priller, and A. Wunder, “In vivo near-infrared fluorescence imaging of matrix metalloproteinase activity after cerebral ischemia,” J. Cereb. Blood Flow Metab. 29(7), 1284–1292 (2009).
[Crossref]

Prokop, S.

A. Aslund, C. J. Sigurdson, T. Klingstedt, S. Grathwohl, T. Bolmont, D. L. Dickstein, E. Glimsdal, S. Prokop, M. Lindgren, P. Konradsson, D. M. Holtzman, P. R. Hof, F. L. Heppner, S. Gandy, M. Jucker, A. Aguzzi, P. Hammarström, and K. P. Nilsson, “Novel pentameric thiophene derivatives for in vitro and in vivo optical imaging of a plethora of protein aggregates in cerebral amyloidoses,” ACS Chem. Biol. 4(8), 673–684 (2009).
[Crossref]

Prymaczok, N. C.

J. A. Gerez, N. C. Prymaczok, E. Rockenstein, U. S. Herrmann, P. Schwarz, A. Adame, R. I. Enchev, T. Courtheoux, P. J. Boersema, R. Riek, M. Peter, A. Aguzzi, E. Masliah, and P. Picotti, “A cullin-RING ubiquitin ligase targets exogenous alpha-synuclein and inhibits Lewy body-like pathology,” Sci. Transl. Med. 11(495), eaau6722 (2019).
[Crossref]

Purcell, M.

E. D. Hostetler, A. M. Walji, Z. Zeng, P. Miller, I. Bennacef, C. Salinas, B. Connolly, L. Gantert, H. Haley, M. Holahan, M. Purcell, K. Riffel, T. G. Lohith, P. Coleman, A. Soriano, A. Ogawa, S. Xu, X. Zhang, E. Joshi, J. Della Rocca, D. Hesk, D. J. Schenk, and J. L. Evelhoch, ““Preclinical Characterization of 18F-MK-6240, a Promising PET Tracer for In Vivo Quantification of Human Neurofibrillary Tangles,” Journal of nuclear medicine : official publication,” J. Nuclear Medicine 57(10), 1599–1606 (2016).
[Crossref]

Quiroz, Y. T.

B. J. Hanseeuw, R. A. Betensky, H. I. L. Jacobs, A. P. Schultz, J. Sepulcre, J. A. Becker, D. M. O. Cosio, M. Farrell, Y. T. Quiroz, E. C. Mormino, R. F. Buckley, K. V. Papp, R. A. Amariglio, I. Dewachter, A. Ivanoiu, W. Huijbers, T. Hedden, G. A. Marshall, J. P. Chhatwal, D. M. Rentz, R. A. Sperling, and K. Johnson, “Association of Amyloid and Tau With Cognition in Preclinical Alzheimer Disease: A Longitudinal Study,” JAMA Neurol. 76(8), 915–924 (2019).
[Crossref]

Rabinovici, G. D.

R. La Joie, A. V. Visani, S. L. Baker, J. A. Brown, V. Bourakova, J. Cha, K. Chaudhary, L. Edwards, L. Iaccarino, M. Janabi, O. H. Lesman-Segev, Z. A. Miller, D. C. Perry, J. P. O’Neil, J. Pham, J. C. Rojas, H. J. Rosen, W. W. Seeley, R. M. Tsai, B. L. Miller, W. J. Jagust, and G. D. Rabinovici, “Prospective longitudinal atrophy in Alzheimer’s disease correlates with the intensity and topography of baseline tau-PET,” Sci. Transl. Med. 12(524), eaau5732 (2020).
[Crossref]

M. Scholl, S. N. Lockhart, D. R. Schonhaut, J. P. O’Neil, M. Janabi, R. Ossenkoppele, S. L. Baker, J. W. Vogel, J. Faria, H. D. Schwimmer, G. D. Rabinovici, and W. J. Jagust, “PET Imaging of Tau Deposition in the Aging Human Brain,” Neuron 89(5), 971–982 (2016).
[Crossref]

Rajamohamedsait, H. B.

S. Krishnaswamy, Y. Lin, W. J. Rajamohamedsait, H. B. Rajamohamedsait, P. Krishnamurthy, and E. M. Sigurdsson, “Antibody-derived in vivo imaging of tau pathology,” J. Neuroscience 34(50), 16835–16850 (2014).
[Crossref]

Rajamohamedsait, W. J.

S. Krishnaswamy, Y. Lin, W. J. Rajamohamedsait, H. B. Rajamohamedsait, P. Krishnamurthy, and E. M. Sigurdsson, “Antibody-derived in vivo imaging of tau pathology,” J. Neuroscience 34(50), 16835–16850 (2014).
[Crossref]

Ramos, E. M.

E. J. Kim, J. L. Hwang, S. E. Gaus, A. L. Nana, J. Deng, J. A. Brown, S. Spina, M. J. Lee, E. M. Ramos, L. T. Grinberg, J. H. Kramer, A. L. Boxer, M. L. Gorno-Tempini, H. J. Rosen, B. L. Miller, and W. W. Seeley, “Evidence of corticofugal tau spreading in patients with frontotemporal dementia,” Acta Neuropathol. 139(1), 27–43 (2020).
[Crossref]

Ramsden, M.

K. SantaCruz, J. Lewis, T. Spires, J. Paulson, L. Kotilinek, M. Ingelsson, A. Guimaraes, M. DeTure, M. Ramsden, E. McGowan, C. Forster, M. Yue, J. Orne, C. Janus, A. Mariash, M. Kuskowski, B. Hyman, M. Hutton, and K. H. Ashe, “Tau Suppression in a Neurodegenerative Mouse Model Improves Memory Function,” Science 309(5733), 476–481 (2005).
[Crossref]

Razansky, D.

Z. Chen, B. Mc Larney, J. Rebling, X. L. Deán-Ben, Q. Zhou, S. Gottschalk, and D. Razansky, “High-Speed Large-Field Multifocal Illumination Fluorescence Microscopy,” Laser Photonics Rev. 14, 1900070 (2020).
[Crossref]

S. Gottschalk, O. Degtyaruk, B. Mc Larney, J. Rebling, M. A. Hutter, X. L. Deán-Ben, S. Shoham, and D. Razansky, “Rapid volumetric optoacoustic imaging of neural dynamics across the mouse brain,” Nat. Biomed. Eng. 3(5), 392–401 (2019).
[Crossref]

R. Ni, Z. Chen, G. Shi, A. Villois, Q. Zhou, P. Arosio, R. M. Nitsch, P. R. Nilsson, J. Klohs, and D. Razansky, “Transcranial in vivo detection of Aβ at single plaque resolution with large-field multifocal illumination fluorescence microscopy,” bioRxiv, 2020.2002.2001.929844 (2020).

R. Ni, X. L. Dean-Ben, D. Kirschenbaum, M. Rudin, Z. Chen, A. Crimi, F. Voigt, P. R. Nilsson, F. Helmchen, R. M. Nitsch, A. Aguzzi, D. Razansky, and J. Klohs, “Whole brain optoacoustic tomography reveals strain-specific regional beta-amyloid densities in Alzheimer`s disease amyloidosis models,” bioRxiv, DOI: 10.1101/2020.1102.1125.964064 (2020).

Rebling, J.

Z. Chen, B. Mc Larney, J. Rebling, X. L. Deán-Ben, Q. Zhou, S. Gottschalk, and D. Razansky, “High-Speed Large-Field Multifocal Illumination Fluorescence Microscopy,” Laser Photonics Rev. 14, 1900070 (2020).
[Crossref]

S. Gottschalk, O. Degtyaruk, B. Mc Larney, J. Rebling, M. A. Hutter, X. L. Deán-Ben, S. Shoham, and D. Razansky, “Rapid volumetric optoacoustic imaging of neural dynamics across the mouse brain,” Nat. Biomed. Eng. 3(5), 392–401 (2019).
[Crossref]

Ren, W.

R. Ni, M. Vaas, W. Ren, and J. Klohs, “Non-invasive detection of acute cerebral hypoxia and subsequent matrix-metalloproteinase activity in a mouse model of cerebral ischemia using multispectral-optoacoustic-tomography,” Neurophotonics 5(1), 015005 (2018).
[Crossref]

Rentz, D.

K. A. Johnson, A. Schultz, R. A. Betensky, J. A. Becker, J. Sepulcre, D. Rentz, E. Mormino, J. Chhatwal, R. Amariglio, K. Papp, G. Marshall, M. Albers, S. Mauro, L. Pepin, J. Alverio, K. Judge, M. Philiossaint, T. Shoup, D. Yokell, B. Dickerson, T. Gomez-Isla, B. Hyman, N. Vasdev, and R. Sperling, “Tau positron emission tomographic imaging in aging and early Alzheimer disease,” Ann Neurol. 79(1), 110–119 (2016).
[Crossref]

Rentz, D. M.

B. J. Hanseeuw, R. A. Betensky, H. I. L. Jacobs, A. P. Schultz, J. Sepulcre, J. A. Becker, D. M. O. Cosio, M. Farrell, Y. T. Quiroz, E. C. Mormino, R. F. Buckley, K. V. Papp, R. A. Amariglio, I. Dewachter, A. Ivanoiu, W. Huijbers, T. Hedden, G. A. Marshall, J. P. Chhatwal, D. M. Rentz, R. A. Sperling, and K. Johnson, “Association of Amyloid and Tau With Cognition in Preclinical Alzheimer Disease: A Longitudinal Study,” JAMA Neurol. 76(8), 915–924 (2019).
[Crossref]

Rhoades, E.

C. H. Lo, C. K. Lim, Z. Ding, S. P. Wickramasinghe, A. R. Braun, K. H. Ashe, E. Rhoades, D. D. Thomas, and J. N. Sachs, “Targeting the ensemble of heterogeneous tau oligomers in cells: A novel small molecule screening platform for tauopathies,” Alzheimer’s & Dementia 15(11), 1489–1502 (2019).
[Crossref]

Riek, R.

B. M. Burmann, J. A. Gerez, I. Matecko-Burmann, S. Campioni, P. Kumari, D. Ghosh, A. Mazur, E. E. Aspholm, D. Sulskis, M. Wawrzyniuk, T. Bock, A. Schmidt, S. G. D. Rudiger, R. Riek, and S. Hiller, “Regulation of alpha-synuclein by chaperones in mammalian cells,” Nature 577(7788), 127–132 (2020).
[Crossref]

J. A. Gerez, N. C. Prymaczok, E. Rockenstein, U. S. Herrmann, P. Schwarz, A. Adame, R. I. Enchev, T. Courtheoux, P. J. Boersema, R. Riek, M. Peter, A. Aguzzi, E. Masliah, and P. Picotti, “A cullin-RING ubiquitin ligase targets exogenous alpha-synuclein and inhibits Lewy body-like pathology,” Sci. Transl. Med. 11(495), eaau6722 (2019).
[Crossref]

Riffel, K.

E. D. Hostetler, A. M. Walji, Z. Zeng, P. Miller, I. Bennacef, C. Salinas, B. Connolly, L. Gantert, H. Haley, M. Holahan, M. Purcell, K. Riffel, T. G. Lohith, P. Coleman, A. Soriano, A. Ogawa, S. Xu, X. Zhang, E. Joshi, J. Della Rocca, D. Hesk, D. J. Schenk, and J. L. Evelhoch, ““Preclinical Characterization of 18F-MK-6240, a Promising PET Tracer for In Vivo Quantification of Human Neurofibrillary Tangles,” Journal of nuclear medicine : official publication,” J. Nuclear Medicine 57(10), 1599–1606 (2016).
[Crossref]

Rigo, F.

K. M. Schoch, S. L. DeVos, R. L. Miller, S. J. Chun, M. Norrbom, D. F. Wozniak, H. N. Dawson, C. F. Bennett, F. Rigo, and T. M. Miller, “Increased 4R-Tau Induces Pathological Changes in a Human-Tau Mouse Model,” Neuron 90(5), 941–947 (2016).
[Crossref]

Rockenstein, E.

J. A. Gerez, N. C. Prymaczok, E. Rockenstein, U. S. Herrmann, P. Schwarz, A. Adame, R. I. Enchev, T. Courtheoux, P. J. Boersema, R. Riek, M. Peter, A. Aguzzi, E. Masliah, and P. Picotti, “A cullin-RING ubiquitin ligase targets exogenous alpha-synuclein and inhibits Lewy body-like pathology,” Sci. Transl. Med. 11(495), eaau6722 (2019).
[Crossref]

Rockwood, J.

J. Lewis, E. McGowan, J. Rockwood, H. Melrose, P. Nacharaju, M. Van Slegtenhorst, K. Gwinn-Hardy, M. Paul Murphy, M. Baker, X. Yu, K. Duff, J. Hardy, A. Corral, W. L. Lin, S. H. Yen, D. W. Dickson, P. Davies, and M. Hutton, “Neurofibrillary tangles, amyotrophy and progressive motor disturbance in mice expressing mutant (P301L) tau protein,” Nat. Genet. 25(4), 402–405 (2000).
[Crossref]

Rojas, J. C.

R. La Joie, A. V. Visani, S. L. Baker, J. A. Brown, V. Bourakova, J. Cha, K. Chaudhary, L. Edwards, L. Iaccarino, M. Janabi, O. H. Lesman-Segev, Z. A. Miller, D. C. Perry, J. P. O’Neil, J. Pham, J. C. Rojas, H. J. Rosen, W. W. Seeley, R. M. Tsai, B. L. Miller, W. J. Jagust, and G. D. Rabinovici, “Prospective longitudinal atrophy in Alzheimer’s disease correlates with the intensity and topography of baseline tau-PET,” Sci. Transl. Med. 12(524), eaau5732 (2020).
[Crossref]

Rosen, H. J.

R. La Joie, A. V. Visani, S. L. Baker, J. A. Brown, V. Bourakova, J. Cha, K. Chaudhary, L. Edwards, L. Iaccarino, M. Janabi, O. H. Lesman-Segev, Z. A. Miller, D. C. Perry, J. P. O’Neil, J. Pham, J. C. Rojas, H. J. Rosen, W. W. Seeley, R. M. Tsai, B. L. Miller, W. J. Jagust, and G. D. Rabinovici, “Prospective longitudinal atrophy in Alzheimer’s disease correlates with the intensity and topography of baseline tau-PET,” Sci. Transl. Med. 12(524), eaau5732 (2020).
[Crossref]

E. J. Kim, J. L. Hwang, S. E. Gaus, A. L. Nana, J. Deng, J. A. Brown, S. Spina, M. J. Lee, E. M. Ramos, L. T. Grinberg, J. H. Kramer, A. L. Boxer, M. L. Gorno-Tempini, H. J. Rosen, B. L. Miller, and W. W. Seeley, “Evidence of corticofugal tau spreading in patients with frontotemporal dementia,” Acta Neuropathol. 139(1), 27–43 (2020).
[Crossref]

Rowe, C. C.

V. L. Villemagne, V. Dore, S. C. Burnham, C. L. Masters, and C. C. Rowe, “Imaging tau and amyloid-beta proteinopathies in Alzheimer disease and other conditions,” Nat. Rev. Neurol. 14(4), 225–236 (2018).
[Crossref]

Royl, G.

J. Klohs, N. Baeva, J. Steinbrink, R. Bourayou, C. Boettcher, G. Royl, D. Megow, U. Dirnagl, J. Priller, and A. Wunder, “In vivo near-infrared fluorescence imaging of matrix metalloproteinase activity after cerebral ischemia,” J. Cereb. Blood Flow Metab. 29(7), 1284–1292 (2009).
[Crossref]

Ruchinskas, A. J.

S. K. Kaufman, D. W. Sanders, T. L. Thomas, A. J. Ruchinskas, J. Vaquer-Alicea, A. M. Sharma, T. M. Miller, and M. I. Diamond, “Tau Prion Strains Dictate Patterns of Cell Pathology, Progression Rate, and Regional Vulnerability In Vivo,” Neuron 92(4), 796–812 (2016).
[Crossref]

Rudiger, S. G. D.

B. M. Burmann, J. A. Gerez, I. Matecko-Burmann, S. Campioni, P. Kumari, D. Ghosh, A. Mazur, E. E. Aspholm, D. Sulskis, M. Wawrzyniuk, T. Bock, A. Schmidt, S. G. D. Rudiger, R. Riek, and S. Hiller, “Regulation of alpha-synuclein by chaperones in mammalian cells,” Nature 577(7788), 127–132 (2020).
[Crossref]

Rudin, M.

M. Hintersteiner, A. Enz, P. Frey, A. L. Jaton, W. Kinzy, R. Kneuer, U. Neumann, M. Rudin, M. Staufenbiel, M. Stoeckli, K. H. Wiederhold, and H. U. Gremlich, “In vivo detection of amyloid-beta deposits by near-infrared imaging using an oxazine-derivative probe,” Nat. Biotechnol. 23(5), 577–583 (2005).
[Crossref]

R. Ni, X. L. Dean-Ben, D. Kirschenbaum, M. Rudin, Z. Chen, A. Crimi, F. Voigt, P. R. Nilsson, F. Helmchen, R. M. Nitsch, A. Aguzzi, D. Razansky, and J. Klohs, “Whole brain optoacoustic tomography reveals strain-specific regional beta-amyloid densities in Alzheimer`s disease amyloidosis models,” bioRxiv, DOI: 10.1101/2020.1102.1125.964064 (2020).

Rudinskiy, N.

K. V. Kuchibhotla, S. Wegmann, K. J. Kopeikina, J. Hawkes, N. Rudinskiy, M. L. Andermann, T. L. Spires-Jones, B. J. Bacskai, and B. T. Hyman, “Neurofibrillary tangle-bearing neurons are functionally integrated in cortical circuits in vivo,” Proc. Natl. Acad. Sci. 111(1), 510–514 (2014).
[Crossref]

Sachs, J. N.

C. H. Lo, C. K. Lim, Z. Ding, S. P. Wickramasinghe, A. R. Braun, K. H. Ashe, E. Rhoades, D. D. Thomas, and J. N. Sachs, “Targeting the ensemble of heterogeneous tau oligomers in cells: A novel small molecule screening platform for tauopathies,” Alzheimer’s & Dementia 15(11), 1489–1502 (2019).
[Crossref]

Sahara, N.

S. Hashimoto, Y. Matsuba, N. Kamano, N. Mihira, N. Sahara, J. Takano, S. I. Muramatsu, T. C. Saido, and T. Saito, “Tau binding protein CAPON induces tau aggregation and neurodegeneration,” Nat. Commun. 10(1), 2394 (2019).
[Crossref]

R. Ni, B. Ji, M. Ono, N. Sahara, M. R. Zhang, I. Aoki, A. Nordberg, T. Suhara, and M. Higuchi, ““Comparative in-vitro and in-vivo quantifications of pathological tau deposits and their association with neurodegeneration in tauopathy mouse models,” Journal of nuclear medicine : official publication,” J. Nucl. Med. 59(6), 960–966 (2018).
[Crossref]

A. Ishikawa, M. Tokunaga, J. Maeda, T. Minamihisamatsu, M. Shimojo, H. Takuwa, M. Ono, R. Ni, S. Hirano, S. Kuwabara, B. Ji, M. R. Zhang, I. Aoki, T. Suhara, M. Higuchi, and N. Sahara, “In Vivo Visualization of Tau Accumulation, Microglial Activation, and Brain Atrophy in a Mouse Model of Tauopathy rTg4510,” J. Alzheimer’s Dis. 61(3), 1037–1052 (2018).
[Crossref]

N. Sahara, M. Shimojo, M. Ono, H. Takuwa, M. Febo, M. Higuchi, and T. Suhara, “In Vivo Tau Imaging for a Diagnostic Platform of Tauopathy Using the rTg4510 Mouse Line,” Front Neurol. 8, 663 (2017).
[Crossref]

M. Ono, N. Sahara, K. Kumata, B. Ji, R. Ni, S. Koga, D. W. Dickson, J. Q. Trojanowski, V. M.-Y. Lee, M. Yoshida, I. Hozumi, Y. Yoshiyama, J. C. v. Swieten, A. Nordberg, T. Suhara, M.-R. Zhang, and M. Higuchi, “Distinct binding of PET ligands PBB3 and AV-1451 to tau fibril strains in neurodegenerative tauopathies,” Brain 140, aww339 (2017).
[Crossref]

M. Maruyama, H. Shimada, T. Suhara, H. Shinotoh, B. Ji, J. Maeda, M. R. Zhang, J. Q. Trojanowski, V. M. Lee, M. Ono, K. Masamoto, H. Takano, N. Sahara, N. Iwata, N. Okamura, S. Furumoto, Y. Kudo, Q. Chang, T. C. Saido, A. Takashima, J. Lewis, M. K. Jang, I. Aoki, H. Ito, and M. Higuchi, “Imaging of tau pathology in a tauopathy mouse model and in Alzheimer patients compared to normal controls,” Neuron 79(6), 1094–1108 (2013).
[Crossref]

Saido, T. C.

S. Hashimoto, Y. Matsuba, N. Kamano, N. Mihira, N. Sahara, J. Takano, S. I. Muramatsu, T. C. Saido, and T. Saito, “Tau binding protein CAPON induces tau aggregation and neurodegeneration,” Nat. Commun. 10(1), 2394 (2019).
[Crossref]

M. Maruyama, H. Shimada, T. Suhara, H. Shinotoh, B. Ji, J. Maeda, M. R. Zhang, J. Q. Trojanowski, V. M. Lee, M. Ono, K. Masamoto, H. Takano, N. Sahara, N. Iwata, N. Okamura, S. Furumoto, Y. Kudo, Q. Chang, T. C. Saido, A. Takashima, J. Lewis, M. K. Jang, I. Aoki, H. Ito, and M. Higuchi, “Imaging of tau pathology in a tauopathy mouse model and in Alzheimer patients compared to normal controls,” Neuron 79(6), 1094–1108 (2013).
[Crossref]

Y. Yoshiyama, M. Higuchi, B. Zhang, S. M. Huang, N. Iwata, T. C. Saido, J. Maeda, T. Suhara, J. Q. Trojanowski, and V. M. Lee, “Synapse loss and microglial activation precede tangles in a P301S tauopathy mouse model,” Neuron 53(3), 337–351 (2007).
[Crossref]

Saito, T.

S. Hashimoto, Y. Matsuba, N. Kamano, N. Mihira, N. Sahara, J. Takano, S. I. Muramatsu, T. C. Saido, and T. Saito, “Tau binding protein CAPON induces tau aggregation and neurodegeneration,” Nat. Commun. 10(1), 2394 (2019).
[Crossref]

Salinas, C.

E. D. Hostetler, A. M. Walji, Z. Zeng, P. Miller, I. Bennacef, C. Salinas, B. Connolly, L. Gantert, H. Haley, M. Holahan, M. Purcell, K. Riffel, T. G. Lohith, P. Coleman, A. Soriano, A. Ogawa, S. Xu, X. Zhang, E. Joshi, J. Della Rocca, D. Hesk, D. J. Schenk, and J. L. Evelhoch, ““Preclinical Characterization of 18F-MK-6240, a Promising PET Tracer for In Vivo Quantification of Human Neurofibrillary Tangles,” Journal of nuclear medicine : official publication,” J. Nuclear Medicine 57(10), 1599–1606 (2016).
[Crossref]

Sanabria Bohorquez, S.

S. Sanabria Bohorquez, J. Marik, A. Ogasawara, J. N. Tinianow, H. S. Gill, O. Barret, G. Tamagnan, D. Alagille, G. Ayalon, P. Manser, T. Bengtsson, M. Ward, S. P. Williams, G. A. Kerchner, J. P. Seibyl, K. Marek, and R. M. Weimer, “[(18)F]GTP1 (Genentech Tau Probe 1), a radioligand for detecting neurofibrillary tangle tau pathology in Alzheimer's disease,” Eur. J. Nucl. Med. Mol. Imaging 46(10), 2077–2089 (2019).
[Crossref]

Sanders, D. W.

S. K. Kaufman, D. W. Sanders, T. L. Thomas, A. J. Ruchinskas, J. Vaquer-Alicea, A. M. Sharma, T. M. Miller, and M. I. Diamond, “Tau Prion Strains Dictate Patterns of Cell Pathology, Progression Rate, and Regional Vulnerability In Vivo,” Neuron 92(4), 796–812 (2016).
[Crossref]

SantaCruz, K.

K. SantaCruz, J. Lewis, T. Spires, J. Paulson, L. Kotilinek, M. Ingelsson, A. Guimaraes, M. DeTure, M. Ramsden, E. McGowan, C. Forster, M. Yue, J. Orne, C. Janus, A. Mariash, M. Kuskowski, B. Hyman, M. Hutton, and K. H. Ashe, “Tau Suppression in a Neurodegenerative Mouse Model Improves Memory Function,” Science 309(5733), 476–481 (2005).
[Crossref]

Sarmiento, J.

C. A. Lasagna-Reeves, D. L. Castillo-Carranza, U. Sengupta, J. Sarmiento, J. Troncoso, G. R. Jackson, and R. Kayed, “Identification of oligomers at early stages of tau aggregation in Alzheimer's disease,” FASEB J. 26(5), 1946–1959 (2012).
[Crossref]

Schellenberg, G. D.

Z. He, J. D. McBride, H. Xu, L. Changolkar, S. J. Kim, B. Zhang, S. Narasimhan, G. S. Gibbons, J. L. Guo, M. Kozak, G. D. Schellenberg, J. Q. Trojanowski, and V. M. Lee, “Transmission of tauopathy strains is independent of their isoform composition,” Nat. Commun. 11(1), 7 (2020).
[Crossref]

Schenk, D. J.

E. D. Hostetler, A. M. Walji, Z. Zeng, P. Miller, I. Bennacef, C. Salinas, B. Connolly, L. Gantert, H. Haley, M. Holahan, M. Purcell, K. Riffel, T. G. Lohith, P. Coleman, A. Soriano, A. Ogawa, S. Xu, X. Zhang, E. Joshi, J. Della Rocca, D. Hesk, D. J. Schenk, and J. L. Evelhoch, ““Preclinical Characterization of 18F-MK-6240, a Promising PET Tracer for In Vivo Quantification of Human Neurofibrillary Tangles,” Journal of nuclear medicine : official publication,” J. Nuclear Medicine 57(10), 1599–1606 (2016).
[Crossref]

Scheres, S. H. W.

A. W. P. Fitzpatrick, B. Falcon, S. He, A. G. Murzin, G. Murshudov, H. J. Garringer, R. A. Crowther, B. Ghetti, M. Goedert, and S. H. W. Scheres, “Cryo-EM structures of tau filaments from Alzheimer's disease,” Nature 547(7662), 185–190 (2017).
[Crossref]

Schieferstein, H.

H. Kroth, F. Oden, J. Molette, H. Schieferstein, F. Capotosti, A. Mueller, M. Berndt, H. Schmitt-Willich, V. Darmency, E. Gabellieri, C. Boudou, T. Juergens, Y. Varisco, E. Vokali, D. T. Hickman, G. Tamagnan, A. Pfeifer, L. Dinkelborg, A. Muhs, and A. Stephens, “Discovery and preclinical characterization of [(18)F]PI-2620, a next-generation tau PET tracer for the assessment of tau pathology in Alzheimer's disease and other tauopathies,” Eur. J. Nucl. Med. Mol. Imaging 46(10), 2178–2189 (2019).
[Crossref]

Schlosser, C.

P. Füger, J. K. Hefendehl, K. Veeraraghavalu, A.-C. Wendeln, C. Schlosser, U. Obermüller, B. M. Wegenast-Braun, J. J. Neher, P. Martus, S. Kohsaka, M. Thunemann, R. Feil, S. S. Sisodia, A. Skodras, and M. Jucker, “Microglia turnover with aging and in an Alzheimer's model via long-term in vivo single-cell imaging,” Nat. Neurosci. 20(10), 1371–1376 (2017).
[Crossref]

Schmidt, A.

B. M. Burmann, J. A. Gerez, I. Matecko-Burmann, S. Campioni, P. Kumari, D. Ghosh, A. Mazur, E. E. Aspholm, D. Sulskis, M. Wawrzyniuk, T. Bock, A. Schmidt, S. G. D. Rudiger, R. Riek, and S. Hiller, “Regulation of alpha-synuclein by chaperones in mammalian cells,” Nature 577(7788), 127–132 (2020).
[Crossref]

Schmitt-Willich, H.

H. Kroth, F. Oden, J. Molette, H. Schieferstein, F. Capotosti, A. Mueller, M. Berndt, H. Schmitt-Willich, V. Darmency, E. Gabellieri, C. Boudou, T. Juergens, Y. Varisco, E. Vokali, D. T. Hickman, G. Tamagnan, A. Pfeifer, L. Dinkelborg, A. Muhs, and A. Stephens, “Discovery and preclinical characterization of [(18)F]PI-2620, a next-generation tau PET tracer for the assessment of tau pathology in Alzheimer's disease and other tauopathies,” Eur. J. Nucl. Med. Mol. Imaging 46(10), 2178–2189 (2019).
[Crossref]

Schoch, K. M.

K. M. Schoch, S. L. DeVos, R. L. Miller, S. J. Chun, M. Norrbom, D. F. Wozniak, H. N. Dawson, C. F. Bennett, F. Rigo, and T. M. Miller, “Increased 4R-Tau Induces Pathological Changes in a Human-Tau Mouse Model,” Neuron 90(5), 941–947 (2016).
[Crossref]

Scholl, M.

M. Scholl, S. N. Lockhart, D. R. Schonhaut, J. P. O’Neil, M. Janabi, R. Ossenkoppele, S. L. Baker, J. W. Vogel, J. Faria, H. D. Schwimmer, G. D. Rabinovici, and W. J. Jagust, “PET Imaging of Tau Deposition in the Aging Human Brain,” Neuron 89(5), 971–982 (2016).
[Crossref]

Schonhaut, D. R.

M. Scholl, S. N. Lockhart, D. R. Schonhaut, J. P. O’Neil, M. Janabi, R. Ossenkoppele, S. L. Baker, J. W. Vogel, J. Faria, H. D. Schwimmer, G. D. Rabinovici, and W. J. Jagust, “PET Imaging of Tau Deposition in the Aging Human Brain,” Neuron 89(5), 971–982 (2016).
[Crossref]

Schraen-Maschke, S.

M. Colin, S. Dujardin, S. Schraen-Maschke, G. Meno-Tetang, C. Duyckaerts, J. P. Courade, and L. Buee, “From the prion-like propagation hypothesis to therapeutic strategies of anti-tau immunotherapy,” Acta Neuropathol. 139(1), 3–25 (2020).
[Crossref]

Schultz, A.

K. A. Johnson, A. Schultz, R. A. Betensky, J. A. Becker, J. Sepulcre, D. Rentz, E. Mormino, J. Chhatwal, R. Amariglio, K. Papp, G. Marshall, M. Albers, S. Mauro, L. Pepin, J. Alverio, K. Judge, M. Philiossaint, T. Shoup, D. Yokell, B. Dickerson, T. Gomez-Isla, B. Hyman, N. Vasdev, and R. Sperling, “Tau positron emission tomographic imaging in aging and early Alzheimer disease,” Ann Neurol. 79(1), 110–119 (2016).
[Crossref]

Schultz, A. P.

B. J. Hanseeuw, R. A. Betensky, H. I. L. Jacobs, A. P. Schultz, J. Sepulcre, J. A. Becker, D. M. O. Cosio, M. Farrell, Y. T. Quiroz, E. C. Mormino, R. F. Buckley, K. V. Papp, R. A. Amariglio, I. Dewachter, A. Ivanoiu, W. Huijbers, T. Hedden, G. A. Marshall, J. P. Chhatwal, D. M. Rentz, R. A. Sperling, and K. Johnson, “Association of Amyloid and Tau With Cognition in Preclinical Alzheimer Disease: A Longitudinal Study,” JAMA Neurol. 76(8), 915–924 (2019).
[Crossref]

Schwarz, P.

J. A. Gerez, N. C. Prymaczok, E. Rockenstein, U. S. Herrmann, P. Schwarz, A. Adame, R. I. Enchev, T. Courtheoux, P. J. Boersema, R. Riek, M. Peter, A. Aguzzi, E. Masliah, and P. Picotti, “A cullin-RING ubiquitin ligase targets exogenous alpha-synuclein and inhibits Lewy body-like pathology,” Sci. Transl. Med. 11(495), eaau6722 (2019).
[Crossref]

Schwimmer, H. D.

M. Scholl, S. N. Lockhart, D. R. Schonhaut, J. P. O’Neil, M. Janabi, R. Ossenkoppele, S. L. Baker, J. W. Vogel, J. Faria, H. D. Schwimmer, G. D. Rabinovici, and W. J. Jagust, “PET Imaging of Tau Deposition in the Aging Human Brain,” Neuron 89(5), 971–982 (2016).
[Crossref]

Seeley, W. W.

R. La Joie, A. V. Visani, S. L. Baker, J. A. Brown, V. Bourakova, J. Cha, K. Chaudhary, L. Edwards, L. Iaccarino, M. Janabi, O. H. Lesman-Segev, Z. A. Miller, D. C. Perry, J. P. O’Neil, J. Pham, J. C. Rojas, H. J. Rosen, W. W. Seeley, R. M. Tsai, B. L. Miller, W. J. Jagust, and G. D. Rabinovici, “Prospective longitudinal atrophy in Alzheimer’s disease correlates with the intensity and topography of baseline tau-PET,” Sci. Transl. Med. 12(524), eaau5732 (2020).
[Crossref]

E. J. Kim, J. L. Hwang, S. E. Gaus, A. L. Nana, J. Deng, J. A. Brown, S. Spina, M. J. Lee, E. M. Ramos, L. T. Grinberg, J. H. Kramer, A. L. Boxer, M. L. Gorno-Tempini, H. J. Rosen, B. L. Miller, and W. W. Seeley, “Evidence of corticofugal tau spreading in patients with frontotemporal dementia,” Acta Neuropathol. 139(1), 27–43 (2020).
[Crossref]

Seibyl, J. P.

A. Mueller, S. Bullich, O. Barret, J. Madonia, M. Berndt, C. Papin, A. Perrotin, N. Koglin, H. Kroth, A. Pfeifer, G. Tamagnan, J. P. Seibyl, K. Marek, S. de Santi, L. M. Dinkelborg, and A. W. Stephens, “Tau PET imaging with (18)F-PI-2620 in patients with Alzheimer's disease and healthy controls: a first-in-human study,” J. Nucl. Med. 61(6), 911–919 (2020).
[Crossref]

S. Sanabria Bohorquez, J. Marik, A. Ogasawara, J. N. Tinianow, H. S. Gill, O. Barret, G. Tamagnan, D. Alagille, G. Ayalon, P. Manser, T. Bengtsson, M. Ward, S. P. Williams, G. A. Kerchner, J. P. Seibyl, K. Marek, and R. M. Weimer, “[(18)F]GTP1 (Genentech Tau Probe 1), a radioligand for detecting neurofibrillary tangle tau pathology in Alzheimer's disease,” Eur. J. Nucl. Med. Mol. Imaging 46(10), 2077–2089 (2019).
[Crossref]

Sengupta, U.

C. A. Lasagna-Reeves, D. L. Castillo-Carranza, U. Sengupta, J. Sarmiento, J. Troncoso, G. R. Jackson, and R. Kayed, “Identification of oligomers at early stages of tau aggregation in Alzheimer's disease,” FASEB J. 26(5), 1946–1959 (2012).
[Crossref]

Sepulcre, J.

B. J. Hanseeuw, R. A. Betensky, H. I. L. Jacobs, A. P. Schultz, J. Sepulcre, J. A. Becker, D. M. O. Cosio, M. Farrell, Y. T. Quiroz, E. C. Mormino, R. F. Buckley, K. V. Papp, R. A. Amariglio, I. Dewachter, A. Ivanoiu, W. Huijbers, T. Hedden, G. A. Marshall, J. P. Chhatwal, D. M. Rentz, R. A. Sperling, and K. Johnson, “Association of Amyloid and Tau With Cognition in Preclinical Alzheimer Disease: A Longitudinal Study,” JAMA Neurol. 76(8), 915–924 (2019).
[Crossref]

K. A. Johnson, A. Schultz, R. A. Betensky, J. A. Becker, J. Sepulcre, D. Rentz, E. Mormino, J. Chhatwal, R. Amariglio, K. Papp, G. Marshall, M. Albers, S. Mauro, L. Pepin, J. Alverio, K. Judge, M. Philiossaint, T. Shoup, D. Yokell, B. Dickerson, T. Gomez-Isla, B. Hyman, N. Vasdev, and R. Sperling, “Tau positron emission tomographic imaging in aging and early Alzheimer disease,” Ann Neurol. 79(1), 110–119 (2016).
[Crossref]

Sharma, A. M.

S. K. Kaufman, D. W. Sanders, T. L. Thomas, A. J. Ruchinskas, J. Vaquer-Alicea, A. M. Sharma, T. M. Miller, and M. I. Diamond, “Tau Prion Strains Dictate Patterns of Cell Pathology, Progression Rate, and Regional Vulnerability In Vivo,” Neuron 92(4), 796–812 (2016).
[Crossref]

Sheehan, P. W.

T. K. Patel, L. Habimana-Griffin, X. Gao, B. Xu, S. Achilefu, K. Alitalo, C. A. McKee, P. W. Sheehan, E. S. Musiek, C. Xiong, D. Coble, and D. M. Holtzman, “Dural lymphatics regulate clearance of extracellular tau from the CNS,” Mol. Neurodegener. 14(1), 11 (2019).
[Crossref]

Sheng, M.

B. Dejanovic, M. A. Huntley, A. De Maziere, W. J. Meilandt, T. Wu, K. Srinivasan, Z. Jiang, V. Gandham, B. A. Friedman, H. Ngu, O. Foreman, R. A. D. Carano, B. Chih, J. Klumperman, C. Bakalarski, J. E. Hanson, and M. Sheng, “Changes in the Synaptic Proteome in Tauopathy and Rescue of Tau-Induced Synapse Loss by C1q Antibodies,” Neuron 100(6), 1322–1336.e7 (2018).
[Crossref]

Shi, G.

R. Ni, Z. Chen, G. Shi, A. Villois, Q. Zhou, P. Arosio, R. M. Nitsch, P. R. Nilsson, J. Klohs, and D. Razansky, “Transcranial in vivo detection of Aβ at single plaque resolution with large-field multifocal illumination fluorescence microscopy,” bioRxiv, 2020.2002.2001.929844 (2020).

Shimada, H.

M. Maruyama, H. Shimada, T. Suhara, H. Shinotoh, B. Ji, J. Maeda, M. R. Zhang, J. Q. Trojanowski, V. M. Lee, M. Ono, K. Masamoto, H. Takano, N. Sahara, N. Iwata, N. Okamura, S. Furumoto, Y. Kudo, Q. Chang, T. C. Saido, A. Takashima, J. Lewis, M. K. Jang, I. Aoki, H. Ito, and M. Higuchi, “Imaging of tau pathology in a tauopathy mouse model and in Alzheimer patients compared to normal controls,” Neuron 79(6), 1094–1108 (2013).
[Crossref]

Shimojo, M.

A. Ishikawa, M. Tokunaga, J. Maeda, T. Minamihisamatsu, M. Shimojo, H. Takuwa, M. Ono, R. Ni, S. Hirano, S. Kuwabara, B. Ji, M. R. Zhang, I. Aoki, T. Suhara, M. Higuchi, and N. Sahara, “In Vivo Visualization of Tau Accumulation, Microglial Activation, and Brain Atrophy in a Mouse Model of Tauopathy rTg4510,” J. Alzheimer’s Dis. 61(3), 1037–1052 (2018).
[Crossref]

N. Sahara, M. Shimojo, M. Ono, H. Takuwa, M. Febo, M. Higuchi, and T. Suhara, “In Vivo Tau Imaging for a Diagnostic Platform of Tauopathy Using the rTg4510 Mouse Line,” Front Neurol. 8, 663 (2017).
[Crossref]

Shinotoh, H.

M. Maruyama, H. Shimada, T. Suhara, H. Shinotoh, B. Ji, J. Maeda, M. R. Zhang, J. Q. Trojanowski, V. M. Lee, M. Ono, K. Masamoto, H. Takano, N. Sahara, N. Iwata, N. Okamura, S. Furumoto, Y. Kudo, Q. Chang, T. C. Saido, A. Takashima, J. Lewis, M. K. Jang, I. Aoki, H. Ito, and M. Higuchi, “Imaging of tau pathology in a tauopathy mouse model and in Alzheimer patients compared to normal controls,” Neuron 79(6), 1094–1108 (2013).
[Crossref]

Shirani, H.

M. Calvo-Rodriguez, S. S. Hou, A. C. Snyder, S. Dujardin, H. Shirani, K. P. R. Nilsson, and B. J. Bacskai, “In vivo detection of tau fibrils and amyloid beta aggregates with luminescent conjugated oligothiophenes and multiphoton microscopy,” Acta Neuropathol. Commun. 7(1), 171 (2019).
[Crossref]

H. Shirani, M. Linares, C. J. Sigurdson, M. Lindgren, P. Norman, and K. P. Nilsson, “A Palette of Fluorescent Thiophene-Based Ligands for the Identification of Protein Aggregates,” Chem. Eur. J. 21(43), 15133–15137 (2015).
[Crossref]

Shoham, S.

S. Gottschalk, O. Degtyaruk, B. Mc Larney, J. Rebling, M. A. Hutter, X. L. Deán-Ben, S. Shoham, and D. Razansky, “Rapid volumetric optoacoustic imaging of neural dynamics across the mouse brain,” Nat. Biomed. Eng. 3(5), 392–401 (2019).
[Crossref]

Shoup, T.

K. A. Johnson, A. Schultz, R. A. Betensky, J. A. Becker, J. Sepulcre, D. Rentz, E. Mormino, J. Chhatwal, R. Amariglio, K. Papp, G. Marshall, M. Albers, S. Mauro, L. Pepin, J. Alverio, K. Judge, M. Philiossaint, T. Shoup, D. Yokell, B. Dickerson, T. Gomez-Isla, B. Hyman, N. Vasdev, and R. Sperling, “Tau positron emission tomographic imaging in aging and early Alzheimer disease,” Ann Neurol. 79(1), 110–119 (2016).
[Crossref]

Sigurdson, C. J.

H. Shirani, M. Linares, C. J. Sigurdson, M. Lindgren, P. Norman, and K. P. Nilsson, “A Palette of Fluorescent Thiophene-Based Ligands for the Identification of Protein Aggregates,” Chem. Eur. J. 21(43), 15133–15137 (2015).
[Crossref]

A. Aslund, C. J. Sigurdson, T. Klingstedt, S. Grathwohl, T. Bolmont, D. L. Dickstein, E. Glimsdal, S. Prokop, M. Lindgren, P. Konradsson, D. M. Holtzman, P. R. Hof, F. L. Heppner, S. Gandy, M. Jucker, A. Aguzzi, P. Hammarström, and K. P. Nilsson, “Novel pentameric thiophene derivatives for in vitro and in vivo optical imaging of a plethora of protein aggregates in cerebral amyloidoses,” ACS Chem. Biol. 4(8), 673–684 (2009).
[Crossref]

Sigurdsson, E. M.

Q. Wu, Y. Lin, J. Gu, and E. M. Sigurdsson, “Dynamic assessment of tau immunotherapies in the brains of live animals by two-photon imaging,” EBioMedicine 35, 270–278 (2018).
[Crossref]

E. E. Congdon and E. M. Sigurdsson, “Tau-targeting therapies for Alzheimer disease,” Nat. Rev. Neurol. 14(7), 399–415 (2018).
[Crossref]

S. Krishnaswamy, Y. Lin, W. J. Rajamohamedsait, H. B. Rajamohamedsait, P. Krishnamurthy, and E. M. Sigurdsson, “Antibody-derived in vivo imaging of tau pathology,” J. Neuroscience 34(50), 16835–16850 (2014).
[Crossref]

Simon, R. A.

T. Klingstedt, A. Aslund, R. A. Simon, L. B. Johansson, J. J. Mason, S. Nystrom, P. Hammarstrom, and K. P. Nilsson, “Synthesis of a library of oligothiophenes and their utilization as fluorescent ligands for spectral assignment of protein aggregates,” Org. Biomol. Chem. 9(24), 8356–8370 (2011).
[Crossref]

Sisodia, S. S.

P. Füger, J. K. Hefendehl, K. Veeraraghavalu, A.-C. Wendeln, C. Schlosser, U. Obermüller, B. M. Wegenast-Braun, J. J. Neher, P. Martus, S. Kohsaka, M. Thunemann, R. Feil, S. S. Sisodia, A. Skodras, and M. Jucker, “Microglia turnover with aging and in an Alzheimer's model via long-term in vivo single-cell imaging,” Nat. Neurosci. 20(10), 1371–1376 (2017).
[Crossref]

Skodras, A.

P. Füger, J. K. Hefendehl, K. Veeraraghavalu, A.-C. Wendeln, C. Schlosser, U. Obermüller, B. M. Wegenast-Braun, J. J. Neher, P. Martus, S. Kohsaka, M. Thunemann, R. Feil, S. S. Sisodia, A. Skodras, and M. Jucker, “Microglia turnover with aging and in an Alzheimer's model via long-term in vivo single-cell imaging,” Nat. Neurosci. 20(10), 1371–1376 (2017).
[Crossref]

B. Wegenast-Braun, A. Skodras, G. Bayraktar, J. Mahler, S. Fritschi, T. Klingstedt, J. Mason, P. Hammarström, K. Nilsson, C. Liebig, and M. Jucker, “Spectral Discrimination of Cerebral Amyloid Lesions after Peripheral Application of Luminescent Conjugated Oligothiophenes,” Am. J. Pathology 181(6), 1953–1960 (2012).
[Crossref]

Snyder, A. C.

M. Calvo-Rodriguez, S. S. Hou, A. C. Snyder, S. Dujardin, H. Shirani, K. P. R. Nilsson, and B. J. Bacskai, “In vivo detection of tau fibrils and amyloid beta aggregates with luminescent conjugated oligothiophenes and multiphoton microscopy,” Acta Neuropathol. Commun. 7(1), 171 (2019).
[Crossref]

Soriano, A.

E. D. Hostetler, A. M. Walji, Z. Zeng, P. Miller, I. Bennacef, C. Salinas, B. Connolly, L. Gantert, H. Haley, M. Holahan, M. Purcell, K. Riffel, T. G. Lohith, P. Coleman, A. Soriano, A. Ogawa, S. Xu, X. Zhang, E. Joshi, J. Della Rocca, D. Hesk, D. J. Schenk, and J. L. Evelhoch, ““Preclinical Characterization of 18F-MK-6240, a Promising PET Tracer for In Vivo Quantification of Human Neurofibrillary Tangles,” Journal of nuclear medicine : official publication,” J. Nuclear Medicine 57(10), 1599–1606 (2016).
[Crossref]

Sperling, R.

K. A. Johnson, A. Schultz, R. A. Betensky, J. A. Becker, J. Sepulcre, D. Rentz, E. Mormino, J. Chhatwal, R. Amariglio, K. Papp, G. Marshall, M. Albers, S. Mauro, L. Pepin, J. Alverio, K. Judge, M. Philiossaint, T. Shoup, D. Yokell, B. Dickerson, T. Gomez-Isla, B. Hyman, N. Vasdev, and R. Sperling, “Tau positron emission tomographic imaging in aging and early Alzheimer disease,” Ann Neurol. 79(1), 110–119 (2016).
[Crossref]

Sperling, R. A.

B. J. Hanseeuw, R. A. Betensky, H. I. L. Jacobs, A. P. Schultz, J. Sepulcre, J. A. Becker, D. M. O. Cosio, M. Farrell, Y. T. Quiroz, E. C. Mormino, R. F. Buckley, K. V. Papp, R. A. Amariglio, I. Dewachter, A. Ivanoiu, W. Huijbers, T. Hedden, G. A. Marshall, J. P. Chhatwal, D. M. Rentz, R. A. Sperling, and K. Johnson, “Association of Amyloid and Tau With Cognition in Preclinical Alzheimer Disease: A Longitudinal Study,” JAMA Neurol. 76(8), 915–924 (2019).
[Crossref]

Spillantini, M. G.

M. G. Spillantini and M. Goedert, “Tau pathology and neurodegeneration,” Lancet Neurol. 12(6), 609–622 (2013).
[Crossref]

P. Delobel, I. Lavenir, G. Fraser, E. Ingram, M. Holzer, B. Ghetti, M. G. Spillantini, R. A. Crowther, and M. Goedert, “Analysis of tau phosphorylation and truncation in a mouse model of human tauopathy,” Am. J. Pathology 172(1), 123–131 (2008).
[Crossref]

Spina, S.

E. J. Kim, J. L. Hwang, S. E. Gaus, A. L. Nana, J. Deng, J. A. Brown, S. Spina, M. J. Lee, E. M. Ramos, L. T. Grinberg, J. H. Kramer, A. L. Boxer, M. L. Gorno-Tempini, H. J. Rosen, B. L. Miller, and W. W. Seeley, “Evidence of corticofugal tau spreading in patients with frontotemporal dementia,” Acta Neuropathol. 139(1), 27–43 (2020).
[Crossref]

Spires, T.

K. SantaCruz, J. Lewis, T. Spires, J. Paulson, L. Kotilinek, M. Ingelsson, A. Guimaraes, M. DeTure, M. Ramsden, E. McGowan, C. Forster, M. Yue, J. Orne, C. Janus, A. Mariash, M. Kuskowski, B. Hyman, M. Hutton, and K. H. Ashe, “Tau Suppression in a Neurodegenerative Mouse Model Improves Memory Function,” Science 309(5733), 476–481 (2005).
[Crossref]

Spires-Jones, T. L.

K. V. Kuchibhotla, S. Wegmann, K. J. Kopeikina, J. Hawkes, N. Rudinskiy, M. L. Andermann, T. L. Spires-Jones, B. J. Bacskai, and B. T. Hyman, “Neurofibrillary tangle-bearing neurons are functionally integrated in cortical circuits in vivo,” Proc. Natl. Acad. Sci. 111(1), 510–514 (2014).
[Crossref]

A. de Calignon, L. M. Fox, R. Pitstick, G. A. Carlson, B. J. Bacskai, T. L. Spires-Jones, and B. T. Hyman, “Caspase activation precedes and leads to tangles,” Nature 464(7292), 1201–1204 (2010).
[Crossref]

Srinivasan, K.

B. Dejanovic, M. A. Huntley, A. De Maziere, W. J. Meilandt, T. Wu, K. Srinivasan, Z. Jiang, V. Gandham, B. A. Friedman, H. Ngu, O. Foreman, R. A. D. Carano, B. Chih, J. Klumperman, C. Bakalarski, J. E. Hanson, and M. Sheng, “Changes in the Synaptic Proteome in Tauopathy and Rescue of Tau-Induced Synapse Loss by C1q Antibodies,” Neuron 100(6), 1322–1336.e7 (2018).
[Crossref]

Staufenbiel, M.

M. Hintersteiner, A. Enz, P. Frey, A. L. Jaton, W. Kinzy, R. Kneuer, U. Neumann, M. Rudin, M. Staufenbiel, M. Stoeckli, K. H. Wiederhold, and H. U. Gremlich, “In vivo detection of amyloid-beta deposits by near-infrared imaging using an oxazine-derivative probe,” Nat. Biotechnol. 23(5), 577–583 (2005).
[Crossref]

Steinbrink, J.

J. Klohs, N. Baeva, J. Steinbrink, R. Bourayou, C. Boettcher, G. Royl, D. Megow, U. Dirnagl, J. Priller, and A. Wunder, “In vivo near-infrared fluorescence imaging of matrix metalloproteinase activity after cerebral ischemia,” J. Cereb. Blood Flow Metab. 29(7), 1284–1292 (2009).
[Crossref]

Stephens, A.

H. Kroth, F. Oden, J. Molette, H. Schieferstein, F. Capotosti, A. Mueller, M. Berndt, H. Schmitt-Willich, V. Darmency, E. Gabellieri, C. Boudou, T. Juergens, Y. Varisco, E. Vokali, D. T. Hickman, G. Tamagnan, A. Pfeifer, L. Dinkelborg, A. Muhs, and A. Stephens, “Discovery and preclinical characterization of [(18)F]PI-2620, a next-generation tau PET tracer for the assessment of tau pathology in Alzheimer's disease and other tauopathies,” Eur. J. Nucl. Med. Mol. Imaging 46(10), 2178–2189 (2019).
[Crossref]

Stephens, A. W.

A. Mueller, S. Bullich, O. Barret, J. Madonia, M. Berndt, C. Papin, A. Perrotin, N. Koglin, H. Kroth, A. Pfeifer, G. Tamagnan, J. P. Seibyl, K. Marek, S. de Santi, L. M. Dinkelborg, and A. W. Stephens, “Tau PET imaging with (18)F-PI-2620 in patients with Alzheimer's disease and healthy controls: a first-in-human study,” J. Nucl. Med. 61(6), 911–919 (2020).
[Crossref]

Stoeckli, M.

M. Hintersteiner, A. Enz, P. Frey, A. L. Jaton, W. Kinzy, R. Kneuer, U. Neumann, M. Rudin, M. Staufenbiel, M. Stoeckli, K. H. Wiederhold, and H. U. Gremlich, “In vivo detection of amyloid-beta deposits by near-infrared imaging using an oxazine-derivative probe,” Nat. Biotechnol. 23(5), 577–583 (2005).
[Crossref]

Suhara, T.

A. Ishikawa, M. Tokunaga, J. Maeda, T. Minamihisamatsu, M. Shimojo, H. Takuwa, M. Ono, R. Ni, S. Hirano, S. Kuwabara, B. Ji, M. R. Zhang, I. Aoki, T. Suhara, M. Higuchi, and N. Sahara, “In Vivo Visualization of Tau Accumulation, Microglial Activation, and Brain Atrophy in a Mouse Model of Tauopathy rTg4510,” J. Alzheimer’s Dis. 61(3), 1037–1052 (2018).
[Crossref]

R. Ni, B. Ji, M. Ono, N. Sahara, M. R. Zhang, I. Aoki, A. Nordberg, T. Suhara, and M. Higuchi, ““Comparative in-vitro and in-vivo quantifications of pathological tau deposits and their association with neurodegeneration in tauopathy mouse models,” Journal of nuclear medicine : official publication,” J. Nucl. Med. 59(6), 960–966 (2018).
[Crossref]

N. Sahara, M. Shimojo, M. Ono, H. Takuwa, M. Febo, M. Higuchi, and T. Suhara, “In Vivo Tau Imaging for a Diagnostic Platform of Tauopathy Using the rTg4510 Mouse Line,” Front Neurol. 8, 663 (2017).
[Crossref]

M. Ono, N. Sahara, K. Kumata, B. Ji, R. Ni, S. Koga, D. W. Dickson, J. Q. Trojanowski, V. M.-Y. Lee, M. Yoshida, I. Hozumi, Y. Yoshiyama, J. C. v. Swieten, A. Nordberg, T. Suhara, M.-R. Zhang, and M. Higuchi, “Distinct binding of PET ligands PBB3 and AV-1451 to tau fibril strains in neurodegenerative tauopathies,” Brain 140, aww339 (2017).
[Crossref]

M. Maruyama, H. Shimada, T. Suhara, H. Shinotoh, B. Ji, J. Maeda, M. R. Zhang, J. Q. Trojanowski, V. M. Lee, M. Ono, K. Masamoto, H. Takano, N. Sahara, N. Iwata, N. Okamura, S. Furumoto, Y. Kudo, Q. Chang, T. C. Saido, A. Takashima, J. Lewis, M. K. Jang, I. Aoki, H. Ito, and M. Higuchi, “Imaging of tau pathology in a tauopathy mouse model and in Alzheimer patients compared to normal controls,” Neuron 79(6), 1094–1108 (2013).
[Crossref]

Y. Yoshiyama, M. Higuchi, B. Zhang, S. M. Huang, N. Iwata, T. C. Saido, J. Maeda, T. Suhara, J. Q. Trojanowski, and V. M. Lee, “Synapse loss and microglial activation precede tangles in a P301S tauopathy mouse model,” Neuron 53(3), 337–351 (2007).
[Crossref]

Sulskis, D.

B. M. Burmann, J. A. Gerez, I. Matecko-Burmann, S. Campioni, P. Kumari, D. Ghosh, A. Mazur, E. E. Aspholm, D. Sulskis, M. Wawrzyniuk, T. Bock, A. Schmidt, S. G. D. Rudiger, R. Riek, and S. Hiller, “Regulation of alpha-synuclein by chaperones in mammalian cells,” Nature 577(7788), 127–132 (2020).
[Crossref]

Swieten, J. C. v.

M. Ono, N. Sahara, K. Kumata, B. Ji, R. Ni, S. Koga, D. W. Dickson, J. Q. Trojanowski, V. M.-Y. Lee, M. Yoshida, I. Hozumi, Y. Yoshiyama, J. C. v. Swieten, A. Nordberg, T. Suhara, M.-R. Zhang, and M. Higuchi, “Distinct binding of PET ligands PBB3 and AV-1451 to tau fibril strains in neurodegenerative tauopathies,” Brain 140, aww339 (2017).
[Crossref]

Takano, H.

M. Maruyama, H. Shimada, T. Suhara, H. Shinotoh, B. Ji, J. Maeda, M. R. Zhang, J. Q. Trojanowski, V. M. Lee, M. Ono, K. Masamoto, H. Takano, N. Sahara, N. Iwata, N. Okamura, S. Furumoto, Y. Kudo, Q. Chang, T. C. Saido, A. Takashima, J. Lewis, M. K. Jang, I. Aoki, H. Ito, and M. Higuchi, “Imaging of tau pathology in a tauopathy mouse model and in Alzheimer patients compared to normal controls,” Neuron 79(6), 1094–1108 (2013).
[Crossref]

Takano, J.

S. Hashimoto, Y. Matsuba, N. Kamano, N. Mihira, N. Sahara, J. Takano, S. I. Muramatsu, T. C. Saido, and T. Saito, “Tau binding protein CAPON induces tau aggregation and neurodegeneration,” Nat. Commun. 10(1), 2394 (2019).
[Crossref]

Takashima, A.

M. Maruyama, H. Shimada, T. Suhara, H. Shinotoh, B. Ji, J. Maeda, M. R. Zhang, J. Q. Trojanowski, V. M. Lee, M. Ono, K. Masamoto, H. Takano, N. Sahara, N. Iwata, N. Okamura, S. Furumoto, Y. Kudo, Q. Chang, T. C. Saido, A. Takashima, J. Lewis, M. K. Jang, I. Aoki, H. Ito, and M. Higuchi, “Imaging of tau pathology in a tauopathy mouse model and in Alzheimer patients compared to normal controls,” Neuron 79(6), 1094–1108 (2013).
[Crossref]

Takuwa, H.

A. Ishikawa, M. Tokunaga, J. Maeda, T. Minamihisamatsu, M. Shimojo, H. Takuwa, M. Ono, R. Ni, S. Hirano, S. Kuwabara, B. Ji, M. R. Zhang, I. Aoki, T. Suhara, M. Higuchi, and N. Sahara, “In Vivo Visualization of Tau Accumulation, Microglial Activation, and Brain Atrophy in a Mouse Model of Tauopathy rTg4510,” J. Alzheimer’s Dis. 61(3), 1037–1052 (2018).
[Crossref]

N. Sahara, M. Shimojo, M. Ono, H. Takuwa, M. Febo, M. Higuchi, and T. Suhara, “In Vivo Tau Imaging for a Diagnostic Platform of Tauopathy Using the rTg4510 Mouse Line,” Front Neurol. 8, 663 (2017).
[Crossref]

Tamagnan, G.

A. Mueller, S. Bullich, O. Barret, J. Madonia, M. Berndt, C. Papin, A. Perrotin, N. Koglin, H. Kroth, A. Pfeifer, G. Tamagnan, J. P. Seibyl, K. Marek, S. de Santi, L. M. Dinkelborg, and A. W. Stephens, “Tau PET imaging with (18)F-PI-2620 in patients with Alzheimer's disease and healthy controls: a first-in-human study,” J. Nucl. Med. 61(6), 911–919 (2020).
[Crossref]

S. Sanabria Bohorquez, J. Marik, A. Ogasawara, J. N. Tinianow, H. S. Gill, O. Barret, G. Tamagnan, D. Alagille, G. Ayalon, P. Manser, T. Bengtsson, M. Ward, S. P. Williams, G. A. Kerchner, J. P. Seibyl, K. Marek, and R. M. Weimer, “[(18)F]GTP1 (Genentech Tau Probe 1), a radioligand for detecting neurofibrillary tangle tau pathology in Alzheimer's disease,” Eur. J. Nucl. Med. Mol. Imaging 46(10), 2077–2089 (2019).
[Crossref]

H. Kroth, F. Oden, J. Molette, H. Schieferstein, F. Capotosti, A. Mueller, M. Berndt, H. Schmitt-Willich, V. Darmency, E. Gabellieri, C. Boudou, T. Juergens, Y. Varisco, E. Vokali, D. T. Hickman, G. Tamagnan, A. Pfeifer, L. Dinkelborg, A. Muhs, and A. Stephens, “Discovery and preclinical characterization of [(18)F]PI-2620, a next-generation tau PET tracer for the assessment of tau pathology in Alzheimer's disease and other tauopathies,” Eur. J. Nucl. Med. Mol. Imaging 46(10), 2178–2189 (2019).
[Crossref]

Thomas, D. D.

C. H. Lo, C. K. Lim, Z. Ding, S. P. Wickramasinghe, A. R. Braun, K. H. Ashe, E. Rhoades, D. D. Thomas, and J. N. Sachs, “Targeting the ensemble of heterogeneous tau oligomers in cells: A novel small molecule screening platform for tauopathies,” Alzheimer’s & Dementia 15(11), 1489–1502 (2019).
[Crossref]

Thomas, T. L.

S. K. Kaufman, D. W. Sanders, T. L. Thomas, A. J. Ruchinskas, J. Vaquer-Alicea, A. M. Sharma, T. M. Miller, and M. I. Diamond, “Tau Prion Strains Dictate Patterns of Cell Pathology, Progression Rate, and Regional Vulnerability In Vivo,” Neuron 92(4), 796–812 (2016).
[Crossref]

Thunemann, M.

P. Füger, J. K. Hefendehl, K. Veeraraghavalu, A.-C. Wendeln, C. Schlosser, U. Obermüller, B. M. Wegenast-Braun, J. J. Neher, P. Martus, S. Kohsaka, M. Thunemann, R. Feil, S. S. Sisodia, A. Skodras, and M. Jucker, “Microglia turnover with aging and in an Alzheimer's model via long-term in vivo single-cell imaging,” Nat. Neurosci. 20(10), 1371–1376 (2017).
[Crossref]

Tinianow, J. N.

S. Sanabria Bohorquez, J. Marik, A. Ogasawara, J. N. Tinianow, H. S. Gill, O. Barret, G. Tamagnan, D. Alagille, G. Ayalon, P. Manser, T. Bengtsson, M. Ward, S. P. Williams, G. A. Kerchner, J. P. Seibyl, K. Marek, and R. M. Weimer, “[(18)F]GTP1 (Genentech Tau Probe 1), a radioligand for detecting neurofibrillary tangle tau pathology in Alzheimer's disease,” Eur. J. Nucl. Med. Mol. Imaging 46(10), 2077–2089 (2019).
[Crossref]

Tokunaga, M.

A. Ishikawa, M. Tokunaga, J. Maeda, T. Minamihisamatsu, M. Shimojo, H. Takuwa, M. Ono, R. Ni, S. Hirano, S. Kuwabara, B. Ji, M. R. Zhang, I. Aoki, T. Suhara, M. Higuchi, and N. Sahara, “In Vivo Visualization of Tau Accumulation, Microglial Activation, and Brain Atrophy in a Mouse Model of Tauopathy rTg4510,” J. Alzheimer’s Dis. 61(3), 1037–1052 (2018).
[Crossref]

Trojanowski, J. Q.

Z. He, J. D. McBride, H. Xu, L. Changolkar, S. J. Kim, B. Zhang, S. Narasimhan, G. S. Gibbons, J. L. Guo, M. Kozak, G. D. Schellenberg, J. Q. Trojanowski, and V. M. Lee, “Transmission of tauopathy strains is independent of their isoform composition,” Nat. Commun. 11(1), 7 (2020).
[Crossref]

M. Ono, N. Sahara, K. Kumata, B. Ji, R. Ni, S. Koga, D. W. Dickson, J. Q. Trojanowski, V. M.-Y. Lee, M. Yoshida, I. Hozumi, Y. Yoshiyama, J. C. v. Swieten, A. Nordberg, T. Suhara, M.-R. Zhang, and M. Higuchi, “Distinct binding of PET ligands PBB3 and AV-1451 to tau fibril strains in neurodegenerative tauopathies,” Brain 140, aww339 (2017).
[Crossref]

M. Maruyama, H. Shimada, T. Suhara, H. Shinotoh, B. Ji, J. Maeda, M. R. Zhang, J. Q. Trojanowski, V. M. Lee, M. Ono, K. Masamoto, H. Takano, N. Sahara, N. Iwata, N. Okamura, S. Furumoto, Y. Kudo, Q. Chang, T. C. Saido, A. Takashima, J. Lewis, M. K. Jang, I. Aoki, H. Ito, and M. Higuchi, “Imaging of tau pathology in a tauopathy mouse model and in Alzheimer patients compared to normal controls,” Neuron 79(6), 1094–1108 (2013).
[Crossref]

Y. Yoshiyama, M. Higuchi, B. Zhang, S. M. Huang, N. Iwata, T. C. Saido, J. Maeda, T. Suhara, J. Q. Trojanowski, and V. M. Lee, “Synapse loss and microglial activation precede tangles in a P301S tauopathy mouse model,” Neuron 53(3), 337–351 (2007).
[Crossref]

V. M. Lee, M. Goedert, and J. Q. Trojanowski, “Neurodegenerative tauopathies,” Annu. Rev. Neurosci. 24(1), 1121–1159 (2001).
[Crossref]

Troncoso, J.

C. A. Lasagna-Reeves, D. L. Castillo-Carranza, U. Sengupta, J. Sarmiento, J. Troncoso, G. R. Jackson, and R. Kayed, “Identification of oligomers at early stages of tau aggregation in Alzheimer's disease,” FASEB J. 26(5), 1946–1959 (2012).
[Crossref]

Tsai, R. M.

R. La Joie, A. V. Visani, S. L. Baker, J. A. Brown, V. Bourakova, J. Cha, K. Chaudhary, L. Edwards, L. Iaccarino, M. Janabi, O. H. Lesman-Segev, Z. A. Miller, D. C. Perry, J. P. O’Neil, J. Pham, J. C. Rojas, H. J. Rosen, W. W. Seeley, R. M. Tsai, B. L. Miller, W. J. Jagust, and G. D. Rabinovici, “Prospective longitudinal atrophy in Alzheimer’s disease correlates with the intensity and topography of baseline tau-PET,” Sci. Transl. Med. 12(524), eaau5732 (2020).
[Crossref]

Vaas, M.

R. Ni, M. Vaas, W. Ren, and J. Klohs, “Non-invasive detection of acute cerebral hypoxia and subsequent matrix-metalloproteinase activity in a mouse model of cerebral ischemia using multispectral-optoacoustic-tomography,” Neurophotonics 5(1), 015005 (2018).
[Crossref]

van Dorpe, J.

J. Gotz, F. Chen, J. van Dorpe, and R. M. Nitsch, “Formation of neurofibrillary tangles in P301 l tau transgenic mice induced by Abeta 42 fibrils,” Science 293(5534), 1491–1495 (2001).
[Crossref]

Van Slegtenhorst, M.

J. Lewis, E. McGowan, J. Rockwood, H. Melrose, P. Nacharaju, M. Van Slegtenhorst, K. Gwinn-Hardy, M. Paul Murphy, M. Baker, X. Yu, K. Duff, J. Hardy, A. Corral, W. L. Lin, S. H. Yen, D. W. Dickson, P. Davies, and M. Hutton, “Neurofibrillary tangles, amyotrophy and progressive motor disturbance in mice expressing mutant (P301L) tau protein,” Nat. Genet. 25(4), 402–405 (2000).
[Crossref]

Vaquer-Alicea, J.

S. K. Kaufman, D. W. Sanders, T. L. Thomas, A. J. Ruchinskas, J. Vaquer-Alicea, A. M. Sharma, T. M. Miller, and M. I. Diamond, “Tau Prion Strains Dictate Patterns of Cell Pathology, Progression Rate, and Regional Vulnerability In Vivo,” Neuron 92(4), 796–812 (2016).
[Crossref]

Varisco, Y.

H. Kroth, F. Oden, J. Molette, H. Schieferstein, F. Capotosti, A. Mueller, M. Berndt, H. Schmitt-Willich, V. Darmency, E. Gabellieri, C. Boudou, T. Juergens, Y. Varisco, E. Vokali, D. T. Hickman, G. Tamagnan, A. Pfeifer, L. Dinkelborg, A. Muhs, and A. Stephens, “Discovery and preclinical characterization of [(18)F]PI-2620, a next-generation tau PET tracer for the assessment of tau pathology in Alzheimer's disease and other tauopathies,” Eur. J. Nucl. Med. Mol. Imaging 46(10), 2178–2189 (2019).
[Crossref]

Vasdev, N.

K. A. Johnson, A. Schultz, R. A. Betensky, J. A. Becker, J. Sepulcre, D. Rentz, E. Mormino, J. Chhatwal, R. Amariglio, K. Papp, G. Marshall, M. Albers, S. Mauro, L. Pepin, J. Alverio, K. Judge, M. Philiossaint, T. Shoup, D. Yokell, B. Dickerson, T. Gomez-Isla, B. Hyman, N. Vasdev, and R. Sperling, “Tau positron emission tomographic imaging in aging and early Alzheimer disease,” Ann Neurol. 79(1), 110–119 (2016).
[Crossref]

Veeraraghavalu, K.

P. Füger, J. K. Hefendehl, K. Veeraraghavalu, A.-C. Wendeln, C. Schlosser, U. Obermüller, B. M. Wegenast-Braun, J. J. Neher, P. Martus, S. Kohsaka, M. Thunemann, R. Feil, S. S. Sisodia, A. Skodras, and M. Jucker, “Microglia turnover with aging and in an Alzheimer's model via long-term in vivo single-cell imaging,” Nat. Neurosci. 20(10), 1371–1376 (2017).
[Crossref]

Velasco, A.

A. Velasco, G. Fraser, P. Delobel, B. Ghetti, I. Lavenir, and M. Goedert, “Detection of filamentous tau inclusions by the fluorescent Congo red derivative FSB [(trans,trans)-1-fluoro-2,5-bis(3-hydroxycarbonyl-4-hydroxy)styrylbenzene],” FEBS Lett. 582(6), 901–906 (2008).
[Crossref]

Verwilst, P.

P. Verwilst, H. S. Kim, S. Kim, C. Kang, and J. S. Kim, “Shedding light on tau protein aggregation: the progress in developing highly selective fluorophores,” Chem. Soc. Rev. 47(7), 2249–2265 (2018).
[Crossref]

Villemagne, V. L.

V. L. Villemagne, V. Dore, S. C. Burnham, C. L. Masters, and C. C. Rowe, “Imaging tau and amyloid-beta proteinopathies in Alzheimer disease and other conditions,” Nat. Rev. Neurol. 14(4), 225–236 (2018).
[Crossref]

Villois, A.

R. Ni, Z. Chen, G. Shi, A. Villois, Q. Zhou, P. Arosio, R. M. Nitsch, P. R. Nilsson, J. Klohs, and D. Razansky, “Transcranial in vivo detection of Aβ at single plaque resolution with large-field multifocal illumination fluorescence microscopy,” bioRxiv, 2020.2002.2001.929844 (2020).

Visani, A. V.

R. La Joie, A. V. Visani, S. L. Baker, J. A. Brown, V. Bourakova, J. Cha, K. Chaudhary, L. Edwards, L. Iaccarino, M. Janabi, O. H. Lesman-Segev, Z. A. Miller, D. C. Perry, J. P. O’Neil, J. Pham, J. C. Rojas, H. J. Rosen, W. W. Seeley, R. M. Tsai, B. L. Miller, W. J. Jagust, and G. D. Rabinovici, “Prospective longitudinal atrophy in Alzheimer’s disease correlates with the intensity and topography of baseline tau-PET,” Sci. Transl. Med. 12(524), eaau5732 (2020).
[Crossref]

Vogel, J. W.

M. Scholl, S. N. Lockhart, D. R. Schonhaut, J. P. O’Neil, M. Janabi, R. Ossenkoppele, S. L. Baker, J. W. Vogel, J. Faria, H. D. Schwimmer, G. D. Rabinovici, and W. J. Jagust, “PET Imaging of Tau Deposition in the Aging Human Brain,” Neuron 89(5), 971–982 (2016).
[Crossref]

Voigt, F.

R. Ni, X. L. Dean-Ben, D. Kirschenbaum, M. Rudin, Z. Chen, A. Crimi, F. Voigt, P. R. Nilsson, F. Helmchen, R. M. Nitsch, A. Aguzzi, D. Razansky, and J. Klohs, “Whole brain optoacoustic tomography reveals strain-specific regional beta-amyloid densities in Alzheimer`s disease amyloidosis models,” bioRxiv, DOI: 10.1101/2020.1102.1125.964064 (2020).

Vokali, E.

H. Kroth, F. Oden, J. Molette, H. Schieferstein, F. Capotosti, A. Mueller, M. Berndt, H. Schmitt-Willich, V. Darmency, E. Gabellieri, C. Boudou, T. Juergens, Y. Varisco, E. Vokali, D. T. Hickman, G. Tamagnan, A. Pfeifer, L. Dinkelborg, A. Muhs, and A. Stephens, “Discovery and preclinical characterization of [(18)F]PI-2620, a next-generation tau PET tracer for the assessment of tau pathology in Alzheimer's disease and other tauopathies,” Eur. J. Nucl. Med. Mol. Imaging 46(10), 2178–2189 (2019).
[Crossref]

von Andrian, U. H.

I. B. Mazo, J.-C. Gutierrez-Ramos, P. S. Frenette, R. O. Hynes, D. D. Wagner, and U. H. von Andrian, “Hematopoietic Progenitor Cell Rolling in Bone Marrow Microvessels: Parallel Contributions by Endothelial Selectins and Vascular Cell Adhesion Molecule 1,” J. Exp. Med. 188(3), 465–474 (1998).
[Crossref]

Wagner, D. D.

I. B. Mazo, J.-C. Gutierrez-Ramos, P. S. Frenette, R. O. Hynes, D. D. Wagner, and U. H. von Andrian, “Hematopoietic Progenitor Cell Rolling in Bone Marrow Microvessels: Parallel Contributions by Endothelial Selectins and Vascular Cell Adhesion Molecule 1,” J. Exp. Med. 188(3), 465–474 (1998).
[Crossref]

Walji, A. M.

E. D. Hostetler, A. M. Walji, Z. Zeng, P. Miller, I. Bennacef, C. Salinas, B. Connolly, L. Gantert, H. Haley, M. Holahan, M. Purcell, K. Riffel, T. G. Lohith, P. Coleman, A. Soriano, A. Ogawa, S. Xu, X. Zhang, E. Joshi, J. Della Rocca, D. Hesk, D. J. Schenk, and J. L. Evelhoch, ““Preclinical Characterization of 18F-MK-6240, a Promising PET Tracer for In Vivo Quantification of Human Neurofibrillary Tangles,” Journal of nuclear medicine : official publication,” J. Nuclear Medicine 57(10), 1599–1606 (2016).
[Crossref]

Ward, M.

S. Sanabria Bohorquez, J. Marik, A. Ogasawara, J. N. Tinianow, H. S. Gill, O. Barret, G. Tamagnan, D. Alagille, G. Ayalon, P. Manser, T. Bengtsson, M. Ward, S. P. Williams, G. A. Kerchner, J. P. Seibyl, K. Marek, and R. M. Weimer, “[(18)F]GTP1 (Genentech Tau Probe 1), a radioligand for detecting neurofibrillary tangle tau pathology in Alzheimer's disease,” Eur. J. Nucl. Med. Mol. Imaging 46(10), 2077–2089 (2019).
[Crossref]

Wawrzyniuk, M.

B. M. Burmann, J. A. Gerez, I. Matecko-Burmann, S. Campioni, P. Kumari, D. Ghosh, A. Mazur, E. E. Aspholm, D. Sulskis, M. Wawrzyniuk, T. Bock, A. Schmidt, S. G. D. Rudiger, R. Riek, and S. Hiller, “Regulation of alpha-synuclein by chaperones in mammalian cells,” Nature 577(7788), 127–132 (2020).
[Crossref]

Wegenast-Braun, B.

B. Wegenast-Braun, A. Skodras, G. Bayraktar, J. Mahler, S. Fritschi, T. Klingstedt, J. Mason, P. Hammarström, K. Nilsson, C. Liebig, and M. Jucker, “Spectral Discrimination of Cerebral Amyloid Lesions after Peripheral Application of Luminescent Conjugated Oligothiophenes,” Am. J. Pathology 181(6), 1953–1960 (2012).
[Crossref]

Wegenast-Braun, B. M.

P. Füger, J. K. Hefendehl, K. Veeraraghavalu, A.-C. Wendeln, C. Schlosser, U. Obermüller, B. M. Wegenast-Braun, J. J. Neher, P. Martus, S. Kohsaka, M. Thunemann, R. Feil, S. S. Sisodia, A. Skodras, and M. Jucker, “Microglia turnover with aging and in an Alzheimer's model via long-term in vivo single-cell imaging,” Nat. Neurosci. 20(10), 1371–1376 (2017).
[Crossref]

Wegmann, S.

K. V. Kuchibhotla, S. Wegmann, K. J. Kopeikina, J. Hawkes, N. Rudinskiy, M. L. Andermann, T. L. Spires-Jones, B. J. Bacskai, and B. T. Hyman, “Neurofibrillary tangle-bearing neurons are functionally integrated in cortical circuits in vivo,” Proc. Natl. Acad. Sci. 111(1), 510–514 (2014).
[Crossref]

Weimer, R. M.

S. Sanabria Bohorquez, J. Marik, A. Ogasawara, J. N. Tinianow, H. S. Gill, O. Barret, G. Tamagnan, D. Alagille, G. Ayalon, P. Manser, T. Bengtsson, M. Ward, S. P. Williams, G. A. Kerchner, J. P. Seibyl, K. Marek, and R. M. Weimer, “[(18)F]GTP1 (Genentech Tau Probe 1), a radioligand for detecting neurofibrillary tangle tau pathology in Alzheimer's disease,” Eur. J. Nucl. Med. Mol. Imaging 46(10), 2077–2089 (2019).
[Crossref]

Wendeln, A.-C.

P. Füger, J. K. Hefendehl, K. Veeraraghavalu, A.-C. Wendeln, C. Schlosser, U. Obermüller, B. M. Wegenast-Braun, J. J. Neher, P. Martus, S. Kohsaka, M. Thunemann, R. Feil, S. S. Sisodia, A. Skodras, and M. Jucker, “Microglia turnover with aging and in an Alzheimer's model via long-term in vivo single-cell imaging,” Nat. Neurosci. 20(10), 1371–1376 (2017).
[Crossref]

Wickramasinghe, S. P.

C. H. Lo, C. K. Lim, Z. Ding, S. P. Wickramasinghe, A. R. Braun, K. H. Ashe, E. Rhoades, D. D. Thomas, and J. N. Sachs, “Targeting the ensemble of heterogeneous tau oligomers in cells: A novel small molecule screening platform for tauopathies,” Alzheimer’s & Dementia 15(11), 1489–1502 (2019).
[Crossref]

Wiederhold, K. H.

M. Hintersteiner, A. Enz, P. Frey, A. L. Jaton, W. Kinzy, R. Kneuer, U. Neumann, M. Rudin, M. Staufenbiel, M. Stoeckli, K. H. Wiederhold, and H. U. Gremlich, “In vivo detection of amyloid-beta deposits by near-infrared imaging using an oxazine-derivative probe,” Nat. Biotechnol. 23(5), 577–583 (2005).
[Crossref]

Williams, S. P.

S. Sanabria Bohorquez, J. Marik, A. Ogasawara, J. N. Tinianow, H. S. Gill, O. Barret, G. Tamagnan, D. Alagille, G. Ayalon, P. Manser, T. Bengtsson, M. Ward, S. P. Williams, G. A. Kerchner, J. P. Seibyl, K. Marek, and R. M. Weimer, “[(18)F]GTP1 (Genentech Tau Probe 1), a radioligand for detecting neurofibrillary tangle tau pathology in Alzheimer's disease,” Eur. J. Nucl. Med. Mol. Imaging 46(10), 2077–2089 (2019).
[Crossref]

Wozniak, D. F.

K. M. Schoch, S. L. DeVos, R. L. Miller, S. J. Chun, M. Norrbom, D. F. Wozniak, H. N. Dawson, C. F. Bennett, F. Rigo, and T. M. Miller, “Increased 4R-Tau Induces Pathological Changes in a Human-Tau Mouse Model,” Neuron 90(5), 941–947 (2016).
[Crossref]

Wu, Q.

Q. Wu, Y. Lin, J. Gu, and E. M. Sigurdsson, “Dynamic assessment of tau immunotherapies in the brains of live animals by two-photon imaging,” EBioMedicine 35, 270–278 (2018).
[Crossref]

Wu, T.

B. Dejanovic, M. A. Huntley, A. De Maziere, W. J. Meilandt, T. Wu, K. Srinivasan, Z. Jiang, V. Gandham, B. A. Friedman, H. Ngu, O. Foreman, R. A. D. Carano, B. Chih, J. Klumperman, C. Bakalarski, J. E. Hanson, and M. Sheng, “Changes in the Synaptic Proteome in Tauopathy and Rescue of Tau-Induced Synapse Loss by C1q Antibodies,” Neuron 100(6), 1322–1336.e7 (2018).
[Crossref]

Wunder, A.

J. Klohs, N. Baeva, J. Steinbrink, R. Bourayou, C. Boettcher, G. Royl, D. Megow, U. Dirnagl, J. Priller, and A. Wunder, “In vivo near-infrared fluorescence imaging of matrix metalloproteinase activity after cerebral ischemia,” J. Cereb. Blood Flow Metab. 29(7), 1284–1292 (2009).
[Crossref]

Xiong, C.

T. K. Patel, L. Habimana-Griffin, X. Gao, B. Xu, S. Achilefu, K. Alitalo, C. A. McKee, P. W. Sheehan, E. S. Musiek, C. Xiong, D. Coble, and D. M. Holtzman, “Dural lymphatics regulate clearance of extracellular tau from the CNS,” Mol. Neurodegener. 14(1), 11 (2019).
[Crossref]

Xu, B.

T. K. Patel, L. Habimana-Griffin, X. Gao, B. Xu, S. Achilefu, K. Alitalo, C. A. McKee, P. W. Sheehan, E. S. Musiek, C. Xiong, D. Coble, and D. M. Holtzman, “Dural lymphatics regulate clearance of extracellular tau from the CNS,” Mol. Neurodegener. 14(1), 11 (2019).
[Crossref]

Xu, H.

Z. He, J. D. McBride, H. Xu, L. Changolkar, S. J. Kim, B. Zhang, S. Narasimhan, G. S. Gibbons, J. L. Guo, M. Kozak, G. D. Schellenberg, J. Q. Trojanowski, and V. M. Lee, “Transmission of tauopathy strains is independent of their isoform composition,” Nat. Commun. 11(1), 7 (2020).
[Crossref]

Xu, S.

E. D. Hostetler, A. M. Walji, Z. Zeng, P. Miller, I. Bennacef, C. Salinas, B. Connolly, L. Gantert, H. Haley, M. Holahan, M. Purcell, K. Riffel, T. G. Lohith, P. Coleman, A. Soriano, A. Ogawa, S. Xu, X. Zhang, E. Joshi, J. Della Rocca, D. Hesk, D. J. Schenk, and J. L. Evelhoch, ““Preclinical Characterization of 18F-MK-6240, a Promising PET Tracer for In Vivo Quantification of Human Neurofibrillary Tangles,” Journal of nuclear medicine : official publication,” J. Nuclear Medicine 57(10), 1599–1606 (2016).
[Crossref]

Yen, S. H.

J. Lewis, E. McGowan, J. Rockwood, H. Melrose, P. Nacharaju, M. Van Slegtenhorst, K. Gwinn-Hardy, M. Paul Murphy, M. Baker, X. Yu, K. Duff, J. Hardy, A. Corral, W. L. Lin, S. H. Yen, D. W. Dickson, P. Davies, and M. Hutton, “Neurofibrillary tangles, amyotrophy and progressive motor disturbance in mice expressing mutant (P301L) tau protein,” Nat. Genet. 25(4), 402–405 (2000).
[Crossref]

Yokell, D.

K. A. Johnson, A. Schultz, R. A. Betensky, J. A. Becker, J. Sepulcre, D. Rentz, E. Mormino, J. Chhatwal, R. Amariglio, K. Papp, G. Marshall, M. Albers, S. Mauro, L. Pepin, J. Alverio, K. Judge, M. Philiossaint, T. Shoup, D. Yokell, B. Dickerson, T. Gomez-Isla, B. Hyman, N. Vasdev, and R. Sperling, “Tau positron emission tomographic imaging in aging and early Alzheimer disease,” Ann Neurol. 79(1), 110–119 (2016).
[Crossref]

Yoshida, M.

M. Ono, N. Sahara, K. Kumata, B. Ji, R. Ni, S. Koga, D. W. Dickson, J. Q. Trojanowski, V. M.-Y. Lee, M. Yoshida, I. Hozumi, Y. Yoshiyama, J. C. v. Swieten, A. Nordberg, T. Suhara, M.-R. Zhang, and M. Higuchi, “Distinct binding of PET ligands PBB3 and AV-1451 to tau fibril strains in neurodegenerative tauopathies,” Brain 140, aww339 (2017).
[Crossref]

Yoshiyama, Y.

M. Ono, N. Sahara, K. Kumata, B. Ji, R. Ni, S. Koga, D. W. Dickson, J. Q. Trojanowski, V. M.-Y. Lee, M. Yoshida, I. Hozumi, Y. Yoshiyama, J. C. v. Swieten, A. Nordberg, T. Suhara, M.-R. Zhang, and M. Higuchi, “Distinct binding of PET ligands PBB3 and AV-1451 to tau fibril strains in neurodegenerative tauopathies,” Brain 140, aww339 (2017).
[Crossref]

Y. Yoshiyama, M. Higuchi, B. Zhang, S. M. Huang, N. Iwata, T. C. Saido, J. Maeda, T. Suhara, J. Q. Trojanowski, and V. M. Lee, “Synapse loss and microglial activation precede tangles in a P301S tauopathy mouse model,” Neuron 53(3), 337–351 (2007).
[Crossref]

Yu, X.

J. Lewis, E. McGowan, J. Rockwood, H. Melrose, P. Nacharaju, M. Van Slegtenhorst, K. Gwinn-Hardy, M. Paul Murphy, M. Baker, X. Yu, K. Duff, J. Hardy, A. Corral, W. L. Lin, S. H. Yen, D. W. Dickson, P. Davies, and M. Hutton, “Neurofibrillary tangles, amyotrophy and progressive motor disturbance in mice expressing mutant (P301L) tau protein,” Nat. Genet. 25(4), 402–405 (2000).
[Crossref]

Yue, M.

K. SantaCruz, J. Lewis, T. Spires, J. Paulson, L. Kotilinek, M. Ingelsson, A. Guimaraes, M. DeTure, M. Ramsden, E. McGowan, C. Forster, M. Yue, J. Orne, C. Janus, A. Mariash, M. Kuskowski, B. Hyman, M. Hutton, and K. H. Ashe, “Tau Suppression in a Neurodegenerative Mouse Model Improves Memory Function,” Science 309(5733), 476–481 (2005).
[Crossref]

Yundung, Y.

R. Ni, Y. Zarb, G. A. Kuhn, R. Müller, Y. Yundung, R. M. Nitsch, L. Kulic, A. Keller, and J. Klohs, “Tau deposition is associated with imaging patterns of tissue calcification in the P301L mouse model of human tauopathy,” bioRxiv, 851915 (2019).

Zarb, Y.

R. Ni, Y. Zarb, G. A. Kuhn, R. Müller, Y. Yundung, R. M. Nitsch, L. Kulic, A. Keller, and J. Klohs, “Tau deposition is associated with imaging patterns of tissue calcification in the P301L mouse model of human tauopathy,” bioRxiv, 851915 (2019).

Zeng, Z.

E. D. Hostetler, A. M. Walji, Z. Zeng, P. Miller, I. Bennacef, C. Salinas, B. Connolly, L. Gantert, H. Haley, M. Holahan, M. Purcell, K. Riffel, T. G. Lohith, P. Coleman, A. Soriano, A. Ogawa, S. Xu, X. Zhang, E. Joshi, J. Della Rocca, D. Hesk, D. J. Schenk, and J. L. Evelhoch, ““Preclinical Characterization of 18F-MK-6240, a Promising PET Tracer for In Vivo Quantification of Human Neurofibrillary Tangles,” Journal of nuclear medicine : official publication,” J. Nuclear Medicine 57(10), 1599–1606 (2016).
[Crossref]

Zhang, B.

Z. He, J. D. McBride, H. Xu, L. Changolkar, S. J. Kim, B. Zhang, S. Narasimhan, G. S. Gibbons, J. L. Guo, M. Kozak, G. D. Schellenberg, J. Q. Trojanowski, and V. M. Lee, “Transmission of tauopathy strains is independent of their isoform composition,” Nat. Commun. 11(1), 7 (2020).
[Crossref]

Y. Yoshiyama, M. Higuchi, B. Zhang, S. M. Huang, N. Iwata, T. C. Saido, J. Maeda, T. Suhara, J. Q. Trojanowski, and V. M. Lee, “Synapse loss and microglial activation precede tangles in a P301S tauopathy mouse model,” Neuron 53(3), 337–351 (2007).
[Crossref]

Zhang, C.

Y. Zhang, C. Zhang, X. Zhong, and D. Zhu, “Quantitative evaluation of SOCS-induced optical clearing efficiency of skull,” Quant. Imaging Med. Surg. 5, 136–142 (2015).
[Crossref]

Zhang, M. R.

R. Ni, B. Ji, M. Ono, N. Sahara, M. R. Zhang, I. Aoki, A. Nordberg, T. Suhara, and M. Higuchi, ““Comparative in-vitro and in-vivo quantifications of pathological tau deposits and their association with neurodegeneration in tauopathy mouse models,” Journal of nuclear medicine : official publication,” J. Nucl. Med. 59(6), 960–966 (2018).
[Crossref]

A. Ishikawa, M. Tokunaga, J. Maeda, T. Minamihisamatsu, M. Shimojo, H. Takuwa, M. Ono, R. Ni, S. Hirano, S. Kuwabara, B. Ji, M. R. Zhang, I. Aoki, T. Suhara, M. Higuchi, and N. Sahara, “In Vivo Visualization of Tau Accumulation, Microglial Activation, and Brain Atrophy in a Mouse Model of Tauopathy rTg4510,” J. Alzheimer’s Dis. 61(3), 1037–1052 (2018).
[Crossref]

M. Maruyama, H. Shimada, T. Suhara, H. Shinotoh, B. Ji, J. Maeda, M. R. Zhang, J. Q. Trojanowski, V. M. Lee, M. Ono, K. Masamoto, H. Takano, N. Sahara, N. Iwata, N. Okamura, S. Furumoto, Y. Kudo, Q. Chang, T. C. Saido, A. Takashima, J. Lewis, M. K. Jang, I. Aoki, H. Ito, and M. Higuchi, “Imaging of tau pathology in a tauopathy mouse model and in Alzheimer patients compared to normal controls,” Neuron 79(6), 1094–1108 (2013).
[Crossref]

Zhang, M.-R.

M. Ono, N. Sahara, K. Kumata, B. Ji, R. Ni, S. Koga, D. W. Dickson, J. Q. Trojanowski, V. M.-Y. Lee, M. Yoshida, I. Hozumi, Y. Yoshiyama, J. C. v. Swieten, A. Nordberg, T. Suhara, M.-R. Zhang, and M. Higuchi, “Distinct binding of PET ligands PBB3 and AV-1451 to tau fibril strains in neurodegenerative tauopathies,” Brain 140, aww339 (2017).
[Crossref]

Zhang, X.

E. D. Hostetler, A. M. Walji, Z. Zeng, P. Miller, I. Bennacef, C. Salinas, B. Connolly, L. Gantert, H. Haley, M. Holahan, M. Purcell, K. Riffel, T. G. Lohith, P. Coleman, A. Soriano, A. Ogawa, S. Xu, X. Zhang, E. Joshi, J. Della Rocca, D. Hesk, D. J. Schenk, and J. L. Evelhoch, ““Preclinical Characterization of 18F-MK-6240, a Promising PET Tracer for In Vivo Quantification of Human Neurofibrillary Tangles,” Journal of nuclear medicine : official publication,” J. Nuclear Medicine 57(10), 1599–1606 (2016).
[Crossref]

Zhang, Y.

Y. Zhang, C. Zhang, X. Zhong, and D. Zhu, “Quantitative evaluation of SOCS-induced optical clearing efficiency of skull,” Quant. Imaging Med. Surg. 5, 136–142 (2015).
[Crossref]

Zhong, X.

Y. Zhang, C. Zhang, X. Zhong, and D. Zhu, “Quantitative evaluation of SOCS-induced optical clearing efficiency of skull,” Quant. Imaging Med. Surg. 5, 136–142 (2015).
[Crossref]

Zhou, Q.

Z. Chen, B. Mc Larney, J. Rebling, X. L. Deán-Ben, Q. Zhou, S. Gottschalk, and D. Razansky, “High-Speed Large-Field Multifocal Illumination Fluorescence Microscopy,” Laser Photonics Rev. 14, 1900070 (2020).
[Crossref]

R. Ni, Z. Chen, G. Shi, A. Villois, Q. Zhou, P. Arosio, R. M. Nitsch, P. R. Nilsson, J. Klohs, and D. Razansky, “Transcranial in vivo detection of Aβ at single plaque resolution with large-field multifocal illumination fluorescence microscopy,” bioRxiv, 2020.2002.2001.929844 (2020).

Zhu, D.

Y. Zhang, C. Zhang, X. Zhong, and D. Zhu, “Quantitative evaluation of SOCS-induced optical clearing efficiency of skull,” Quant. Imaging Med. Surg. 5, 136–142 (2015).
[Crossref]

ACS Chem. Biol. (1)

A. Aslund, C. J. Sigurdson, T. Klingstedt, S. Grathwohl, T. Bolmont, D. L. Dickstein, E. Glimsdal, S. Prokop, M. Lindgren, P. Konradsson, D. M. Holtzman, P. R. Hof, F. L. Heppner, S. Gandy, M. Jucker, A. Aguzzi, P. Hammarström, and K. P. Nilsson, “Novel pentameric thiophene derivatives for in vitro and in vivo optical imaging of a plethora of protein aggregates in cerebral amyloidoses,” ACS Chem. Biol. 4(8), 673–684 (2009).
[Crossref]

Acta Neuropathol. (2)

M. Colin, S. Dujardin, S. Schraen-Maschke, G. Meno-Tetang, C. Duyckaerts, J. P. Courade, and L. Buee, “From the prion-like propagation hypothesis to therapeutic strategies of anti-tau immunotherapy,” Acta Neuropathol. 139(1), 3–25 (2020).
[Crossref]

E. J. Kim, J. L. Hwang, S. E. Gaus, A. L. Nana, J. Deng, J. A. Brown, S. Spina, M. J. Lee, E. M. Ramos, L. T. Grinberg, J. H. Kramer, A. L. Boxer, M. L. Gorno-Tempini, H. J. Rosen, B. L. Miller, and W. W. Seeley, “Evidence of corticofugal tau spreading in patients with frontotemporal dementia,” Acta Neuropathol. 139(1), 27–43 (2020).
[Crossref]

Acta Neuropathol. Commun. (1)

M. Calvo-Rodriguez, S. S. Hou, A. C. Snyder, S. Dujardin, H. Shirani, K. P. R. Nilsson, and B. J. Bacskai, “In vivo detection of tau fibrils and amyloid beta aggregates with luminescent conjugated oligothiophenes and multiphoton microscopy,” Acta Neuropathol. Commun. 7(1), 171 (2019).
[Crossref]

Alzheimer’s & Dementia (1)

C. H. Lo, C. K. Lim, Z. Ding, S. P. Wickramasinghe, A. R. Braun, K. H. Ashe, E. Rhoades, D. D. Thomas, and J. N. Sachs, “Targeting the ensemble of heterogeneous tau oligomers in cells: A novel small molecule screening platform for tauopathies,” Alzheimer’s & Dementia 15(11), 1489–1502 (2019).
[Crossref]

Am. J. Pathology (2)

B. Wegenast-Braun, A. Skodras, G. Bayraktar, J. Mahler, S. Fritschi, T. Klingstedt, J. Mason, P. Hammarström, K. Nilsson, C. Liebig, and M. Jucker, “Spectral Discrimination of Cerebral Amyloid Lesions after Peripheral Application of Luminescent Conjugated Oligothiophenes,” Am. J. Pathology 181(6), 1953–1960 (2012).
[Crossref]

P. Delobel, I. Lavenir, G. Fraser, E. Ingram, M. Holzer, B. Ghetti, M. G. Spillantini, R. A. Crowther, and M. Goedert, “Analysis of tau phosphorylation and truncation in a mouse model of human tauopathy,” Am. J. Pathology 172(1), 123–131 (2008).
[Crossref]

Ann Neurol. (1)

K. A. Johnson, A. Schultz, R. A. Betensky, J. A. Becker, J. Sepulcre, D. Rentz, E. Mormino, J. Chhatwal, R. Amariglio, K. Papp, G. Marshall, M. Albers, S. Mauro, L. Pepin, J. Alverio, K. Judge, M. Philiossaint, T. Shoup, D. Yokell, B. Dickerson, T. Gomez-Isla, B. Hyman, N. Vasdev, and R. Sperling, “Tau positron emission tomographic imaging in aging and early Alzheimer disease,” Ann Neurol. 79(1), 110–119 (2016).
[Crossref]

Annu. Rev. Neurosci. (1)

V. M. Lee, M. Goedert, and J. Q. Trojanowski, “Neurodegenerative tauopathies,” Annu. Rev. Neurosci. 24(1), 1121–1159 (2001).
[Crossref]

Blood (1)

F. Lassailly, K. Foster, L. Lopez-Onieva, E. Currie, and D. Bonnet, “Multimodal imaging reveals structural and functional heterogeneity in different bone marrow compartments: functional implications on hematopoietic stem cells,” Blood 122(10), 1730–1740 (2013).
[Crossref]

Brain (2)

M. Ono, N. Sahara, K. Kumata, B. Ji, R. Ni, S. Koga, D. W. Dickson, J. Q. Trojanowski, V. M.-Y. Lee, M. Yoshida, I. Hozumi, Y. Yoshiyama, J. C. v. Swieten, A. Nordberg, T. Suhara, M.-R. Zhang, and M. Higuchi, “Distinct binding of PET ligands PBB3 and AV-1451 to tau fibril strains in neurodegenerative tauopathies,” Brain 140, aww339 (2017).
[Crossref]

P. Marinkovic, S. Blumenstock, P. M. Goltstein, V. Korzhova, F. Peters, A. Knebl, and J. Herms, “In vivo imaging reveals reduced activity of neuronal circuits in a mouse tauopathy model,” Brain 142(4), 1051–1062 (2019).
[Crossref]

Chem. Eur. J. (1)

H. Shirani, M. Linares, C. J. Sigurdson, M. Lindgren, P. Norman, and K. P. Nilsson, “A Palette of Fluorescent Thiophene-Based Ligands for the Identification of Protein Aggregates,” Chem. Eur. J. 21(43), 15133–15137 (2015).
[Crossref]

Chem. Soc. Rev. (1)

P. Verwilst, H. S. Kim, S. Kim, C. Kang, and J. S. Kim, “Shedding light on tau protein aggregation: the progress in developing highly selective fluorophores,” Chem. Soc. Rev. 47(7), 2249–2265 (2018).
[Crossref]

Curr. Opin. Chem. Biol. (1)

I. Gregor and J. Enderlein, “Image scanning microscopy,” Curr. Opin. Chem. Biol. 51, 74–83 (2019).
[Crossref]

EBioMedicine (1)

Q. Wu, Y. Lin, J. Gu, and E. M. Sigurdsson, “Dynamic assessment of tau immunotherapies in the brains of live animals by two-photon imaging,” EBioMedicine 35, 270–278 (2018).
[Crossref]

Eur. J. Nucl. Med. Mol. Imaging (2)

H. Kroth, F. Oden, J. Molette, H. Schieferstein, F. Capotosti, A. Mueller, M. Berndt, H. Schmitt-Willich, V. Darmency, E. Gabellieri, C. Boudou, T. Juergens, Y. Varisco, E. Vokali, D. T. Hickman, G. Tamagnan, A. Pfeifer, L. Dinkelborg, A. Muhs, and A. Stephens, “Discovery and preclinical characterization of [(18)F]PI-2620, a next-generation tau PET tracer for the assessment of tau pathology in Alzheimer's disease and other tauopathies,” Eur. J. Nucl. Med. Mol. Imaging 46(10), 2178–2189 (2019).
[Crossref]

S. Sanabria Bohorquez, J. Marik, A. Ogasawara, J. N. Tinianow, H. S. Gill, O. Barret, G. Tamagnan, D. Alagille, G. Ayalon, P. Manser, T. Bengtsson, M. Ward, S. P. Williams, G. A. Kerchner, J. P. Seibyl, K. Marek, and R. M. Weimer, “[(18)F]GTP1 (Genentech Tau Probe 1), a radioligand for detecting neurofibrillary tangle tau pathology in Alzheimer's disease,” Eur. J. Nucl. Med. Mol. Imaging 46(10), 2077–2089 (2019).
[Crossref]

FASEB J. (1)

C. A. Lasagna-Reeves, D. L. Castillo-Carranza, U. Sengupta, J. Sarmiento, J. Troncoso, G. R. Jackson, and R. Kayed, “Identification of oligomers at early stages of tau aggregation in Alzheimer's disease,” FASEB J. 26(5), 1946–1959 (2012).
[Crossref]

FEBS Lett. (1)

A. Velasco, G. Fraser, P. Delobel, B. Ghetti, I. Lavenir, and M. Goedert, “Detection of filamentous tau inclusions by the fluorescent Congo red derivative FSB [(trans,trans)-1-fluoro-2,5-bis(3-hydroxycarbonyl-4-hydroxy)styrylbenzene],” FEBS Lett. 582(6), 901–906 (2008).
[Crossref]

Front Neurol. (1)

N. Sahara, M. Shimojo, M. Ono, H. Takuwa, M. Febo, M. Higuchi, and T. Suhara, “In Vivo Tau Imaging for a Diagnostic Platform of Tauopathy Using the rTg4510 Mouse Line,” Front Neurol. 8, 663 (2017).
[Crossref]

J. Alzheimer’s Dis. (1)

A. Ishikawa, M. Tokunaga, J. Maeda, T. Minamihisamatsu, M. Shimojo, H. Takuwa, M. Ono, R. Ni, S. Hirano, S. Kuwabara, B. Ji, M. R. Zhang, I. Aoki, T. Suhara, M. Higuchi, and N. Sahara, “In Vivo Visualization of Tau Accumulation, Microglial Activation, and Brain Atrophy in a Mouse Model of Tauopathy rTg4510,” J. Alzheimer’s Dis. 61(3), 1037–1052 (2018).
[Crossref]

J. Biol. Chem. (1)

J. Gotz, F. Chen, R. Barmettler, and R. M. Nitsch, “Tau filament formation in transgenic mice expressing P301L tau,” J. Biol. Chem. 276(1), 529–534 (2001).
[Crossref]

J. Cereb. Blood Flow Metab. (1)

J. Klohs, N. Baeva, J. Steinbrink, R. Bourayou, C. Boettcher, G. Royl, D. Megow, U. Dirnagl, J. Priller, and A. Wunder, “In vivo near-infrared fluorescence imaging of matrix metalloproteinase activity after cerebral ischemia,” J. Cereb. Blood Flow Metab. 29(7), 1284–1292 (2009).
[Crossref]

J. Exp. Med. (1)

I. B. Mazo, J.-C. Gutierrez-Ramos, P. S. Frenette, R. O. Hynes, D. D. Wagner, and U. H. von Andrian, “Hematopoietic Progenitor Cell Rolling in Bone Marrow Microvessels: Parallel Contributions by Endothelial Selectins and Vascular Cell Adhesion Molecule 1,” J. Exp. Med. 188(3), 465–474 (1998).
[Crossref]

J. Neuroscience (1)

S. Krishnaswamy, Y. Lin, W. J. Rajamohamedsait, H. B. Rajamohamedsait, P. Krishnamurthy, and E. M. Sigurdsson, “Antibody-derived in vivo imaging of tau pathology,” J. Neuroscience 34(50), 16835–16850 (2014).
[Crossref]

J. Nucl. Med. (2)

R. Ni, B. Ji, M. Ono, N. Sahara, M. R. Zhang, I. Aoki, A. Nordberg, T. Suhara, and M. Higuchi, ““Comparative in-vitro and in-vivo quantifications of pathological tau deposits and their association with neurodegeneration in tauopathy mouse models,” Journal of nuclear medicine : official publication,” J. Nucl. Med. 59(6), 960–966 (2018).
[Crossref]

A. Mueller, S. Bullich, O. Barret, J. Madonia, M. Berndt, C. Papin, A. Perrotin, N. Koglin, H. Kroth, A. Pfeifer, G. Tamagnan, J. P. Seibyl, K. Marek, S. de Santi, L. M. Dinkelborg, and A. W. Stephens, “Tau PET imaging with (18)F-PI-2620 in patients with Alzheimer's disease and healthy controls: a first-in-human study,” J. Nucl. Med. 61(6), 911–919 (2020).
[Crossref]

J. Nuclear Medicine (1)

E. D. Hostetler, A. M. Walji, Z. Zeng, P. Miller, I. Bennacef, C. Salinas, B. Connolly, L. Gantert, H. Haley, M. Holahan, M. Purcell, K. Riffel, T. G. Lohith, P. Coleman, A. Soriano, A. Ogawa, S. Xu, X. Zhang, E. Joshi, J. Della Rocca, D. Hesk, D. J. Schenk, and J. L. Evelhoch, ““Preclinical Characterization of 18F-MK-6240, a Promising PET Tracer for In Vivo Quantification of Human Neurofibrillary Tangles,” Journal of nuclear medicine : official publication,” J. Nuclear Medicine 57(10), 1599–1606 (2016).
[Crossref]

JAMA Neurol. (1)

B. J. Hanseeuw, R. A. Betensky, H. I. L. Jacobs, A. P. Schultz, J. Sepulcre, J. A. Becker, D. M. O. Cosio, M. Farrell, Y. T. Quiroz, E. C. Mormino, R. F. Buckley, K. V. Papp, R. A. Amariglio, I. Dewachter, A. Ivanoiu, W. Huijbers, T. Hedden, G. A. Marshall, J. P. Chhatwal, D. M. Rentz, R. A. Sperling, and K. Johnson, “Association of Amyloid and Tau With Cognition in Preclinical Alzheimer Disease: A Longitudinal Study,” JAMA Neurol. 76(8), 915–924 (2019).
[Crossref]

Lancet Neurol. (1)

M. G. Spillantini and M. Goedert, “Tau pathology and neurodegeneration,” Lancet Neurol. 12(6), 609–622 (2013).
[Crossref]

Laser Photonics Rev. (1)

Z. Chen, B. Mc Larney, J. Rebling, X. L. Deán-Ben, Q. Zhou, S. Gottschalk, and D. Razansky, “High-Speed Large-Field Multifocal Illumination Fluorescence Microscopy,” Laser Photonics Rev. 14, 1900070 (2020).
[Crossref]

Mol. Neurodegener. (1)

T. K. Patel, L. Habimana-Griffin, X. Gao, B. Xu, S. Achilefu, K. Alitalo, C. A. McKee, P. W. Sheehan, E. S. Musiek, C. Xiong, D. Coble, and D. M. Holtzman, “Dural lymphatics regulate clearance of extracellular tau from the CNS,” Mol. Neurodegener. 14(1), 11 (2019).
[Crossref]

Nat. Biomed. Eng. (1)

S. Gottschalk, O. Degtyaruk, B. Mc Larney, J. Rebling, M. A. Hutter, X. L. Deán-Ben, S. Shoham, and D. Razansky, “Rapid volumetric optoacoustic imaging of neural dynamics across the mouse brain,” Nat. Biomed. Eng. 3(5), 392–401 (2019).
[Crossref]

Nat. Biotechnol. (1)

M. Hintersteiner, A. Enz, P. Frey, A. L. Jaton, W. Kinzy, R. Kneuer, U. Neumann, M. Rudin, M. Staufenbiel, M. Stoeckli, K. H. Wiederhold, and H. U. Gremlich, “In vivo detection of amyloid-beta deposits by near-infrared imaging using an oxazine-derivative probe,” Nat. Biotechnol. 23(5), 577–583 (2005).
[Crossref]

Nat. Commun. (2)

Z. He, J. D. McBride, H. Xu, L. Changolkar, S. J. Kim, B. Zhang, S. Narasimhan, G. S. Gibbons, J. L. Guo, M. Kozak, G. D. Schellenberg, J. Q. Trojanowski, and V. M. Lee, “Transmission of tauopathy strains is independent of their isoform composition,” Nat. Commun. 11(1), 7 (2020).
[Crossref]

S. Hashimoto, Y. Matsuba, N. Kamano, N. Mihira, N. Sahara, J. Takano, S. I. Muramatsu, T. C. Saido, and T. Saito, “Tau binding protein CAPON induces tau aggregation and neurodegeneration,” Nat. Commun. 10(1), 2394 (2019).
[Crossref]

Nat. Genet. (1)

J. Lewis, E. McGowan, J. Rockwood, H. Melrose, P. Nacharaju, M. Van Slegtenhorst, K. Gwinn-Hardy, M. Paul Murphy, M. Baker, X. Yu, K. Duff, J. Hardy, A. Corral, W. L. Lin, S. H. Yen, D. W. Dickson, P. Davies, and M. Hutton, “Neurofibrillary tangles, amyotrophy and progressive motor disturbance in mice expressing mutant (P301L) tau protein,” Nat. Genet. 25(4), 402–405 (2000).
[Crossref]

Nat. Neurosci. (1)

P. Füger, J. K. Hefendehl, K. Veeraraghavalu, A.-C. Wendeln, C. Schlosser, U. Obermüller, B. M. Wegenast-Braun, J. J. Neher, P. Martus, S. Kohsaka, M. Thunemann, R. Feil, S. S. Sisodia, A. Skodras, and M. Jucker, “Microglia turnover with aging and in an Alzheimer's model via long-term in vivo single-cell imaging,” Nat. Neurosci. 20(10), 1371–1376 (2017).
[Crossref]

Nat. Rev. Neurol. (2)

V. L. Villemagne, V. Dore, S. C. Burnham, C. L. Masters, and C. C. Rowe, “Imaging tau and amyloid-beta proteinopathies in Alzheimer disease and other conditions,” Nat. Rev. Neurol. 14(4), 225–236 (2018).
[Crossref]

E. E. Congdon and E. M. Sigurdsson, “Tau-targeting therapies for Alzheimer disease,” Nat. Rev. Neurol. 14(7), 399–415 (2018).
[Crossref]

Nature (3)

B. M. Burmann, J. A. Gerez, I. Matecko-Burmann, S. Campioni, P. Kumari, D. Ghosh, A. Mazur, E. E. Aspholm, D. Sulskis, M. Wawrzyniuk, T. Bock, A. Schmidt, S. G. D. Rudiger, R. Riek, and S. Hiller, “Regulation of alpha-synuclein by chaperones in mammalian cells,” Nature 577(7788), 127–132 (2020).
[Crossref]

A. de Calignon, L. M. Fox, R. Pitstick, G. A. Carlson, B. J. Bacskai, T. L. Spires-Jones, and B. T. Hyman, “Caspase activation precedes and leads to tangles,” Nature 464(7292), 1201–1204 (2010).
[Crossref]

A. W. P. Fitzpatrick, B. Falcon, S. He, A. G. Murzin, G. Murshudov, H. J. Garringer, R. A. Crowther, B. Ghetti, M. Goedert, and S. H. W. Scheres, “Cryo-EM structures of tau filaments from Alzheimer's disease,” Nature 547(7662), 185–190 (2017).
[Crossref]

Neuron (6)

S. K. Kaufman, D. W. Sanders, T. L. Thomas, A. J. Ruchinskas, J. Vaquer-Alicea, A. M. Sharma, T. M. Miller, and M. I. Diamond, “Tau Prion Strains Dictate Patterns of Cell Pathology, Progression Rate, and Regional Vulnerability In Vivo,” Neuron 92(4), 796–812 (2016).
[Crossref]

K. M. Schoch, S. L. DeVos, R. L. Miller, S. J. Chun, M. Norrbom, D. F. Wozniak, H. N. Dawson, C. F. Bennett, F. Rigo, and T. M. Miller, “Increased 4R-Tau Induces Pathological Changes in a Human-Tau Mouse Model,” Neuron 90(5), 941–947 (2016).
[Crossref]

B. Dejanovic, M. A. Huntley, A. De Maziere, W. J. Meilandt, T. Wu, K. Srinivasan, Z. Jiang, V. Gandham, B. A. Friedman, H. Ngu, O. Foreman, R. A. D. Carano, B. Chih, J. Klumperman, C. Bakalarski, J. E. Hanson, and M. Sheng, “Changes in the Synaptic Proteome in Tauopathy and Rescue of Tau-Induced Synapse Loss by C1q Antibodies,” Neuron 100(6), 1322–1336.e7 (2018).
[Crossref]

M. Maruyama, H. Shimada, T. Suhara, H. Shinotoh, B. Ji, J. Maeda, M. R. Zhang, J. Q. Trojanowski, V. M. Lee, M. Ono, K. Masamoto, H. Takano, N. Sahara, N. Iwata, N. Okamura, S. Furumoto, Y. Kudo, Q. Chang, T. C. Saido, A. Takashima, J. Lewis, M. K. Jang, I. Aoki, H. Ito, and M. Higuchi, “Imaging of tau pathology in a tauopathy mouse model and in Alzheimer patients compared to normal controls,” Neuron 79(6), 1094–1108 (2013).
[Crossref]

M. Scholl, S. N. Lockhart, D. R. Schonhaut, J. P. O’Neil, M. Janabi, R. Ossenkoppele, S. L. Baker, J. W. Vogel, J. Faria, H. D. Schwimmer, G. D. Rabinovici, and W. J. Jagust, “PET Imaging of Tau Deposition in the Aging Human Brain,” Neuron 89(5), 971–982 (2016).
[Crossref]

Y. Yoshiyama, M. Higuchi, B. Zhang, S. M. Huang, N. Iwata, T. C. Saido, J. Maeda, T. Suhara, J. Q. Trojanowski, and V. M. Lee, “Synapse loss and microglial activation precede tangles in a P301S tauopathy mouse model,” Neuron 53(3), 337–351 (2007).
[Crossref]

Neurophotonics (1)

R. Ni, M. Vaas, W. Ren, and J. Klohs, “Non-invasive detection of acute cerebral hypoxia and subsequent matrix-metalloproteinase activity in a mouse model of cerebral ischemia using multispectral-optoacoustic-tomography,” Neurophotonics 5(1), 015005 (2018).
[Crossref]

Org. Biomol. Chem. (1)

T. Klingstedt, A. Aslund, R. A. Simon, L. B. Johansson, J. J. Mason, S. Nystrom, P. Hammarstrom, and K. P. Nilsson, “Synthesis of a library of oligothiophenes and their utilization as fluorescent ligands for spectral assignment of protein aggregates,” Org. Biomol. Chem. 9(24), 8356–8370 (2011).
[Crossref]

Proc. Natl. Acad. Sci. (1)

K. V. Kuchibhotla, S. Wegmann, K. J. Kopeikina, J. Hawkes, N. Rudinskiy, M. L. Andermann, T. L. Spires-Jones, B. J. Bacskai, and B. T. Hyman, “Neurofibrillary tangle-bearing neurons are functionally integrated in cortical circuits in vivo,” Proc. Natl. Acad. Sci. 111(1), 510–514 (2014).
[Crossref]

Quant. Imaging Med. Surg. (1)

Y. Zhang, C. Zhang, X. Zhong, and D. Zhu, “Quantitative evaluation of SOCS-induced optical clearing efficiency of skull,” Quant. Imaging Med. Surg. 5, 136–142 (2015).
[Crossref]

Sci. Transl. Med. (2)

J. A. Gerez, N. C. Prymaczok, E. Rockenstein, U. S. Herrmann, P. Schwarz, A. Adame, R. I. Enchev, T. Courtheoux, P. J. Boersema, R. Riek, M. Peter, A. Aguzzi, E. Masliah, and P. Picotti, “A cullin-RING ubiquitin ligase targets exogenous alpha-synuclein and inhibits Lewy body-like pathology,” Sci. Transl. Med. 11(495), eaau6722 (2019).
[Crossref]

R. La Joie, A. V. Visani, S. L. Baker, J. A. Brown, V. Bourakova, J. Cha, K. Chaudhary, L. Edwards, L. Iaccarino, M. Janabi, O. H. Lesman-Segev, Z. A. Miller, D. C. Perry, J. P. O’Neil, J. Pham, J. C. Rojas, H. J. Rosen, W. W. Seeley, R. M. Tsai, B. L. Miller, W. J. Jagust, and G. D. Rabinovici, “Prospective longitudinal atrophy in Alzheimer’s disease correlates with the intensity and topography of baseline tau-PET,” Sci. Transl. Med. 12(524), eaau5732 (2020).
[Crossref]

Science (2)

K. SantaCruz, J. Lewis, T. Spires, J. Paulson, L. Kotilinek, M. Ingelsson, A. Guimaraes, M. DeTure, M. Ramsden, E. McGowan, C. Forster, M. Yue, J. Orne, C. Janus, A. Mariash, M. Kuskowski, B. Hyman, M. Hutton, and K. H. Ashe, “Tau Suppression in a Neurodegenerative Mouse Model Improves Memory Function,” Science 309(5733), 476–481 (2005).
[Crossref]

J. Gotz, F. Chen, J. van Dorpe, and R. M. Nitsch, “Formation of neurofibrillary tangles in P301 l tau transgenic mice induced by Abeta 42 fibrils,” Science 293(5534), 1491–1495 (2001).
[Crossref]

Other (4)

R. Ni, Z. Chen, G. Shi, A. Villois, Q. Zhou, P. Arosio, R. M. Nitsch, P. R. Nilsson, J. Klohs, and D. Razansky, “Transcranial in vivo detection of Aβ at single plaque resolution with large-field multifocal illumination fluorescence microscopy,” bioRxiv, 2020.2002.2001.929844 (2020).

R. Ni, Y. Zarb, G. A. Kuhn, R. Müller, Y. Yundung, R. M. Nitsch, L. Kulic, A. Keller, and J. Klohs, “Tau deposition is associated with imaging patterns of tissue calcification in the P301L mouse model of human tauopathy,” bioRxiv, 851915 (2019).

R. Ni, X. L. Dean-Ben, D. Kirschenbaum, M. Rudin, Z. Chen, A. Crimi, F. Voigt, P. R. Nilsson, F. Helmchen, R. M. Nitsch, A. Aguzzi, D. Razansky, and J. Klohs, “Whole brain optoacoustic tomography reveals strain-specific regional beta-amyloid densities in Alzheimer`s disease amyloidosis models,” bioRxiv, DOI: 10.1101/2020.1102.1125.964064 (2020).

J. Klohs, “An Integrated View on Vascular Dysfunction in Alzheimer’s Disease,” Neurodegenerative Diseases (2020).

Cited By

OSA participates in Crossref's Cited-By Linking service. Citing articles from OSA journals and other participating publishers are listed here.

Alert me when this article is cited.


Figures (5)

Fig. 1.
Fig. 1. Comparison of the selectivity of different fluorescent probes to protein aggregates. Binding of (a) Thioflavin-T, (b) AOI987, and (c-f) LCOs HS-169, HS-84, h-FTAA and q-FTAA to recombinant Aβ42 fibril, and tau fibril.

View in Article | Download Full Size | PPT Slide | PDF

Fig. 2.
Fig. 2. Evaluation of the cellular binding of luminescent conjugated oligothiophenes on P301L mouse brain tissue sections. Horizontal cortical brain sections from 10 months-of-age P301L mouse stained with (a) q-FTAA (green)/DAPI (white); (b, c) h-FTAA (green)/DAPI (white) and zoom-in; (e) HS-169 (red)/DAPI (white), and (f, g) HS-84 (green)/DAPI (white) and zoom-in;. Scale bar = 200 μm (a, b, e, f), 10 μm (c, g); (d, h) Lambda spectrum mapping of h-FTAA (c) and HS-84 (g) staining on P301L mouse brain slices showing the peak of binding.

View in Article | Download Full Size | PPT Slide | PDF

Fig. 3.
Fig. 3. In vivo large-field multifocal illumination (LMI) imaging of tauopathy. (a-c) In vivo LMI n the brain of P301L mice at 10- and 17 months-of-age, and non-transgenic littermate (NTL) at pre-injection and following i.v. tail vein bolus injection of h-FTAA till120 min post-injection. Fluorescence intensity (F.I.) normalized to pre-injection values; (d) Quantification of Fpost/Fpre) injection over time; NTL, n = 3, P301L n = 4; (e) Higher normalized F60-120 min/Fpre in P301L compare to NTL mice, *** p < 0.001 two-way ANOVA. Scale bar = 200 μm (a-c). (f-g) Corresponding LMI and widefield (WF) imaging and zoom-in views at 80 minutes post-injection in P301L mouse (b).

View in Article | Download Full Size | PPT Slide | PDF

Fig. 4.
Fig. 4. Ex vivo large-field multifocal illumination (LMI) imaging compared to widefield (WF) fluorescence microscopy of tauopathy in P301L mouse brain. (a-b) Ex vivo WF and LMI imaging of one P301L mouse brain (signal ROI (red square), and background region (bk, blue square)); (c-d) Ex vivo LMI and zoom-in showing signal spots in the cortex of P301L mouse brain; Normalized representative LMI imaging in (e-h) 10 months-old P301L and (i-l) age-matched non-transgenic littermate mouse; (e, i) in vivo mouse head at 120 min post-injection, (f, j) ex vivo skull, (g, k) ex vivo whole brain and (h, l) zoomed-in coronal brain slices; (m) Higher contrast-to-noise ratio (CNR) in LMI imaging compared to widefield imaging analyzed using over P301 l mouse ex vivo cortex; (n) Quantification of signals in the brain and in the skull in P301L and non-transgenic littermate mice; * p < 0.05, ** p < 0.01, *** p < 0.001 t-test (m, n).

View in Article | Download Full Size | PPT Slide | PDF

Fig. 5.
Fig. 5. Specificity of h-FTAA for tauopathy in P301L mouse brain tissue sections. (a-c) Immunohistochemistry of horizontal brain sections from the cortex and hippocampus of P301L mouse, demonstrating co-localization of AT-8, AT-100 and h-FTAA to tauopathy in P301L mouse brain; (d-g) No specific signals in the cortex and hippocampus of non-transgenic littermate mouse brain are stained by AT-8/ h-FTAA or AT-100/h-FTAA. (a, b, d, e) AT-8 (red), (c, f, g) AT-100 (red), h-FTAA (green), DAPI (white).

View in Article | Download Full Size | PPT Slide | PDF

Equations (1)

Equations on this page are rendered with MathJax. Learn more.

C N R = ( S _ R O I 1 − S _ R O I 2 ) N

Metrics