P. V. Jena, P. S. Shirude, B. Okumus, K. Laxmi-Reddy, F. Godde, I. Huc, S. Balasubramanian, and T. Ha, “G-Quadruplex DNA Bound by a Synthetic Ligand is Highly Dynamic,” J. Am. Chem. Soc. 131(35), 12522–12523 (2009).
[Crossref]
[PubMed]
D. Evanko, “Nature Milestones in Light Microscopy. Milestone 17. Single molecules in the dark,” Nature (October): (2009), doi:.
H. P. Lu, “Single-molecule protein interaction conformational dynamics,” Curr. Pharm. Biotechnol. 10(5), 522–531 (2009).
[Crossref]
[PubMed]
T. Cordes, J. Vogelsang, and P. Tinnefeld, “On the Mechanism of Trolox as Antiblinking and Antibleaching Reagent,” J. Am. Chem. Soc. 131, 5018 (2009).
[Crossref]
[PubMed]
E. Meiss, H. Konno, G. Groth, and T. Hisabori, “Molecular processes of inhibition and stimulation of ATP synthase caused by the phytotoxin tentoxin,” J. Biol. Chem. 283(36), 24594–24553 (2008).
[Crossref]
[PubMed]
R. Luchowski, E. G. Matveeva, I. Gryczynski, E. A. Terpetschnig, L. Patsenker, G. Laczko, J. Borejdo, and Z. Gryczynski, “Single Molecule Studies of Multiple-Fluorophore Labeled Antibodies. Effect of Homo-FRET on the Number of Photons Available Before Photobleaching,” Curr. Pharm. Biotechnol. 9(5), 411–420 (2008).
[Crossref]
[PubMed]
R. Luchowski, P. Sarkar, S. Bharill, G. Laczko, J. Borejdo, Z. Gryczynski, and I. Gryczynski, “Fluorescence polarization standard for near infrared spectroscopy and microscopy,” Appl. Opt. 47(33), 6257–6265 (2008).
[Crossref]
[PubMed]
I. Gregor and J. Enderlein, “Time-resolved methods in biophysics. 3. Fluorescence lifetime correlation spectroscopy,” Photochem. Photobiol. Sci. 6(1), 13–18 (2007).
[Crossref]
[PubMed]
A. M. De Grand, S. J. Lomnes, D. S. Lee, M. Pietrzykowski, S. Ohnishi, T. G. Morgan, A. Gogbashian, R. G. Laurence, and J. V. Frangioni, “Tissue-like phantoms for near-infrared fluorescence imaging system assessment and the training of surgeons,” J. Biomed. Opt. 11(1), 10 (2006).
[Crossref]
S. Syed, G. E. Snyder, C. Franzini-Armstrong, P. R. Selvin, and Y. E. Goldman, “Adaptability of myosin V studied by simultaneous detection of position and orientation,” EMBO J. 25(9), 1795–1803 (2006).
[Crossref]
[PubMed]
S. Hohng and T. Ha, “Single-molecule quantum-dot fluorescence resonance energy transfer,” ChemPhysChem 6(5), 956–960 (2005).
[Crossref]
[PubMed]
J. Enderlein and I. Gregor, “Using fluorescence lifetime for discriminating detector afterpulsing in fluorescence-correlation spectroscopy,” Rev. Sci. Instrum. 76(3), 5 (2005).
[Crossref]
S. A. Rosenberg, M. E. Quinlan, J. N. Forkey, and Y. E. Goldman, “Rotational motions of macro-molecules by single-molecule fluorescence microscopy,” Acc. Chem. Res. 38(7), 583–593 (2005).
[Crossref]
[PubMed]
M. L. Barcellona, S. Gammon, T. Hazlett, M. A. Digman, and E. Gratton, “Polarized fluorescence Correlation spectroscopy of DNA-DAPI complexes,” Microsc. Res. Tech. 65(4-5), 205–217 (2004).
[Crossref]
S. Hohng, C. Joo, and T. Ha, “Single-molecule three-color FRET,” Biophys. J. 87(2), 1328–1337 (2004).
[Crossref]
[PubMed]
J. N. Forkey, M. E. Quinlan, M. A. Shaw, J. E. T. Corrie, and Y. E. Goldman, “Three-dimensional structural dynamics of myosin V by single-molecule fluorescence polarization,” Nature 422(6930), 399–404 (2003).
[Crossref]
[PubMed]
A. Yildiz, J. N. Forkey, S. A. McKinney, T. Ha, Y. E. Goldman, and P. R. Selvin, “Myosin V walks hand-over-hand: single fluorophore imaging with 1.5-nm localization,” Science 300(5628), 2061–2065 (2003).
[Crossref]
[PubMed]
L. Edman, Z. Földes-Papp, S. Wennmalm, and R. Rigler, “The fluctuating enzyme: a single molecule approach,” Chem. Phys. 247(1), 11–22 (1999).
[Crossref]
A. P. Bartko and R. M. Dickson, “Imaging three-dimensional single molecule orientations,” J. Phys. Chem. B 103(51), 11237–11241 (1999).
[Crossref]
H. P. Lu, L. Xun, and X. S. Xie, “Single-molecule enzymatic dynamics,” Science 282(5395), 1877–1882 (1998).
[Crossref]
[PubMed]
M. Tokunaga, K. Kitamura, K. Saito, A. H. Iwane, and T. Yanagida, “Single molecule imaging of fluorophores and enzymatic reactions achieved by objective-type total internal reflection fluorescence microscopy,” Biochem. Biophys. Res. Commun. 235(1), 47–53 (1997).
[Crossref]
[PubMed]
E. L. Elson and D. Magde, “Fluorescence correlation spectroscopy. I. Conceptual basis and theory,” Biopolymers 13(1), 1–27 (1974).
[Crossref]
D. Magde, E. L. Elson, and W. W. Webb, “Fluorescence correlation spectroscopy. II. An experimental realization,” Biopolymers 13(1), 29–61 (1974).
[Crossref]
[PubMed]
D. Magde, E. L. Elson, and W. W. Webb, “Thermodynamic fluctuations in reacting system: measurements by fluorescence correlation spectroscopy,” Phys. Rev. Lett. 29(11), 705–708 (1972).
[Crossref]
P. V. Jena, P. S. Shirude, B. Okumus, K. Laxmi-Reddy, F. Godde, I. Huc, S. Balasubramanian, and T. Ha, “G-Quadruplex DNA Bound by a Synthetic Ligand is Highly Dynamic,” J. Am. Chem. Soc. 131(35), 12522–12523 (2009).
[Crossref]
[PubMed]
M. L. Barcellona, S. Gammon, T. Hazlett, M. A. Digman, and E. Gratton, “Polarized fluorescence Correlation spectroscopy of DNA-DAPI complexes,” Microsc. Res. Tech. 65(4-5), 205–217 (2004).
[Crossref]
A. P. Bartko and R. M. Dickson, “Imaging three-dimensional single molecule orientations,” J. Phys. Chem. B 103(51), 11237–11241 (1999).
[Crossref]
R. Luchowski, P. Sarkar, S. Bharill, G. Laczko, J. Borejdo, Z. Gryczynski, and I. Gryczynski, “Fluorescence polarization standard for near infrared spectroscopy and microscopy,” Appl. Opt. 47(33), 6257–6265 (2008).
[Crossref]
[PubMed]
R. Luchowski, E. G. Matveeva, I. Gryczynski, E. A. Terpetschnig, L. Patsenker, G. Laczko, J. Borejdo, and Z. Gryczynski, “Single Molecule Studies of Multiple-Fluorophore Labeled Antibodies. Effect of Homo-FRET on the Number of Photons Available Before Photobleaching,” Curr. Pharm. Biotechnol. 9(5), 411–420 (2008).
[Crossref]
[PubMed]
T. Cordes, J. Vogelsang, and P. Tinnefeld, “On the Mechanism of Trolox as Antiblinking and Antibleaching Reagent,” J. Am. Chem. Soc. 131, 5018 (2009).
[Crossref]
[PubMed]
J. N. Forkey, M. E. Quinlan, M. A. Shaw, J. E. T. Corrie, and Y. E. Goldman, “Three-dimensional structural dynamics of myosin V by single-molecule fluorescence polarization,” Nature 422(6930), 399–404 (2003).
[Crossref]
[PubMed]
A. M. De Grand, S. J. Lomnes, D. S. Lee, M. Pietrzykowski, S. Ohnishi, T. G. Morgan, A. Gogbashian, R. G. Laurence, and J. V. Frangioni, “Tissue-like phantoms for near-infrared fluorescence imaging system assessment and the training of surgeons,” J. Biomed. Opt. 11(1), 10 (2006).
[Crossref]
A. P. Bartko and R. M. Dickson, “Imaging three-dimensional single molecule orientations,” J. Phys. Chem. B 103(51), 11237–11241 (1999).
[Crossref]
M. L. Barcellona, S. Gammon, T. Hazlett, M. A. Digman, and E. Gratton, “Polarized fluorescence Correlation spectroscopy of DNA-DAPI complexes,” Microsc. Res. Tech. 65(4-5), 205–217 (2004).
[Crossref]
L. Edman, Z. Földes-Papp, S. Wennmalm, and R. Rigler, “The fluctuating enzyme: a single molecule approach,” Chem. Phys. 247(1), 11–22 (1999).
[Crossref]
D. Magde, E. L. Elson, and W. W. Webb, “Fluorescence correlation spectroscopy. II. An experimental realization,” Biopolymers 13(1), 29–61 (1974).
[Crossref]
[PubMed]
E. L. Elson and D. Magde, “Fluorescence correlation spectroscopy. I. Conceptual basis and theory,” Biopolymers 13(1), 1–27 (1974).
[Crossref]
D. Magde, E. L. Elson, and W. W. Webb, “Thermodynamic fluctuations in reacting system: measurements by fluorescence correlation spectroscopy,” Phys. Rev. Lett. 29(11), 705–708 (1972).
[Crossref]
I. Gregor and J. Enderlein, “Time-resolved methods in biophysics. 3. Fluorescence lifetime correlation spectroscopy,” Photochem. Photobiol. Sci. 6(1), 13–18 (2007).
[Crossref]
[PubMed]
J. Enderlein and I. Gregor, “Using fluorescence lifetime for discriminating detector afterpulsing in fluorescence-correlation spectroscopy,” Rev. Sci. Instrum. 76(3), 5 (2005).
[Crossref]
D. Evanko, “Nature Milestones in Light Microscopy. Milestone 17. Single molecules in the dark,” Nature (October): (2009), doi:.
L. Edman, Z. Földes-Papp, S. Wennmalm, and R. Rigler, “The fluctuating enzyme: a single molecule approach,” Chem. Phys. 247(1), 11–22 (1999).
[Crossref]
S. A. Rosenberg, M. E. Quinlan, J. N. Forkey, and Y. E. Goldman, “Rotational motions of macro-molecules by single-molecule fluorescence microscopy,” Acc. Chem. Res. 38(7), 583–593 (2005).
[Crossref]
[PubMed]
J. N. Forkey, M. E. Quinlan, M. A. Shaw, J. E. T. Corrie, and Y. E. Goldman, “Three-dimensional structural dynamics of myosin V by single-molecule fluorescence polarization,” Nature 422(6930), 399–404 (2003).
[Crossref]
[PubMed]
A. Yildiz, J. N. Forkey, S. A. McKinney, T. Ha, Y. E. Goldman, and P. R. Selvin, “Myosin V walks hand-over-hand: single fluorophore imaging with 1.5-nm localization,” Science 300(5628), 2061–2065 (2003).
[Crossref]
[PubMed]
A. M. De Grand, S. J. Lomnes, D. S. Lee, M. Pietrzykowski, S. Ohnishi, T. G. Morgan, A. Gogbashian, R. G. Laurence, and J. V. Frangioni, “Tissue-like phantoms for near-infrared fluorescence imaging system assessment and the training of surgeons,” J. Biomed. Opt. 11(1), 10 (2006).
[Crossref]
S. Syed, G. E. Snyder, C. Franzini-Armstrong, P. R. Selvin, and Y. E. Goldman, “Adaptability of myosin V studied by simultaneous detection of position and orientation,” EMBO J. 25(9), 1795–1803 (2006).
[Crossref]
[PubMed]
M. L. Barcellona, S. Gammon, T. Hazlett, M. A. Digman, and E. Gratton, “Polarized fluorescence Correlation spectroscopy of DNA-DAPI complexes,” Microsc. Res. Tech. 65(4-5), 205–217 (2004).
[Crossref]
P. V. Jena, P. S. Shirude, B. Okumus, K. Laxmi-Reddy, F. Godde, I. Huc, S. Balasubramanian, and T. Ha, “G-Quadruplex DNA Bound by a Synthetic Ligand is Highly Dynamic,” J. Am. Chem. Soc. 131(35), 12522–12523 (2009).
[Crossref]
[PubMed]
A. M. De Grand, S. J. Lomnes, D. S. Lee, M. Pietrzykowski, S. Ohnishi, T. G. Morgan, A. Gogbashian, R. G. Laurence, and J. V. Frangioni, “Tissue-like phantoms for near-infrared fluorescence imaging system assessment and the training of surgeons,” J. Biomed. Opt. 11(1), 10 (2006).
[Crossref]
S. Syed, G. E. Snyder, C. Franzini-Armstrong, P. R. Selvin, and Y. E. Goldman, “Adaptability of myosin V studied by simultaneous detection of position and orientation,” EMBO J. 25(9), 1795–1803 (2006).
[Crossref]
[PubMed]
S. A. Rosenberg, M. E. Quinlan, J. N. Forkey, and Y. E. Goldman, “Rotational motions of macro-molecules by single-molecule fluorescence microscopy,” Acc. Chem. Res. 38(7), 583–593 (2005).
[Crossref]
[PubMed]
J. N. Forkey, M. E. Quinlan, M. A. Shaw, J. E. T. Corrie, and Y. E. Goldman, “Three-dimensional structural dynamics of myosin V by single-molecule fluorescence polarization,” Nature 422(6930), 399–404 (2003).
[Crossref]
[PubMed]
A. Yildiz, J. N. Forkey, S. A. McKinney, T. Ha, Y. E. Goldman, and P. R. Selvin, “Myosin V walks hand-over-hand: single fluorophore imaging with 1.5-nm localization,” Science 300(5628), 2061–2065 (2003).
[Crossref]
[PubMed]
M. L. Barcellona, S. Gammon, T. Hazlett, M. A. Digman, and E. Gratton, “Polarized fluorescence Correlation spectroscopy of DNA-DAPI complexes,” Microsc. Res. Tech. 65(4-5), 205–217 (2004).
[Crossref]
I. Gregor and J. Enderlein, “Time-resolved methods in biophysics. 3. Fluorescence lifetime correlation spectroscopy,” Photochem. Photobiol. Sci. 6(1), 13–18 (2007).
[Crossref]
[PubMed]
J. Enderlein and I. Gregor, “Using fluorescence lifetime for discriminating detector afterpulsing in fluorescence-correlation spectroscopy,” Rev. Sci. Instrum. 76(3), 5 (2005).
[Crossref]
E. Meiss, H. Konno, G. Groth, and T. Hisabori, “Molecular processes of inhibition and stimulation of ATP synthase caused by the phytotoxin tentoxin,” J. Biol. Chem. 283(36), 24594–24553 (2008).
[Crossref]
[PubMed]
R. Luchowski, P. Sarkar, S. Bharill, G. Laczko, J. Borejdo, Z. Gryczynski, and I. Gryczynski, “Fluorescence polarization standard for near infrared spectroscopy and microscopy,” Appl. Opt. 47(33), 6257–6265 (2008).
[Crossref]
[PubMed]
R. Luchowski, E. G. Matveeva, I. Gryczynski, E. A. Terpetschnig, L. Patsenker, G. Laczko, J. Borejdo, and Z. Gryczynski, “Single Molecule Studies of Multiple-Fluorophore Labeled Antibodies. Effect of Homo-FRET on the Number of Photons Available Before Photobleaching,” Curr. Pharm. Biotechnol. 9(5), 411–420 (2008).
[Crossref]
[PubMed]
R. Luchowski, E. G. Matveeva, I. Gryczynski, E. A. Terpetschnig, L. Patsenker, G. Laczko, J. Borejdo, and Z. Gryczynski, “Single Molecule Studies of Multiple-Fluorophore Labeled Antibodies. Effect of Homo-FRET on the Number of Photons Available Before Photobleaching,” Curr. Pharm. Biotechnol. 9(5), 411–420 (2008).
[Crossref]
[PubMed]
R. Luchowski, P. Sarkar, S. Bharill, G. Laczko, J. Borejdo, Z. Gryczynski, and I. Gryczynski, “Fluorescence polarization standard for near infrared spectroscopy and microscopy,” Appl. Opt. 47(33), 6257–6265 (2008).
[Crossref]
[PubMed]
P. V. Jena, P. S. Shirude, B. Okumus, K. Laxmi-Reddy, F. Godde, I. Huc, S. Balasubramanian, and T. Ha, “G-Quadruplex DNA Bound by a Synthetic Ligand is Highly Dynamic,” J. Am. Chem. Soc. 131(35), 12522–12523 (2009).
[Crossref]
[PubMed]
S. Hohng and T. Ha, “Single-molecule quantum-dot fluorescence resonance energy transfer,” ChemPhysChem 6(5), 956–960 (2005).
[Crossref]
[PubMed]
S. Hohng, C. Joo, and T. Ha, “Single-molecule three-color FRET,” Biophys. J. 87(2), 1328–1337 (2004).
[Crossref]
[PubMed]
A. Yildiz, J. N. Forkey, S. A. McKinney, T. Ha, Y. E. Goldman, and P. R. Selvin, “Myosin V walks hand-over-hand: single fluorophore imaging with 1.5-nm localization,” Science 300(5628), 2061–2065 (2003).
[Crossref]
[PubMed]
M. L. Barcellona, S. Gammon, T. Hazlett, M. A. Digman, and E. Gratton, “Polarized fluorescence Correlation spectroscopy of DNA-DAPI complexes,” Microsc. Res. Tech. 65(4-5), 205–217 (2004).
[Crossref]
E. Meiss, H. Konno, G. Groth, and T. Hisabori, “Molecular processes of inhibition and stimulation of ATP synthase caused by the phytotoxin tentoxin,” J. Biol. Chem. 283(36), 24594–24553 (2008).
[Crossref]
[PubMed]
S. Hohng and T. Ha, “Single-molecule quantum-dot fluorescence resonance energy transfer,” ChemPhysChem 6(5), 956–960 (2005).
[Crossref]
[PubMed]
S. Hohng, C. Joo, and T. Ha, “Single-molecule three-color FRET,” Biophys. J. 87(2), 1328–1337 (2004).
[Crossref]
[PubMed]
P. V. Jena, P. S. Shirude, B. Okumus, K. Laxmi-Reddy, F. Godde, I. Huc, S. Balasubramanian, and T. Ha, “G-Quadruplex DNA Bound by a Synthetic Ligand is Highly Dynamic,” J. Am. Chem. Soc. 131(35), 12522–12523 (2009).
[Crossref]
[PubMed]
M. Tokunaga, K. Kitamura, K. Saito, A. H. Iwane, and T. Yanagida, “Single molecule imaging of fluorophores and enzymatic reactions achieved by objective-type total internal reflection fluorescence microscopy,” Biochem. Biophys. Res. Commun. 235(1), 47–53 (1997).
[Crossref]
[PubMed]
P. V. Jena, P. S. Shirude, B. Okumus, K. Laxmi-Reddy, F. Godde, I. Huc, S. Balasubramanian, and T. Ha, “G-Quadruplex DNA Bound by a Synthetic Ligand is Highly Dynamic,” J. Am. Chem. Soc. 131(35), 12522–12523 (2009).
[Crossref]
[PubMed]
S. Hohng, C. Joo, and T. Ha, “Single-molecule three-color FRET,” Biophys. J. 87(2), 1328–1337 (2004).
[Crossref]
[PubMed]
M. Tokunaga, K. Kitamura, K. Saito, A. H. Iwane, and T. Yanagida, “Single molecule imaging of fluorophores and enzymatic reactions achieved by objective-type total internal reflection fluorescence microscopy,” Biochem. Biophys. Res. Commun. 235(1), 47–53 (1997).
[Crossref]
[PubMed]
E. Meiss, H. Konno, G. Groth, and T. Hisabori, “Molecular processes of inhibition and stimulation of ATP synthase caused by the phytotoxin tentoxin,” J. Biol. Chem. 283(36), 24594–24553 (2008).
[Crossref]
[PubMed]
R. Luchowski, P. Sarkar, S. Bharill, G. Laczko, J. Borejdo, Z. Gryczynski, and I. Gryczynski, “Fluorescence polarization standard for near infrared spectroscopy and microscopy,” Appl. Opt. 47(33), 6257–6265 (2008).
[Crossref]
[PubMed]
R. Luchowski, E. G. Matveeva, I. Gryczynski, E. A. Terpetschnig, L. Patsenker, G. Laczko, J. Borejdo, and Z. Gryczynski, “Single Molecule Studies of Multiple-Fluorophore Labeled Antibodies. Effect of Homo-FRET on the Number of Photons Available Before Photobleaching,” Curr. Pharm. Biotechnol. 9(5), 411–420 (2008).
[Crossref]
[PubMed]
A. M. De Grand, S. J. Lomnes, D. S. Lee, M. Pietrzykowski, S. Ohnishi, T. G. Morgan, A. Gogbashian, R. G. Laurence, and J. V. Frangioni, “Tissue-like phantoms for near-infrared fluorescence imaging system assessment and the training of surgeons,” J. Biomed. Opt. 11(1), 10 (2006).
[Crossref]
P. V. Jena, P. S. Shirude, B. Okumus, K. Laxmi-Reddy, F. Godde, I. Huc, S. Balasubramanian, and T. Ha, “G-Quadruplex DNA Bound by a Synthetic Ligand is Highly Dynamic,” J. Am. Chem. Soc. 131(35), 12522–12523 (2009).
[Crossref]
[PubMed]
A. M. De Grand, S. J. Lomnes, D. S. Lee, M. Pietrzykowski, S. Ohnishi, T. G. Morgan, A. Gogbashian, R. G. Laurence, and J. V. Frangioni, “Tissue-like phantoms for near-infrared fluorescence imaging system assessment and the training of surgeons,” J. Biomed. Opt. 11(1), 10 (2006).
[Crossref]
A. M. De Grand, S. J. Lomnes, D. S. Lee, M. Pietrzykowski, S. Ohnishi, T. G. Morgan, A. Gogbashian, R. G. Laurence, and J. V. Frangioni, “Tissue-like phantoms for near-infrared fluorescence imaging system assessment and the training of surgeons,” J. Biomed. Opt. 11(1), 10 (2006).
[Crossref]
H. P. Lu, “Single-molecule protein interaction conformational dynamics,” Curr. Pharm. Biotechnol. 10(5), 522–531 (2009).
[Crossref]
[PubMed]
H. P. Lu, L. Xun, and X. S. Xie, “Single-molecule enzymatic dynamics,” Science 282(5395), 1877–1882 (1998).
[Crossref]
[PubMed]
R. Luchowski, E. G. Matveeva, I. Gryczynski, E. A. Terpetschnig, L. Patsenker, G. Laczko, J. Borejdo, and Z. Gryczynski, “Single Molecule Studies of Multiple-Fluorophore Labeled Antibodies. Effect of Homo-FRET on the Number of Photons Available Before Photobleaching,” Curr. Pharm. Biotechnol. 9(5), 411–420 (2008).
[Crossref]
[PubMed]
R. Luchowski, P. Sarkar, S. Bharill, G. Laczko, J. Borejdo, Z. Gryczynski, and I. Gryczynski, “Fluorescence polarization standard for near infrared spectroscopy and microscopy,” Appl. Opt. 47(33), 6257–6265 (2008).
[Crossref]
[PubMed]
D. Magde, E. L. Elson, and W. W. Webb, “Fluorescence correlation spectroscopy. II. An experimental realization,” Biopolymers 13(1), 29–61 (1974).
[Crossref]
[PubMed]
E. L. Elson and D. Magde, “Fluorescence correlation spectroscopy. I. Conceptual basis and theory,” Biopolymers 13(1), 1–27 (1974).
[Crossref]
D. Magde, E. L. Elson, and W. W. Webb, “Thermodynamic fluctuations in reacting system: measurements by fluorescence correlation spectroscopy,” Phys. Rev. Lett. 29(11), 705–708 (1972).
[Crossref]
R. Luchowski, E. G. Matveeva, I. Gryczynski, E. A. Terpetschnig, L. Patsenker, G. Laczko, J. Borejdo, and Z. Gryczynski, “Single Molecule Studies of Multiple-Fluorophore Labeled Antibodies. Effect of Homo-FRET on the Number of Photons Available Before Photobleaching,” Curr. Pharm. Biotechnol. 9(5), 411–420 (2008).
[Crossref]
[PubMed]
A. Yildiz, J. N. Forkey, S. A. McKinney, T. Ha, Y. E. Goldman, and P. R. Selvin, “Myosin V walks hand-over-hand: single fluorophore imaging with 1.5-nm localization,” Science 300(5628), 2061–2065 (2003).
[Crossref]
[PubMed]
E. Meiss, H. Konno, G. Groth, and T. Hisabori, “Molecular processes of inhibition and stimulation of ATP synthase caused by the phytotoxin tentoxin,” J. Biol. Chem. 283(36), 24594–24553 (2008).
[Crossref]
[PubMed]
A. M. De Grand, S. J. Lomnes, D. S. Lee, M. Pietrzykowski, S. Ohnishi, T. G. Morgan, A. Gogbashian, R. G. Laurence, and J. V. Frangioni, “Tissue-like phantoms for near-infrared fluorescence imaging system assessment and the training of surgeons,” J. Biomed. Opt. 11(1), 10 (2006).
[Crossref]
A. M. De Grand, S. J. Lomnes, D. S. Lee, M. Pietrzykowski, S. Ohnishi, T. G. Morgan, A. Gogbashian, R. G. Laurence, and J. V. Frangioni, “Tissue-like phantoms for near-infrared fluorescence imaging system assessment and the training of surgeons,” J. Biomed. Opt. 11(1), 10 (2006).
[Crossref]
P. V. Jena, P. S. Shirude, B. Okumus, K. Laxmi-Reddy, F. Godde, I. Huc, S. Balasubramanian, and T. Ha, “G-Quadruplex DNA Bound by a Synthetic Ligand is Highly Dynamic,” J. Am. Chem. Soc. 131(35), 12522–12523 (2009).
[Crossref]
[PubMed]
R. Luchowski, E. G. Matveeva, I. Gryczynski, E. A. Terpetschnig, L. Patsenker, G. Laczko, J. Borejdo, and Z. Gryczynski, “Single Molecule Studies of Multiple-Fluorophore Labeled Antibodies. Effect of Homo-FRET on the Number of Photons Available Before Photobleaching,” Curr. Pharm. Biotechnol. 9(5), 411–420 (2008).
[Crossref]
[PubMed]
A. M. De Grand, S. J. Lomnes, D. S. Lee, M. Pietrzykowski, S. Ohnishi, T. G. Morgan, A. Gogbashian, R. G. Laurence, and J. V. Frangioni, “Tissue-like phantoms for near-infrared fluorescence imaging system assessment and the training of surgeons,” J. Biomed. Opt. 11(1), 10 (2006).
[Crossref]
S. A. Rosenberg, M. E. Quinlan, J. N. Forkey, and Y. E. Goldman, “Rotational motions of macro-molecules by single-molecule fluorescence microscopy,” Acc. Chem. Res. 38(7), 583–593 (2005).
[Crossref]
[PubMed]
J. N. Forkey, M. E. Quinlan, M. A. Shaw, J. E. T. Corrie, and Y. E. Goldman, “Three-dimensional structural dynamics of myosin V by single-molecule fluorescence polarization,” Nature 422(6930), 399–404 (2003).
[Crossref]
[PubMed]
L. Edman, Z. Földes-Papp, S. Wennmalm, and R. Rigler, “The fluctuating enzyme: a single molecule approach,” Chem. Phys. 247(1), 11–22 (1999).
[Crossref]
S. A. Rosenberg, M. E. Quinlan, J. N. Forkey, and Y. E. Goldman, “Rotational motions of macro-molecules by single-molecule fluorescence microscopy,” Acc. Chem. Res. 38(7), 583–593 (2005).
[Crossref]
[PubMed]
M. Tokunaga, K. Kitamura, K. Saito, A. H. Iwane, and T. Yanagida, “Single molecule imaging of fluorophores and enzymatic reactions achieved by objective-type total internal reflection fluorescence microscopy,” Biochem. Biophys. Res. Commun. 235(1), 47–53 (1997).
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