Detection of single fluorescent proteins inside eukaryotic cells using two-photon fluorescence

G. W. Li and X. S. Xie, “Central dogma at the single-molecule level in living cells,” Nature 475(7356), 308–315 (2011).
[Crossref] [PubMed]

T. A. Planchon, L. Gao, D. E. Milkie, M. W. Davidson, J. A. Galbraith, C. G. Galbraith, and E. Betzig, “Rapid three-dimensional isotropic imaging of living cells using Bessel beam plane illumination,” Nat. Methods 8(5), 417–423 (2011).
[Crossref] [PubMed]

F. Cella Zanacchi, Z. Lavagnino, M. Perrone Donnorso, A. Del Bue, L. Furia, M. Faretta, and A. Diaspro, “Live-cell 3D super-resolution imaging in thick biological samples,” Nat. Methods 8(12), 1047–1049 (2011).
[Crossref] [PubMed]

M. Drobizhev, N. S. Makarov, S. E. Tillo, T. E. Hughes, and A. Rebane, “Two-photon absorption properties of fluorescent proteins,” Nat. Methods 8(5), 393–399 (2011).
[Crossref] [PubMed]

X. Hou and W. Cheng, “Single-molecule detection using continuous wave excitation of two-photon fluorescence,” Opt. Lett. 36(16), 3185–3187 (2011).
[Crossref] [PubMed]

W. Cheng, X. Hou, and F. Ye, “Use of tapered amplifier diode laser for biological-friendly high-resolution optical trapping,” Opt. Lett. 35(17), 2988–2990 (2010).
[Crossref] [PubMed]

J. G. Ritter, R. Veith, A. Veenendaal, J. P. Siebrasse, and U. Kubitscheck, “Light sheet microscopy for single molecule tracking in living tissue,” PLoS ONE 5(7), e11639 (2010).
[Crossref] [PubMed]

P. D. Simonson, H. A. Deberg, P. Ge, J. K. Alexander, O. Jeyifous, W. N. Green, and P. R. Selvin, “Counting bungarotoxin binding sites of nicotinic acetylcholine receptors in mammalian cells with high signal/noise ratios,” Biophys. J. 99(10), L81–L83 (2010).
[Crossref] [PubMed]

M. Drobizhev, S. Tillo, N. S. Makarov, T. E. Hughes, and A. Rebane, “Absolute two-photon absorption spectra and two-photon brightness of orange and red fluorescent proteins,” J. Phys. Chem. B 113(4), 855–859 (2009).
[Crossref] [PubMed]

J. R. Moffitt, Y. R. Chemla, K. Aathavan, S. Grimes, P. J. Jardine, D. L. Anderson, and C. Bustamante, “Intersubunit coordination in a homomeric ring ATPase,” Nature 457(7228), 446–450 (2009).
[Crossref] [PubMed]

M. D. Cahalan and I. Parker, “Choreography of cell motility and interaction dynamics imaged by two-photon microscopy in lymphoid organs,” Annu. Rev. Immunol. 26(1), 585–626 (2008).
[Crossref] [PubMed]

W. Ji, P. Xu, Z. Li, J. Lu, L. Liu, Y. Zhan, Y. Chen, B. Hille, T. Xu, and L. Chen, “Functional stoichiometry of the unitary calcium-release-activated calcium channel,” Proc. Natl. Acad. Sci. U.S.A. 105(36), 13668–13673 (2008).
[Crossref] [PubMed]

J. T. Groves, R. Parthasarathy, and M. B. Forstner, “Fluorescence imaging of membrane dynamics,” Annu. Rev. Biomed. Eng. 10(1), 311–338 (2008).
[Crossref] [PubMed]

S. C. Kohout, M. H. Ulbrich, S. C. Bell, and E. Y. Isacoff, “Subunit organization and functional transitions in Ci-VSP,” Nat. Struct. Mol. Biol. 15(1), 106–108 (2008).
[Crossref] [PubMed]

M. H. Ulbrich and E. Y. Isacoff, “Subunit counting in membrane-bound proteins,” Nat. Methods 4(4), 319–321 (2007).
[PubMed]

E. Toprak and P. R. Selvin, “New fluorescent tools for watching nanometer-scale conformational changes of single molecules,” Annu. Rev. Biophys. Biomol. Struct. 36(1), 349–369 (2007).
[Crossref] [PubMed]

M. C. Leake, J. H. Chandler, G. H. Wadhams, F. Bai, R. M. Berry, and J. P. Armitage, “Stoichiometry and turnover in single, functioning membrane protein complexes,” Nature 443(7109), 355–358 (2006).
[Crossref] [PubMed]

K. Svoboda and R. Yasuda, “Principles of two-photon excitation microscopy and its applications to neuroscience,” Neuron 50(6), 823–839 (2006).
[Crossref] [PubMed]

H. W. Ai, J. N. Henderson, S. J. Remington, and R. E. Campbell, “Directed evolution of a monomeric, bright and photostable version of Clavularia cyan fluorescent protein: structural characterization and applications in fluorescence imaging,” Biochem. J. 400(3), 531–540 (2006).
[Crossref] [PubMed]

F. Helmchen and W. Denk, “Deep tissue two-photon microscopy,” Nat. Methods 2(12), 932–940 (2005).
[Crossref] [PubMed]

N. J. Carter and R. A. Cross, “Mechanics of the kinesin step,” Nature 435(7040), 308–312 (2005).
[Crossref] [PubMed]

P. J. Schuck, K. A. Willets, D. P. Fromm, R. J. Twieg, and W. E. Moerner, “A novel fluorophore for two-photon-excited single-molecule fluorescence,” Chem. Phys. 318(1-2), 7–11 (2005).
[Crossref]

N. C. Shaner, P. A. Steinbach, and R. Y. Tsien, “A guide to choosing fluorescent proteins,” Nat. Methods 2(12), 905–909 (2005).
[Crossref] [PubMed]

W. R. Zipfel, R. M. Williams, and W. W. Webb, “Nonlinear magic: multiphoton microscopy in the biosciences,” Nat. Biotechnol. 21(11), 1369–1377 (2003).
[Crossref] [PubMed]

T. Ha, I. Rasnik, W. Cheng, H. P. Babcock, G. H. Gauss, T. M. Lohman, and S. Chu, “Initiation and re-initiation of DNA unwinding by the Escherichia coli Rep helicase,” Nature 419(6907), 638–641 (2002).
[Crossref] [PubMed]

N. Billinton and A. W. Knight, “Seeing the wood through the trees: a review of techniques for distinguishing green fluorescent protein from endogenous autofluorescence,” Anal. Biochem. 291(2), 175–197 (2001).
[Crossref] [PubMed]

E. Schaeffer, R. Geleziunas, and W. C. Greene, “Human immunodeficiency virus type 1 Nef functions at the level of virus entry by enhancing cytoplasmic delivery of virions,” J. Virol. 75(6), 2993–3000 (2001).
[Crossref] [PubMed]

P. T. So, C. Y. Dong, B. R. Masters, and K. M. Berland, “Two-photon excitation fluorescence microscopy,” Annu. Rev. Biomed. Eng. 2(1), 399–429 (2000).
[Crossref] [PubMed]

D. W. Piston, “Imaging living cells and tissues by two-photon excitation microscopy,” Trends Cell Biol. 9(2), 66–69 (1999).
[Crossref] [PubMed]

W. E. Moerner and M. Orrit, “Illuminating single molecules in condensed matter,” Science 283(5408), 1670–1676 (1999).
[Crossref] [PubMed]

E. J. Peterman, S. Brasselet, and W. E. Moerner, “The fluorescence dynamics of single molecules of green fluorescent protein,” J. Phys. Chem. A 103(49), 10553–10560 (1999).
[Crossref]

J. M. Squirrell, D. L. Wokosin, J. G. White, and B. D. Bavister, “Long-term two-photon fluorescence imaging of mammalian embryos without compromising viability,” Nat. Biotechnol. 17(8), 763–767 (1999).
[Crossref] [PubMed]

S. W. Hell, M. Booth, S. Wilms, C. M. Schnetter, A. K. Kirsch, D. J. Arndt-Jovin, and T. M. Jovin, “Two-photon near- and far-field fluorescence microscopy with continuous-wave excitation,” Opt. Lett. 23(15), 1238–1240 (1998).
[Crossref] [PubMed]

H. P. Lu, L. Xun, and X. S. Xie, “Single-molecule enzymatic dynamics,” Science 282(5395), 1877–1882 (1998).
[Crossref] [PubMed]

E. J. Sánchez, L. Novotny, G. R. Holtom, and X. S. Xie, “Room-temperature fluorescence imaging and spectroscopy of single molecules by two-photon excitation,” J. Phys. Chem. A 101(38), 7019–7023 (1997).
[Crossref]

W. Denk, J. H. Strickler, and W. W. Webb, “Two-photon laser scanning fluorescence microscopy,” Science 248(4951), 73–76 (1990).
[Crossref] [PubMed]

D. Axelrod, T. P. Burghardt, and N. L. Thompson, “Total internal reflection fluorescence,” Annu. Rev. Biophys. Bioeng. 13(1), 247–268 (1984).
[Crossref] [PubMed]

S. D. Smith, M. Shatsky, P. S. Cohen, R. Warnke, M. P. Link, and B. E. Glader, “Monoclonal antibody and enzymatic profiles of human malignant T-lymphoid cells and derived cell lines,” Cancer Res. 44(12 Pt 1), 5657–5660 (1984).
[PubMed]

W. Kaiser and C. G. B. Garrett, “2-Photon excitation in Caf2–Eu2+,” Phys. Rev. Lett. 7(6), 229–231 (1961).
[Crossref]

J. R. Moffitt, Y. R. Chemla, K. Aathavan, S. Grimes, P. J. Jardine, D. L. Anderson, and C. Bustamante, “Intersubunit coordination in a homomeric ring ATPase,” Nature 457(7228), 446–450 (2009).
[Crossref] [PubMed]

H. W. Ai, J. N. Henderson, S. J. Remington, and R. E. Campbell, “Directed evolution of a monomeric, bright and photostable version of Clavularia cyan fluorescent protein: structural characterization and applications in fluorescence imaging,” Biochem. J. 400(3), 531–540 (2006).
[Crossref] [PubMed]

P. D. Simonson, H. A. Deberg, P. Ge, J. K. Alexander, O. Jeyifous, W. N. Green, and P. R. Selvin, “Counting bungarotoxin binding sites of nicotinic acetylcholine receptors in mammalian cells with high signal/noise ratios,” Biophys. J. 99(10), L81–L83 (2010).
[Crossref] [PubMed]

J. R. Moffitt, Y. R. Chemla, K. Aathavan, S. Grimes, P. J. Jardine, D. L. Anderson, and C. Bustamante, “Intersubunit coordination in a homomeric ring ATPase,” Nature 457(7228), 446–450 (2009).
[Crossref] [PubMed]

M. C. Leake, J. H. Chandler, G. H. Wadhams, F. Bai, R. M. Berry, and J. P. Armitage, “Stoichiometry and turnover in single, functioning membrane protein complexes,” Nature 443(7109), 355–358 (2006).
[Crossref] [PubMed]

S. W. Hell, M. Booth, S. Wilms, C. M. Schnetter, A. K. Kirsch, D. J. Arndt-Jovin, and T. M. Jovin, “Two-photon near- and far-field fluorescence microscopy with continuous-wave excitation,” Opt. Lett. 23(15), 1238–1240 (1998).
[Crossref] [PubMed]

D. Axelrod, T. P. Burghardt, and N. L. Thompson, “Total internal reflection fluorescence,” Annu. Rev. Biophys. Bioeng. 13(1), 247–268 (1984).
[Crossref] [PubMed]

T. Ha, I. Rasnik, W. Cheng, H. P. Babcock, G. H. Gauss, T. M. Lohman, and S. Chu, “Initiation and re-initiation of DNA unwinding by the Escherichia coli Rep helicase,” Nature 419(6907), 638–641 (2002).
[Crossref] [PubMed]

M. C. Leake, J. H. Chandler, G. H. Wadhams, F. Bai, R. M. Berry, and J. P. Armitage, “Stoichiometry and turnover in single, functioning membrane protein complexes,” Nature 443(7109), 355–358 (2006).
[Crossref] [PubMed]

J. M. Squirrell, D. L. Wokosin, J. G. White, and B. D. Bavister, “Long-term two-photon fluorescence imaging of mammalian embryos without compromising viability,” Nat. Biotechnol. 17(8), 763–767 (1999).
[Crossref] [PubMed]

S. C. Kohout, M. H. Ulbrich, S. C. Bell, and E. Y. Isacoff, “Subunit organization and functional transitions in Ci-VSP,” Nat. Struct. Mol. Biol. 15(1), 106–108 (2008).
[Crossref] [PubMed]

P. T. So, C. Y. Dong, B. R. Masters, and K. M. Berland, “Two-photon excitation fluorescence microscopy,” Annu. Rev. Biomed. Eng. 2(1), 399–429 (2000).
[Crossref] [PubMed]

M. C. Leake, J. H. Chandler, G. H. Wadhams, F. Bai, R. M. Berry, and J. P. Armitage, “Stoichiometry and turnover in single, functioning membrane protein complexes,” Nature 443(7109), 355–358 (2006).
[Crossref] [PubMed]

T. A. Planchon, L. Gao, D. E. Milkie, M. W. Davidson, J. A. Galbraith, C. G. Galbraith, and E. Betzig, “Rapid three-dimensional isotropic imaging of living cells using Bessel beam plane illumination,” Nat. Methods 8(5), 417–423 (2011).
[Crossref] [PubMed]

N. Billinton and A. W. Knight, “Seeing the wood through the trees: a review of techniques for distinguishing green fluorescent protein from endogenous autofluorescence,” Anal. Biochem. 291(2), 175–197 (2001).
[Crossref] [PubMed]

S. W. Hell, M. Booth, S. Wilms, C. M. Schnetter, A. K. Kirsch, D. J. Arndt-Jovin, and T. M. Jovin, “Two-photon near- and far-field fluorescence microscopy with continuous-wave excitation,” Opt. Lett. 23(15), 1238–1240 (1998).
[Crossref] [PubMed]

E. J. Peterman, S. Brasselet, and W. E. Moerner, “The fluorescence dynamics of single molecules of green fluorescent protein,” J. Phys. Chem. A 103(49), 10553–10560 (1999).
[Crossref]

D. Axelrod, T. P. Burghardt, and N. L. Thompson, “Total internal reflection fluorescence,” Annu. Rev. Biophys. Bioeng. 13(1), 247–268 (1984).
[Crossref] [PubMed]

J. R. Moffitt, Y. R. Chemla, K. Aathavan, S. Grimes, P. J. Jardine, D. L. Anderson, and C. Bustamante, “Intersubunit coordination in a homomeric ring ATPase,” Nature 457(7228), 446–450 (2009).
[Crossref] [PubMed]

M. D. Cahalan and I. Parker, “Choreography of cell motility and interaction dynamics imaged by two-photon microscopy in lymphoid organs,” Annu. Rev. Immunol. 26(1), 585–626 (2008).
[Crossref] [PubMed]

H. W. Ai, J. N. Henderson, S. J. Remington, and R. E. Campbell, “Directed evolution of a monomeric, bright and photostable version of Clavularia cyan fluorescent protein: structural characterization and applications in fluorescence imaging,” Biochem. J. 400(3), 531–540 (2006).
[Crossref] [PubMed]

N. J. Carter and R. A. Cross, “Mechanics of the kinesin step,” Nature 435(7040), 308–312 (2005).
[Crossref] [PubMed]

F. Cella Zanacchi, Z. Lavagnino, M. Perrone Donnorso, A. Del Bue, L. Furia, M. Faretta, and A. Diaspro, “Live-cell 3D super-resolution imaging in thick biological samples,” Nat. Methods 8(12), 1047–1049 (2011).
[Crossref] [PubMed]

M. C. Leake, J. H. Chandler, G. H. Wadhams, F. Bai, R. M. Berry, and J. P. Armitage, “Stoichiometry and turnover in single, functioning membrane protein complexes,” Nature 443(7109), 355–358 (2006).
[Crossref] [PubMed]

J. R. Moffitt, Y. R. Chemla, K. Aathavan, S. Grimes, P. J. Jardine, D. L. Anderson, and C. Bustamante, “Intersubunit coordination in a homomeric ring ATPase,” Nature 457(7228), 446–450 (2009).
[Crossref] [PubMed]

W. Ji, P. Xu, Z. Li, J. Lu, L. Liu, Y. Zhan, Y. Chen, B. Hille, T. Xu, and L. Chen, “Functional stoichiometry of the unitary calcium-release-activated calcium channel,” Proc. Natl. Acad. Sci. U.S.A. 105(36), 13668–13673 (2008).
[Crossref] [PubMed]

W. Ji, P. Xu, Z. Li, J. Lu, L. Liu, Y. Zhan, Y. Chen, B. Hille, T. Xu, and L. Chen, “Functional stoichiometry of the unitary calcium-release-activated calcium channel,” Proc. Natl. Acad. Sci. U.S.A. 105(36), 13668–13673 (2008).
[Crossref] [PubMed]

X. Hou and W. Cheng, “Single-molecule detection using continuous wave excitation of two-photon fluorescence,” Opt. Lett. 36(16), 3185–3187 (2011).
[Crossref] [PubMed]

W. Cheng, X. Hou, and F. Ye, “Use of tapered amplifier diode laser for biological-friendly high-resolution optical trapping,” Opt. Lett. 35(17), 2988–2990 (2010).
[Crossref] [PubMed]

T. Ha, I. Rasnik, W. Cheng, H. P. Babcock, G. H. Gauss, T. M. Lohman, and S. Chu, “Initiation and re-initiation of DNA unwinding by the Escherichia coli Rep helicase,” Nature 419(6907), 638–641 (2002).
[Crossref] [PubMed]

T. Ha, I. Rasnik, W. Cheng, H. P. Babcock, G. H. Gauss, T. M. Lohman, and S. Chu, “Initiation and re-initiation of DNA unwinding by the Escherichia coli Rep helicase,” Nature 419(6907), 638–641 (2002).
[Crossref] [PubMed]

S. D. Smith, M. Shatsky, P. S. Cohen, R. Warnke, M. P. Link, and B. E. Glader, “Monoclonal antibody and enzymatic profiles of human malignant T-lymphoid cells and derived cell lines,” Cancer Res. 44(12 Pt 1), 5657–5660 (1984).
[PubMed]

N. J. Carter and R. A. Cross, “Mechanics of the kinesin step,” Nature 435(7040), 308–312 (2005).
[Crossref] [PubMed]

T. A. Planchon, L. Gao, D. E. Milkie, M. W. Davidson, J. A. Galbraith, C. G. Galbraith, and E. Betzig, “Rapid three-dimensional isotropic imaging of living cells using Bessel beam plane illumination,” Nat. Methods 8(5), 417–423 (2011).
[Crossref] [PubMed]

P. D. Simonson, H. A. Deberg, P. Ge, J. K. Alexander, O. Jeyifous, W. N. Green, and P. R. Selvin, “Counting bungarotoxin binding sites of nicotinic acetylcholine receptors in mammalian cells with high signal/noise ratios,” Biophys. J. 99(10), L81–L83 (2010).
[Crossref] [PubMed]

F. Cella Zanacchi, Z. Lavagnino, M. Perrone Donnorso, A. Del Bue, L. Furia, M. Faretta, and A. Diaspro, “Live-cell 3D super-resolution imaging in thick biological samples,” Nat. Methods 8(12), 1047–1049 (2011).
[Crossref] [PubMed]

F. Helmchen and W. Denk, “Deep tissue two-photon microscopy,” Nat. Methods 2(12), 932–940 (2005).
[Crossref] [PubMed]

W. Denk, J. H. Strickler, and W. W. Webb, “Two-photon laser scanning fluorescence microscopy,” Science 248(4951), 73–76 (1990).
[Crossref] [PubMed]

F. Cella Zanacchi, Z. Lavagnino, M. Perrone Donnorso, A. Del Bue, L. Furia, M. Faretta, and A. Diaspro, “Live-cell 3D super-resolution imaging in thick biological samples,” Nat. Methods 8(12), 1047–1049 (2011).
[Crossref] [PubMed]

P. T. So, C. Y. Dong, B. R. Masters, and K. M. Berland, “Two-photon excitation fluorescence microscopy,” Annu. Rev. Biomed. Eng. 2(1), 399–429 (2000).
[Crossref] [PubMed]

M. Drobizhev, N. S. Makarov, S. E. Tillo, T. E. Hughes, and A. Rebane, “Two-photon absorption properties of fluorescent proteins,” Nat. Methods 8(5), 393–399 (2011).
[Crossref] [PubMed]

M. Drobizhev, S. Tillo, N. S. Makarov, T. E. Hughes, and A. Rebane, “Absolute two-photon absorption spectra and two-photon brightness of orange and red fluorescent proteins,” J. Phys. Chem. B 113(4), 855–859 (2009).
[Crossref] [PubMed]

F. Cella Zanacchi, Z. Lavagnino, M. Perrone Donnorso, A. Del Bue, L. Furia, M. Faretta, and A. Diaspro, “Live-cell 3D super-resolution imaging in thick biological samples,” Nat. Methods 8(12), 1047–1049 (2011).
[Crossref] [PubMed]

J. T. Groves, R. Parthasarathy, and M. B. Forstner, “Fluorescence imaging of membrane dynamics,” Annu. Rev. Biomed. Eng. 10(1), 311–338 (2008).
[Crossref] [PubMed]

P. J. Schuck, K. A. Willets, D. P. Fromm, R. J. Twieg, and W. E. Moerner, “A novel fluorophore for two-photon-excited single-molecule fluorescence,” Chem. Phys. 318(1-2), 7–11 (2005).
[Crossref]

F. Cella Zanacchi, Z. Lavagnino, M. Perrone Donnorso, A. Del Bue, L. Furia, M. Faretta, and A. Diaspro, “Live-cell 3D super-resolution imaging in thick biological samples,” Nat. Methods 8(12), 1047–1049 (2011).
[Crossref] [PubMed]

T. A. Planchon, L. Gao, D. E. Milkie, M. W. Davidson, J. A. Galbraith, C. G. Galbraith, and E. Betzig, “Rapid three-dimensional isotropic imaging of living cells using Bessel beam plane illumination,” Nat. Methods 8(5), 417–423 (2011).
[Crossref] [PubMed]

T. A. Planchon, L. Gao, D. E. Milkie, M. W. Davidson, J. A. Galbraith, C. G. Galbraith, and E. Betzig, “Rapid three-dimensional isotropic imaging of living cells using Bessel beam plane illumination,” Nat. Methods 8(5), 417–423 (2011).
[Crossref] [PubMed]

T. A. Planchon, L. Gao, D. E. Milkie, M. W. Davidson, J. A. Galbraith, C. G. Galbraith, and E. Betzig, “Rapid three-dimensional isotropic imaging of living cells using Bessel beam plane illumination,” Nat. Methods 8(5), 417–423 (2011).
[Crossref] [PubMed]

W. Kaiser and C. G. B. Garrett, “2-Photon excitation in Caf2–Eu2+,” Phys. Rev. Lett. 7(6), 229–231 (1961).
[Crossref]

T. Ha, I. Rasnik, W. Cheng, H. P. Babcock, G. H. Gauss, T. M. Lohman, and S. Chu, “Initiation and re-initiation of DNA unwinding by the Escherichia coli Rep helicase,” Nature 419(6907), 638–641 (2002).
[Crossref] [PubMed]

P. D. Simonson, H. A. Deberg, P. Ge, J. K. Alexander, O. Jeyifous, W. N. Green, and P. R. Selvin, “Counting bungarotoxin binding sites of nicotinic acetylcholine receptors in mammalian cells with high signal/noise ratios,” Biophys. J. 99(10), L81–L83 (2010).
[Crossref] [PubMed]

E. Schaeffer, R. Geleziunas, and W. C. Greene, “Human immunodeficiency virus type 1 Nef functions at the level of virus entry by enhancing cytoplasmic delivery of virions,” J. Virol. 75(6), 2993–3000 (2001).
[Crossref] [PubMed]

S. D. Smith, M. Shatsky, P. S. Cohen, R. Warnke, M. P. Link, and B. E. Glader, “Monoclonal antibody and enzymatic profiles of human malignant T-lymphoid cells and derived cell lines,” Cancer Res. 44(12 Pt 1), 5657–5660 (1984).
[PubMed]

P. D. Simonson, H. A. Deberg, P. Ge, J. K. Alexander, O. Jeyifous, W. N. Green, and P. R. Selvin, “Counting bungarotoxin binding sites of nicotinic acetylcholine receptors in mammalian cells with high signal/noise ratios,” Biophys. J. 99(10), L81–L83 (2010).
[Crossref] [PubMed]

E. Schaeffer, R. Geleziunas, and W. C. Greene, “Human immunodeficiency virus type 1 Nef functions at the level of virus entry by enhancing cytoplasmic delivery of virions,” J. Virol. 75(6), 2993–3000 (2001).
[Crossref] [PubMed]

J. R. Moffitt, Y. R. Chemla, K. Aathavan, S. Grimes, P. J. Jardine, D. L. Anderson, and C. Bustamante, “Intersubunit coordination in a homomeric ring ATPase,” Nature 457(7228), 446–450 (2009).
[Crossref] [PubMed]

J. T. Groves, R. Parthasarathy, and M. B. Forstner, “Fluorescence imaging of membrane dynamics,” Annu. Rev. Biomed. Eng. 10(1), 311–338 (2008).
[Crossref] [PubMed]

T. Ha, I. Rasnik, W. Cheng, H. P. Babcock, G. H. Gauss, T. M. Lohman, and S. Chu, “Initiation and re-initiation of DNA unwinding by the Escherichia coli Rep helicase,” Nature 419(6907), 638–641 (2002).
[Crossref] [PubMed]

S. W. Hell, M. Booth, S. Wilms, C. M. Schnetter, A. K. Kirsch, D. J. Arndt-Jovin, and T. M. Jovin, “Two-photon near- and far-field fluorescence microscopy with continuous-wave excitation,” Opt. Lett. 23(15), 1238–1240 (1998).
[Crossref] [PubMed]

F. Helmchen and W. Denk, “Deep tissue two-photon microscopy,” Nat. Methods 2(12), 932–940 (2005).
[Crossref] [PubMed]

H. W. Ai, J. N. Henderson, S. J. Remington, and R. E. Campbell, “Directed evolution of a monomeric, bright and photostable version of Clavularia cyan fluorescent protein: structural characterization and applications in fluorescence imaging,” Biochem. J. 400(3), 531–540 (2006).
[Crossref] [PubMed]

W. Ji, P. Xu, Z. Li, J. Lu, L. Liu, Y. Zhan, Y. Chen, B. Hille, T. Xu, and L. Chen, “Functional stoichiometry of the unitary calcium-release-activated calcium channel,” Proc. Natl. Acad. Sci. U.S.A. 105(36), 13668–13673 (2008).
[Crossref] [PubMed]

E. J. Sánchez, L. Novotny, G. R. Holtom, and X. S. Xie, “Room-temperature fluorescence imaging and spectroscopy of single molecules by two-photon excitation,” J. Phys. Chem. A 101(38), 7019–7023 (1997).
[Crossref]

X. Hou and W. Cheng, “Single-molecule detection using continuous wave excitation of two-photon fluorescence,” Opt. Lett. 36(16), 3185–3187 (2011).
[Crossref] [PubMed]

W. Cheng, X. Hou, and F. Ye, “Use of tapered amplifier diode laser for biological-friendly high-resolution optical trapping,” Opt. Lett. 35(17), 2988–2990 (2010).
[Crossref] [PubMed]

M. Drobizhev, N. S. Makarov, S. E. Tillo, T. E. Hughes, and A. Rebane, “Two-photon absorption properties of fluorescent proteins,” Nat. Methods 8(5), 393–399 (2011).
[Crossref] [PubMed]

M. Drobizhev, S. Tillo, N. S. Makarov, T. E. Hughes, and A. Rebane, “Absolute two-photon absorption spectra and two-photon brightness of orange and red fluorescent proteins,” J. Phys. Chem. B 113(4), 855–859 (2009).
[Crossref] [PubMed]

S. C. Kohout, M. H. Ulbrich, S. C. Bell, and E. Y. Isacoff, “Subunit organization and functional transitions in Ci-VSP,” Nat. Struct. Mol. Biol. 15(1), 106–108 (2008).
[Crossref] [PubMed]

M. H. Ulbrich and E. Y. Isacoff, “Subunit counting in membrane-bound proteins,” Nat. Methods 4(4), 319–321 (2007).
[PubMed]

J. R. Moffitt, Y. R. Chemla, K. Aathavan, S. Grimes, P. J. Jardine, D. L. Anderson, and C. Bustamante, “Intersubunit coordination in a homomeric ring ATPase,” Nature 457(7228), 446–450 (2009).
[Crossref] [PubMed]

P. D. Simonson, H. A. Deberg, P. Ge, J. K. Alexander, O. Jeyifous, W. N. Green, and P. R. Selvin, “Counting bungarotoxin binding sites of nicotinic acetylcholine receptors in mammalian cells with high signal/noise ratios,” Biophys. J. 99(10), L81–L83 (2010).
[Crossref] [PubMed]

W. Ji, P. Xu, Z. Li, J. Lu, L. Liu, Y. Zhan, Y. Chen, B. Hille, T. Xu, and L. Chen, “Functional stoichiometry of the unitary calcium-release-activated calcium channel,” Proc. Natl. Acad. Sci. U.S.A. 105(36), 13668–13673 (2008).
[Crossref] [PubMed]

S. W. Hell, M. Booth, S. Wilms, C. M. Schnetter, A. K. Kirsch, D. J. Arndt-Jovin, and T. M. Jovin, “Two-photon near- and far-field fluorescence microscopy with continuous-wave excitation,” Opt. Lett. 23(15), 1238–1240 (1998).
[Crossref] [PubMed]

W. Kaiser and C. G. B. Garrett, “2-Photon excitation in Caf2–Eu2+,” Phys. Rev. Lett. 7(6), 229–231 (1961).
[Crossref]

S. W. Hell, M. Booth, S. Wilms, C. M. Schnetter, A. K. Kirsch, D. J. Arndt-Jovin, and T. M. Jovin, “Two-photon near- and far-field fluorescence microscopy with continuous-wave excitation,” Opt. Lett. 23(15), 1238–1240 (1998).
[Crossref] [PubMed]

N. Billinton and A. W. Knight, “Seeing the wood through the trees: a review of techniques for distinguishing green fluorescent protein from endogenous autofluorescence,” Anal. Biochem. 291(2), 175–197 (2001).
[Crossref] [PubMed]

S. C. Kohout, M. H. Ulbrich, S. C. Bell, and E. Y. Isacoff, “Subunit organization and functional transitions in Ci-VSP,” Nat. Struct. Mol. Biol. 15(1), 106–108 (2008).
[Crossref] [PubMed]

J. G. Ritter, R. Veith, A. Veenendaal, J. P. Siebrasse, and U. Kubitscheck, “Light sheet microscopy for single molecule tracking in living tissue,” PLoS ONE 5(7), e11639 (2010).
[Crossref] [PubMed]

F. Cella Zanacchi, Z. Lavagnino, M. Perrone Donnorso, A. Del Bue, L. Furia, M. Faretta, and A. Diaspro, “Live-cell 3D super-resolution imaging in thick biological samples,” Nat. Methods 8(12), 1047–1049 (2011).
[Crossref] [PubMed]

M. C. Leake, J. H. Chandler, G. H. Wadhams, F. Bai, R. M. Berry, and J. P. Armitage, “Stoichiometry and turnover in single, functioning membrane protein complexes,” Nature 443(7109), 355–358 (2006).
[Crossref] [PubMed]

G. W. Li and X. S. Xie, “Central dogma at the single-molecule level in living cells,” Nature 475(7356), 308–315 (2011).
[Crossref] [PubMed]

W. Ji, P. Xu, Z. Li, J. Lu, L. Liu, Y. Zhan, Y. Chen, B. Hille, T. Xu, and L. Chen, “Functional stoichiometry of the unitary calcium-release-activated calcium channel,” Proc. Natl. Acad. Sci. U.S.A. 105(36), 13668–13673 (2008).
[Crossref] [PubMed]

S. D. Smith, M. Shatsky, P. S. Cohen, R. Warnke, M. P. Link, and B. E. Glader, “Monoclonal antibody and enzymatic profiles of human malignant T-lymphoid cells and derived cell lines,” Cancer Res. 44(12 Pt 1), 5657–5660 (1984).
[PubMed]

W. Ji, P. Xu, Z. Li, J. Lu, L. Liu, Y. Zhan, Y. Chen, B. Hille, T. Xu, and L. Chen, “Functional stoichiometry of the unitary calcium-release-activated calcium channel,” Proc. Natl. Acad. Sci. U.S.A. 105(36), 13668–13673 (2008).
[Crossref] [PubMed]

T. Ha, I. Rasnik, W. Cheng, H. P. Babcock, G. H. Gauss, T. M. Lohman, and S. Chu, “Initiation and re-initiation of DNA unwinding by the Escherichia coli Rep helicase,” Nature 419(6907), 638–641 (2002).
[Crossref] [PubMed]

H. P. Lu, L. Xun, and X. S. Xie, “Single-molecule enzymatic dynamics,” Science 282(5395), 1877–1882 (1998).
[Crossref] [PubMed]

W. Ji, P. Xu, Z. Li, J. Lu, L. Liu, Y. Zhan, Y. Chen, B. Hille, T. Xu, and L. Chen, “Functional stoichiometry of the unitary calcium-release-activated calcium channel,” Proc. Natl. Acad. Sci. U.S.A. 105(36), 13668–13673 (2008).
[Crossref] [PubMed]

M. Drobizhev, N. S. Makarov, S. E. Tillo, T. E. Hughes, and A. Rebane, “Two-photon absorption properties of fluorescent proteins,” Nat. Methods 8(5), 393–399 (2011).
[Crossref] [PubMed]

M. Drobizhev, S. Tillo, N. S. Makarov, T. E. Hughes, and A. Rebane, “Absolute two-photon absorption spectra and two-photon brightness of orange and red fluorescent proteins,” J. Phys. Chem. B 113(4), 855–859 (2009).
[Crossref] [PubMed]

P. T. So, C. Y. Dong, B. R. Masters, and K. M. Berland, “Two-photon excitation fluorescence microscopy,” Annu. Rev. Biomed. Eng. 2(1), 399–429 (2000).
[Crossref] [PubMed]

T. A. Planchon, L. Gao, D. E. Milkie, M. W. Davidson, J. A. Galbraith, C. G. Galbraith, and E. Betzig, “Rapid three-dimensional isotropic imaging of living cells using Bessel beam plane illumination,” Nat. Methods 8(5), 417–423 (2011).
[Crossref] [PubMed]

P. J. Schuck, K. A. Willets, D. P. Fromm, R. J. Twieg, and W. E. Moerner, “A novel fluorophore for two-photon-excited single-molecule fluorescence,” Chem. Phys. 318(1-2), 7–11 (2005).
[Crossref]

W. E. Moerner and M. Orrit, “Illuminating single molecules in condensed matter,” Science 283(5408), 1670–1676 (1999).
[Crossref] [PubMed]

E. J. Peterman, S. Brasselet, and W. E. Moerner, “The fluorescence dynamics of single molecules of green fluorescent protein,” J. Phys. Chem. A 103(49), 10553–10560 (1999).
[Crossref]

J. R. Moffitt, Y. R. Chemla, K. Aathavan, S. Grimes, P. J. Jardine, D. L. Anderson, and C. Bustamante, “Intersubunit coordination in a homomeric ring ATPase,” Nature 457(7228), 446–450 (2009).
[Crossref] [PubMed]

E. J. Sánchez, L. Novotny, G. R. Holtom, and X. S. Xie, “Room-temperature fluorescence imaging and spectroscopy of single molecules by two-photon excitation,” J. Phys. Chem. A 101(38), 7019–7023 (1997).
[Crossref]

W. E. Moerner and M. Orrit, “Illuminating single molecules in condensed matter,” Science 283(5408), 1670–1676 (1999).
[Crossref] [PubMed]

M. D. Cahalan and I. Parker, “Choreography of cell motility and interaction dynamics imaged by two-photon microscopy in lymphoid organs,” Annu. Rev. Immunol. 26(1), 585–626 (2008).
[Crossref] [PubMed]

J. T. Groves, R. Parthasarathy, and M. B. Forstner, “Fluorescence imaging of membrane dynamics,” Annu. Rev. Biomed. Eng. 10(1), 311–338 (2008).
[Crossref] [PubMed]

F. Cella Zanacchi, Z. Lavagnino, M. Perrone Donnorso, A. Del Bue, L. Furia, M. Faretta, and A. Diaspro, “Live-cell 3D super-resolution imaging in thick biological samples,” Nat. Methods 8(12), 1047–1049 (2011).
[Crossref] [PubMed]

E. J. Peterman, S. Brasselet, and W. E. Moerner, “The fluorescence dynamics of single molecules of green fluorescent protein,” J. Phys. Chem. A 103(49), 10553–10560 (1999).
[Crossref]

D. W. Piston, “Imaging living cells and tissues by two-photon excitation microscopy,” Trends Cell Biol. 9(2), 66–69 (1999).
[Crossref] [PubMed]

T. A. Planchon, L. Gao, D. E. Milkie, M. W. Davidson, J. A. Galbraith, C. G. Galbraith, and E. Betzig, “Rapid three-dimensional isotropic imaging of living cells using Bessel beam plane illumination,” Nat. Methods 8(5), 417–423 (2011).
[Crossref] [PubMed]

T. Ha, I. Rasnik, W. Cheng, H. P. Babcock, G. H. Gauss, T. M. Lohman, and S. Chu, “Initiation and re-initiation of DNA unwinding by the Escherichia coli Rep helicase,” Nature 419(6907), 638–641 (2002).
[Crossref] [PubMed]

M. Drobizhev, N. S. Makarov, S. E. Tillo, T. E. Hughes, and A. Rebane, “Two-photon absorption properties of fluorescent proteins,” Nat. Methods 8(5), 393–399 (2011).
[Crossref] [PubMed]

M. Drobizhev, S. Tillo, N. S. Makarov, T. E. Hughes, and A. Rebane, “Absolute two-photon absorption spectra and two-photon brightness of orange and red fluorescent proteins,” J. Phys. Chem. B 113(4), 855–859 (2009).
[Crossref] [PubMed]

H. W. Ai, J. N. Henderson, S. J. Remington, and R. E. Campbell, “Directed evolution of a monomeric, bright and photostable version of Clavularia cyan fluorescent protein: structural characterization and applications in fluorescence imaging,” Biochem. J. 400(3), 531–540 (2006).
[Crossref] [PubMed]

J. G. Ritter, R. Veith, A. Veenendaal, J. P. Siebrasse, and U. Kubitscheck, “Light sheet microscopy for single molecule tracking in living tissue,” PLoS ONE 5(7), e11639 (2010).
[Crossref] [PubMed]

E. J. Sánchez, L. Novotny, G. R. Holtom, and X. S. Xie, “Room-temperature fluorescence imaging and spectroscopy of single molecules by two-photon excitation,” J. Phys. Chem. A 101(38), 7019–7023 (1997).
[Crossref]

E. Schaeffer, R. Geleziunas, and W. C. Greene, “Human immunodeficiency virus type 1 Nef functions at the level of virus entry by enhancing cytoplasmic delivery of virions,” J. Virol. 75(6), 2993–3000 (2001).
[Crossref] [PubMed]

S. W. Hell, M. Booth, S. Wilms, C. M. Schnetter, A. K. Kirsch, D. J. Arndt-Jovin, and T. M. Jovin, “Two-photon near- and far-field fluorescence microscopy with continuous-wave excitation,” Opt. Lett. 23(15), 1238–1240 (1998).
[Crossref] [PubMed]

P. J. Schuck, K. A. Willets, D. P. Fromm, R. J. Twieg, and W. E. Moerner, “A novel fluorophore for two-photon-excited single-molecule fluorescence,” Chem. Phys. 318(1-2), 7–11 (2005).
[Crossref]

P. D. Simonson, H. A. Deberg, P. Ge, J. K. Alexander, O. Jeyifous, W. N. Green, and P. R. Selvin, “Counting bungarotoxin binding sites of nicotinic acetylcholine receptors in mammalian cells with high signal/noise ratios,” Biophys. J. 99(10), L81–L83 (2010).
[Crossref] [PubMed]

E. Toprak and P. R. Selvin, “New fluorescent tools for watching nanometer-scale conformational changes of single molecules,” Annu. Rev. Biophys. Biomol. Struct. 36(1), 349–369 (2007).
[Crossref] [PubMed]

N. C. Shaner, P. A. Steinbach, and R. Y. Tsien, “A guide to choosing fluorescent proteins,” Nat. Methods 2(12), 905–909 (2005).
[Crossref] [PubMed]

S. D. Smith, M. Shatsky, P. S. Cohen, R. Warnke, M. P. Link, and B. E. Glader, “Monoclonal antibody and enzymatic profiles of human malignant T-lymphoid cells and derived cell lines,” Cancer Res. 44(12 Pt 1), 5657–5660 (1984).
[PubMed]

J. G. Ritter, R. Veith, A. Veenendaal, J. P. Siebrasse, and U. Kubitscheck, “Light sheet microscopy for single molecule tracking in living tissue,” PLoS ONE 5(7), e11639 (2010).
[Crossref] [PubMed]

P. D. Simonson, H. A. Deberg, P. Ge, J. K. Alexander, O. Jeyifous, W. N. Green, and P. R. Selvin, “Counting bungarotoxin binding sites of nicotinic acetylcholine receptors in mammalian cells with high signal/noise ratios,” Biophys. J. 99(10), L81–L83 (2010).
[Crossref] [PubMed]

S. D. Smith, M. Shatsky, P. S. Cohen, R. Warnke, M. P. Link, and B. E. Glader, “Monoclonal antibody and enzymatic profiles of human malignant T-lymphoid cells and derived cell lines,” Cancer Res. 44(12 Pt 1), 5657–5660 (1984).
[PubMed]

P. T. So, C. Y. Dong, B. R. Masters, and K. M. Berland, “Two-photon excitation fluorescence microscopy,” Annu. Rev. Biomed. Eng. 2(1), 399–429 (2000).
[Crossref] [PubMed]

J. M. Squirrell, D. L. Wokosin, J. G. White, and B. D. Bavister, “Long-term two-photon fluorescence imaging of mammalian embryos without compromising viability,” Nat. Biotechnol. 17(8), 763–767 (1999).
[Crossref] [PubMed]

N. C. Shaner, P. A. Steinbach, and R. Y. Tsien, “A guide to choosing fluorescent proteins,” Nat. Methods 2(12), 905–909 (2005).
[Crossref] [PubMed]

W. Denk, J. H. Strickler, and W. W. Webb, “Two-photon laser scanning fluorescence microscopy,” Science 248(4951), 73–76 (1990).
[Crossref] [PubMed]

K. Svoboda and R. Yasuda, “Principles of two-photon excitation microscopy and its applications to neuroscience,” Neuron 50(6), 823–839 (2006).
[Crossref] [PubMed]

D. Axelrod, T. P. Burghardt, and N. L. Thompson, “Total internal reflection fluorescence,” Annu. Rev. Biophys. Bioeng. 13(1), 247–268 (1984).
[Crossref] [PubMed]

M. Drobizhev, S. Tillo, N. S. Makarov, T. E. Hughes, and A. Rebane, “Absolute two-photon absorption spectra and two-photon brightness of orange and red fluorescent proteins,” J. Phys. Chem. B 113(4), 855–859 (2009).
[Crossref] [PubMed]

M. Drobizhev, N. S. Makarov, S. E. Tillo, T. E. Hughes, and A. Rebane, “Two-photon absorption properties of fluorescent proteins,” Nat. Methods 8(5), 393–399 (2011).
[Crossref] [PubMed]

E. Toprak and P. R. Selvin, “New fluorescent tools for watching nanometer-scale conformational changes of single molecules,” Annu. Rev. Biophys. Biomol. Struct. 36(1), 349–369 (2007).
[Crossref] [PubMed]

N. C. Shaner, P. A. Steinbach, and R. Y. Tsien, “A guide to choosing fluorescent proteins,” Nat. Methods 2(12), 905–909 (2005).
[Crossref] [PubMed]

P. J. Schuck, K. A. Willets, D. P. Fromm, R. J. Twieg, and W. E. Moerner, “A novel fluorophore for two-photon-excited single-molecule fluorescence,” Chem. Phys. 318(1-2), 7–11 (2005).
[Crossref]

S. C. Kohout, M. H. Ulbrich, S. C. Bell, and E. Y. Isacoff, “Subunit organization and functional transitions in Ci-VSP,” Nat. Struct. Mol. Biol. 15(1), 106–108 (2008).
[Crossref] [PubMed]

M. H. Ulbrich and E. Y. Isacoff, “Subunit counting in membrane-bound proteins,” Nat. Methods 4(4), 319–321 (2007).
[PubMed]

J. G. Ritter, R. Veith, A. Veenendaal, J. P. Siebrasse, and U. Kubitscheck, “Light sheet microscopy for single molecule tracking in living tissue,” PLoS ONE 5(7), e11639 (2010).
[Crossref] [PubMed]

J. G. Ritter, R. Veith, A. Veenendaal, J. P. Siebrasse, and U. Kubitscheck, “Light sheet microscopy for single molecule tracking in living tissue,” PLoS ONE 5(7), e11639 (2010).
[Crossref] [PubMed]

M. C. Leake, J. H. Chandler, G. H. Wadhams, F. Bai, R. M. Berry, and J. P. Armitage, “Stoichiometry and turnover in single, functioning membrane protein complexes,” Nature 443(7109), 355–358 (2006).
[Crossref] [PubMed]

S. D. Smith, M. Shatsky, P. S. Cohen, R. Warnke, M. P. Link, and B. E. Glader, “Monoclonal antibody and enzymatic profiles of human malignant T-lymphoid cells and derived cell lines,” Cancer Res. 44(12 Pt 1), 5657–5660 (1984).
[PubMed]

W. R. Zipfel, R. M. Williams, and W. W. Webb, “Nonlinear magic: multiphoton microscopy in the biosciences,” Nat. Biotechnol. 21(11), 1369–1377 (2003).
[Crossref] [PubMed]

W. Denk, J. H. Strickler, and W. W. Webb, “Two-photon laser scanning fluorescence microscopy,” Science 248(4951), 73–76 (1990).
[Crossref] [PubMed]

J. M. Squirrell, D. L. Wokosin, J. G. White, and B. D. Bavister, “Long-term two-photon fluorescence imaging of mammalian embryos without compromising viability,” Nat. Biotechnol. 17(8), 763–767 (1999).
[Crossref] [PubMed]

P. J. Schuck, K. A. Willets, D. P. Fromm, R. J. Twieg, and W. E. Moerner, “A novel fluorophore for two-photon-excited single-molecule fluorescence,” Chem. Phys. 318(1-2), 7–11 (2005).
[Crossref]

W. R. Zipfel, R. M. Williams, and W. W. Webb, “Nonlinear magic: multiphoton microscopy in the biosciences,” Nat. Biotechnol. 21(11), 1369–1377 (2003).
[Crossref] [PubMed]

S. W. Hell, M. Booth, S. Wilms, C. M. Schnetter, A. K. Kirsch, D. J. Arndt-Jovin, and T. M. Jovin, “Two-photon near- and far-field fluorescence microscopy with continuous-wave excitation,” Opt. Lett. 23(15), 1238–1240 (1998).
[Crossref] [PubMed]

J. M. Squirrell, D. L. Wokosin, J. G. White, and B. D. Bavister, “Long-term two-photon fluorescence imaging of mammalian embryos without compromising viability,” Nat. Biotechnol. 17(8), 763–767 (1999).
[Crossref] [PubMed]

G. W. Li and X. S. Xie, “Central dogma at the single-molecule level in living cells,” Nature 475(7356), 308–315 (2011).
[Crossref] [PubMed]

H. P. Lu, L. Xun, and X. S. Xie, “Single-molecule enzymatic dynamics,” Science 282(5395), 1877–1882 (1998).
[Crossref] [PubMed]

E. J. Sánchez, L. Novotny, G. R. Holtom, and X. S. Xie, “Room-temperature fluorescence imaging and spectroscopy of single molecules by two-photon excitation,” J. Phys. Chem. A 101(38), 7019–7023 (1997).
[Crossref]

W. Ji, P. Xu, Z. Li, J. Lu, L. Liu, Y. Zhan, Y. Chen, B. Hille, T. Xu, and L. Chen, “Functional stoichiometry of the unitary calcium-release-activated calcium channel,” Proc. Natl. Acad. Sci. U.S.A. 105(36), 13668–13673 (2008).
[Crossref] [PubMed]

W. Ji, P. Xu, Z. Li, J. Lu, L. Liu, Y. Zhan, Y. Chen, B. Hille, T. Xu, and L. Chen, “Functional stoichiometry of the unitary calcium-release-activated calcium channel,” Proc. Natl. Acad. Sci. U.S.A. 105(36), 13668–13673 (2008).
[Crossref] [PubMed]

H. P. Lu, L. Xun, and X. S. Xie, “Single-molecule enzymatic dynamics,” Science 282(5395), 1877–1882 (1998).
[Crossref] [PubMed]

K. Svoboda and R. Yasuda, “Principles of two-photon excitation microscopy and its applications to neuroscience,” Neuron 50(6), 823–839 (2006).
[Crossref] [PubMed]

W. Cheng, X. Hou, and F. Ye, “Use of tapered amplifier diode laser for biological-friendly high-resolution optical trapping,” Opt. Lett. 35(17), 2988–2990 (2010).
[Crossref] [PubMed]

W. Ji, P. Xu, Z. Li, J. Lu, L. Liu, Y. Zhan, Y. Chen, B. Hille, T. Xu, and L. Chen, “Functional stoichiometry of the unitary calcium-release-activated calcium channel,” Proc. Natl. Acad. Sci. U.S.A. 105(36), 13668–13673 (2008).
[Crossref] [PubMed]

W. R. Zipfel, R. M. Williams, and W. W. Webb, “Nonlinear magic: multiphoton microscopy in the biosciences,” Nat. Biotechnol. 21(11), 1369–1377 (2003).
[Crossref] [PubMed]

N. Billinton and A. W. Knight, “Seeing the wood through the trees: a review of techniques for distinguishing green fluorescent protein from endogenous autofluorescence,” Anal. Biochem. 291(2), 175–197 (2001).
[Crossref] [PubMed]

P. T. So, C. Y. Dong, B. R. Masters, and K. M. Berland, “Two-photon excitation fluorescence microscopy,” Annu. Rev. Biomed. Eng. 2(1), 399–429 (2000).
[Crossref] [PubMed]

J. T. Groves, R. Parthasarathy, and M. B. Forstner, “Fluorescence imaging of membrane dynamics,” Annu. Rev. Biomed. Eng. 10(1), 311–338 (2008).
[Crossref] [PubMed]

D. Axelrod, T. P. Burghardt, and N. L. Thompson, “Total internal reflection fluorescence,” Annu. Rev. Biophys. Bioeng. 13(1), 247–268 (1984).
[Crossref] [PubMed]

E. Toprak and P. R. Selvin, “New fluorescent tools for watching nanometer-scale conformational changes of single molecules,” Annu. Rev. Biophys. Biomol. Struct. 36(1), 349–369 (2007).
[Crossref] [PubMed]

M. D. Cahalan and I. Parker, “Choreography of cell motility and interaction dynamics imaged by two-photon microscopy in lymphoid organs,” Annu. Rev. Immunol. 26(1), 585–626 (2008).
[Crossref] [PubMed]

H. W. Ai, J. N. Henderson, S. J. Remington, and R. E. Campbell, “Directed evolution of a monomeric, bright and photostable version of Clavularia cyan fluorescent protein: structural characterization and applications in fluorescence imaging,” Biochem. J. 400(3), 531–540 (2006).
[Crossref] [PubMed]

P. D. Simonson, H. A. Deberg, P. Ge, J. K. Alexander, O. Jeyifous, W. N. Green, and P. R. Selvin, “Counting bungarotoxin binding sites of nicotinic acetylcholine receptors in mammalian cells with high signal/noise ratios,” Biophys. J. 99(10), L81–L83 (2010).
[Crossref] [PubMed]

S. D. Smith, M. Shatsky, P. S. Cohen, R. Warnke, M. P. Link, and B. E. Glader, “Monoclonal antibody and enzymatic profiles of human malignant T-lymphoid cells and derived cell lines,” Cancer Res. 44(12 Pt 1), 5657–5660 (1984).
[PubMed]

P. J. Schuck, K. A. Willets, D. P. Fromm, R. J. Twieg, and W. E. Moerner, “A novel fluorophore for two-photon-excited single-molecule fluorescence,” Chem. Phys. 318(1-2), 7–11 (2005).
[Crossref]

E. J. Peterman, S. Brasselet, and W. E. Moerner, “The fluorescence dynamics of single molecules of green fluorescent protein,” J. Phys. Chem. A 103(49), 10553–10560 (1999).
[Crossref]

E. J. Sánchez, L. Novotny, G. R. Holtom, and X. S. Xie, “Room-temperature fluorescence imaging and spectroscopy of single molecules by two-photon excitation,” J. Phys. Chem. A 101(38), 7019–7023 (1997).
[Crossref]

M. Drobizhev, S. Tillo, N. S. Makarov, T. E. Hughes, and A. Rebane, “Absolute two-photon absorption spectra and two-photon brightness of orange and red fluorescent proteins,” J. Phys. Chem. B 113(4), 855–859 (2009).
[Crossref] [PubMed]

E. Schaeffer, R. Geleziunas, and W. C. Greene, “Human immunodeficiency virus type 1 Nef functions at the level of virus entry by enhancing cytoplasmic delivery of virions,” J. Virol. 75(6), 2993–3000 (2001).
[Crossref] [PubMed]

W. R. Zipfel, R. M. Williams, and W. W. Webb, “Nonlinear magic: multiphoton microscopy in the biosciences,” Nat. Biotechnol. 21(11), 1369–1377 (2003).
[Crossref] [PubMed]

J. M. Squirrell, D. L. Wokosin, J. G. White, and B. D. Bavister, “Long-term two-photon fluorescence imaging of mammalian embryos without compromising viability,” Nat. Biotechnol. 17(8), 763–767 (1999).
[Crossref] [PubMed]

M. H. Ulbrich and E. Y. Isacoff, “Subunit counting in membrane-bound proteins,” Nat. Methods 4(4), 319–321 (2007).
[PubMed]

N. C. Shaner, P. A. Steinbach, and R. Y. Tsien, “A guide to choosing fluorescent proteins,” Nat. Methods 2(12), 905–909 (2005).
[Crossref] [PubMed]

T. A. Planchon, L. Gao, D. E. Milkie, M. W. Davidson, J. A. Galbraith, C. G. Galbraith, and E. Betzig, “Rapid three-dimensional isotropic imaging of living cells using Bessel beam plane illumination,” Nat. Methods 8(5), 417–423 (2011).
[Crossref] [PubMed]

F. Cella Zanacchi, Z. Lavagnino, M. Perrone Donnorso, A. Del Bue, L. Furia, M. Faretta, and A. Diaspro, “Live-cell 3D super-resolution imaging in thick biological samples,” Nat. Methods 8(12), 1047–1049 (2011).
[Crossref] [PubMed]

M. Drobizhev, N. S. Makarov, S. E. Tillo, T. E. Hughes, and A. Rebane, “Two-photon absorption properties of fluorescent proteins,” Nat. Methods 8(5), 393–399 (2011).
[Crossref] [PubMed]

F. Helmchen and W. Denk, “Deep tissue two-photon microscopy,” Nat. Methods 2(12), 932–940 (2005).
[Crossref] [PubMed]

S. C. Kohout, M. H. Ulbrich, S. C. Bell, and E. Y. Isacoff, “Subunit organization and functional transitions in Ci-VSP,” Nat. Struct. Mol. Biol. 15(1), 106–108 (2008).
[Crossref] [PubMed]

M. C. Leake, J. H. Chandler, G. H. Wadhams, F. Bai, R. M. Berry, and J. P. Armitage, “Stoichiometry and turnover in single, functioning membrane protein complexes,” Nature 443(7109), 355–358 (2006).
[Crossref] [PubMed]

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