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Volumn 67, Issue , 2016, Pages 565-585

Single-Molecule Studies in Live Cells

Author keywords

Live cell imaging; Single particle tracking; Super resolution imaging

Indexed keywords

BIOINFORMATICS; MOLECULES; OPTICAL RESOLVING POWER; PHYSIOLOGICAL MODELS; SELF ASSEMBLY; STOCHASTIC SYSTEMS;

EID: 84973334723     PISSN: 0066426X     EISSN: 15451593     Source Type: Book Series    
DOI: 10.1146/annurev-physchem-040215-112451     Document Type: Article
Times cited : (44)

References (125)
  • 1
    • 0028281482 scopus 로고
    • Automated detection and tracking of individual and clustered cell surface low density lipoprotein receptor molecules
    • Ghosh RN, Webb WW. 1994. Automated detection and tracking of individual and clustered cell surface low density lipoprotein receptor molecules. Biophys. J. 66(5):1301-18
    • (1994) Biophys. J. , vol.66 , Issue.5 , pp. 1301-1318
    • Ghosh, R.N.1    Webb, W.W.2
  • 2
    • 0027504198 scopus 로고
    • Confined lateral diffusion of membrane receptors as studied by single particle tracking (nanovid microscopy). Effects of calcium-induced differentiation in cultured epithelial cells
    • Kusumi A, Sako Y, Yamamoto M. 1993. Confined lateral diffusion of membrane receptors as studied by single particle tracking (nanovid microscopy). Effects of calcium-induced differentiation in cultured epithelial cells. Biophys. J. 65(5):2021-40
    • (1993) Biophys. J. , vol.65 , Issue.5 , pp. 2021-2040
    • Kusumi, A.1    Sako, Y.2    Yamamoto, M.3
  • 3
    • 0142116238 scopus 로고    scopus 로고
    • Diffusion dynamics of glycine receptors revealed by single-quantum dot tracking
    • Dahan M, Lévi S, Luccardini C, Rostaing P, Riveau B, Triller A. 2003. Diffusion dynamics of glycine receptors revealed by single-quantum dot tracking. Science 302(5644):442-45
    • (2003) Science , vol.302 , Issue.5644 , pp. 442-445
    • Dahan, M.1    Lévi, S.2    Luccardini, C.3    Rostaing, P.4    Riveau, B.5    Triller, A.6
  • 4
    • 84929673223 scopus 로고    scopus 로고
    • Imaging live-cell dynamics and structure at the single-molecule level
    • Liu Z, Lavis LD, Betzig E. 2015. Imaging live-cell dynamics and structure at the single-molecule level. Mol. Cell 58(4):644-59
    • (2015) Mol. Cell , vol.58 , Issue.4 , pp. 644-659
    • Liu, Z.1    Lavis, L.D.2    Betzig, E.3
  • 6
    • 84859920287 scopus 로고    scopus 로고
    • Live-cell super-resolution imaging with synthetic fluorophores
    • van de Linde S, Heilemann M, Sauer M. 2012. Live-cell super-resolution imaging with synthetic fluorophores. Annu. Rev. Phys. Chem. 63(1):519-40
    • (2012) Annu. Rev. Phys. Chem. , vol.63 , Issue.1 , pp. 519-540
    • Van De Linde, S.1    Heilemann, M.2    Sauer, M.3
  • 7
    • 0037072602 scopus 로고    scopus 로고
    • A photoactivatable GFP for selective photolabeling of proteins and cells
    • Patterson GH, Lippincott-Schwartz J. 2002. A photoactivatable GFP for selective photolabeling of proteins and cells. Science 297(5588):1873-77
    • (2002) Science , vol.297 , Issue.5588 , pp. 1873-1877
    • Patterson, G.H.1    Lippincott-Schwartz, J.2
  • 8
    • 0036789916 scopus 로고    scopus 로고
    • An optical marker based on the UV-induced green-to-red photoconversion of a fluorescent protein
    • Ando R, Hama H, Yamamoto-Hino M, Mizuno H, Miyawaki A. 2002. An optical marker based on the UV-induced green-to-red photoconversion of a fluorescent protein. PNAS 99(20):12651-56
    • (2002) PNAS , vol.99 , Issue.20 , pp. 12651-12656
    • Ando, R.1    Hama, H.2    Yamamoto-Hino, M.3    Mizuno, H.4    Miyawaki, A.5
  • 10
    • 33845360042 scopus 로고    scopus 로고
    • Ultra-high resolution imaging by fluorescence photoactivation localization microscopy
    • Hess ST, Girirajan TPK, Mason MD. 2006. Ultra-high resolution imaging by fluorescence photoactivation localization microscopy. Biophys. J. 91(11):4258-72
    • (2006) Biophys. J. , vol.91 , Issue.11 , pp. 4258-4272
    • Hess, S.T.1    Girirajan, T.P.K.2    Mason, M.D.3
  • 11
    • 36849053761 scopus 로고    scopus 로고
    • Dynamic clustered distribution of hemagglutinin resolved at 40 nm in living cell membranes discriminates between raft theories
    • Hess ST, Gould TJ, Gudheti MV, Maas SA, Mills KD, Zimmerberg J. 2007. Dynamic clustered distribution of hemagglutinin resolved at 40 nm in living cell membranes discriminates between raft theories. PNAS 104(44):17370-75
    • (2007) PNAS , vol.104 , Issue.44 , pp. 17370-17375
    • Hess, S.T.1    Gould, T.J.2    Gudheti, M.V.3    Maas, S.A.4    Mills, K.D.5    Zimmerberg, J.6
  • 12
    • 38749148048 scopus 로고    scopus 로고
    • High-density mapping of singlemolecule trajectories with photoactivated localization microscopy
    • Manley S, Gillette JM, Patterson GH, Shroff H, Hess HF, et al. 2008. High-density mapping of singlemolecule trajectories with photoactivated localization microscopy. Nat. Methods 5(2):155-57
    • (2008) Nat. Methods , vol.5 , Issue.2 , pp. 155-157
    • Manley, S.1    Gillette, J.M.2    Patterson, G.H.3    Shroff, H.4    Hess, H.F.5
  • 13
    • 50349088658 scopus 로고    scopus 로고
    • Investigating intracellular dynamics of FtsZ cytoskeleton with photoactivation singlemolecule tracking
    • Niu L, Yu J. 2008. Investigating intracellular dynamics of FtsZ cytoskeleton with photoactivation singlemolecule tracking. Biophys. J. 95(4):2009-16
    • (2008) Biophys. J. , vol.95 , Issue.4 , pp. 2009-2016
    • Niu, L.1    Yu, J.2
  • 14
    • 48049092838 scopus 로고    scopus 로고
    • Halotag: A novel protein labeling technology for cell imaging and protein analysis
    • Los GV, Encell LP, McDougall MG, Hartzell DD, Karassina N, et al. 2008. Halotag: A novel protein labeling technology for cell imaging and protein analysis. ACS Chem. Biol. 3(6):373-82
    • (2008) ACS Chem. Biol. , vol.3 , Issue.6 , pp. 373-382
    • Los, G.V.1    Encell, L.P.2    McDougall, M.G.3    Hartzell, D.D.4    Karassina, N.5
  • 15
    • 33749026335 scopus 로고    scopus 로고
    • Sub-diffraction-limit imaging by stochastic optical reconstruction microscopy (STORM)
    • Rust MJ, Bates M, Zhuang X. 2006. Sub-diffraction-limit imaging by stochastic optical reconstruction microscopy (STORM). Nat. Methods 3(10):793-96
    • (2006) Nat. Methods , vol.3 , Issue.10 , pp. 793-796
    • Rust, M.J.1    Bates, M.2    Zhuang, X.3
  • 17
    • 39149145486 scopus 로고    scopus 로고
    • An engineered protein tag for multiprotein labeling in living cells
    • Gautier A, Juillerat A, Heinis C, Corrêa IR, Kindermann M, et al. 2008. An engineered protein tag for multiprotein labeling in living cells. Chem. Biol. 15(2):128-36
    • (2008) Chem. Biol. , vol.15 , Issue.2 , pp. 128-136
    • Gautier, A.1    Juillerat, A.2    Heinis, C.3    Corrêa, I.R.4    Kindermann, M.5
  • 20
    • 84860361727 scopus 로고    scopus 로고
    • Segregation of molecules at cell division reveals native protein localization
    • Landgraf D, Okumus B, Chien P, Baker TA, Paulsson J. 2012. Segregation of molecules at cell division reveals native protein localization. Nat. Methods 9(5):480-82
    • (2012) Nat. Methods , vol.9 , Issue.5 , pp. 480-482
    • Landgraf, D.1    Okumus, B.2    Chien, P.3    Baker, T.A.4    Paulsson, J.5
  • 21
    • 84900314611 scopus 로고    scopus 로고
    • CRISPR-Cas systems for editing, regulating and targeting genomes
    • Sander JD, Joung JK. 2014. CRISPR-Cas systems for editing, regulating and targeting genomes. Nat. Biotechnol. 32(4):347-55
    • (2014) Nat. Biotechnol. , vol.32 , Issue.4 , pp. 347-355
    • Sander, J.D.1    Joung, J.K.2
  • 22
    • 84863202666 scopus 로고    scopus 로고
    • Single-cell systems biology by super-resolution imaging and combinatorial labeling
    • Lubeck E, Cai L. 2012. Single-cell systems biology by super-resolution imaging and combinatorial labeling. Nat. Methods 9(7):743-48
    • (2012) Nat. Methods , vol.9 , Issue.7 , pp. 743-748
    • Lubeck, E.1    Cai, L.2
  • 23
    • 84865548009 scopus 로고    scopus 로고
    • Super-resolution fluorescence imaging of organelles in live cells with photoswitchable membrane probes
    • Shim S-H, Xia C, Zhong G, Babcock HP, Vaughan JC, et al. 2012. Super-resolution fluorescence imaging of organelles in live cells with photoswitchable membrane probes. PNAS 109(35):13978-83
    • (2012) PNAS , vol.109 , Issue.35 , pp. 13978-13983
    • Shim, S.-H.1    Xia, C.2    Zhong, G.3    Babcock, H.P.4    Vaughan, J.C.5
  • 26
    • 84896393806 scopus 로고    scopus 로고
    • Single-molecule super-resolution light-sheet microscopy
    • Hu YS, Zimmerley M, Li Y, Watters R, Cang H. 2014. Single-molecule super-resolution light-sheet microscopy. ChemPhysChem 15(4):577-86
    • (2014) ChemPhysChem , vol.15 , Issue.4 , pp. 577-586
    • Hu, Y.S.1    Zimmerley, M.2    Li, Y.3    Watters, R.4    Cang, H.5
  • 27
    • 0027270794 scopus 로고
    • Orthogonal-plane fluorescence optical sectioning: Threedimensional imaging of macroscopic biological specimens
    • Voie AH, Burns DH, Spelman FA. 1993. Orthogonal-plane fluorescence optical sectioning: threedimensional imaging of macroscopic biological specimens. J. Microsc. 170(3):229-36
    • (1993) J. Microsc. , vol.170 , Issue.3 , pp. 229-236
    • Voie, A.H.1    Burns, D.H.2    Spelman, F.A.3
  • 28
    • 80055070317 scopus 로고    scopus 로고
    • Inverted selective plane illumination microscopy (iSPIM) enables coupled cell identity lineaging and neurodevelopmental imaging in Caenorhabditis elegans
    • Wu Y, Ghitani A, Christensen R, Santella A, Du Z, et al. 2011. Inverted selective plane illumination microscopy (iSPIM) enables coupled cell identity lineaging and neurodevelopmental imaging in Caenorhabditis elegans. PNAS 108(43):17708-13
    • (2011) PNAS , vol.108 , Issue.43 , pp. 17708-17713
    • Wu, Y.1    Ghitani, A.2    Christensen, R.3    Santella, A.4    Du, Z.5
  • 29
    • 84892562730 scopus 로고    scopus 로고
    • Spatial organization of RNA polymerase II inside a mammalian cell nucleus revealed by reflected light-sheet superresolution microscopy
    • Zhao ZW, Roy R, Gebhardt JCM, Suter DM, Chapman AR, Xie XS. 2014. Spatial organization of RNA polymerase II inside a mammalian cell nucleus revealed by reflected light-sheet superresolution microscopy. PNAS 111(2):681-86
    • (2014) PNAS , vol.111 , Issue.2 , pp. 681-686
    • Zhao, Z.W.1    Roy, R.2    Gebhardt, J.C.M.3    Suter, D.M.4    Chapman, A.R.5    Xie, X.S.6
  • 30
    • 79955586247 scopus 로고    scopus 로고
    • Rapid three-dimensional isotropic imaging of living cells using Bessel beam plane illumination
    • Planchon TA, Gao L, Milkie DE, Davidson MW, Galbraith JA, et al. 2011. Rapid three-dimensional isotropic imaging of living cells using Bessel beam plane illumination. Nat. Methods 8(5):417-23
    • (2011) Nat. Methods , vol.8 , Issue.5 , pp. 417-423
    • Planchon, T.A.1    Gao, L.2    Milkie, D.E.3    Davidson, M.W.4    Galbraith, J.A.5
  • 31
    • 84908251017 scopus 로고    scopus 로고
    • Lattice light-sheet microscopy: Imaging molecules to embryos at high spatiotemporal resolution
    • Chen B-C, LegantWR,WangK, ShaoL,Milkie DE, et al. 2014. Lattice light-sheet microscopy: imaging molecules to embryos at high spatiotemporal resolution. Science 346(6208):1257998
    • (2014) Science , vol.346 , Issue.6208 , pp. 1257998
    • Chen, B.-C.1    Legant, W.R.2    Wang, K.3    Shao, L.4    Milkie, D.E.5
  • 32
    • 84870860504 scopus 로고    scopus 로고
    • Noninvasive imaging beyond the diffraction limit of 3D dynamics in thickly fluorescent specimens
    • Gao L, Shao L, Higgins CD, Poulton JS, Peifer M, et al. 2012. Noninvasive imaging beyond the diffraction limit of 3D dynamics in thickly fluorescent specimens. Cell 151(6):1370-85
    • (2012) Cell , vol.151 , Issue.6 , pp. 1370-1385
    • Gao, L.1    Shao, L.2    Higgins, C.D.3    Poulton, J.S.4    Peifer, M.5
  • 33
    • 4043090758 scopus 로고    scopus 로고
    • Optical sectioning deep inside live embryos by selective plane illumination microscopy
    • Huisken J, Swoger J, Bene FD, Wittbrodt J, Stelzer EHK. 2004. Optical sectioning deep inside live embryos by selective plane illumination microscopy. Science 305(5686):1007-9
    • (2004) Science , vol.305 , Issue.5686 , pp. 1007-1009
    • Huisken, J.1    Swoger, J.2    Bene, F.D.3    Wittbrodt, J.4    Stelzer, E.H.K.5
  • 34
    • 82355190241 scopus 로고    scopus 로고
    • Super-resolution 3D microscopy of live whole cells using structured illumination
    • Shao L, Kner P, Rego EH, GustafssonMGL. 2011. Super-resolution 3D microscopy of live whole cells using structured illumination. Nat. Methods 8(12):1044-46
    • (2011) Nat. Methods , vol.8 , Issue.12 , pp. 1044-1046
    • Shao, L.1    Kner, P.2    Rego, E.H.3    Gustafsson, M.G.L.4
  • 35
    • 17844375949 scopus 로고    scopus 로고
    • Single-molecule analysis of epidermal growth factor signaling that leads to ultrasensitive calcium response
    • Uyemura T, Takagi H, Yanagida T, Sako Y. 2005. Single-molecule analysis of epidermal growth factor signaling that leads to ultrasensitive calcium response. Biophys. J. 88(5):3720-30
    • (2005) Biophys. J. , vol.88 , Issue.5 , pp. 3720-3730
    • Uyemura, T.1    Takagi, H.2    Yanagida, T.3    Sako, Y.4
  • 36
    • 84973392151 scopus 로고    scopus 로고
    • Single molecule imaging of nucleocytoplasmic transport in cells and quantitative analysis of interaction with nuclear pores
    • Tokunaga M, Imamoto N. 2002. Single molecule imaging of nucleocytoplasmic transport in cells and quantitative analysis of interaction with nuclear pores. Biophys. J. 82:44a
    • (2002) Biophys. J. , vol.82 , pp. 44a
    • Tokunaga, M.1    Imamoto, N.2
  • 37
    • 38749118235 scopus 로고    scopus 로고
    • Highly inclined thin illumination enables clear single-molecule imaging in cells
    • Tokunaga M, Imamoto N, Sakata-Sogawa K. 2008. Highly inclined thin illumination enables clear single-molecule imaging in cells. Nat. Methods 5(2):159-61
    • (2008) Nat. Methods , vol.5 , Issue.2 , pp. 159-161
    • Tokunaga, M.1    Imamoto, N.2    Sakata-Sogawa, K.3
  • 38
    • 37249038050 scopus 로고    scopus 로고
    • Variable-angle epifluorescence microscopy: A new way to look at protein dynamics in the plant cell cortex
    • Konopka CA, Bednarek SY. 2008. Variable-angle epifluorescence microscopy: A new way to look at protein dynamics in the plant cell cortex. Plant J. 53(1):186-96
    • (2008) Plant J. , vol.53 , Issue.1 , pp. 186-196
    • Konopka, C.A.1    Bednarek, S.Y.2
  • 39
    • 0030956033 scopus 로고    scopus 로고
    • Single-particle tracking: Applications to membrane dynamics
    • Saxton MJ, Jacobson K. 1997. Single-particle tracking: applications to membrane dynamics. Annu. Rev. Biophys. Biomol. Struct. 26(1):373-99
    • (1997) Annu. Rev. Biophys. Biomol. Struct. , vol.26 , Issue.1 , pp. 373-399
    • Saxton, M.J.1    Jacobson, K.2
  • 40
    • 0030953956 scopus 로고    scopus 로고
    • Single-particle tracking: The distribution of diffusion coefficients
    • Saxton MJ. 1997. Single-particle tracking: The distribution of diffusion coefficients. Biophys. J. 72(4):1744-53
    • (1997) Biophys. J. , vol.72 , Issue.4 , pp. 1744-1753
    • Saxton, M.J.1
  • 42
    • 80053119179 scopus 로고    scopus 로고
    • Probability distribution of the time-averaged mean-square displacement of a Gaussian process
    • Grebenkov DS. 2011. Probability distribution of the time-averaged mean-square displacement of a Gaussian process. Phys. Rev. E 84(3):031124
    • (2011) Phys. Rev. e , vol.84 , Issue.3 , pp. 031124
    • Grebenkov, D.S.1
  • 43
    • 77955121849 scopus 로고    scopus 로고
    • Statistics of camera-based single-particle tracking
    • Berglund AJ. 2010. Statistics of camera-based single-particle tracking. Phys. Rev. E 82(1):011917
    • (2010) Phys. Rev. e , vol.82 , Issue.1 , pp. 011917
    • Berglund, A.J.1
  • 44
    • 0036231415 scopus 로고    scopus 로고
    • Precise nanometer localization analysis for individual fluorescent probes
    • Thompson RE, Larson DR, Webb WW. 2002. Precise nanometer localization analysis for individual fluorescent probes. Biophys. J. 82(5):2775-83
    • (2002) Biophys. J. , vol.82 , Issue.5 , pp. 2775-2783
    • Thompson, R.E.1    Larson, D.R.2    Webb, W.W.3
  • 45
    • 1142291717 scopus 로고    scopus 로고
    • Localization accuracy in single-molecule microscopy
    • Ober RJ, Ram S, Ward ES. 2004. Localization accuracy in single-molecule microscopy. Biophys. J. 86(2):1185-200
    • (2004) Biophys. J. , vol.86 , Issue.2 , pp. 1185-1200
    • Ober, R.J.1    Ram, S.2    Ward, E.S.3
  • 46
    • 0036787587 scopus 로고    scopus 로고
    • Apparent subdiffusion inherent to single particle tracking
    • Martin DS, Forstner MB, Käs JA. 2002. Apparent subdiffusion inherent to single particle tracking. Biophys. J. 83(4):2109-17
    • (2002) Biophys. J. , vol.83 , Issue.4 , pp. 2109-2117
    • Martin, D.S.1    Forstner, M.B.2    Käs, J.A.3
  • 47
    • 11244278527 scopus 로고    scopus 로고
    • Static and dynamic errors in particle tracking microrheology
    • Savin T, Doyle PS. 2005. Static and dynamic errors in particle tracking microrheology. Biophys. J. 88(1):623-38
    • (2005) Biophys. J. , vol.88 , Issue.1 , pp. 623-638
    • Savin, T.1    Doyle, P.S.2
  • 48
    • 20444492647 scopus 로고    scopus 로고
    • Membrane lateral mobility obstructed by polymer-tethered lipids studied at the single molecule level
    • Deverall MA, Gindl E, Sinner E-K, Besir H, Ruehe J, et al. 2005. Membrane lateral mobility obstructed by polymer-tethered lipids studied at the single molecule level. Biophys. J. 88(3):1875-86
    • (2005) Biophys. J. , vol.88 , Issue.3 , pp. 1875-1886
    • Deverall, M.A.1    Gindl, E.2    Sinner, E.-K.3    Besir, H.4    Ruehe, J.5
  • 50
    • 84891870942 scopus 로고    scopus 로고
    • Mapping the energy and diffusion landscapes of membrane proteins at the cell surface using high-density single-molecule imaging and Bayesian inference: Application to the multiscale dynamics of glycine receptors in the neuronalmembrane
    • Masson J-B,Dionne P, Salvatico C, RennerM, SpechtCG, et al. 2014. Mapping the energy and diffusion landscapes of membrane proteins at the cell surface using high-density single-molecule imaging and Bayesian inference: application to the multiscale dynamics of glycine receptors in the neuronalmembrane. Biophys. J. 106(1):74-83
    • (2014) Biophys. J. , vol.106 , Issue.1 , pp. 74-83
    • Masson, J.-B.1    Dionne, P.2    Salvatico, C.3    Renner, M.4    Specht, C.G.5
  • 51
    • 84946057629 scopus 로고    scopus 로고
    • Extracting diffusive states of Rho GTPase in live cells: Towards in vivo biochemistry
    • Koo P,Weitzmann M, Sabanaygam C, van Golen K, Mochrie S. 2015. Extracting diffusive states of Rho GTPase in live cells: towards in vivo biochemistry. PLOS Comput. Biol. 11:e1004297
    • (2015) PLOS Comput. Biol. , vol.11 , pp. e1004297
    • Koo, P.1    Weitzmann, M.2    Sabanaygam, C.3    Van Golen, K.4    Mochrie, S.5
  • 53
    • 84859095006 scopus 로고    scopus 로고
    • Optimal estimates of the diffusion coefficient of a single Brownian trajectory
    • Boyer D, Dean DS,Mejía-Monasterio C, Oshanin G. 2012. Optimal estimates of the diffusion coefficient of a single Brownian trajectory. Phys. Rev. E 85(3):031136
    • (2012) Phys. Rev. e , vol.85 , Issue.3 , pp. 031136
    • Boyer, D.1    Dean, D.S.2    Mejía-Monasterio, C.3    Oshanin, G.4
  • 54
    • 0024610919 scopus 로고
    • A tutorial on hidden Markov models and selected applications in speech recognition
    • Rabiner L. 1989. A tutorial on hidden Markov models and selected applications in speech recognition. Proc. IEEE 77(2):257-86
    • (1989) Proc. IEEE , vol.77 , Issue.2 , pp. 257-286
    • Rabiner, L.1
  • 55
    • 0033807604 scopus 로고    scopus 로고
    • Hidden Markov modeling for single channel kinetics with filtering and correlated noise
    • Qin F, Auerbach A, Sachs F. 2000. Hidden Markov modeling for single channel kinetics with filtering and correlated noise. Biophys. J. 79(4):1928-44
    • (2000) Biophys. J. , vol.79 , Issue.4 , pp. 1928-1944
    • Qin, F.1    Auerbach, A.2    Sachs, F.3
  • 56
    • 0036213026 scopus 로고    scopus 로고
    • Applying hidden Markov models to the analysis of single ion channel activity
    • Venkataramanan L, Sigworth FJ. 2002. Applying hidden Markov models to the analysis of single ion channel activity. Biophys. J. 82(4):1930-42
    • (2002) Biophys. J. , vol.82 , Issue.4 , pp. 1930-1942
    • Venkataramanan, L.1    Sigworth, F.J.2
  • 57
    • 33746747438 scopus 로고    scopus 로고
    • Analysis of single-molecule fret trajectories using hidden Markov modeling
    • McKinney SA, Joo C, Ha T. 2006. Analysis of single-molecule fret trajectories using hidden Markov modeling. Biophys. J. 91(5):1941-51
    • (2006) Biophys. J. , vol.91 , Issue.5 , pp. 1941-1951
    • McKinney, S.A.1    Joo, C.2    Ha, T.3
  • 58
    • 73449090455 scopus 로고    scopus 로고
    • Learning rates and states from biophysical time series: A Bayesian approach to model selection and single-molecule FRET data
    • Bronson JE, Fei J, Hofman JM, Gonzalez RL, Wiggins CH. 2009. Learning rates and states from biophysical time series: A Bayesian approach to model selection and single-molecule FRET data. Biophys. J. 97(12):3196-205
    • (2009) Biophys. J. , vol.97 , Issue.12 , pp. 3196-3205
    • Bronson, J.E.1    Fei, J.2    Hofman, J.M.3    Gonzalez, R.L.4    Wiggins, C.H.5
  • 59
    • 77950460037 scopus 로고    scopus 로고
    • Spatial control of EGF receptor activation by reversible dimerization on living cells
    • Chung I, Akita R, Vandlen R, Toomre D, Schlessinger J, Mellman I. 2010. Spatial control of EGF receptor activation by reversible dimerization on living cells. Nature 464(7289):783-87
    • (2010) Nature , vol.464 , Issue.7289 , pp. 783-787
    • Chung, I.1    Akita, R.2    Vandlen, R.3    Toomre, D.4    Schlessinger, J.5    Mellman, I.6
  • 60
    • 84874642927 scopus 로고    scopus 로고
    • Extracting intracellular diffusive states and transition rates from single-molecule tracking data
    • Persson F, Lindén M, Unoson C, Elf J. 2013. Extracting intracellular diffusive states and transition rates from single-molecule tracking data. Nat. Methods 10(3):265-69
    • (2013) Nat. Methods , vol.10 , Issue.3 , pp. 265-269
    • Persson, F.1    Lindén, M.2    Unoson, C.3    Elf, J.4
  • 62
    • 84940590684 scopus 로고    scopus 로고
    • Inferring transient particle transport dynamics in live cells
    • Monnier N, Barry Z, Park HY, SuK-C, KatzZ, et al. 2015. Inferring transient particle transport dynamics in live cells. Nat. Methods 12:838-40
    • (2015) Nat. Methods , vol.12 , pp. 838-840
    • Monnier, N.1    Barry, Z.2    Park, H.Y.3    Su, K.-C.4    Katz, Z.5
  • 63
    • 84882253569 scopus 로고    scopus 로고
    • Performance ofBayesian model selection criteria forGaussian mixturemodels
    • ed. M-H Chen, DK Dey, P Müller, D Sun, K Ye. New York: Springer
    • SteeleRJ, Raftery A. 2010. Performance ofBayesian model selection criteria forGaussian mixturemodels. In Frontiers of Statistical Decision Making and Bayesian Analysis, ed. M-H Chen, DK Dey, P Müller, D Sun, K Ye, pp. 113-130. New York: Springer
    • (2010) Frontiers of Statistical Decision Making and Bayesian Analysis , pp. 113-130
    • Steele, R.J.1    Raftery, A.2
  • 64
    • 0039587949 scopus 로고    scopus 로고
    • Single-molecule microscopy on model membranes reveals anomalous diffusion
    • Schütz GJ, Schindler H, Schmidt T. 1997. Single-molecule microscopy on model membranes reveals anomalous diffusion. Biophys. J. 73(2):1073-80
    • (1997) Biophys. J. , vol.73 , Issue.2 , pp. 1073-1080
    • Schütz, G.J.1    Schindler, H.2    Schmidt, T.3
  • 65
    • 0002641421 scopus 로고    scopus 로고
    • The random walk's guide to anomalous diffusion: A fractional dynamics approach
    • Metzler R, Klafter J. 2000. The random walk's guide to anomalous diffusion: A fractional dynamics approach. Phys. Rep. 339(1):1-77
    • (2000) Phys. Rep. , vol.339 , Issue.1 , pp. 1-77
    • Metzler, R.1    Klafter, J.2
  • 66
    • 27744586782 scopus 로고    scopus 로고
    • Weak ergodicity breaking in the continuous-time random walk
    • Bel G, Barkai E. 2005. Weak ergodicity breaking in the continuous-time random walk. Phys. Rev. Lett. 94(24):240602
    • (2005) Phys. Rev. Lett. , vol.94 , Issue.24 , pp. 240602
    • Bel, G.1    Barkai, E.2
  • 67
    • 79955601345 scopus 로고    scopus 로고
    • Ergodic and nonergodic processes coexist in the plasma membrane as observed by single-molecule tracking
    • Weigel AV, Simon B, Tamkun MM, Krapf D. 2011. Ergodic and nonergodic processes coexist in the plasma membrane as observed by single-molecule tracking. PNAS 108(16):6438-43
    • (2011) PNAS , vol.108 , Issue.16 , pp. 6438-6443
    • Weigel, A.V.1    Simon, B.2    Tamkun, M.M.3    Krapf, D.4
  • 69
    • 84862729107 scopus 로고    scopus 로고
    • When Brownian diffusion is not Gaussian
    • Wang B, Kuo J, Bae SC, Granick S. 2012. When Brownian diffusion is not Gaussian. Nat. Mater. 11(6):481-85
    • (2012) Nat. Mater. , vol.11 , Issue.6 , pp. 481-485
    • Wang, B.1    Kuo, J.2    Bae, S.C.3    Granick, S.4
  • 70
    • 0029005840 scopus 로고
    • Revisiting the fluid mosaic model of membranes
    • Jacobson K, Sheets ED, Simson R. 1995. Revisiting the fluid mosaic model of membranes. Science 268(5216):1441-42
    • (1995) Science , vol.268 , Issue.5216 , pp. 1441-1442
    • Jacobson, K.1    Sheets, E.D.2    Simson, R.3
  • 71
    • 0029946890 scopus 로고    scopus 로고
    • Constrained diffusion or immobile fraction on cell surfaces: A new interpretation
    • Feder TJ, Brust-Mascher I, Slattery JP, Baird B,Webb WW. 1996. Constrained diffusion or immobile fraction on cell surfaces: A new interpretation. Biophys. J. 70(6):2767-73
    • (1996) Biophys. J. , vol.70 , Issue.6 , pp. 2767-2773
    • Feder, T.J.1    Brust-Mascher, I.2    Slattery, J.P.3    Baird, B.4    Webb, W.W.5
  • 72
    • 42949083695 scopus 로고    scopus 로고
    • Live-cell photoactivated localization microscopy of nanoscale adhesion dynamics
    • Shroff H, Galbraith CG, Galbraith JA, Betzig E. 2008. Live-cell photoactivated localization microscopy of nanoscale adhesion dynamics. Nat. Methods 5:417-23
    • (2008) Nat. Methods , vol.5 , pp. 417-423
    • Shroff, H.1    Galbraith, C.G.2    Galbraith, J.A.3    Betzig, E.4
  • 73
    • 84879692643 scopus 로고    scopus 로고
    • Video-rate nanoscopy using sCMOS camera-specific single-molecule localization algorithms
    • Huang F, Hartwich TMP, Rivera-Molina FE, Lin Y, Duim WC, et al. 2013. Video-rate nanoscopy using sCMOS camera-specific single-molecule localization algorithms. Nat. Methods 10(7):653-58
    • (2013) Nat. Methods , vol.10 , Issue.7 , pp. 653-658
    • Huang, F.1    Hartwich, T.M.P.2    Rivera-Molina, F.E.3    Lin, Y.4    Duim, W.C.5
  • 75
    • 84867912724 scopus 로고    scopus 로고
    • Counting single photoactivatable fluorescent molecules by photoactivated localization microscopy (PALM)
    • Lee S-H, Shin JY, Lee A, Bustamante C. 2012. Counting single photoactivatable fluorescent molecules by photoactivated localization microscopy (PALM). PNAS 109(43):17436-41
    • (2012) PNAS , vol.109 , Issue.43 , pp. 17436-17441
    • Lee, S.-H.1    Shin, J.Y.2    Lee, A.3    Bustamante, C.4
  • 76
    • 84885061266 scopus 로고    scopus 로고
    • Counting molecules in single organelles with superresolution microscopy allows tracking of the endosome maturation trajectory
    • Puchner EM, Walter JM, Kasper R, Huang B, Lim WA. 2013. Counting molecules in single organelles with superresolution microscopy allows tracking of the endosome maturation trajectory. PNAS 110(40):16015-20
    • (2013) PNAS , vol.110 , Issue.40 , pp. 16015-16020
    • Puchner, E.M.1    Walter, J.M.2    Kasper, R.3    Huang, B.4    Lim, W.A.5
  • 77
    • 79960806755 scopus 로고    scopus 로고
    • Quantitative photo activated localization microscopy: Unraveling the effects of photoblinking
    • Annibale P, Vanni S, Scarselli M, Rothlisberger U, Radenovic A. 2011. Quantitative photo activated localization microscopy: unraveling the effects of photoblinking. PLOS ONE 6(7):e22678
    • (2011) PLOS ONE , vol.6 , Issue.7 , pp. e22678
    • Annibale, P.1    Vanni, S.2    Scarselli, M.3    Rothlisberger, U.4    Radenovic, A.5
  • 78
    • 84920972458 scopus 로고    scopus 로고
    • Stochastic approach to the molecular counting problem in superresolution microscopy
    • Rollins GC, Shin JY, Bustamante C, Pressé S. 2015. Stochastic approach to the molecular counting problem in superresolution microscopy. PNAS 112(2):E110-18
    • (2015) PNAS , vol.112 , Issue.2 , pp. E110-E118
    • Rollins, G.C.1    Shin, J.Y.2    Bustamante, C.3    Pressé, S.4
  • 80
    • 84873340760 scopus 로고    scopus 로고
    • Accelerating 3B single-molecule super-resolution microscopy with cloud computing
    • Hu YS, Nan X, Sengupta P, Lippincott-Schwartz J, Cang H. 2013. Accelerating 3B single-molecule super-resolution microscopy with cloud computing. Nat. Methods 10(2):96-97
    • (2013) Nat. Methods , vol.10 , Issue.2 , pp. 96-97
    • Hu, Y.S.1    Nan, X.2    Sengupta, P.3    Lippincott-Schwartz, J.4    Cang, H.5
  • 81
    • 84888272028 scopus 로고    scopus 로고
    • Fast compressed sensing analysis for super-resolution imaging using L1-homotopy
    • Babcock HP, Moffitt JR, Cao Y, Zhuang X. 2013. Fast compressed sensing analysis for super-resolution imaging using L1-homotopy. Opt. Express 21(23):28583
    • (2013) Opt. Express , vol.21 , Issue.23 , pp. 28583
    • Babcock, H.P.1    Moffitt, J.R.2    Cao, Y.3    Zhuang, X.4
  • 82
    • 84863210726 scopus 로고    scopus 로고
    • Faster storm using compressed sensing
    • Zhu L, Zhang W, Elnatan D, Huang B. 2012. Faster storm using compressed sensing. Nat. Methods 9(7):721-23
    • (2012) Nat. Methods , vol.9 , Issue.7 , pp. 721-723
    • Zhu, L.1    Zhang, W.2    Elnatan, D.3    Huang, B.4
  • 83
    • 84861180866 scopus 로고    scopus 로고
    • Statistical deconvolution for superresolution fluorescence microscopy
    • Mukamel EA, Babcock H, Zhuang X. 2012. Statistical deconvolution for superresolution fluorescence microscopy. Biophys. J. 102(10):2391-400
    • (2012) Biophys. J. , vol.102 , Issue.10 , pp. 2391-2400
    • Mukamel, E.A.1    Babcock, H.2    Zhuang, X.3
  • 84
    • 76049117057 scopus 로고    scopus 로고
    • Fast, background-free, 3D super-resolution optical fluctuation imaging (SOFI)
    • Dertinger T, Colyer R, Iyer G, Weiss S, Enderlein J. 2009. Fast, background-free, 3D super-resolution optical fluctuation imaging (SOFI). PNAS 106(52):22287-92
    • (2009) PNAS , vol.106 , Issue.52 , pp. 22287-22292
    • Dertinger, T.1    Colyer, R.2    Iyer, G.3    Weiss, S.4    Enderlein, J.5
  • 85
    • 84899708461 scopus 로고    scopus 로고
    • Spatial covariance reconstructive (SCORE) superresolution fluorescence microscopy
    • Deng Y, Sun M, Lin P-H, Ma J, Shaevitz JW. 2014. Spatial covariance reconstructive (SCORE) superresolution fluorescence microscopy. PLOS ONE 9(4):e94807
    • (2014) PLOS ONE , vol.9 , Issue.4 , pp. e94807
    • Deng, Y.1    Sun, M.2    Lin, P.-H.3    Ma, J.4    Shaevitz, J.W.5
  • 86
    • 84863584294 scopus 로고    scopus 로고
    • Widely accessible method for superresolution fluorescence imaging of living systems
    • Dedecker P, Mo GCH, Dertinger T, Zhang J. 2012. Widely accessible method for superresolution fluorescence imaging of living systems. PNAS 109(27):10909-14
    • (2012) PNAS , vol.109 , Issue.27 , pp. 10909-10914
    • Dedecker, P.1    Mo, G.C.H.2    Dertinger, T.3    Zhang, J.4
  • 87
    • 84873666238 scopus 로고    scopus 로고
    • Simple super-resolution live-cell imaging based on diffusion-assisted Förster resonance energy transfer
    • Cho S, Jang J, Song C, Lee H, Ganesan P, et al. 2013. Simple super-resolution live-cell imaging based on diffusion-assisted Förster resonance energy transfer. Sci. Rep. 3:1208
    • (2013) Sci. Rep. , vol.3 , pp. 1208
    • Cho, S.1    Jang, J.2    Song, C.3    Lee, H.4    Ganesan, P.5
  • 88
    • 84876221513 scopus 로고    scopus 로고
    • Higher-order assemblies in a new paradigm of signal transduction
    • Wu H. 2013. Higher-order assemblies in a new paradigm of signal transduction. Cell 153(2):287-92
    • (2013) Cell , vol.153 , Issue.2 , pp. 287-292
    • Wu, H.1
  • 89
    • 77951620965 scopus 로고    scopus 로고
    • Spatial organization and signal transduction at intercellular junctions
    • Manz BN, Groves JT. 2010. Spatial organization and signal transduction at intercellular junctions. Nat. Rev. Mol. Cell Biol. 11(5):342-52
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , Issue.5 , pp. 342-352
    • Manz, B.N.1    Groves, J.T.2
  • 90
    • 84861403073 scopus 로고    scopus 로고
    • Receptor signaling clusters in the immune synapse
    • Dustin ML, Groves JT. 2012. Receptor signaling clusters in the immune synapse. Annu. Rev. Biophys. 41:543-56
    • (2012) Annu. Rev. Biophys. , vol.41 , pp. 543-556
    • Dustin, M.L.1    Groves, J.T.2
  • 91
    • 84889583170 scopus 로고    scopus 로고
    • Pleomorphic ensembles: Formation of large clusters composed of weakly interacting multivalent molecules
    • Falkenberg CV, Blinov ML, Loew LM. 2013. Pleomorphic ensembles: formation of large clusters composed of weakly interacting multivalent molecules. Biophys. J. 105(11):2451-60
    • (2013) Biophys. J. , vol.105 , Issue.11 , pp. 2451-2460
    • Falkenberg, C.V.1    Blinov, M.L.2    Loew, L.M.3
  • 93
    • 20444404267 scopus 로고    scopus 로고
    • Single-molecule microscopy reveals plasma membrane microdomains created by protein-protein networks that exclude or trap signaling molecules in T cells
    • Douglass AD, Vale RD. 2005. Single-molecule microscopy reveals plasma membrane microdomains created by protein-protein networks that exclude or trap signaling molecules in T cells. Cell 121:937-50
    • (2005) Cell , vol.121 , pp. 937-950
    • Douglass, A.D.1    Vale, R.D.2
  • 94
    • 77249114784 scopus 로고    scopus 로고
    • TCR-peptide-MHC interactions in situ show accelerated kinetics and increased affinity
    • Huppa JB, Axmann M, Mörtelmaier MA, Lillemeier BF, Newell EW, et al. 2010. TCR-peptide-MHC interactions in situ show accelerated kinetics and increased affinity. Nature 463:963-67
    • (2010) Nature , vol.463 , pp. 963-967
    • Huppa, J.B.1    Axmann, M.2    Mörtelmaier, M.A.3    Lillemeier, B.F.4    Newell, E.W.5
  • 95
    • 77950809538 scopus 로고    scopus 로고
    • The kinetics of two-dimensional TCR and pMHC interactions determine T-cell responsiveness
    • Huang J, Zarnitsyna VI, Liu B, Edwards LJ, Jiang N, et al. 2010. The kinetics of two-dimensional TCR and pMHC interactions determine T-cell responsiveness. Nature 464:932-36
    • (2010) Nature , vol.464 , pp. 932-936
    • Huang, J.1    Zarnitsyna, V.I.2    Liu, B.3    Edwards, L.J.4    Jiang, N.5
  • 96
    • 84880089372 scopus 로고    scopus 로고
    • Direct single molecule measurement of TCR triggering by agonist pMHC in living primary T cells
    • O'Donoghue GP, Pielak RM, Smoligovets AA, Lin JJ, Groves JT. 2013. Direct single molecule measurement of TCR triggering by agonist pMHC in living primary T cells. eLife 2:e00778
    • (2013) ELife , vol.2 , pp. e00778
    • O'Donoghue, G.P.1    Pielak, R.M.2    Smoligovets, A.A.3    Lin, J.J.4    Groves, J.T.5
  • 97
    • 77953896432 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • Lemmon MA, Schlessinger J. 2010. Cell signaling by receptor tyrosine kinases. Cell 141(7):1117-34
    • (2010) Cell , vol.141 , Issue.7 , pp. 1117-1134
    • Lemmon, M.A.1    Schlessinger, J.2
  • 99
    • 84861520898 scopus 로고    scopus 로고
    • Spatial regulation of receptor tyrosine kinases in development and cancer
    • Casaletto JB, McClatchey AI. 2012. Spatial regulation of receptor tyrosine kinases in development and cancer. Nat. Rev. Cancer 12(6):387-400
    • (2012) Nat. Rev. Cancer , vol.12 , Issue.6 , pp. 387-400
    • Casaletto, J.B.1    McClatchey, A.I.2
  • 100
    • 79551711208 scopus 로고    scopus 로고
    • Full characterization of GPCR monomer-dimer dynamic equilibrium by single molecule imaging
    • Kasai RS, Suzuki KGN, Prossnitz ER, Koyama-Honda I, Nakada C, et al. 2011. Full characterization of GPCR monomer-dimer dynamic equilibrium by single molecule imaging. J. Cell Biol. 192(3):463-80
    • (2011) J. Cell Biol. , vol.192 , Issue.3 , pp. 463-480
    • Kasai, R.S.1    Suzuki, K.G.N.2    Prossnitz, E.R.3    Koyama-Honda, I.4    Nakada, C.5
  • 101
    • 33846453991 scopus 로고    scopus 로고
    • Transient directed motions of GABA(A) receptors in growth cones detected by a speed correlation index
    • Bouzigues C, Dahan M. 2007. Transient directed motions of GABA(A) receptors in growth cones detected by a speed correlation index. Biophys. J. 92(2):654-60
    • (2007) Biophys. J. , vol.92 , Issue.2 , pp. 654-660
    • Bouzigues, C.1    Dahan, M.2
  • 102
    • 77249150932 scopus 로고    scopus 로고
    • Formation and dissociation ofM1 muscarinic receptor dimers seen by total internal reflection fluorescence imaging of single molecules
    • Hern JA, Baig AH,Mashanov GI, Birdsall B, Corrie JET, et al. 2010. Formation and dissociation ofM1 muscarinic receptor dimers seen by total internal reflection fluorescence imaging of single molecules. PNAS 107(6):2693-98
    • (2010) PNAS , vol.107 , Issue.6 , pp. 2693-2698
    • Hern, J.A.1    Baig, A.H.2    Mashanov, G.I.3    Birdsall, B.4    Corrie, J.E.T.5
  • 103
    • 84872195772 scopus 로고    scopus 로고
    • Single-molecule analysis of fluorescently labeled G-protein-coupled receptors reveals complexes with distinct dynamics and organization
    • Calebiro D, Rieken F, Wagner J, Sungkaworn T, ZabelU, et al. 2013. Single-molecule analysis of fluorescently labeled G-protein-coupled receptors reveals complexes with distinct dynamics and organization. PNAS 110(2):743-48
    • (2013) PNAS , vol.110 , Issue.2 , pp. 743-748
    • Calebiro, D.1    Rieken, F.2    Wagner, J.3    Sungkaworn, T.4    Zabel, U.5
  • 104
    • 84890612981 scopus 로고    scopus 로고
    • Single-molecule imaging revealed dynamic GPCR dimerization
    • Kasai RS, Kusumi A. 2014. Single-molecule imaging revealed dynamic GPCR dimerization. Curr. Opin. Cell Biol. 27:78-86
    • (2014) Curr. Opin. Cell Biol. , vol.27 , pp. 78-86
    • Kasai, R.S.1    Kusumi, A.2
  • 105
    • 80051978813 scopus 로고    scopus 로고
    • Cytoskeletal control of CD36 diffusion promotes its receptor and signaling function
    • Jaqaman K, Kuwata H, Touret N, Collins R, Trimble WS, et al. 2011. Cytoskeletal control of CD36 diffusion promotes its receptor and signaling function. Cell 146(4):593-606
    • (2011) Cell , vol.146 , Issue.4 , pp. 593-606
    • Jaqaman, K.1    Kuwata, H.2    Touret, N.3    Collins, R.4    Trimble, W.S.5
  • 107
    • 84865560488 scopus 로고    scopus 로고
    • Fast rebinding increases dwell time of Src homology 2 (SH2)-containing proteins near the plasma membrane
    • Oh D, Ogiue-Ikeda M, Jadwin JA, Machida K,Mayer BJ, Yu J. 2012. Fast rebinding increases dwell time of Src homology 2 (SH2)-containing proteins near the plasma membrane. PNAS 109(35):14024-29
    • (2012) PNAS , vol.109 , Issue.35 , pp. 14024-14029
    • Oh, D.1    Ogiue-Ikeda, M.2    Jadwin, J.A.3    Machida, K.4    Mayer, B.J.5    Yu, J.6
  • 108
    • 0842346438 scopus 로고    scopus 로고
    • Specificity in signal transduction: From phosphotyrosine-SH2 domain interactions to complex cellular systems
    • Pawson T. 2004. Specificity in signal transduction: from phosphotyrosine-SH2 domain interactions to complex cellular systems. Cell 116(2):191-203
    • (2004) Cell , vol.116 , Issue.2 , pp. 191-203
    • Pawson, T.1
  • 109
    • 0029063148 scopus 로고
    • Kinetic proofreading in T-cell receptor signal transduction
    • McKeithan TW. 1995. Kinetic proofreading in T-cell receptor signal transduction. PNAS 92(11):5042-46
    • (1995) PNAS , vol.92 , Issue.11 , pp. 5042-5046
    • McKeithan, T.W.1
  • 110
    • 84862908850 scopus 로고    scopus 로고
    • Extensive promoter-centered chromatin interactions provide a topological basis for transcription regulation
    • Li G, Ruan X, Auerbach RK, Sandhu KS, ZhengM, et al. 2012. Extensive promoter-centered chromatin interactions provide a topological basis for transcription regulation. Cell 148(1-2):84-98
    • (2012) Cell , vol.148 , Issue.1-2 , pp. 84-98
    • Li, G.1    Ruan, X.2    Auerbach, R.K.3    Sandhu, K.S.4    Zheng, M.5
  • 111
    • 84881243248 scopus 로고    scopus 로고
    • Real-time dynamics of RNA polymerase II clustering in live human cells
    • Cisse II, Izeddin I, Causse SZ, Boudarene L, Senecal A, et al. 2013. Real-time dynamics of RNA polymerase II clustering in live human cells. Science 341(6146):664-67
    • (2013) Science , vol.341 , Issue.6146 , pp. 664-667
    • Cisse, I.I.1    Izeddin, I.2    Causse, S.Z.3    Boudarene, L.4    Senecal, A.5
  • 112
    • 84903392046 scopus 로고    scopus 로고
    • Single-molecule tracking in live cells reveals distinct target-search strategies of transcription factors in the nucleus
    • Izeddin I, Récamier V, Bosanac L, Cissé II, Boudarene L, et al. 2014. Single-molecule tracking in live cells reveals distinct target-search strategies of transcription factors in the nucleus. eLife 3:e02230
    • (2014) ELife , vol.3 , pp. e02230
    • Izeddin, I.1    Récamier, V.2    Bosanac, L.3    Cissé, I.I.4    Boudarene, L.5
  • 113
    • 84929665381 scopus 로고    scopus 로고
    • 3D imaging of Sox2 enhancer clusters in embryonic stem cells
    • Liu Z, Legant WR, Chen B-C, Li L, Grimm JB, et al. 2014. 3D imaging of Sox2 enhancer clusters in embryonic stem cells. eLife 3:e04236
    • (2014) ELife , vol.3 , pp. e04236
    • Liu, Z.1    Legant, W.R.2    Chen, B.-C.3    Li, L.4    Grimm, J.B.5
  • 114
    • 0019887628 scopus 로고
    • Diffusion-driven mechanisms of protein translocation on nucleic acids. 1. Models and theory
    • Berg OG, Winter RB, Von Hippel PH. 1981. Diffusion-driven mechanisms of protein translocation on nucleic acids. 1. Models and theory. Biochemistry 20(24):6929-48
    • (1981) Biochemistry , vol.20 , Issue.24 , pp. 6929-6948
    • Berg, O.G.1    Winter, R.B.2    Von Hippel, P.H.3
  • 115
    • 84862624197 scopus 로고    scopus 로고
    • The lac repressor displays facilitated diffusion in living cells
    • Hammar P, Leroy P, Mahmutovic A, Marklund EG, Berg OG, Elf J. 2012. The lac repressor displays facilitated diffusion in living cells. Science 336(6088):1595-98
    • (2012) Science , vol.336 , Issue.6088 , pp. 1595-1598
    • Hammar, P.1    Leroy, P.2    Mahmutovic, A.3    Marklund, E.G.4    Berg, O.G.5    Elf, J.6
  • 116
    • 84896338378 scopus 로고    scopus 로고
    • Single-molecule dynamics of enhanceosome assembly in embryonic stem cells
    • Chen J, Zhang Z, Li L, Chen B-C, Revyakin A, et al. 2014. Single-molecule dynamics of enhanceosome assembly in embryonic stem cells. Cell 156(6):1274-85
    • (2014) Cell , vol.156 , Issue.6 , pp. 1274-1285
    • Chen, J.1    Zhang, Z.2    Li, L.3    Chen, B.-C.4    Revyakin, A.5
  • 117
    • 0035654078 scopus 로고    scopus 로고
    • Dentritic spines: Structure, dynamics and regulation
    • Hering H, Sheng M. 2001. Dentritic spines: structure, dynamics and regulation. Nat. Rev. Neurosci. 2(12):880-88
    • (2001) Nat. Rev. Neurosci. , vol.2 , Issue.12 , pp. 880-888
    • Hering, H.1    Sheng, M.2
  • 118
    • 77954484935 scopus 로고    scopus 로고
    • Single-molecule discrimination of discrete perisynaptic and distributed sites of actin filament assembly within dendritic spines
    • Frost NA, Shroff H, Kong H, Betzig E, Blanpied TA. 2010. Single-molecule discrimination of discrete perisynaptic and distributed sites of actin filament assembly within dendritic spines. Neuron 67(1):86-99
    • (2010) Neuron , vol.67 , Issue.1 , pp. 86-99
    • Frost, N.A.1    Shroff, H.2    Kong, H.3    Betzig, E.4    Blanpied, T.A.5
  • 119
    • 70450184120 scopus 로고    scopus 로고
    • Investigating sub-spine actin dynamics in rat hippocampal neurons with super-resolution optical imaging
    • TatavartyV, Kim E-J, Rodionov V, Yu J. 2009. Investigating sub-spine actin dynamics in rat hippocampal neurons with super-resolution optical imaging. PLOS ONE 4(11):e7724
    • (2009) PLOS ONE , vol.4 , Issue.11 , pp. e7724
    • Tatavarty, V.1    Kim, E.-J.2    Rodionov, V.3    Yu, J.4
  • 120
    • 84919344270 scopus 로고    scopus 로고
    • Nanoscale segregation of actin nucleation and elongation factors determines dendritic spine protrusion
    • Chazeau A, Mehidi A, Nair D, Gautier JJ, Leduc C, et al. 2014. Nanoscale segregation of actin nucleation and elongation factors determines dendritic spine protrusion. EMBO J. 33:2745-64
    • (2014) EMBO J. , vol.33 , pp. 2745-2764
    • Chazeau, A.1    Mehidi, A.2    Nair, D.3    Gautier, J.J.4    Leduc, C.5
  • 121
    • 84865270885 scopus 로고    scopus 로고
    • Polarization of actin cytoskeleton is reduced in dendritic protrusions during early spine development in hippocampal neuron
    • Tatavarty V, Das S, Yu J. 2012. Polarization of actin cytoskeleton is reduced in dendritic protrusions during early spine development in hippocampal neuron. Mol. Biol. Cell 23(16):3167-77
    • (2012) Mol. Biol. Cell , vol.23 , Issue.16 , pp. 3167-3177
    • Tatavarty, V.1    Das, S.2    Yu, J.3
  • 122
    • 84867628844 scopus 로고    scopus 로고
    • Heterogeneity of AMPA receptor trafficking and molecular interactions revealed by superresolution analysis of live cell imaging
    • Hoze N, Nair D, Hosy E, Sieben C, Manley S, et al. 2012. Heterogeneity of AMPA receptor trafficking and molecular interactions revealed by superresolution analysis of live cell imaging. PNAS 109(42):17052-57
    • (2012) PNAS , vol.109 , Issue.42 , pp. 17052-17057
    • Hoze, N.1    Nair, D.2    Hosy, E.3    Sieben, C.4    Manley, S.5
  • 124
    • 84881139928 scopus 로고    scopus 로고
    • Super-resolution imaging reveals that AMPA receptors inside synapses are dynamically organized in nanodomains regulated by PSD95
    • Nair D, Hosy E, Petersen JD, Constals A, Giannone G, et al. 2013. Super-resolution imaging reveals that AMPA receptors inside synapses are dynamically organized in nanodomains regulated by PSD95. J. Neurosci. 33(32):13204-24
    • (2013) J. Neurosci. , vol.33 , Issue.32 , pp. 13204-13224
    • Nair, D.1    Hosy, E.2    Petersen, J.D.3    Constals, A.4    Giannone, G.5
  • 125
    • 84921827802 scopus 로고    scopus 로고
    • Single-molecule tracking of small GTPase Rac1 uncovers spatial regulation of membrane translocation and mechanism for polarized signaling
    • Das S, Yin T, Yang Q, Zhang J, Wu YI, Yu J. 2015. Single-molecule tracking of small GTPase Rac1 uncovers spatial regulation of membrane translocation and mechanism for polarized signaling. PNAS 112(3):E267-76
    • (2015) PNAS , vol.112 , Issue.3 , pp. E267-E276
    • Das, S.1    Yin, T.2    Yang, Q.3    Zhang, J.4    Wu, Y.I.5    Yu, J.6


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