메뉴 건너뛰기




Volumn 3, Issue 11, 2011, Pages

Fluorescence techniques to study lipid dynamics

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE LIPID;

EID: 84863954596     PISSN: None     EISSN: 19430264     Source Type: Journal    
DOI: 10.1101/cshperspect.a009803     Document Type: Article
Times cited : (87)

References (234)
  • 1
    • 0141728404 scopus 로고    scopus 로고
    • How the confocal laser scanning microscope entered biological research
    • Amos WB, White JG. 2003. How the confocal laser scanning microscope entered biological research. Biol Cell 95: 335-342.
    • (2003) Biol Cell , vol.95 , pp. 335-342
    • Amos, W.B.1    White, J.G.2
  • 2
    • 0026528045 scopus 로고
    • Tracking of cell-surface receptors by fluorescence digital imaging microscopy using a charge-coupled device camera-Low-density-lipoprotein and influenza-virus receptor mobility at 48C
    • Anderson CM, Georgiou GN, Morrison IEG, Stevenson GVW, Cherry RJ. 1992. Tracking of cell-surface receptors by fluorescence digital imaging microscopy using a charge-coupled device camera-Low-density-lipoprotein and influenza-virus receptor mobility at 48C. J Cell Sci 101: 415-425.
    • (1992) J Cell Sci , vol.101 , pp. 415-425
    • Anderson, C.M.1    Georgiou, G.N.2    Morrison, I.E.G.3    Stevenson, G.V.W.4    Cherry, R.J.5
  • 3
    • 77955067950 scopus 로고    scopus 로고
    • Duration of fusion pore opening and the amount of hormone released are regulated by myosin II during kiss-and-run exocytosis
    • Aoki R, Kitaguchi T, Oya M, Yanagihara Y, Sato M, Miyawaki A, Tsuboi T. 2010. Duration of fusion pore opening and the amount of hormone released are regulated by myosin II during kiss-and-run exocytosis. Biochem J 429: 497-504.
    • (2010) Biochem J , vol.429 , pp. 497-504
    • Aoki, R.1    Kitaguchi, T.2    Oya, M.3    Yanagihara, Y.4    Sato, M.5    Miyawaki, A.6    Tsuboi, T.7
  • 4
    • 0017348085 scopus 로고
    • Cell-surface heating during fluorescence photobleaching recovery experiments
    • Axelrod D. 1977. Cell-surface heating during fluorescence photobleaching recovery experiments. Biophys J 18: 129-131.
    • (1977) Biophys J , vol.18 , pp. 129-131
    • Axelrod, D.1
  • 5
    • 57949112733 scopus 로고    scopus 로고
    • Chapter 7: Total internal reflection fluorescence microscopy
    • Axelrod D. 2008. Chapter 7: Total internal reflection fluorescence microscopy. Methods Cell Biology 89: 169-221.
    • (2008) Methods Cell Biology , vol.89 , pp. 169-221
    • Axelrod, D.1
  • 6
    • 0020659058 scopus 로고
    • Total internal reflection fluorescent microscopy
    • Axelrod D, Thompson NL, Burghardt TP. 1983. Total internal reflection fluorescent microscopy. J Microsc 129: 19-28.
    • (1983) J Microsc , vol.129 , pp. 19-28
    • Axelrod, D.1    Thompson, N.L.2    Burghardt, T.P.3
  • 7
    • 0017192686 scopus 로고
    • Mobility measurement by analysis of fluorescence photobleaching recovery kinetics
    • Axelrod D, Koppel DE, Schlessinger J, Elson E, Webb WW. 1976. Mobility measurement by analysis of fluorescence photobleaching recovery kinetics. Biophys J 16: 1055-1069.
    • (1976) Biophys J , vol.16 , pp. 1055-1069
    • Axelrod, D.1    Koppel, D.E.2    Schlessinger, J.3    Elson, E.4    Webb, W.W.5
  • 8
    • 14744278787 scopus 로고    scopus 로고
    • Sterol structure determines the separation of phases and the curvature of the liquid-ordered phase in model membranes
    • Bacia K, Schwille P, Kurzchalia T. 2005. Sterol structure determines the separation of phases and the curvature of the liquid-ordered phase in model membranes. Proc Natl Acad Sci 102: 3272-3277.
    • (2005) Proc Natl Acad Sci , vol.102 , pp. 3272-3277
    • Bacia, K.1    Schwille, P.2    Kurzchalia, T.3
  • 9
    • 4143091360 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy relates rafts in model and native membranes
    • Bacia K, Scherfeld D, Kahya N, Schwille P. 2004. Fluorescence correlation spectroscopy relates rafts in model and native membranes. Biophys J 87: 1034-1043.
    • (2004) Biophys J , vol.87 , pp. 1034-1043
    • Bacia, K.1    Scherfeld, D.2    Kahya, N.3    Schwille, P.4
  • 10
    • 72249114997 scopus 로고    scopus 로고
    • Homo-FRET imaging enables quantification of protein cluster sizes with subcellular resolution
    • Bader AN, Hofman EG, Voortman J, Henegouwen P, Gerritsen HC. 2009. Homo-FRET imaging enables quantification of protein cluster sizes with subcellular resolution. Biophys J 97: 2613-2622.
    • (2009) Biophys J , vol.97 , pp. 2613-2622
    • Bader, A.N.1    Hofman, E.G.2    Voortman, J.3    Henegouwen, P.4    Gerritsen, H.C.5
  • 11
    • 0037278149 scopus 로고    scopus 로고
    • Direct observation of lipid domains in free standing bilayers: From simple to complex lipid mixtures
    • Bagatolli LA. 2003. Direct observation of lipid domains in free standing bilayers: From simple to complex lipid mixtures. Chem Phys Lipids 122: 137-145.
    • (2003) Chem Phys Lipids , vol.122 , pp. 137-145
    • Bagatolli, L.A.1
  • 12
    • 0032826460 scopus 로고    scopus 로고
    • Two-photon fluorescence microscopy observation of shape changes at the phase transition in phospholipid giant unilamellar vesicles
    • Bagatolli LA, Gratton E. 1999. Two-photon fluorescence microscopy observation of shape changes at the phase transition in phospholipid giant unilamellar vesicles. Biophys J 77: 2090-2101.
    • (1999) Biophys J , vol.77 , pp. 2090-2101
    • Bagatolli, L.A.1    Gratton, E.2
  • 13
    • 0034081731 scopus 로고    scopus 로고
    • Two photon fluorescence microscopy of coexisting lipid domains in giant unilamellar vesicles of binary phospholipid mixtures
    • Bagatolli LA, Gratton E. 2000a. Two photon fluorescence microscopy of coexisting lipid domains in giant unilamellar vesicles of binary phospholipid mixtures. Biophys J 78: 290-305.
    • (2000) Biophys J , vol.78 , pp. 290-305
    • Bagatolli, L.A.1    Gratton, E.2
  • 14
    • 0033932033 scopus 로고    scopus 로고
    • A correlation between lipid domain shape and binary phospholipid mixture composition in free standing bilayers: A two-photon fluorescence microscopy study
    • Bagatolli LA, Gratton E. 2000b. A correlation between lipid domain shape and binary phospholipid mixture composition in free standing bilayers: A two-photon fluorescence microscopy study. Biophys J 79: 434-447.
    • (2000) Biophys J , vol.79 , pp. 434-447
    • Bagatolli, L.A.1    Gratton, E.2
  • 15
    • 12244278268 scopus 로고    scopus 로고
    • Giant vesicles, laurdan, and two-photon fluorescence microscopy: Evidence of lipid lateral separation in bilayers
    • Bagatolli LA, Sanchez SA, Hazlett T, Gratton E. 2003. Giant vesicles, laurdan, and two-photon fluorescence microscopy: Evidence of lipid lateral separation in bilayers. Biophotonics 360: 481-500.
    • (2003) Biophotonics , vol.360 , pp. 481-500
    • Bagatolli, L.A.1    Sanchez, S.A.2    Hazlett, T.3    Gratton, E.4
  • 16
    • 0020459573 scopus 로고
    • Diffusion of low density lipoprotein-receptor complex on human fibroblasts
    • Barak LS, Webb WW. 1982. Diffusion of low density lipoprotein-receptor complex on human fibroblasts. J Cell Biol 95: 846-852.
    • (1982) J Cell Biol , vol.95 , pp. 846-852
    • Barak, L.S.1    Webb, W.W.2
  • 17
    • 0033082668 scopus 로고    scopus 로고
    • Fluorescence lifetime imaging microscopy: Spatial resolution of biochemical processes in the cell
    • Bastiaens PIH, Squire A. 1999. Fluorescence lifetime imaging microscopy: Spatial resolution of biochemical processes in the cell. Trends Cell Biol 9: 48-52.
    • (1999) Trends Cell Biol , vol.9 , pp. 48-52
    • Bastiaens, P.I.H.1    Squire, A.2
  • 19
    • 0038699021 scopus 로고    scopus 로고
    • How to determine diffusion coefficients in planar phospholipid systems by confocal fluorescence correlation spectroscopy
    • Benda A, Benes M, Marecek V, Lhotsky A, Hermens WT, Hof M. 2003. How to determine diffusion coefficients in planar phospholipid systems by confocal fluorescence correlation spectroscopy. Langmuir 19: 4120-4126.
    • (2003) Langmuir , vol.19 , pp. 4120-4126
    • Benda, A.1    Benes, M.2    Marecek, V.3    Lhotsky, A.4    Hermens, W.T.5    Hof, M.6
  • 22
    • 0018576112 scopus 로고
    • Confocal scanning light-microscopy with high aperture immersion lenses
    • Brakenhoff GJ, Blom P, Barends P. 1979. Confocal scanning light-microscopy with high aperture immersion lenses. J Microsc 117: 219-232.
    • (1979) J Microsc , vol.117 , pp. 219-232
    • Brakenhoff, G.J.1    Blom, P.2    Barends, P.3
  • 23
    • 46749099837 scopus 로고    scopus 로고
    • Total internal reflection microscopy for live imaging of cellular uptake of sub-micron nonfluorescent particles
    • Byrne GD, Pitter MC, Zhang J, Falcone FH, Stolnik S, Somekh MG. 2008. Total internal reflection microscopy for live imaging of cellular uptake of sub-micron nonfluorescent particles. J Microsc 231: 168-179.
    • (2008) J Microsc , vol.231 , pp. 168-179
    • Byrne, G.D.1    Pitter, M.C.2    Zhang, J.3    Falcone, F.H.4    Stolnik, S.5    Somekh, M.G.6
  • 24
    • 27144531262 scopus 로고    scopus 로고
    • Cholesterol modulated antibody binding in supported lipid membranes as determined by total internal reflectance microscopy on a microfabricated high-throughput glass chip
    • Cannon B, Weaver N, Pu QS, Thiagarajan V, Liu SR, Huang JY, Vaughn MW, Cheng KH. 2005. Cholesterol modulated antibody binding in supported lipid membranes as determined by total internal reflectance microscopy on a microfabricated high-throughput glass chip. Langmuir 21: 9666-9674.
    • (2005) Langmuir , vol.21 , pp. 9666-9674
    • Cannon, B.1    Weaver, N.2    Pu, Q.S.3    Thiagarajan, V.4    Liu, S.R.5    Huang, J.Y.6    Vaughn, M.W.7    Cheng, K.H.8
  • 25
    • 0034817343 scopus 로고    scopus 로고
    • Quantitative comparison of algorithms for tracking single fluorescent particles
    • Cheezum MK, Walker WF, Guilford WH.2001. Quantitative comparison of algorithms for tracking single fluorescent particles. Biophys J 81: 2378-2388.
    • (2001) Biophys J , vol.81 , pp. 2378-2388
    • Cheezum, M.K.1    Walker, W.F.2    Guilford, W.H.3
  • 26
    • 34547181885 scopus 로고    scopus 로고
    • Raft domain reorganization driven by short-and long-chain ceramide: Acombined AFM and FCS study
    • Chiantia S, Kahya N, Schwille P. 2007. Raft domain reorganization driven by short-and long-chain ceramide: Acombined AFM and FCS study. Langmuir 23: 7659-7665.
    • (2007) Langmuir , vol.23 , pp. 7659-7665
    • Chiantia, S.1    Kahya, N.2    Schwille, P.3
  • 27
    • 58149196402 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy in membrane structure elucidation
    • Chiantia S, Ries J, Schwille P. 2009. Fluorescence correlation spectroscopy in membrane structure elucidation. Biochim Biophys Acta 1788: 225-233.
    • (2009) Biochim Biophys Acta , vol.1788 , pp. 225-233
    • Chiantia, S.1    Ries, J.2    Schwille, P.3
  • 29
    • 33845406090 scopus 로고    scopus 로고
    • Preferential accumulation of A β(1-42) on gel phase domains of lipid bilayers: An AFM and fluorescence study
    • Choucair A, Chakrapani M, Chakravarthy B, Katsaras J, Johnston LJ. 2007. Preferential accumulation of A β(1-42) on gel phase domains of lipid bilayers: An AFM and fluorescence study. Biochim Biophys Acta 1768: 146-154.
    • (2007) Biochim Biophys Acta , vol.1768 , pp. 146-154
    • Choucair, A.1    Chakrapani, M.2    Chakravarthy, B.3    Katsaras, J.4    Johnston, L.J.5
  • 31
    • 34250668824 scopus 로고    scopus 로고
    • Ganglioside partitioning and aggregation in phaseseparated monolayers characterized by bodipy GM1 monomer/dimer emission
    • Coban O, Burger M, Laliberte M, Ianoul A, Johnston LJ. 2007. Ganglioside partitioning and aggregation in phaseseparated monolayers characterized by bodipy GM1 monomer/dimer emission. Langmuir 23: 6704-6711.
    • (2007) Langmuir , vol.23 , pp. 6704-6711
    • Coban, O.1    Burger, M.2    Laliberte, M.3    Ianoul, A.4    Johnston, L.J.5
  • 32
    • 0142116238 scopus 로고    scopus 로고
    • Diffusion dynamics of glycine receptors revealed by single-quantum dot tracking
    • Dahan M, Levi S, Luccardini C, Rostaing P, Riveau B, Triller A. 2003. Diffusion dynamics of glycine receptors revealed by single-quantum dot tracking. Science 302: 442-445.
    • (2003) Science , vol.302 , pp. 442-445
    • Dahan, M.1    Levi, S.2    Luccardini, C.3    Rostaing, P.4    Riveau, B.5    Triller, A.6
  • 33
    • 0015919993 scopus 로고
    • Photomicrography of corneal endothelial cells in-vivo
    • Davidovi P, Egger MD. 1973. Photomicrography of corneal endothelial cells in-vivo. Nature 244: 366-367.
    • (1973) Nature , vol.244 , pp. 366-367
    • Davidovi, P.1    Egger, M.D.2
  • 34
    • 33746902390 scopus 로고    scopus 로고
    • Accounting for triplet and saturation effects in FCS measurements
    • Davis LM, Shen. 2006. Accounting for triplet and saturation effects in FCS measurements. Curr Pharm Biotechnol 7: 287-301.
    • (2006) Curr Pharm Biotechnol , vol.7 , pp. 287-301
    • Davis, L.M.S.1
  • 35
    • 0022400414 scopus 로고
    • Probing microtubule-dependent intracellular motility with nanometer particle video ultramicroscopy (nanovid ultramicroscopy)
    • Debrabander M, Geuens G, Nuydens R, Moeremans M, Demey J. 1985. Probing microtubule-dependent intracellular motility with nanometer particle video ultramicroscopy (nanovid ultramicroscopy). Cytobios 43: 273-283.
    • (1985) Cytobios , vol.43 , pp. 273-283
    • Debrabander, M.1    Geuens, G.2    Nuydens, R.3    Moeremans, M.4    Demey, J.5
  • 36
    • 0026053736 scopus 로고
    • Lateral diffusion and retrograde movements of individual cell-surface components on single motile cells observed with nanovid microscopy
    • Debrabander M, Nuydens R, Ishihara A, Holifield B, Jacobson K, Geerts H. 1991. Lateral diffusion and retrograde movements of individual cell-surface components on single motile cells observed with nanovid microscopy. J Cell Biol 112: 111-124.
    • (1991) J Cell Biol , vol.112 , pp. 111-124
    • Debrabander, M.1    Nuydens, R.2    Ishihara, A.3    Holifield, B.4    Jacobson, K.5    Geerts, H.6
  • 37
    • 3543141297 scopus 로고    scopus 로고
    • Photobleaching, mobility, and compartmentalisation: Inferences in fluorescence correlation spectroscopy
    • Delon A, Usson Y, Derouard J, Biben T, Souchier C. 2004. Photobleaching, mobility, and compartmentalisation: Inferences in fluorescence correlation spectroscopy. J Fluorescence 14: 255-267.
    • (2004) J Fluorescence , vol.14 , pp. 255-267
    • Delon, A.1    Usson, Y.2    Derouard, J.3    Biben, T.4    Souchier, C.5
  • 38
    • 0025342635 scopus 로고
    • 2-photon laser scanning fluorescence microscopy
    • Denk W, Strickler JH, Webb WW. 1990. 2-photon laser scanning fluorescence microscopy. Science 248: 73-76.
    • (1990) Science , vol.248 , pp. 73-76
    • Denk, W.1    Strickler, J.H.2    Webb, W.W.3
  • 39
    • 33847275531 scopus 로고    scopus 로고
    • Two-focus fluorescence correlation spectroscopy: A new tool for accurate and absolute diffusion measurements
    • Dertinger T, Pacheco V, von der Hocht I, Hartmann R, Gregor I, Enderlein J. 2007. Two-focus fluorescence correlation spectroscopy: A new tool for accurate and absolute diffusion measurements. Chemphyschem 8: 433-443.
    • (2007) Chemphyschem , vol.8 , pp. 433-443
    • Dertinger, T.1    Pacheco, V.2    von der Hocht, I.3    Hartmann, R.4    Gregor, I.5    Enderlein, J.6
  • 40
    • 33745447698 scopus 로고    scopus 로고
    • Lateral organization of a membrane protein in a supported binary lipid domain: Direct observation of the organization of bacterial light-harvesting complex 2 by total internal reflection fluorescence microscopy
    • Dewa T, Sugiura R, Suemori Y, Sugimoto M, Takeuchi T, Hiro A, Iida K, Gardiner AT, Cogdell RJ, Nango M. 2006. Lateral organization of a membrane protein in a supported binary lipid domain: Direct observation of the organization of bacterial light-harvesting complex 2 by total internal reflection fluorescence microscopy. Langmuir 22: 5412-5418.
    • (2006) Langmuir , vol.22 , pp. 5412-5418
    • Dewa, T.1    Sugiura, R.2    Suemori, Y.3    Sugimoto, M.4    Takeuchi, T.5    Hiro, A.6    Iida, K.7    Gardiner, A.T.8    Cogdell, R.J.9    Nango, M.10
  • 42
    • 68949093921 scopus 로고    scopus 로고
    • Imaging barriers to diffusion by pair correlation functions
    • Digman MA, Gratton E. 2009. Imaging barriers to diffusion by pair correlation functions. Biophys J 97: 665-673.
    • (2009) Biophys J , vol.97 , pp. 665-673
    • Digman, M.A.1    Gratton, E.2
  • 43
    • 0035678612 scopus 로고    scopus 로고
    • Photobleaching and stabilization of fluorophores used for single-molecule analysis with one-and two-photon excitation
    • Dittrich PS, Schwille P. 2001. Photobleaching and stabilization of fluorophores used for single-molecule analysis with one-and two-photon excitation. Appl Phys B 73: 829-837.
    • (2001) Appl Phys B , vol.73 , pp. 829-837
    • Dittrich, P.S.1    Schwille, P.2
  • 44
    • 21244447355 scopus 로고    scopus 로고
    • Distribution, lateral mobility and function of membrane proteins incorporated into giant unilamellar vesicles
    • Doeven MK, Folgering JHA, Krasnikov V, Geertsma ER, van den Bogaart G, Poolman B. 2005. Distribution, lateral mobility and function of membrane proteins incorporated into giant unilamellar vesicles. Biophys J 88: 1134-1142.
    • (2005) Biophys J , vol.88 , pp. 1134-1142
    • Doeven, M.K.1    Folgering, J.H.A.2    Krasnikov, V.3    Geertsma, E.R.4    van den Bogaart, G.5    Poolman, B.6
  • 46
    • 0026539874 scopus 로고
    • Patches, posts and fences: Proteins and plasma membrane domains
    • Edidin M. 1992. Patches, posts and fences: Proteins and plasma membrane domains. Trends Cell Biol 2: 376-380.
    • (1992) Trends Cell Biol , vol.2 , pp. 376-380
    • Edidin, M.1
  • 47
    • 0014213139 scopus 로고
    • New reflected-light microscope for viewing unstained brain and ganglion cells
    • Egger MD, Petran M. 1967. New reflected-light microscope for viewing unstained brain and ganglion cells. Science 157: 305-307.
    • (1967) Science , vol.157 , pp. 305-307
    • Egger, M.D.1    Petran, M.2
  • 49
    • 0028229903 scopus 로고
    • Sorting single molecules-Application to diagnostics and evolutionary biotechnology
    • Eigen M, Rigler R. 1994. Sorting single molecules-Application to diagnostics and evolutionary biotechnology. Proc Natl Acad Sci 91: 5740-5747.
    • (1994) Proc Natl Acad Sci , vol.91 , pp. 5740-5747
    • Eigen, M.1    Rigler, R.2
  • 50
    • 0030763228 scopus 로고    scopus 로고
    • Nuclear membrane dynamics and reassembly in living cells: Targeting of an inner nuclear membrane protein in interphase and mitosis
    • Ellenberg J, Siggia ED, Moreira JE, Smith CL, Presley JF, Worman HJ, Lippincott-Schwartz J. 1997. Nuclear membrane dynamics and reassembly in living cells: Targeting of an inner nuclear membrane protein in interphase and mitosis. J Cell Biol 138: 1193-1206.
    • (1997) J Cell Biol , vol.138 , pp. 1193-1206
    • Ellenberg, J.1    Siggia, E.D.2    Moreira, J.E.3    Smith, C.L.4    Presley, J.F.5    Worman, H.J.6    Lippincott-Schwartz, J.7
  • 51
    • 0016379116 scopus 로고
    • Fluorescence correlation spectroscopy. 1. Conceptual basis and theory
    • Elson EL, Magde D. 1974. Fluorescence correlation spectroscopy. 1. Conceptual basis and theory. Biopolymers 13: 1-27.
    • (1974) Biopolymers , vol.13 , pp. 1-27
    • Elson, E.L.1    Magde, D.2
  • 52
    • 27744530935 scopus 로고    scopus 로고
    • Performance of fluorescence correlation spectroscopy for measuring diffusion and concentration
    • Enderlein J, Gregor I, Patra D, Dertinger T, Kaupp UB. 2005. Performance of fluorescence correlation spectroscopy for measuring diffusion and concentration. Chemphyschem 6: 2324-2336.
    • (2005) Chemphyschem , vol.6 , pp. 2324-2336
    • Enderlein, J.1    Gregor, I.2    Patra, D.3    Dertinger, T.4    Kaupp, U.B.5
  • 54
    • 0035836585 scopus 로고    scopus 로고
    • Tamoxifen perturbs lipid bilayer order and permeability: Comparison of DSC, fluorescence anisotropy, Laurdan generalized polarization and carboxyfluorescein leakage studies
    • Engelke M, Bojarski P, Bloss R, Diehl H. 2001. Tamoxifen perturbs lipid bilayer order and permeability: Comparison of DSC, fluorescence anisotropy, Laurdan generalized polarization and carboxyfluorescein leakage studies. Biophys Chem 90: 157-173.
    • (2001) Biophys Chem , vol.90 , pp. 157-173
    • Engelke, M.1    Bojarski, P.2    Bloss, R.3    Diehl, H.4
  • 55
    • 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. Biophysical J 70: 2767-2773.
    • (1996) Biophysical J , vol.70 , pp. 2767-2773
    • Feder, T.J.1    Brust Mascher, I.2    Slattery, J.P.3    Baird, B.4    Webb, W.W.5
  • 56
    • 84981779372 scopus 로고
    • Intermolecular energy migration and fluorescence
    • Förster T. 1948. Intermolecular energy migration and fluorescence. Ann Phys 2: 55-75.
    • (1948) Ann Phys , vol.2 , pp. 55-75
    • Förster, T.1
  • 57
    • 67649992483 scopus 로고    scopus 로고
    • Single-molecule fluorescence imaging of peptide binding to supported lipid bilayers
    • Fox CB, Wayment JR, Myers GA, Endicott SK, Harris JM. 2009. Single-molecule fluorescence imaging of peptide binding to supported lipid bilayers. Anal Chem 81: 5130-5138.
    • (2009) Anal Chem , vol.81 , pp. 5130-5138
    • Fox, C.B.1    Wayment, J.R.2    Myers, G.A.3    Endicott, S.K.4    Harris, J.M.5
  • 58
    • 15944425187 scopus 로고
    • Dynamics of nonspecific adsorption of insulin to erythrocyte membrane
    • Fulbright RM, Axelrod D. 1993. Dynamics of nonspecific adsorption of insulin to erythrocyte membrane. J Fluor 3: 1-16.
    • (1993) J Fluor , vol.3 , pp. 1-16
    • Fulbright, R.M.1    Axelrod, D.2
  • 59
    • 0029010607 scopus 로고
    • Oligomerization of epidermal growth-factor receptors on a431 cells studied by time-resolved fluorescence imaging microscopy-A stereochemical model for tyrosine kinase receptor activation
    • Gadella TWJ, Jovin TM. 1995. Oligomerization of epidermal growth-factor receptors on a431 cells studied by time-resolved fluorescence imaging microscopy-A stereochemical model for tyrosine kinase receptor activation. J Cell Biol 129: 1543-1558.
    • (1995) J Cell Biol , vol.129 , pp. 1543-1558
    • Gadella, T.W.J.1    Jovin, T.M.2
  • 60
  • 62
    • 77649226985 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy for the study of membrane dynamics and organization in giant unilamellar vesicles
    • García-Sáez AJ, Carrer DC, Schwille P. 2010. Fluorescence correlation spectroscopy for the study of membrane dynamics and organization in giant unilamellar vesicles. Meth Mol Biol 606: 493-508.
    • (2010) Meth Mol Biol , vol.606 , pp. 493-508
    • García-Sáez, A.J.1    Carrer, D.C.2    Schwille, P.3
  • 63
    • 72149121153 scopus 로고    scopus 로고
    • Quantitative imaging of molecular order in lipid membranes using two-photon fluorescence polarimetry
    • Gasecka A, Han TJ, Favard C, Cho BR, Brasselet S. 2009. Quantitative imaging of molecular order in lipid membranes using two-photon fluorescence polarimetry. Biophys J 97: 2854-2862.
    • (2009) Biophys J , vol.97 , pp. 2854-2862
    • Gasecka, A.1    Han, T.J.2    Favard, C.3    Cho, B.R.4    Brasselet, S.5
  • 65
    • 0023871621 scopus 로고
    • Tracking kinesindriven movements with nanometre-scale precision
    • Gelles J, Schnapp BJ, Sheetz MP. 1988. Tracking kinesindriven movements with nanometre-scale precision. Nature 331: 450-453.
    • (1988) Nature , vol.331 , pp. 450-453
    • Gelles, J.1    Schnapp, B.J.2    Sheetz, M.P.3
  • 66
    • 0028281482 scopus 로고
    • Automated detection and tracking of individual and clustered cell-surface lowdensity-lipoprotein receptor molecules
    • Ghosh RN, Webb WW. 1994. Automated detection and tracking of individual and clustered cell-surface lowdensity-lipoprotein receptor molecules. Biophys J 66: 1301-1318.
    • (1994) Biophys J , vol.66 , pp. 1301-1318
    • Ghosh, R.N.1    Webb, W.W.2
  • 67
    • 0035899985 scopus 로고    scopus 로고
    • Fluorescence anisotropy measurements of lipid order in plasma membranes and lipid rafts from RBL-2H3 mast cells
    • Gidwani A, Holowka D, Baird B. 2001. Fluorescence anisotropy measurements of lipid order in plasma membranes and lipid rafts from RBL-2H3 mast cells. Biochemistry 40: 12422-12429.
    • (2001) Biochemistry , vol.40 , pp. 12422-12429
    • Gidwani, A.1    Holowka, D.2    Baird, B.3
  • 68
    • 1542399850 scopus 로고    scopus 로고
    • Lipid raft proteins have a random distribution during localized activation of the T-cell receptor
    • Glebov OO, Nichols BJ. 2004. Lipid raft proteins have a random distribution during localized activation of the T-cell receptor. Nat Cell Biol 6: 238-243.
    • (2004) Nat Cell Biol , vol.6 , pp. 238-243
    • Glebov, O.O.1    Nichols, B.J.2
  • 70
    • 34250973664 scopus 로고
    • Über dieWahrscheinlichkeit des Zusammenwirkens zweier Lichtquanten in einem Elementarakt
    • Goppert M. 1929. Über dieWahrscheinlichkeit des Zusammenwirkens zweier Lichtquanten in einem Elementarakt. Naturwissenschaften 17: 932-932.
    • (1929) Naturwissenschaften , vol.17 , pp. 932
    • Goppert, M.1
  • 71
    • 0031956092 scopus 로고    scopus 로고
    • Quantitative fluorescence resonance energy transfer measurements using fluorescence microscopy
    • Gordon GW, Berry G, Liang XH, Levine B, Herman B. 1998. Quantitative fluorescence resonance energy transfer measurements using fluorescence microscopy. Biophys J 74: 2702-2713.
    • (1998) Biophys J , vol.74 , pp. 2702-2713
    • Gordon, G.W.1    Berry, G.2    Liang, X.H.3    Levine, B.4    Herman, B.5
  • 72
    • 0028936853 scopus 로고
    • Analysis of simulated and experimental fluorescence recovery after photobleaching. Data for two diffusing components
    • Gordon GW, Chazotte B, Wang XF, Herman B. 1995. Analysis of simulated and experimental fluorescence recovery after photobleaching. Data for two diffusing components. Biophys J 68: 766-778.
    • (1995) Biophys J , vol.68 , pp. 766-778
    • Gordon, G.W.1    Chazotte, B.2    Wang, X.F.3    Herman, B.4
  • 76
    • 13444306203 scopus 로고    scopus 로고
    • Optical saturation in fluorescence correlation spectroscopy under continuouswave and pulsed excitation
    • Gregor I, Patra D, Enderlein J. 2005. Optical saturation in fluorescence correlation spectroscopy under continuouswave and pulsed excitation. Chemphyschem 6: 164-170.
    • (2005) Chemphyschem , vol.6 , pp. 164-170
    • Gregor, I.1    Patra, D.2    Enderlein, J.3
  • 77
    • 42149089925 scopus 로고    scopus 로고
    • Molecular diffusion measurement in lipid bilayers over wide concentration ranges: A comparative study
    • Guo L, Har JY, Sankaran J, Hong YM, Kannan B, Wohland T. 2008. Molecular diffusion measurement in lipid bilayers over wide concentration ranges: A comparative study. Chemphyschem 9: 721-728.
    • (2008) Chemphyschem , vol.9 , pp. 721-728
    • Guo, L.1    Har, J.Y.2    Sankaran, J.3    Hong, Y.M.4    Kannan, B.5    Wohland, T.6
  • 78
  • 79
    • 0035818530 scopus 로고    scopus 로고
    • Cholesterol depletion induces large scale domain segregation in living cell membranes
    • Hao MM, Mukherjee S, Maxfield FR. 2001. Cholesterol depletion induces large scale domain segregation in living cell membranes. Proc Natl Acad Sci 98: 13072-13077.
    • (2001) Proc Natl Acad Sci , vol.98 , pp. 13072-13077
    • Hao, M.M.1    Mukherjee, S.2    Maxfield, F.R.3
  • 80
    • 0032506222 scopus 로고    scopus 로고
    • Dynamics of fluorescence fluctuations in green fluorescent protein observed by fluorescence correlation spectroscopy
    • Haupts U, Maiti S, Schwille P, Webb WW. 1998. Dynamics of fluorescence fluctuations in green fluorescent protein observed by fluorescence correlation spectroscopy. Proc Natl Acad Sci 95: 13573-13578.
    • (1998) Proc Natl Acad Sci , vol.95 , pp. 13573-13578
    • Haupts, U.1    Maiti, S.2    Schwille, P.3    Webb, W.W.4
  • 81
    • 55049135085 scopus 로고    scopus 로고
    • Stimulated emission depletion (STED) nanoscopy of a fluorescent proteinlabeled organelle inside a living cell
    • Hein B, Willig KI, Hell SW. 2008. Stimulated emission depletion (STED) nanoscopy of a fluorescent proteinlabeled organelle inside a living cell. Proc Natl Acad Sci 105: 14271-14276.
    • (2008) Proc Natl Acad Sci , vol.105 , pp. 14271-14276
    • Hein, B.1    Willig, K.I.2    Hell, S.W.3
  • 82
    • 0034641711 scopus 로고    scopus 로고
    • Simultaneous two-photon excitation of distinct labels for dual-color fluorescence crosscorrelation analysis
    • Heinze KG, Koltermann A, Schwille P. 2000. Simultaneous two-photon excitation of distinct labels for dual-color fluorescence crosscorrelation analysis. Proc Natl Acad Sci 97: 10377-10382.
    • (2000) Proc Natl Acad Sci , vol.97 , pp. 10377-10382
    • Heinze, K.G.1    Koltermann, A.2    Schwille, P.3
  • 83
    • 0036708472 scopus 로고    scopus 로고
    • Twophoton fluorescence coincidence analysis: Rapid measurements of enzyme kinetics
    • Heinze KG, Rarbach M, Jahnz M, Schwille P. 2002. Twophoton fluorescence coincidence analysis: Rapid measurements of enzyme kinetics. Biophys J 83: 1671-1681.
    • (2002) Biophys J , vol.83 , pp. 1671-1681
    • Heinze, K.G.1    Rarbach, M.2    Jahnz, M.3    Schwille, P.4
  • 84
    • 0001295176 scopus 로고
    • Kinetics of epidermal growth factor/receptor binding on cells measured by total internal reflection/fluorescence recovery after photobleaching
    • Hellen E, Axelrod D. 1991. Kinetics of epidermal growth factor/receptor binding on cells measured by total internal reflection/fluorescence recovery after photobleaching. J Fluor 1: 113-128.
    • (1991) J Fluor , vol.1 , pp. 113-128
    • Hellen, E.1    Axelrod, D.2
  • 85
    • 0016471374 scopus 로고
    • Nonlinear optical microscope using second-harmonic generation
    • Hellwarth R, Christensen P. 1975. Nonlinear optical microscope using second-harmonic generation. Appl Opt 14: 247-248.
    • (1975) Appl Opt , vol.14 , pp. 247-248
    • Hellwarth, R.1    Christensen, P.2
  • 86
    • 0036789423 scopus 로고    scopus 로고
    • Focal volume optics and experimental artifacts in confocal fluorescence correlation spectroscopy
    • Hess ST, Webb WW. 2002. Focal volume optics and experimental artifacts in confocal fluorescence correlation spectroscopy. Biophys J 83: 2300-2317.
    • (2002) Biophys J , vol.83 , pp. 2300-2317
    • Hess, S.T.1    Webb, W.W.2
  • 89
    • 77953021658 scopus 로고    scopus 로고
    • Characterization of horizontal lipid bilayers as a model system to study lipid phase separation
    • Honigmann A, Walter C, Erdmann F, Eggeling C, Wagner R. 2010. Characterization of horizontal lipid bilayers as a model system to study lipid phase separation. Biophys J 98: 2886-2894.
    • (2010) Biophys J , vol.98 , pp. 2886-2894
    • Honigmann, A.1    Walter, C.2    Erdmann, F.3    Eggeling, C.4    Wagner, R.5
  • 90
    • 72249104759 scopus 로고    scopus 로고
    • Optical saturation as a versatile tool to enhance resolution in confocal microscopy
    • Humpolickova J, Benda A, Enderlein J. 2009. Optical saturation as a versatile tool to enhance resolution in confocal microscopy. Biophys J 97: 2623-2629.
    • (2009) Biophys J , vol.97 , pp. 2623-2629
    • Humpolickova, J.1    Benda, A.2    Enderlein, J.3
  • 92
    • 0020808444 scopus 로고
    • Fluorescence correlation spectroscopy and photobleaching recovery of multiple binding reactions. 1. Theory and FCS measurements
    • Icenogle RD, Elson EL. 1983a. Fluorescence correlation spectroscopy and photobleaching recovery of multiple binding reactions. 1. Theory and FCS measurements. Biopolymers 22: 1919-1948.
    • (1983) Biopolymers , vol.22 , pp. 1919-1948
    • Icenogle, R.D.1    Elson, E.L.2
  • 93
    • 0020807256 scopus 로고
    • Fluorescence correlation spectroscopy and photobleaching recovery of multiple binding reactions. 2. FPR AND FCS measurements at low and high DNA concentrations
    • Icenogle RD, Elson EL. 1983b. Fluorescence correlation spectroscopy and photobleaching recovery of multiple binding reactions. 2. FPR AND FCS measurements at low and high DNA concentrations. Biopolymers 22: 1949-1966.
    • (1983) Biopolymers , vol.22 , pp. 1949-1966
    • Icenogle, R.D.1    Elson, E.L.2
  • 94
    • 69249213490 scopus 로고    scopus 로고
    • Enzymatic generation of ceramide induces membrane restructuring: Correlated AFM and fluorescence imaging of supported bilayers
    • Ira S Zou, Ramirez DMC, Vanderlip S, Ogilvie W, Jakubek ZJ, Johnston LJ. 2009. Enzymatic generation of ceramide induces membrane restructuring: Correlated AFM and fluorescence imaging of supported bilayers. J Struct Biol 168: 78-89.
    • (2009) J Struct Biol , vol.168 , pp. 78-89
    • Ira, S.Z.1    Ramirez, D.M.C.2    Vanderlip, S.3    Ogilvie, W.4    Jakubek, Z.J.5    Johnston, L.J.6
  • 95
    • 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: 1441-1442.
    • (1995) Science , vol.268 , pp. 1441-1442
    • Jacobson, K.1    Sheets, E.D.2    Simson, R.3
  • 98
    • 70350596338 scopus 로고    scopus 로고
    • Protein adsorption and displacement at lipid layers determined by total internal reflection fluorescence (TIRF)
    • Jorgensen L, Wood GK, Rosenkrands I, Petersen C, Christensen D. 2009. Protein adsorption and displacement at lipid layers determined by total internal reflection fluorescence (TIRF). J Lipo Res 19: 99-104.
    • (2009) J Lipo Res , vol.19 , pp. 99-104
    • Jorgensen, L.1    Wood, G.K.2    Rosenkrands, I.3    Petersen, C.4    Christensen, D.5
  • 99
    • 80055119873 scopus 로고    scopus 로고
    • Imaging exocytosis in retinal bipolar cells with TIRF microscopy
    • Joselevitch C, Zenisek D. 2009. Imaging exocytosis in retinal bipolar cells with TIRF microscopy. J Vis Exp 9: 1305.
    • (2009) J Vis Exp , vol.9 , pp. 1305
    • Joselevitch, C.1    Zenisek, D.2
  • 101
    • 77956671277 scopus 로고    scopus 로고
    • Fluorescent probe partitioning in giant unilamellar vesicles of 'lipid raft' mixtures
    • Juhasz J, Davis JH, Sharom FJ. 2010. Fluorescent probe partitioning in giant unilamellar vesicles of 'lipid raft' mixtures. Biochem J 430: 415-423.
    • (2010) Biochem J , vol.430 , pp. 415-423
    • Juhasz, J.1    Davis, J.H.2    Sharom, F.J.3
  • 103
    • 33645294105 scopus 로고    scopus 로고
    • Fluorescence correlation studies of lipid domains in model membranes (Review)
    • Kahya N, Schwille P. 2006a. Fluorescence correlation studies of lipid domains in model membranes (Review). Mol Membr Biol 23: 29-39.
    • (2006) Mol Membr Biol , vol.23 , pp. 29-39
    • Kahya, N.1    Schwille, P.2
  • 104
    • 33749343217 scopus 로고    scopus 로고
    • How phospholipid-cholesterol interactions modulate lipid lateral diffusion, as revealed by fluorescence correlation spectroscopy
    • Kahya N, Schwille P. 2006b. How phospholipid-cholesterol interactions modulate lipid lateral diffusion, as revealed by fluorescence correlation spectroscopy. J Fluorescence 16: 671-678.
    • (2006) J Fluorescence , vol.16 , pp. 671-678
    • Kahya, N.1    Schwille, P.2
  • 105
    • 0041461861 scopus 로고    scopus 로고
    • Probing lipid mobility of raft-exhibiting model membranes by fluorescence correlation spectroscopy
    • Kahya N, Scherfeld D, Bacia K, Poolman B, Schwille P. 2003. Probing lipid mobility of raft-exhibiting model membranes by fluorescence correlation spectroscopy. J Biol Chem 278: 28109-28115.
    • (2003) J Biol Chem , vol.278 , pp. 28109-28115
    • Kahya, N.1    Scherfeld, D.2    Bacia, K.3    Poolman, B.4    Schwille, P.5
  • 106
    • 1942454738 scopus 로고    scopus 로고
    • Lipid domain formation and dynamics in giant unilamellar vesicles explored by fluorescence correlation spectroscopy
    • Kahya N, Scherfeld D, Bacia K, Schwille P. 2004. Lipid domain formation and dynamics in giant unilamellar vesicles explored by fluorescence correlation spectroscopy. J Struct Biol 147: 77-89.
    • (2004) J Struct Biol , vol.147 , pp. 77-89
    • Kahya, N.1    Scherfeld, D.2    Bacia, K.3    Schwille, P.4
  • 109
    • 27344440992 scopus 로고    scopus 로고
    • Fleeting glimpses of lipid rafts: How biophysics is being used to track them
    • Kenworthy AK. 2005. Fleeting glimpses of lipid rafts: How biophysics is being used to track them. J Invest Med 53: 312-317.
    • (2005) J Invest Med , vol.53 , pp. 312-317
    • Kenworthy, A.K.1
  • 110
    • 38949174738 scopus 로고    scopus 로고
    • Fluorescence recovery after photobleaching studies of lipid rafts
    • Kenworthy AK. 2007. Fluorescence recovery after photobleaching studies of lipid rafts. Methods Mol Biol 398: 179-192.
    • (2007) Methods Mol Biol , vol.398 , pp. 179-192
    • Kenworthy, A.K.1
  • 111
    • 0032514258 scopus 로고    scopus 로고
    • Distribution of a glycosylphosphatidylinositol-anchored protein at the apical surface of MDCK cells examined at a resolution of,100 angstrom using imaging fluorescence resonance energy transfer
    • Kenworthy AK, Edidin M. 1998, Distribution of a glycosylphosphatidylinositol-anchored protein at the apical surface of MDCK cells examined at a resolution of,100 angstrom using imaging fluorescence resonance energy transfer. J Cell Biol 142: 69-84.
    • (1998) J Cell Biol , vol.142 , pp. 69-84
    • Kenworthy, A.K.1    Edidin, M.2
  • 112
    • 0032605667 scopus 로고    scopus 로고
    • Imaging fluorescence resonance energy transfer as probe of membrane organization and molecular associations of GPI-anchored proteins
    • Kenworthy AK, Edidin M. 1999. Imaging fluorescence resonance energy transfer as probe of membrane organization and molecular associations of GPI-anchored proteins. Methods Mol Biol 116: 37-49.
    • (1999) Methods Mol Biol , vol.116 , pp. 37-49
    • Kenworthy, A.K.1    Edidin, M.2
  • 114
    • 0034075971 scopus 로고    scopus 로고
    • Highresolution FRET microscopy of cholera toxin B-subunit and GPI-anchored proteins in cell plasma membranes
    • Kenworthy AK, Petranova N, Edidin M. 2000. Highresolution FRET microscopy of cholera toxin B-subunit and GPI-anchored proteins in cell plasma membranes. Mol Biol Cell 11: 1645-1655.
    • (2000) Mol Biol Cell , vol.11 , pp. 1645-1655
    • Kenworthy, A.K.1    Petranova, N.2    Edidin, M.3
  • 115
    • 35748946937 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy in living cells
    • Kim SA, Heinze KG, Schwille P. 2007. Fluorescence correlation spectroscopy in living cells. Nat Methods 4: 963-973.
    • (2007) Nat Methods , vol.4 , pp. 963-973
    • Kim, S.A.1    Heinze, K.G.2    Schwille, P.3
  • 118
    • 35848938682 scopus 로고    scopus 로고
    • YFP photoconversion revisited: Confirmation of the CFP-like species
    • Kirber MT, Chen K, Keaney JF. 2007. YFP photoconversion revisited: Confirmation of the CFP-like species. Nat Methods 4: 767-768.
    • (2007) Nat Methods , vol.4 , pp. 767-768
    • Kirber, M.T.1    Chen, K.2    Keaney, J.F.3
  • 119
  • 120
    • 0033587719 scopus 로고    scopus 로고
    • Characterization of lipid bilayer phases by confocal microscopy and fluorescence correlation spectroscopy
    • Korlach J, Schwille P, Webb WW, Feigenson GW. 1999. Characterization of lipid bilayer phases by confocal microscopy and fluorescence correlation spectroscopy. Proc Natl Acad Sci 96: 8461-8466.
    • (1999) Proc Natl Acad Sci , vol.96 , pp. 8461-8466
    • Korlach, J.1    Schwille, P.2    Webb, W.W.3    Feigenson, G.W.4
  • 122
    • 59449096824 scopus 로고    scopus 로고
    • Visualization of lipid domains in giant unilamellar vesicles using an environment-sensitive membrane probe based on 3-hydroxyflavone
    • Klymchenko AS, Oncul S, Didier P, Schaub E, Bagatolli L, Duportail G, Mely Y. 2009. Visualization of lipid domains in giant unilamellar vesicles using an environment-sensitive membrane probe based on 3-hydroxyflavone. Biochim Biophys Acta 1788: 495-499.
    • (2009) Biochim Biophys Acta , vol.1788 , pp. 495-499
    • Klymchenko, A.S.1    Oncul, S.2    Didier, P.3    Schaub, E.4    Bagatolli, L.5    Duportail, G.6    Mely, Y.7
  • 123
    • 0027504198 scopus 로고
    • Confined lateral diffusion of membrane-receptors as studied by singleparticle tracking (NANOVID microscopy)-Effects of calcium-induced differentiation in cultured epithelialcells
    • Kusumi A, Sako Y, Yamamoto M. 1993. Confined lateral diffusion of membrane-receptors as studied by singleparticle tracking (NANOVID microscopy)-Effects of calcium-induced differentiation in cultured epithelialcells. Biophys J 65: 2021-2040.
    • (1993) Biophys J , vol.65 , pp. 2021-2040
    • Kusumi, A.1    Sako, Y.2    Yamamoto, M.3
  • 124
    • 17844364513 scopus 로고    scopus 로고
    • Paradigm shift of the plasma membrane concept from the twodimensional continuum fluid to the partitioned fluid: High-speed single-molecule tracking of membrane molecules
    • Kusumi A, Nakada C, Ritchie K, Murase K, Suzuki K, Murakoshi H, Kasai RS, Kondo J, Fujiwara T. 2005. Paradigm shift of the plasma membrane concept from the twodimensional continuum fluid to the partitioned fluid: High-speed single-molecule tracking of membrane molecules. Annu Rev Biophys Biomol Struct 34: U351-U354.
    • (2005) Annu Rev Biophys Biomol Struct , vol.34
    • Kusumi, A.1    Nakada, C.2    Ritchie, K.3    Murase, K.4    Suzuki, K.5    Murakoshi, H.6    Kasai, R.S.7    Kondo, J.8    Fujiwara, T.9
  • 126
  • 127
    • 0037425587 scopus 로고    scopus 로고
    • EGF regulation of PITP dynamics is blocked by inhibitors of phospholipase C and of the Ras-MAP kinase pathway
    • Larijani B, Allen-Baume V, Morgan CP, Li M, Cockcroft S. 2003. EGF regulation of PITP dynamics is blocked by inhibitors of phospholipase C and of the Ras-MAP kinase pathway. Curr Biol 13: 78-84.
    • (2003) Curr Biol , vol.13 , pp. 78-84
    • Larijani, B.1    Allen-Baume, V.2    Morgan, C.P.3    Li, M.4    Cockcroft, S.5
  • 128
    • 0025823340 scopus 로고
    • Direct observation of Brownian-motion of lipids in a membrane
    • Lee GM, Ishihara A, Jacobson KA. 1991. Direct observation of Brownian-motion of lipids in a membrane. Proc Natl Acad Sci 88: 6274-6278.
    • (1991) Proc Natl Acad Sci , vol.88 , pp. 6274-6278
    • Lee, G.M.1    Ishihara, A.2    Jacobson, K.A.3
  • 130
    • 34548305123 scopus 로고    scopus 로고
    • Exploring dynamics in living cells by tracking single particles
    • Levi V, Gratton E. 2007. Exploring dynamics in living cells by tracking single particles. Cell Biochem Biophys 48: 1-15.
    • (2007) Cell Biochem Biophys , vol.48 , pp. 1-15
    • Levi, V.1    Gratton, E.2
  • 131
    • 22144445955 scopus 로고    scopus 로고
    • 3-D particle tracking in a two-photon microscope: Application to the study of molecular dynamics in cells
    • Levi V, Ruan QQ, Gratton E. 2005. 3-D particle tracking in a two-photon microscope: Application to the study of molecular dynamics in cells, Biophys J 88: 2919-2928.
    • (2005) Biophys J , vol.88 , pp. 2919-2928
    • Levi, V.1    Ruan, Q.Q.2    Gratton, E.3
  • 132
    • 33646122208 scopus 로고    scopus 로고
    • Melanosomes transported by myosin-V in Xenopus melanophores perform slow 35 nm steps
    • Levi V, Gelfand VI, Serpinskaya AS, Gratton E. 2006a. Melanosomes transported by myosin-V in Xenopus melanophores perform slow 35 nm steps. Biophys J 90: L7-L9.
    • (2006) Biophys J , vol.90
    • Levi, V.1    Gelfand, V.I.2    Serpinskaya, A.S.3    Gratton, E.4
  • 133
    • 33644548583 scopus 로고    scopus 로고
    • Organelle transport along microtubules in Xenopus melanophores: Evidence for cooperation between multiple motors
    • Levi V, Serpinskaya AS, Gratton E, Gelfand V. 2006b. Organelle transport along microtubules in Xenopus melanophores: Evidence for cooperation between multiple motors. Biophys J 90: 318-327.
    • (2006) Biophys J , vol.90 , pp. 318-327
    • Levi, V.1    Serpinskaya, A.S.2    Gratton, E.3    Gelfand, V.4
  • 135
    • 48249097851 scopus 로고    scopus 로고
    • Plasma membranes are poised for activation of raft phase coalescence at physiological temperature
    • Lingwood D, Ries J, Schwille P, Simons K. 2008. Plasma membranes are poised for activation of raft phase coalescence at physiological temperature. Proc Natl Acad Sci 105: 10005-10010.
    • (2008) Proc Natl Acad Sci , vol.105 , pp. 10005-10010
    • Lingwood, D.1    Ries, J.2    Schwille, P.3    Simons, K.4
  • 137
    • 0042338695 scopus 로고    scopus 로고
    • Photobleaching and photoactivation: Following protein dynamics in living cells
    • Lippincott-Schwartz J, Altan-Bonnet N, Patterson GH. 2003. Photobleaching and photoactivation: Following protein dynamics in living cells. Nat Cell Biol Suppl: S7-S14.
    • (2003) Nat Cell Biol , Issue.SUPPL.
    • Lippincott-Schwartz, J.1    Altan-Bonnet, N.2    Patterson, G.H.3
  • 138
    • 45449108968 scopus 로고    scopus 로고
    • Comparison of optical saturation effects in conventional and dual-focus fluorescence correlation spectroscopy
    • Loman A, Dertinger T, Koberling F, Enderlein J. 2008. Comparison of optical saturation effects in conventional and dual-focus fluorescence correlation spectroscopy. Chem Phys Lett 459: 18-21.
    • (2008) Chem Phys Lett , vol.459 , pp. 18-21
    • Loman, A.1    Dertinger, T.2    Koberling, F.3    Enderlein, J.4
  • 139
    • 4344582882 scopus 로고    scopus 로고
    • In vivo plasma membrane organization: Results of biophysical approaches
    • Lommerse PHM, Spaink HP, Schmidt T. 2004. In vivo plasma membrane organization: Results of biophysical approaches. Biochim Biophys Acta 1664: 119-131.
    • (2004) Biochim Biophys Acta , vol.1664 , pp. 119-131
    • Lommerse, P.H.M.1    Spaink, H.P.2    Schmidt, T.3
  • 140
    • 77954763297 scopus 로고    scopus 로고
    • Lipid diffusion in planar membranes investigated by fluorescence correlation spectroscopy
    • Machan R, Hof M. 2010. Lipid diffusion in planar membranes investigated by fluorescence correlation spectroscopy. Biochim Biophys Acta 1798: 1377-1391.
    • (2010) Biochim Biophys Acta , vol.1798 , pp. 1377-1391
    • Machan, R.1    Hof, M.2
  • 141
    • 0016366591 scopus 로고
    • Fluorescence correlation spectroscopy. 2. Experimental realization
    • Magde D, Elson EL, Webb WW. 1974. Fluorescence correlation spectroscopy. 2. Experimental realization. Biopolymers 13: 29-61.
    • (1974) Biopolymers , vol.13 , pp. 29-61
    • Magde, D.1    Elson, E.L.2    Webb, W.W.3
  • 142
    • 35949038838 scopus 로고
    • Thermodynamic fluctuations in a reacting system-Measurement by fluorescence correlation spectroscopy
    • Magde D, Webb WW, Elson E. 1972. Thermodynamic fluctuations in a reacting system-Measurement by fluorescence correlation spectroscopy. Phys Rev Lett 29: 705.
    • (1972) Phys Rev Lett , vol.29 , pp. 705
    • Magde, D.1    Webb, W.W.2    Elson, E.3
  • 143
    • 0017801658 scopus 로고
    • Fluorescence correlation spectroscopy. 3. Uniform translation and laminarflow
    • Magde D, Webb WW, Elson EL. 1978. Fluorescence correlation spectroscopy. 3. Uniform translation and laminarflow. Biopolymers 17: 361-376.
    • (1978) Biopolymers , vol.17 , pp. 361-376
    • Magde, D.1    Webb, W.W.2    Elson, E.L.3
  • 144
    • 54049110711 scopus 로고    scopus 로고
    • Use of Bodipylabeled sphingolipid and cholesterol analogs to examine membrane microdomains in cells
    • Marks DL, Bittman R, Pagano RE. 2008. Use of Bodipylabeled sphingolipid and cholesterol analogs to examine membrane microdomains in cells. Histochem Cell Biol 130: 819-832.
    • (2008) Histochem Cell Biol , vol.130 , pp. 819-832
    • Marks, D.L.1    Bittman, R.2    Pagano, R.E.3
  • 145
    • 31044439024 scopus 로고    scopus 로고
    • Phase coexistence and connectivity in the apical membrane of polarized epithelial cells
    • Meder D, Moreno MJ, Verkade P, Vaz WLC, Simons K. 2006. Phase coexistence and connectivity in the apical membrane of polarized epithelial cells. Proc Natl Acad Sci 103: 329-334.
    • (2006) Proc Natl Acad Sci , vol.103 , pp. 329-334
    • Meder, D.1    Moreno, M.J.2    Verkade, P.3    Vaz, W.L.C.4    Simons, K.5
  • 146
    • 19344375254 scopus 로고    scopus 로고
    • Coupling between clathrin-coated-pit invagination, cortactin recruitment, and membrane scission observed in live cells
    • Merrifield CJ, Perrais D, Zenisek D. 2005. Coupling between clathrin-coated-pit invagination, cortactin recruitment, and membrane scission observed in live cells. Cell 121: 593-606.
    • (2005) Cell , vol.121 , pp. 593-606
    • Merrifield, C.J.1    Perrais, D.2    Zenisek, D.3
  • 147
    • 0036714223 scopus 로고    scopus 로고
    • Imaging actin and dynamin recruitment during invagination of single clathrin-coated pits
    • Merrifield CJ, Feldman ME, Wan L, Almers W. 2002. Imaging actin and dynamin recruitment during invagination of single clathrin-coated pits. Nat Cell Biol 4: 691-698.
    • (2002) Nat Cell Biol , vol.4 , pp. 691-698
    • Merrifield, C.J.1    Feldman, M.E.2    Wan, L.3    Almers, W.4
  • 148
    • 0033021689 scopus 로고    scopus 로고
    • Resolution of fluorescence correlation measurements
    • Meseth U, Wohland T, Rigler R, Vogel H. 1999. Resolution of fluorescence correlation measurements. Biophys J 76: 1619-1631.
    • (1999) Biophys J , vol.76 , pp. 1619-1631
    • Meseth, U.1    Wohland, T.2    Rigler, R.3    Vogel, H.4
  • 149
    • 0021222922 scopus 로고
    • Bacterial toxins-Cellular mechanisms of action
    • Middlebrook JL, Dorland RB. 1984. Bacterial toxins-Cellular mechanisms of action. Microbiological Rev 48: 199-221.
    • (1984) Microbiological Rev , vol.48 , pp. 199-221
    • Middlebrook, J.L.1    Dorland, R.B.2
  • 150
    • 63649109490 scopus 로고    scopus 로고
    • M1 gangliosides designed for exploring lipid membrane properties and specific membrane-target interactions
    • M1 gangliosides designed for exploring lipid membrane properties and specific membrane-target interactions. Chem Phys Lipids 159: 38-44.
    • (2009) Chem Phys Lipids , vol.159 , pp. 38-44
    • Mikhalyov, I.1    Gretskaya, N.2    Johansson, L.B.A.3
  • 151
    • 0141867740 scopus 로고    scopus 로고
    • Illuminating protein interactions in tissue using confocal and two-photon excitation fluorescent resonance energy transfer microscopy
    • Mills JD, Stone JR, Rubin DG, Melon DE, Okonkwo DO, Periasamy A, Helm GA. 2003. Illuminating protein interactions in tissue using confocal and two-photon excitation fluorescent resonance energy transfer microscopy. J Biomed Opt 8: 347-356.
    • (2003) J Biomed Opt , vol.8 , pp. 347-356
    • Mills, J.D.1    Stone, J.R.2    Rubin, D.G.3    Melon, D.E.4    Okonkwo, D.O.5    Periasamy, A.6    Helm, G.A.7
  • 152
    • 0034581516 scopus 로고    scopus 로고
    • Monitoring protein conformations and interactions by fluorescence resonance energy transfer between mutants of green fluorescent protein
    • Miyawaki A, Tsien RY. 2000. Monitoring protein conformations and interactions by fluorescence resonance energy transfer between mutants of green fluorescent protein. Appl Chim Genes Hybrid Prot Pt B 327: 472-500.
    • (2000) Appl Chim Genes Hybrid Prot Pt B , vol.327 , pp. 472-500
    • Miyawaki, A.1    Tsien, R.Y.2
  • 154
    • 78650528229 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy in vivo
    • Mütze J, Ohrt T, Schwille P. 2011. Fluorescence correlation spectroscopy in vivo. Laser Photon Rev 5: 52-67.
    • (2011) Laser Photon Rev , vol.5 , pp. 52-67
    • Mütze, J.1    Ohrt, T.2    Schwille, P.3
  • 155
    • 84934439303 scopus 로고    scopus 로고
    • Imaging exocytosis of single insulin secretory granules with TIRF microscopy
    • Nagamatsu S, Ohara-Imaizumi M. 2008. Imaging exocytosis of single insulin secretory granules with TIRF microscopy. Methods Mol Biol 440: 259-268.
    • (2008) Methods Mol Biol , vol.440 , pp. 259-268
    • Nagamatsu, S.1    Ohara-Imaizumi, M.2
  • 156
    • 33645241165 scopus 로고    scopus 로고
    • Identifying optimal lipid raft characteristics required to promote nanoscale protein-protein interactions on the plasma membrane
    • Nicolau DV, Burrage K, Parton RG, Hancock JF. 2006. Identifying optimal lipid raft characteristics required to promote nanoscale protein-protein interactions on the plasma membrane. Mol Cell Biol 26: 313-323.
    • (2006) Mol Cell Biol , vol.26 , pp. 313-323
    • Nicolau, D.V.1    Burrage, K.2    Parton, R.G.3    Hancock, J.F.4
  • 157
    • 0033555935 scopus 로고    scopus 로고
    • Membrane interactions of a constitutively active GFP-Ki-Ras 4B and their role in signaling-Evidence from lateral mobility studies
    • Niv H, Gutman O, Henis YI, Kloog Y. 1999. Membrane interactions of a constitutively active GFP-Ki-Ras 4B and their role in signaling-Evidence from lateral mobility studies. J Biol Chem 274: 1606-1613.
    • (1999) J Biol Chem , vol.274 , pp. 1606-1613
    • Niv, H.1    Gutman, O.2    Henis, Y.I.3    Kloog, Y.4
  • 158
    • 0037182579 scopus 로고    scopus 로고
    • Activated K-Ras and H-Ras display different interactions with saturable nonraft sites at the surface of live cells
    • Niv H, Gutman O, Kloog Y, Henis YI. 2002. Activated K-Ras and H-Ras display different interactions with saturable nonraft sites at the surface of live cells. J Cell Biol 157: 865-872.
    • (2002) J Cell Biol , vol.157 , pp. 865-872
    • Niv, H.1    Gutman, O.2    Kloog, Y.3    Henis, Y.I.4
  • 159
    • 70349954766 scopus 로고    scopus 로고
    • Imaging exocytosis of single glucagon-like peptide-1 containing granules in a murine enteroendocrine cell line with total internal reflection fluorescent microscopy
    • Ohara-Imaizumi M, Aoyagi K, Akimoto Y, Nakamichi Y, Nishiwaki C, Kawakami H, Nagamatsu S. 2009. Imaging exocytosis of single glucagon-like peptide-1 containing granules in a murine enteroendocrine cell line with total internal reflection fluorescent microscopy. Biochem Biophys Res Comm 390: 16-20.
    • (2009) Biochem Biophys Res Comm , vol.390 , pp. 16-20
    • Ohara-Imaizumi, M.1    Aoyagi, K.2    Akimoto, Y.3    Nakamichi, Y.4    Nishiwaki, C.5    Kawakami, H.6    Nagamatsu, S.7
  • 160
    • 65549141786 scopus 로고    scopus 로고
    • Probing membrane order and topography in supported lipid bilayers by combined polarized total internal reflection fluorescence-atomic force microscopy
    • Oreopoulos J, Yip CM. 2009. Probing membrane order and topography in supported lipid bilayers by combined polarized total internal reflection fluorescence-atomic force microscopy. Biophys J 96: 1970-1984.
    • (2009) Biophys J , vol.96 , pp. 1970-1984
    • Oreopoulos, J.1    Yip, C.M.2
  • 161
    • 0030950269 scopus 로고    scopus 로고
    • Twophoton fluorescence microscopy of Laurdan generalized polarization domains in model and natural membranes
    • Parasassi T, Gratton E, Yu W M, Wilson P, Levi M. 1997. Twophoton fluorescence microscopy of Laurdan generalized polarization domains in model and natural membranes. Biophys J 72: 2413-2429.
    • (1997) Biophys J , vol.72 , pp. 2413-2429
    • Parasassi, T.1    Gratton, E.2    Yu, W.M.3    Wilson, P.4    Levi, M.5
  • 162
    • 0022545162 scopus 로고
    • Scanning fluorescence correlation spectroscopy. 1. Theory and simulation of aggregation measurements
    • Petersen NO. 1986. Scanning fluorescence correlation spectroscopy. 1. Theory and simulation of aggregation measurements. Biophys J 49: 809-815.
    • (1986) Biophys J , vol.49 , pp. 809-815
    • Petersen, N.O.1
  • 163
    • 0022495392 scopus 로고
    • Scanning fluorescence correlation spectroscopy. 2. Application to virus glycoprotein aggregation
    • Petersen NO, Johnson DC, Schlesinger MJ. 1986. Scanning fluorescence correlation spectroscopy. 2. Application to virus glycoprotein aggregation. Biophys J 49: 817-820.
    • (1986) Biophys J , vol.49 , pp. 817-820
    • Petersen, N.O.1    Johnson, D.C.2    Schlesinger, M.J.3
  • 164
    • 38949147878 scopus 로고    scopus 로고
    • Precise measurement of diffusion coefficients using scanning fluorescence correlation spectroscopy
    • Petrasek Z, Schwille P. 2008. Precise measurement of diffusion coefficients using scanning fluorescence correlation spectroscopy. Biophys J 94: 1437-1448.
    • (2008) Biophys J , vol.94 , pp. 1437-1448
    • Petrasek, Z.1    Schwille, P.2
  • 165
    • 77957043923 scopus 로고    scopus 로고
    • Scanning FCS for the characterization of protein dynamics in live cells
    • Petrasek Z, Ries J, Schwille P. 2010. Scanning FCS for the characterization of protein dynamics in live cells. Meth Enzymol 472: 317-343.
    • (2010) Meth Enzymol , vol.472 , pp. 317-343
    • Petrasek, Z.1    Ries, J.2    Schwille, P.3
  • 166
    • 67049127785 scopus 로고    scopus 로고
    • State of the art and novel trends in fluorescence correlation spectroscopy
    • In, (ed. Resch-Genger U),. Springer-Verlag, Berlin
    • Petrov E, Schwille P. 2007. State of the art and novel trends in fluorescence correlation spectroscopy. In Standardization and quality assurance in fluorescence measurements II (ed. Resch-Genger U), pp. 145-197. Springer-Verlag, Berlin.
    • (2007) Standardization and quality assurance in fluorescence measurements II , pp. 145-197
    • Petrov, E.1    Schwille, P.2
  • 167
    • 1642377367 scopus 로고    scopus 로고
    • Measurement of dynamic protein binding to chromatin in vivo, using photobleaching microscopy
    • Phair RD, Gorski SA, Misteli T. 2004. Measurement of dynamic protein binding to chromatin in vivo, using photobleaching microscopy. Methods Enzymol 375: 393-414.
    • (2004) Methods Enzymol , vol.375 , pp. 393-414
    • Phair, R.D.1    Gorski, S.A.2    Misteli, T.3
  • 168
    • 65749107160 scopus 로고    scopus 로고
    • Dynamic partitioning of a glycosyl-phosphatidylinositol-anchored protein in glycosphingolipid-rich microdomains imaged by single-quantum dot tracking
    • Pinaud F, Michalet X, Iyer G, Margeat E, Moore HP, Weiss S. 2009. Dynamic partitioning of a glycosyl-phosphatidylinositol-anchored protein in glycosphingolipid-rich microdomains imaged by single-quantum dot tracking. Traffic 10: 691-712.
    • (2009) Traffic , vol.10 , pp. 691-712
    • Pinaud, F.1    Michalet, X.2    Iyer, G.3    Margeat, E.4    Moore, H.P.5    Weiss, S.6
  • 169
    • 34548417621 scopus 로고    scopus 로고
    • Fluorescent protein FRET: The good, the bad and the ugly
    • Piston DW, Kremers GJ. 2007. Fluorescent protein FRET: The good, the bad and the ugly. Trends Biochem Sci 32: 407-414.
    • (2007) Trends Biochem Sci , vol.32 , pp. 407-414
    • Piston, D.W.1    Kremers, G.J.2
  • 170
    • 33745453853 scopus 로고    scopus 로고
    • 3D particle tracking on a two-photon microscope
    • Ragan T, Huang HD, So P, Gratton E. 2006. 3D particle tracking on a two-photon microscope. J Fluorescence 16: 325-336.
    • (2006) J Fluorescence , vol.16 , pp. 325-336
    • Ragan, T.1    Huang, H.D.2    So, P.3    Gratton, E.4
  • 171
    • 33747194557 scopus 로고    scopus 로고
    • Studying slow membrane dynamics with continuous wave scanning fluorescence correlation spectroscopy
    • Ries J, Schwille P. 2006. Studying slow membrane dynamics with continuous wave scanning fluorescence correlation spectroscopy. Biophys J 91: 1915-1924.
    • (2006) Biophys J , vol.91 , pp. 1915-1924
    • Ries, J.1    Schwille, P.2
  • 172
    • 65549152467 scopus 로고    scopus 로고
    • Accurate determination of membrane dynamics with line-scan FCS
    • Ries J, Chiantia S, Schwille P. 2009b. Accurate determination of membrane dynamics with line-scan FCS. Biophys J 96: 1999-2008.
    • (2009) Biophys J , vol.96 , pp. 1999-2008
    • Ries, J.1    Chiantia, S.2    Schwille, P.3
  • 173
    • 45149085544 scopus 로고    scopus 로고
    • Total internal reflection fluorescence correlation spectroscopy: Effects of lateral diffusion and surface-generated fluorescence
    • Ries J, Petrov EP, Schwille P. 2008. Total internal reflection fluorescence correlation spectroscopy: Effects of lateral diffusion and surface-generated fluorescence. Biophys J 95: 390-399.
    • (2008) Biophys J , vol.95 , pp. 390-399
    • Ries, J.1    Petrov, E.P.2    Schwille, P.3
  • 174
    • 69549126014 scopus 로고    scopus 로고
    • Modular scanning FCS quantifies receptor-ligand interactions in living multicellular organisms
    • U643-U631
    • Ries J, Yu SR, Burkhardt M, Brand M, Schwille P. 2009a. Modular scanning FCS quantifies receptor-ligand interactions in living multicellular organisms. Nat Methods 6: U643-U631.
    • (2009) Nat Methods , vol.6
    • Ries, J.1    Yu, S.R.2    Burkhardt, M.3    Brand, M.4    Schwille, P.5
  • 175
    • 0027317178 scopus 로고
    • Fluorescence correlation spectroscopy with high count rate and lowbackground-Analysis of translational diffusion
    • Rigler R, Mets U, Widengren J, Kask P. 1993. Fluorescence correlation spectroscopy with high count rate and lowbackground-Analysis of translational diffusion. Euro Biophys J Biophys Lett 22: 169-175.
    • (1993) Euro Biophys J Biophys Lett , vol.22 , pp. 169-175
    • Rigler, R.1    Mets, U.2    Widengren, J.3    Kask, P.4
  • 178
    • 0029117442 scopus 로고
    • Theory and application of fluorescence homotransfer to melittin oligomerization
    • Runnels LW, Scarlata SF. 1995. Theory and application of fluorescence homotransfer to melittin oligomerization. Biophys J 69: 1569-1583.
    • (1995) Biophys J , vol.69 , pp. 1569-1583
    • Runnels, L.W.1    Scarlata, S.F.2
  • 179
    • 0036751701 scopus 로고    scopus 로고
    • Alexa and Oregon Green dyes as fluorescence anisotropy probes for measuring protein-protein and protein-nucleic acid interactions
    • Rusinova E, Tretyachenko-Ladokhina V, Vele OE, Senear DF, Ross JBA. 2002. Alexa and Oregon Green dyes as fluorescence anisotropy probes for measuring protein-protein and protein-nucleic acid interactions. Anal Biochem 308: 18-25.
    • (2002) Anal Biochem , vol.308 , pp. 18-25
    • Rusinova, E.1    Tretyachenko-Ladokhina, V.2    Vele, O.E.3    Senear, D.F.4    Ross, J.B.A.5
  • 180
    • 34547823631 scopus 로고    scopus 로고
    • A 10-angstrom spectroscopic ruler applied to short polyprolines
    • Sahoo H, Roccatano D, Hennig A, Nau WM. 2007. A 10-angstrom spectroscopic ruler applied to short polyprolines. J Am Chem Soc 129: 9762-9772.
    • (2007) J Am Chem Soc , vol.129 , pp. 9762-9772
    • Sahoo, H.1    Roccatano, D.2    Hennig, A.3    Nau, W.M.4
  • 181
    • 0033779765 scopus 로고    scopus 로고
    • Single-molecule imaging of EGFR signalling on the surface of living cells
    • Sako Y, Minoghchi S, Yanagida T. 2000. Single-molecule imaging of EGFR signalling on the surface of living cells. Nat Cell Biol 2: 168-172.
    • (2000) Nat Cell Biol , vol.2 , pp. 168-172
    • Sako, Y.1    Minoghchi, S.2    Yanagida, T.3
  • 182
    • 0028140412 scopus 로고
    • Anomalous diffusion due to obstacles-A Monte Carlo study
    • Saxton MJ. 1994a. Anomalous diffusion due to obstacles-A Monte Carlo study. Biophys J 66: 394-401.
    • (1994) Biophys J , vol.66 , pp. 394-401
    • Saxton, M.J.1
  • 183
    • 0028170954 scopus 로고
    • Single-particle tracking-Models of directed transport
    • Saxton MJ. 1994b. Single-particle tracking-Models of directed transport. Biophys J 67: 2110-2119.
    • (1994) Biophys J , vol.67 , pp. 2110-2119
    • Saxton, M.J.1
  • 184
    • 0029163176 scopus 로고
    • Single-tracking-effects of corrals
    • Saxton MJ. 1995. Single-tracking-effects of corrals. Biophys J 69: 389-398.
    • (1995) Biophys J , vol.69 , pp. 389-398
    • Saxton, M.J.1
  • 185
    • 0030050141 scopus 로고    scopus 로고
    • Anomalous diffusion due to binding: A Monte Carlo study
    • Saxton MJ. 1996a. Anomalous diffusion due to binding: A Monte Carlo study, Biophys J 70: 1250-1262.
    • (1996) Biophys J , vol.70 , pp. 1250-1262
    • Saxton, M.J.1
  • 186
    • 4244183420 scopus 로고    scopus 로고
    • Single-particle tracking: New methods of data analysis
    • Saxton MJ. 1996b. Single-particle tracking: New methods of data analysis, Biophys J 70: TU415-TU415.
    • (1996) Biophys J , vol.70
    • Saxton, M.J.1
  • 187
    • 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: 1744-1753.
    • (1997) Biophys J , vol.72 , pp. 1744-1753
    • Saxton, M.J.1
  • 188
    • 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: 373-399.
    • (1997) Annu Rev Biophys Biomol Struct , vol.26 , pp. 373-399
    • Saxton, M.J.1    Jacobson, K.2
  • 189
    • 0344982102 scopus 로고    scopus 로고
    • Lipid dynamics and domain formation in model membranes composed of ternary mixtures of unsaturated and saturated phosphatidylcholines and cholesterol
    • Scherfeld D, Kahya N, Schwille P. 2003. Lipid dynamics and domain formation in model membranes composed of ternary mixtures of unsaturated and saturated phosphatidylcholines and cholesterol. Biophys J 85: 3758-3768.
    • (2003) Biophys J , vol.85 , pp. 3758-3768
    • Scherfeld, D.1    Kahya, N.2    Schwille, P.3
  • 192
    • 0039587949 scopus 로고    scopus 로고
    • Single-molecule microscopy on model membranes reveals anomalous diffusion
    • Schutz GJ, Schindler H, Schmidt T. 1997. Single-molecule microscopy on model membranes reveals anomalous diffusion. Biophys J 73: 1073-1080.
    • (1997) Biophys J , vol.73 , pp. 1073-1080
    • Schutz, G.J.1    Schindler, H.2    Schmidt, T.3
  • 193
    • 0037874731 scopus 로고    scopus 로고
    • Properties of lipid microdomains in a muscle cell membrane visualized by single molecule microscopy
    • Schutz GJ, Kada G, Pastushenko VP, Schindler H. 2000. Properties of lipid microdomains in a muscle cell membrane visualized by single molecule microscopy. EMBO J 19: 892-901.
    • (2000) EMBO J , vol.19 , pp. 892-901
    • Schutz, G.J.1    Kada, G.2    Pastushenko, V.P.3    Schindler, H.4
  • 195
    • 0242322534 scopus 로고    scopus 로고
    • TIR-FCS: Staying on the surface can sometimes be better
    • Schwille P. 2003. TIR-FCS: Staying on the surface can sometimes be better. Biophys J 85: 2783-2784.
    • (2003) Biophys J , vol.85 , pp. 2783-2784
    • Schwille, P.1
  • 196
    • 23044526373 scopus 로고    scopus 로고
    • Two-photon fluorescence cross-correlation spectroscopy
    • Schwille P, Heinze KG. 2001. Two-photon fluorescence cross-correlation spectroscopy. Chemphyschem 2: 269-272.
    • (2001) Chemphyschem , vol.2 , pp. 269-272
    • Schwille, P.1    Heinze, K.G.2
  • 197
    • 0033167917 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy with single-molecule sensitivity on cell and model membranes
    • Schwille P, Korlach J, Webb WW. 1999a. Fluorescence correlation spectroscopy with single-molecule sensitivity on cell and model membranes. Cytometry 36: 176-182.
    • (1999) Cytometry , vol.36 , pp. 176-182
    • Schwille, P.1    Korlach, J.2    Webb, W.W.3
  • 198
    • 0030895059 scopus 로고    scopus 로고
    • Dual-color fluorescence cross-correlation spectroscopy for multicomponent diffusional analysis in solution
    • Schwille P, Meyer Almes FJ, Rigler R. 1997. Dual-color fluorescence cross-correlation spectroscopy for multicomponent diffusional analysis in solution. Biophys J 72: 1878-1886.
    • (1997) Biophys J , vol.72 , pp. 1878-1886
    • Schwille, P.1    Meyer Almes, F.J.2    Rigler, R.3
  • 199
    • 0032828419 scopus 로고    scopus 로고
    • Molecular dynamics in living cells observed by fluorescence correlation spectroscopy with one-and two-photon excitation
    • Schwille P, Haupts U, Maiti S, Webb WW. 1999b. Molecular dynamics in living cells observed by fluorescence correlation spectroscopy with one-and two-photon excitation. Biophys J 77: 2251-2265.
    • (1999) Biophys J , vol.77 , pp. 2251-2265
    • Schwille, P.1    Haupts, U.2    Maiti, S.3    Webb, W.W.4
  • 200
    • 84863891709 scopus 로고    scopus 로고
    • Two-photon fluorescence correlation spectroscopy
    • In, (ed. Fujimoto JG, Farkas D). Oxford University Press, Oxford
    • Schwille P, Heinze K, Dittrich P, Haustein E. 2009. Two-photon fluorescence correlation spectroscopy. In Biomedical optical imaging (ed. Fujimoto JG, Farkas D). Oxford University Press, Oxford.
    • (2009) Biomedical optical imaging
    • Schwille, P.1    Heinze, K.2    Dittrich, P.3    Haustein, E.4
  • 202
    • 0027765482 scopus 로고
    • Tracking nanometer movements of single motor molecules
    • Sheetz MP, Kuo SC. 1993. Tracking nanometer movements of single motor molecules. Meth Cell Biol 39: 129-136.
    • (1993) Meth Cell Biol , vol.39 , pp. 129-136
    • Sheetz, M.P.1    Kuo, S.C.2
  • 203
    • 0018462482 scopus 로고
    • Effect of spherical-aberration on the imaging properties of scanning optical microscopes
    • Sheppard CJR, Wilson T.1979. Effect of spherical-aberration on the imaging properties of scanning optical microscopes. Appl Opt 18: 1058-1063.
    • (1979) Appl Opt , vol.18 , pp. 1058-1063
    • Sheppard, C.J.R.1    Wilson, T.2
  • 204
    • 33745052350 scopus 로고    scopus 로고
    • Cyclodextrins but not compactin inhibit the lateral diffusion of membrane proteins independent of cholesterol
    • Shvartsman DE, Gutman O, Tietz A, Henis. 2006. Cyclodextrins but not compactin inhibit the lateral diffusion of membrane proteins independent of cholesterol. Traffic 7: 917-926.
    • (2006) Traffic , vol.7 , pp. 917-926
    • Shvartsman, D.E.1    Gutman, O.2    Tietz, A.3    Henis4
  • 205
    • 39049110236 scopus 로고    scopus 로고
    • Measuring protein mobility by photobleaching GFP chimeras in living cells
    • Snapp EL, Altan N, Lippincott-Schwartz J. 2003. Measuring protein mobility by photobleaching GFP chimeras in living cells. Curr Protoc Cell Biol 21: 2121.
    • (2003) Curr Protoc Cell Biol , vol.21 , pp. 2121
    • Snapp, E.L.1    Altan, N.2    Lippincott-Schwartz, J.3
  • 206
    • 77449103109 scopus 로고    scopus 로고
    • A method for analyzing protein-protein interactions in the plasma membrane of live B cells by fluorescence resonance energy transfer imaging as acquired by total internal reflection fluorescence microscopy
    • Sohn HW, Tolar P, Brzostowski J, Pierce SK. 2010. A method for analyzing protein-protein interactions in the plasma membrane of live B cells by fluorescence resonance energy transfer imaging as acquired by total internal reflection fluorescence microscopy. Methods Mol Biol 591: 159-183.
    • (2010) Methods Mol Biol , vol.591 , pp. 159-183
    • Sohn, H.W.1    Tolar, P.2    Brzostowski, J.3    Pierce, S.K.4
  • 207
    • 0020568317 scopus 로고
    • Theoretical analysis of fluorescence photobleaching recovery experiments
    • Soumpasis DM. 1983. Theoretical analysis of fluorescence photobleaching recovery experiments. Biophysical J 41: 95-97.
    • (1983) Biophysical J , vol.41 , pp. 95-97
    • Soumpasis, D.M.1
  • 208
    • 70350674917 scopus 로고    scopus 로고
    • Live cell multicolor imaging of lipid droplets with a new dye, LD540
    • Spandl J, White DJ, Peychl J, Thiele C. 2009. Live cell multicolor imaging of lipid droplets with a new dye, LD540. Traffic 10: 1579-1584.
    • (2009) Traffic , vol.10 , pp. 1579-1584
    • Spandl, J.1    White, D.J.2    Peychl, J.3    Thiele, C.4
  • 209
    • 2942690158 scopus 로고    scopus 로고
    • Analysis of binding reactions by fluorescence recovery after photobleaching
    • Sprague BL, Pego RL, Stavreva DA, McNally JG. 2004. Analysis of binding reactions by fluorescence recovery after photobleaching. Biophys J 86: 3473-3495.
    • (2004) Biophys J , vol.86 , pp. 3473-3495
    • Sprague, B.L.1    Pego, R.L.2    Stavreva, D.A.3    McNally, J.G.4
  • 210
    • 13244291467 scopus 로고    scopus 로고
    • FRAP analysis of binding: Proper and fitting
    • Sprague BL, McNally JG. 2005. FRAP analysis of binding: Proper and fitting. Trends in Cell Biol 15: 84-91.
    • (2005) Trends in Cell Biol , vol.15 , pp. 84-91
    • Sprague, B.L.1    McNally, J.G.2
  • 211
    • 0242385390 scopus 로고    scopus 로고
    • Molecular simulation study of phospholipid bilayers and insights of the interactions with disaccharides
    • Sum AK, Faller R, de Pablo JJ. 2003. Molecular simulation study of phospholipid bilayers and insights of the interactions with disaccharides. Biophys J 85: 2830-2844.
    • (2003) Biophys J , vol.85 , pp. 2830-2844
    • Sum, A.K.1    Faller, R.2    de Pablo, J.J.3
  • 212
    • 33748939242 scopus 로고    scopus 로고
    • Single-molecule analysis of epidermal growth factor binding on the surface of living cells
    • Teramura Y, Ichinose J, Takagi H, Nishida K, Yanagida T, Sako Y. 2006. Single-molecule analysis of epidermal growth factor binding on the surface of living cells. EMBO J 25: 4215-4222.
    • (2006) EMBO J , vol.25 , pp. 4215-4222
    • Teramura, Y.1    Ichinose, J.2    Takagi, H.3    Nishida, K.4    Yanagida, T.5    Sako, Y.6
  • 213
    • 47149111389 scopus 로고    scopus 로고
    • Cell biology of lipid droplets
    • Thiele C, Spandl J. 2008. Cell biology of lipid droplets. Curr Opin Cell Biol 20: 378-385.
    • (2008) Curr Opin Cell Biol , vol.20 , pp. 378-385
    • Thiele, C.1    Spandl, J.2
  • 214
    • 0032563615 scopus 로고    scopus 로고
    • Regulation mechanism of the lateral diffusion of band 3 in erythrocyte membranes by the membrane skeleton
    • Tomishige M, Sako Y, Kusumi A. 1998. Regulation mechanism of the lateral diffusion of band 3 in erythrocyte membranes by the membrane skeleton. J Cell Biol 142: 989-1000.
    • (1998) J Cell Biol , vol.142 , pp. 989-1000
    • Tomishige, M.1    Sako, Y.2    Kusumi, A.3
  • 215
    • 34547611047 scopus 로고    scopus 로고
    • Threedimensional particle tracking via bifocal imaging
    • Toprak E, Balci H, Blehm BH, Selvin PR. 2007. Threedimensional particle tracking via bifocal imaging. Nano Lett 7: 2043-2045.
    • (2007) Nano Lett , vol.7 , pp. 2043-2045
    • Toprak, E.1    Balci, H.2    Blehm, B.H.3    Selvin, P.R.4
  • 219
    • 0032552054 scopus 로고    scopus 로고
    • GPI-anchored proteins are organized in submicron domains at the cell surface
    • Varma R, Mayor S. 1998. GPI-anchored proteins are organized in submicron domains at the cell surface. Nature 394: 798-801.
    • (1998) Nature , vol.394 , pp. 798-801
    • Varma, R.1    Mayor, S.2
  • 220
    • 12244270658 scopus 로고    scopus 로고
    • Organization in lipid membranes containing cholesterol
    • Veatch SL, Keller SL. 2002. Organization in lipid membranes containing cholesterol. Phys Rev Lett 89: 268101-268104.
    • (2002) Phys Rev Lett , vol.89 , pp. 268101-268104
    • Veatch, S.L.1    Keller, S.L.2
  • 221
    • 0242385346 scopus 로고    scopus 로고
    • Separation of liquid phases in giant vesicles of ternary mixtures of phospholipids and cholesterol
    • Veatch SL, Keller SL. 2003. Separation of liquid phases in giant vesicles of ternary mixtures of phospholipids and cholesterol. Biophys J 85: 3074-3083.
    • (2003) Biophys J , vol.85 , pp. 3074-3083
    • Veatch, S.L.1    Keller, S.L.2
  • 222
    • 0141867742 scopus 로고    scopus 로고
    • Oneand two-photon fluorescence resonance energy transfer microscopy to establish a clustered distribution of receptor-ligand complexes in endocytic membranes
    • Wallrabe H, Stanley M, Periasamy A, Barroso M. 2003. Oneand two-photon fluorescence resonance energy transfer microscopy to establish a clustered distribution of receptor-ligand complexes in endocytic membranes. J Biomed Opt 8: 339-346.
    • (2003) J Biomed Opt , vol.8 , pp. 339-346
    • Wallrabe, H.1    Stanley, M.2    Periasamy, A.3    Barroso, M.4
  • 223
    • 28444443820 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy diffusion laws to probe the submicron cell membrane organization
    • Wawrezinieck L, Rigneault H, Marguet D, Lenne PF. 2005. Fluorescence correlation spectroscopy diffusion laws to probe the submicron cell membrane organization. Biophys J 89: 4029-4042.
    • (2005) Biophys J , vol.89 , pp. 4029-4042
    • Wawrezinieck, L.1    Rigneault, H.2    Marguet, D.3    Lenne, P.F.4
  • 224
    • 0036106455 scopus 로고    scopus 로고
    • Analysis of ligand binding by two-colour fluorescence cross-correlation spectroscopy
    • Weidemann T, Wachsmuth M, Tewes M, Rippe K, Langowski J. 2002. Analysis of ligand binding by two-colour fluorescence cross-correlation spectroscopy. Single Mol 3: 49-61.
    • (2002) Single Mol , vol.3 , pp. 49-61
    • Weidemann, T.1    Wachsmuth, M.2    Tewes, M.3    Rippe, K.4    Langowski, J.5
  • 225
    • 4444279082 scopus 로고    scopus 로고
    • Challenges and artifacts in quantitative photobleaching experiments
    • Weiss M. 2004. Challenges and artifacts in quantitative photobleaching experiments. Traffic 5: 662-671.
    • (2004) Traffic , vol.5 , pp. 662-671
    • Weiss, M.1
  • 227
    • 0024489156 scopus 로고
    • Designing, building, and using a fluorescence recovery after photobleaching instrument
    • In, (ed. Taylor DL, Wang Y-L),. Academic Press, New York
    • Wolf DE. 1989. Designing, building, and using a fluorescence recovery after photobleaching instrument. In Methods in cell biology (ed. Taylor DL, Wang Y-L), pp. 271-332. Academic Press, New York.
    • (1989) Methods in cell biology , pp. 271-332
    • Wolf, D.E.1
  • 228
    • 78649668571 scopus 로고    scopus 로고
    • Focus on composition and interaction potential of single-pass transmembrane domains
    • Worch R, Bokel C, Hofinger S, Schwille P, Weidemann T. 2010. Focus on composition and interaction potential of single-pass transmembrane domains. Proteomics 10: 4196-4208.
    • (2010) Proteomics , vol.10 , pp. 4196-4208
    • Worch, R.1    Bokel, C.2    Hofinger, S.3    Schwille, P.4    Weidemann, T.5
  • 229
    • 0032535138 scopus 로고    scopus 로고
    • FRET microscopy demonstrates molecular association of non-specific lipid transfer protein (nsL-TP) with fatty acid oxidation enzymes in peroxisomes
    • Wouters FS, Bastiaens PIH, Wirtz KWA, Jovin TM. 1998. FRET microscopy demonstrates molecular association of non-specific lipid transfer protein (nsL-TP) with fatty acid oxidation enzymes in peroxisomes. EMBO J 17: 7179-7189.
    • (1998) EMBO J , vol.17 , pp. 7179-7189
    • Wouters, F.S.1    Bastiaens, P.I.H.2    Wirtz, K.W.A.3    Jovin, T.M.4
  • 230
    • 0037832404 scopus 로고    scopus 로고
    • Myosin V walks hand-over-hand: Single fluorophore imaging with 1.5-nm localization
    • Yildiz A, Forkey JN, McKinney SA, Ha T, Goldman YE, Selvin PR. 2003. Myosin V walks hand-over-hand: Single fluorophore imaging with 1.5-nm localization. Science 300: 2061-2065.
    • (2003) Science , vol.300 , pp. 2061-2065
    • Yildiz, A.1    Forkey, J.N.2    McKinney, S.A.3    Ha, T.4    Goldman, Y.E.5    Selvin, P.R.6
  • 231
    • 4444364789 scopus 로고    scopus 로고
    • Myosin VI steps via a handover-hand mechanism with its lever arm undergoing fluctuations when attached to actin
    • Yildiz A, Park H, Safer D, Yang ZH, Chen LQ, Selvin PR, Sweeney HL. 2004a. Myosin VI steps via a handover-hand mechanism with its lever arm undergoing fluctuations when attached to actin. J Biol Chem 279: 37223-37226.
    • (2004) J Biol Chem , vol.279 , pp. 37223-37226
    • Yildiz, A.1    Park, H.2    Safer, D.3    Yang, Z.H.4    Chen, L.Q.5    Selvin, P.R.6    Sweeney, H.L.7
  • 233
    • 57749186680 scopus 로고    scopus 로고
    • Receptor overexpression or inhibition alters cell surface dynamics of EGF-EGFR interaction: New insights from real-time single molecule analysis
    • Yu CX, Hale J, Ritchie K, Prasad NK, Irudayaraj J. 2009. Receptor overexpression or inhibition alters cell surface dynamics of EGF-EGFR interaction: New insights from real-time single molecule analysis. Biochem Biophys Res Commun 378: 376-382.
    • (2009) Biochem Biophys Res Commun , vol.378 , pp. 376-382
    • Yu, C.X.1    Hale, J.2    Ritchie, K.3    Prasad, N.K.4    Irudayaraj, J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.