메뉴 건너뛰기




Volumn 34, Issue , 2005, Pages 351-378

Paradigm shift of the plasma membrane concept from the two-dimensional continuum fluid to the partitioned fluid: High-speed single-molecule tracking of membrane molecules

Author keywords

Actin based membrane skeleton fence model; Anchored transmembrane protein pickets; Plasma membrane compartments; Single fluorescent molecule video imaging; Single particle tracking

Indexed keywords

ACTIN; MEMBRANE PROTEIN;

EID: 17844364513     PISSN: 10568700     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.biophys.34.040204.144637     Document Type: Review
Times cited : (986)

References (82)
  • 1
    • 0028838793 scopus 로고
    • Fluctuations and membrane heterogeneity
    • Abney JR, Scalettar BA. 1995. Fluctuations and membrane heterogeneity. Biophys. Chem. 57:27-36
    • (1995) Biophys. Chem. , vol.57 , pp. 27-36
    • Abney, J.R.1    Scalettar, B.A.2
  • 3
    • 0028343033 scopus 로고
    • Molecular organization and dynamics in bacteriorhodopsin-rich reconstituted membranes: Discrimination of lipid environments by the oxygen transport parameter using a pulse ESR spin-labeling technique
    • Ashikawa I, Yin JJ, Subczynski WK, Kouyama T, Hyde JS, Kusumi A. 1994. Molecular organization and dynamics in bacteriorhodopsin-rich reconstituted membranes: discrimination of lipid environments by the oxygen transport parameter using a pulse ESR spin-labeling technique. Biochemistry 33:4947-52
    • (1994) Biochemistry , vol.33 , pp. 4947-4952
    • Ashikawa, I.1    Yin, J.J.2    Subczynski, W.K.3    Kouyama, T.4    Hyde, J.S.5    Kusumi, A.6
  • 4
    • 0007856922 scopus 로고
    • Lateral motion of fluorescently labeled acetylcholine receptors in membranes of developing muscle fibers
    • Axelrod D, Ravdin P, Koppel DE, Schlessinger J, Webb WW, et al. 1976. Lateral motion of fluorescently labeled acetylcholine receptors in membranes of developing muscle fibers. Proc. Natl. Acad. Sci. USA 73:4594-98
    • (1976) Proc. Natl. Acad. Sci. USA , vol.73 , pp. 4594-4598
    • Axelrod, D.1    Ravdin, P.2    Koppel, D.E.3    Schlessinger, J.4    Webb, W.W.5
  • 5
    • 0028160276 scopus 로고
    • The effect of hydrodynamic interactions on the tracer and gradient diffusion of integral membrane-proteins in lipid bilayers
    • Bussell SJ, Hammer DA, Koch DL. 1994. The effect of hydrodynamic interactions on the tracer and gradient diffusion of integral membrane-proteins in lipid bilayers. J. Fluid Mech. 258:167-90
    • (1994) J. Fluid Mech. , vol.258 , pp. 167-190
    • Bussell, S.J.1    Hammer, D.A.2    Koch, D.L.3
  • 6
    • 0028901482 scopus 로고
    • Effect of hydrodynamic interactions on the diffusion of integral membrane proteins: Diffusion in plasma membranes
    • Bussell SJ, Koch DL, Hammer DA. 1995. Effect of hydrodynamic interactions on the diffusion of integral membrane proteins: diffusion in plasma membranes. Biophys. J. 68:1836-49
    • (1995) Biophys. J. , vol.68 , pp. 1836-1849
    • Bussell, S.J.1    Koch, D.L.2    Hammer, D.A.3
  • 7
    • 0019631401 scopus 로고
    • Lateral mobility of erythrocyte membrane proteins studied by the fluorescence photobleaching recovery technique
    • Chang CH, Takeuchi H, Ito T, Machida K, Ohnishi S. 1981. Lateral mobility of erythrocyte membrane proteins studied by the fluorescence photobleaching recovery technique. J. Biochem. 90:997-1004
    • (1981) J. Biochem. , vol.90 , pp. 997-1004
    • Chang, C.H.1    Takeuchi, H.2    Ito, T.3    Machida, K.4    Ohnishi, S.5
  • 8
    • 0022400414 scopus 로고
    • Probing microtubule-dependent intracellular motility with nanometre particle video ultramicroscopy (nanovid ultramicroscopy)
    • De Brabander M, Geuens G, Nuydens R, Moeremans M, De Mey J. 1985. Probing microtubule-dependent intracellular motility with nanometre particle video ultramicroscopy (nanovid ultramicroscopy). Cytobios 43:273-83
    • (1985) Cytobios , vol.43 , pp. 273-283
    • De Brabander, M.1    Geuens, G.2    Nuydens, R.3    Moeremans, M.4    De Mey, J.5
  • 9
    • 0023745656 scopus 로고
    • Dynamic behavior of the transferrin receptor followed in living epidermoid carcinoma (A431) cells with nanovid microscopy
    • De Brabander M, Nuydens R, Geerts H, Hopkins CR. 1988. Dynamic behavior of the transferrin receptor followed in living epidermoid carcinoma (A431) cells with nanovid microscopy. Cell Motil. Cytoskelet. 9:30-47
    • (1988) Cell Motil. Cytoskelet. , vol.9 , pp. 30-47
    • De Brabander, M.1    Nuydens, R.2    Geerts, H.3    Hopkins, C.R.4
  • 10
    • 0026053736 scopus 로고
    • Lateral diffusion and retrograde movements of individual cell surface components on single motile cells observed with nanovid microscopy
    • De Brabander 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. 112:111-24
    • (1991) J. Cell. Biol. , vol.112 , pp. 111-124
    • De Brabander, M.1    Nuydens, R.2    Ishihara, A.3    Holifield, B.4    Jacobson, K.5    Geerts, H.6
  • 12
    • 0035845497 scopus 로고    scopus 로고
    • Partitioning of Thy-1, GM1, and cross-linked phospholipid analogs into lipid rafts reconstituted in supported model membrane monolayers
    • Dietrich C, Volovyk ZN, Levi M, Thompson NL, Jacobson K. 2001. Partitioning of Thy-1, GM1, and cross-linked phospholipid analogs into lipid rafts reconstituted in supported model membrane monolayers. Proc. Natl. Acad. Sci. USA 98:10642-47
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 10642-10647
    • Dietrich, C.1    Volovyk, Z.N.2    Levi, M.3    Thompson, N.L.4    Jacobson, K.5
  • 13
    • 0026320864 scopus 로고
    • Lateral movements of membrane glycoproteins restricted by dynamic cytoplasmic barriers
    • Edidin M, Kuo SC, Sheetz MP. 1991. Lateral movements of membrane glycoproteins restricted by dynamic cytoplasmic barriers. Science 254:1379-82
    • (1991) Science , vol.254 , pp. 1379-1382
    • Edidin, M.1    Kuo, S.C.2    Sheetz, M.P.3
  • 14
    • 0028325756 scopus 로고
    • Truncation mutants define and locate cytoplasmic barriers to lateral mobility of membrane glycoproteins
    • Edidin M, Zuniga MC, Sheetz MP. 1994. Truncation mutants define and locate cytoplasmic barriers to lateral mobility of membrane glycoproteins. Proc. Natl. Acad. Sci. USA 91:3378-82
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 3378-3382
    • Edidin, M.1    Zuniga, M.C.2    Sheetz, M.P.3
  • 15
    • 0030611604 scopus 로고    scopus 로고
    • Integrin alphaIIb beta3 reconstituted into lipid bilayers is nonclustered in its activated state but clusters after fibrinogen binding
    • Erb EM, Tangemann K, Bohrmann B, Muller B, Engel J. 1997. Integrin alphaIIb beta3 reconstituted into lipid bilayers is nonclustered in its activated state but clusters after fibrinogen binding. Biochemistry 36:7395-402
    • (1997) Biochemistry , vol.36 , pp. 7395-7402
    • Erb, E.M.1    Tangemann, K.2    Bohrmann, B.3    Muller, B.4    Engel, J.5
  • 16
    • 4143057045 scopus 로고    scopus 로고
    • Endocytotic elimination and domain-selective tethering constitute a potential mechanism of protein segregation at the axonal initial segment
    • Fache MP, Moussif A, Fernandes F, Giraud P, Garrido JJ, Dargent B. 2004. Endocytotic elimination and domain-selective tethering constitute a potential mechanism of protein segregation at the axonal initial segment. J. Cell Biol. 166:571-78
    • (2004) J. Cell Biol. , vol.166 , pp. 571-578
    • Fache, M.P.1    Moussif, A.2    Fernandes, F.3    Giraud, P.4    Garrido, J.J.5    Dargent, B.6
  • 17
    • 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. 70:2767-73
    • (1996) Biophys. 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
  • 19
    • 0023871621 scopus 로고
    • Tracking kinesin-driven movements with nanometre-scale precision
    • Gelles J, Schnapp BJ, Sheetz MP. 1988. Tracking kinesin-driven movements with nanometre-scale precision. Nature 331:450-53
    • (1988) Nature , vol.331 , pp. 450-453
    • Gelles, J.1    Schnapp, B.J.2    Sheetz, M.P.3
  • 20
    • 0022999198 scopus 로고
    • Schistosomula of Schistosoma mansoni use lysophosphatidylcholine to lyse adherent human red blood cells and immobilize red cell membrane components
    • Golan DE, Brown CS, Cianci CM, Furlong ST, Caulfield JP. 1986. Schistosomula of Schistosoma mansoni use lysophosphatidylcholine to lyse adherent human red blood cells and immobilize red cell membrane components. J. Cell Biol. 103:819-28
    • (1986) J. Cell Biol. , vol.103 , pp. 819-828
    • Golan, D.E.1    Brown, C.S.2    Cianci, C.M.3    Furlong, S.T.4    Caulfield, J.P.5
  • 21
    • 0019190475 scopus 로고
    • Lateral mobility of band 3 in the human erythrocyte membrane studied by fluorescence photobleaching recovery: Evidence for control by cytoskeletal interactions
    • Golan DE, Veatch W. 1980. Lateral mobility of band 3 in the human erythrocyte membrane studied by fluorescence photobleaching recovery: evidence for control by cytoskeletal interactions. Proc. Natl. Acad. Sci. USA 77:2537-41
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 2537-2541
    • Golan, D.E.1    Veatch, W.2
  • 23
    • 0034995774 scopus 로고    scopus 로고
    • Single molecule imaging of green fluorescent proteins in living cells: E-cadherin forms oligomers on the free cell surface
    • Iino R, Koyama I, Kusumi A. 2001. Single molecule imaging of green fluorescent proteins in living cells: E-cadherin forms oligomers on the free cell surface. Biophys. J. 80:2667-77
    • (2001) Biophys. J. , vol.80 , pp. 2667-2677
    • Iino, R.1    Koyama, I.2    Kusumi, A.3
  • 25
    • 0021401320 scopus 로고
    • Lateral diffusion of lipids and glycophorin in solid phosphatidylcholine bilayers. The role of structural defects
    • Kapitza HG, Ruppel DA, Galla HJ, Sackmann E. 1984. Lateral diffusion of lipids and glycophorin in solid phosphatidylcholine bilayers. The role of structural defects. Biophys. J. 45:577-87
    • (1984) Biophys. J. , vol.45 , pp. 577-587
    • Kapitza, H.G.1    Ruppel, D.A.2    Galla, H.J.3    Sackmann, E.4
  • 27
    • 0024375302 scopus 로고
    • Forward transport of glycoproteins on leading lamellipodia in locomoting cells
    • Kucik DF, Elson EL, Sheetz MP. 1989. Forward transport of glycoproteins on leading lamellipodia in locomoting cells. Nature 340:315-17
    • (1989) Nature , vol.340 , pp. 315-317
    • Kucik, D.F.1    Elson, E.L.2    Sheetz, M.P.3
  • 28
    • 0020455954 scopus 로고
    • Spin-label saturation-transfer electron spin resonance detection of transient association of rhodopsin in reconstituted membranes
    • Kusumi A, Hyde JS. 1982. Spin-label saturation-transfer electron spin resonance detection of transient association of rhodopsin in reconstituted membranes. Biochemistry 21:5978-83
    • (1982) Biochemistry , vol.21 , pp. 5978-5983
    • Kusumi, A.1    Hyde, J.S.2
  • 29
    • 20544464040 scopus 로고    scopus 로고
    • Single-molecule imaging of diffusion, recruitment, and activation of signaling molecules in living cells
    • ed. S Damjanovich. Heidelberg: Springer-Verlag. In press
    • Kusumi A, Murakoshi H, Murase K, Fujiwara T. 2005. Single-molecule imaging of diffusion, recruitment, and activation of signaling molecules in living cells. In Biophysical Aspects of Transmembrane Signaling, ed. S Damjanovich. Heidelberg: Springer-Verlag. In press
    • (2005) Biophysical Aspects of Transmembrane Signaling
    • Kusumi, A.1    Murakoshi, H.2    Murase, K.3    Fujiwara, T.4
  • 30
    • 0030222116 scopus 로고    scopus 로고
    • Cell surface organization by the membrane skeleton
    • Kusumi A, Sako Y. 1996. Cell surface organization by the membrane skeleton. Curr. Opin. Cell. Biol. 8:566-74
    • (1996) Curr. Opin. Cell. Biol. , vol.8 , pp. 566-574
    • Kusumi, A.1    Sako, Y.2
  • 31
    • 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. 65:2021-40
    • (1993) Biophys. J. , vol.65 , pp. 2021-2040
    • Kusumi, A.1    Sako, Y.2    Yamamoto, M.3
  • 32
    • 0345564815 scopus 로고    scopus 로고
    • Membrane cholesterol, lateral mobility, and the phosphatidylinositol 4,5-bisphosphate-dependent organization of cell actin
    • Kwik J, Boyle S, Fooksman D, Margolis L, Sheetz MP, Edidin M. 2003. Membrane cholesterol, lateral mobility, and the phosphatidylinositol 4,5-bisphosphate-dependent organization of cell actin. Proc. Natl. Acad. Sci. USA 100: 13964-69
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 13964-13969
    • Kwik, J.1    Boyle, S.2    Fooksman, D.3    Margolis, L.4    Sheetz, M.P.5    Edidin, M.6
  • 33
    • 0027392157 scopus 로고
    • Unconfined lateral diffusion and an estimate of pericellular matrix viscosity revealed by measuring the mobility of gold-tagged lipids
    • Lee GM, Zhang F, Ishihara A, McNeil CL, Jacobson KA. 1993. Unconfined lateral diffusion and an estimate of pericellular matrix viscosity revealed by measuring the mobility of gold-tagged lipids. J. Cell. Biol. 120:25-35
    • (1993) J. Cell. Biol. , vol.120 , pp. 25-35
    • Lee, G.M.1    Zhang, F.2    Ishihara, A.3    McNeil, C.L.4    Jacobson, K.A.5
  • 35
    • 2942662120 scopus 로고    scopus 로고
    • Ultrafine membrane compartments for molecular diffusion as revealed by single molecule techniques
    • Murase K, Fujiwara T, Umemura Y, Suzuki K, Iino R, et al. 2004. Ultrafine membrane compartments for molecular diffusion as revealed by single molecule techniques. Biophys. J. 86:4075-93
    • (2004) Biophys. J. , vol.86 , pp. 4075-4093
    • Murase, K.1    Fujiwara, T.2    Umemura, Y.3    Suzuki, K.4    Iino, R.5
  • 36
    • 0026783791 scopus 로고
    • Long tail kinetics in biophysics?
    • Nagle JF. 1992. Long tail kinetics in biophysics? Biophys. J. 63:366-70
    • (1992) Biophys. J. , vol.63 , pp. 366-370
    • Nagle, J.F.1
  • 37
    • 0038726090 scopus 로고    scopus 로고
    • Accumulation of anchored proteins forms membrane diffusion barriers during neuronal polarization
    • Nakada C, Ritchie K, Oba Y, Nakamura M, Hotta Y, et al. 2003. Accumulation of anchored proteins forms membrane diffusion barriers during neuronal polarization. Nat. Cell. Biol. 5:626-32
    • (2003) Nat. Cell. Biol. , vol.5 , pp. 626-632
    • Nakada, C.1    Ritchie, K.2    Oba, Y.3    Nakamura, M.4    Hotta, Y.5
  • 38
    • 0032961873 scopus 로고    scopus 로고
    • Characterization of an intrinsically fluorescent gonadotropin-releasing hormone receptor and effects of ligand binding on receptor lateral diffusion
    • Nelson S, Horvat RD, Malvey J, Roess DA, Barisas BG, Clay CM. 1999. Characterization of an intrinsically fluorescent gonadotropin-releasing hormone receptor and effects of ligand binding on receptor lateral diffusion. Endocrinology 140:950-57
    • (1999) Endocrinology , vol.140 , pp. 950-957
    • Nelson, S.1    Horvat, R.D.2    Malvey, J.3    Roess, D.A.4    Barisas, B.G.5    Clay, C.M.6
  • 39
    • 0028110178 scopus 로고
    • Lateral mobility of Na,K-ATPase and membrane lipids in renal cells. Importance of cytoskeletal integrity
    • Paller MS. 1994. Lateral mobility of Na,K-ATPase and membrane lipids in renal cells. Importance of cytoskeletal integrity. J. Membr. Biol. 142:127-35
    • (1994) J. Membr. Biol. , vol.142 , pp. 127-135
    • Paller, M.S.1
  • 40
    • 0025931149 scopus 로고
    • Influence of phospholipid unsaturation on the cholesterol distribution in membranes
    • Pasenkiewicz-Gierula M, Subczynski WK, Kusumi A. 1991. Influence of phospholipid unsaturation on the cholesterol distribution in membranes. Biochimie 73:1311-16
    • (1991) Biochimie , vol.73 , pp. 1311-1316
    • Pasenkiewicz-Gierula, M.1    Subczynski, W.K.2    Kusumi, A.3
  • 41
    • 0012050693 scopus 로고
    • Lateral and rotational diffusion of bacteriorhodopsin in lipid bilayers: Experimental test of the Saffman-Delbrück equations
    • Peters R, Cherry RJ. 1982. Lateral and rotational diffusion of bacteriorhodopsin in lipid bilayers: experimental test of the Saffman-Delbrück equations. Proc. Natl. Acad. Sci. USA 79:4317-21
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 4317-4321
    • Peters, R.1    Cherry, R.J.2
  • 42
    • 0000895333 scopus 로고
    • Exact analytic solutions for diffusion impeded by an infinite array of partially permeable barriers
    • Powles GJ, Mallett MJD, Rickayzen G, Evans WAB. 1992. Exact analytic solutions for diffusion impeded by an infinite array of partially permeable barriers. Proc. R. Soc. London A 436:391-403
    • (1992) Proc. R. Soc. London A , vol.436 , pp. 391-403
    • Powles, G.J.1    Mallett, M.J.D.2    Rickayzen, G.3    Evans, W.A.B.4
  • 43
    • 0025997180 scopus 로고
    • Single particle tracking. Analysis of diffusion and flow in two-dimensional systems
    • Qian H, Sheetz MP, Elson EL. 1991. Single particle tracking. Analysis of diffusion and flow in two-dimensional systems. Biophys. J. 60:910-21
    • (1991) Biophys. J. , vol.60 , pp. 910-921
    • Qian, H.1    Sheetz, M.P.2    Elson, E.L.3
  • 44
    • 0034522937 scopus 로고    scopus 로고
    • Luteinizing hormone receptors are self-associated in the plasma membrane
    • Roess DA, Horvat RD, Munnelly H, Barisas BG. 2000. Luteinizing hormone receptors are self-associated in the plasma membrane. Endocrinology 141:4518-23
    • (2000) Endocrinology , vol.141 , pp. 4518-4523
    • Roess, D.A.1    Horvat, R.D.2    Munnelly, H.3    Barisas, B.G.4
  • 46
    • 0028243194 scopus 로고
    • Compartmentalized structure of the plasma membrane for receptor movements as revealed by a nanometer-level motion analysis
    • Sako Y, Kusumi A. 1994. Compartmentalized structure of the plasma membrane for receptor movements as revealed by a nanometer-level motion analysis. J. Cell. Biol. 125:1251-64
    • (1994) J. Cell. Biol. , vol.125 , pp. 1251-1264
    • Sako, Y.1    Kusumi, A.2
  • 47
    • 0029014265 scopus 로고
    • Barriers for lateral diffusion of transferrin receptor in the plasma membrane as characterized by receptor dragging by laser tweezers: Fence versus tether
    • Sako Y, Kusumi A. 1995. Barriers for lateral diffusion of transferrin receptor in the plasma membrane as characterized by receptor dragging by laser tweezers: fence versus tether. J. Cell. Biol. 129:1559-74
    • (1995) J. Cell. Biol. , vol.129 , pp. 1559-1574
    • Sako, Y.1    Kusumi, A.2
  • 48
    • 0032498847 scopus 로고    scopus 로고
    • Cytoplasmic regulation of the movement of E-cadherin on the free cell surface as studied by optical tweezers and single particle tracking: Corralling and tethering by the membrane skeleton
    • Sako Y, Nagafuchi A, Tsukita S, Takeichi M, Kusumi A. 1998. Cytoplasmic regulation of the movement of E-cadherin on the free cell surface as studied by optical tweezers and single particle tracking: corralling and tethering by the membrane skeleton. J. Cell. Biol. 140:1227-40
    • (1998) J. Cell. Biol. , vol.140 , pp. 1227-1240
    • Sako, Y.1    Nagafuchi, A.2    Tsukita, S.3    Takeichi, M.4    Kusumi, A.5
  • 49
    • 0020174113 scopus 로고
    • Lateral diffusion in an archipelago. Effects of impermeable patches on diffusion in a cell membrane
    • Saxton MJ. 1982. Lateral diffusion in an archipelago. Effects of impermeable patches on diffusion in a cell membrane. Biophys. J. 39:165-73
    • (1982) Biophys. J. , vol.39 , pp. 165-173
    • Saxton, M.J.1
  • 50
    • 0023492928 scopus 로고
    • Lateral diffusion in an archipelago. The effect of mobile obstacles
    • Saxton MJ. 1987. Lateral diffusion in an archipelago. The effect of mobile obstacles. Biophys. J. 52:989-97
    • (1987) Biophys. J. , vol.52 , pp. 989-997
    • Saxton, M.J.1
  • 51
    • 0024723988 scopus 로고
    • Lateral diffusion in an archipelago. Distance dependence of the diffusion coefficient
    • Saxton MJ. 1989. Lateral diffusion in an archipelago. Distance dependence of the diffusion coefficient. Biophys. J. 56:615-22
    • (1989) Biophys. J. , vol.56 , pp. 615-622
    • Saxton, M.J.1
  • 52
    • 0024596077 scopus 로고
    • The spectrin network as a barrier to lateral diffusion in erythrocytes. A percolation analysis
    • Saxton MJ. 1989. The spectrin network as a barrier to lateral diffusion in erythrocytes. A percolation analysis. Biophys. J. 55:21-28
    • (1989) Biophys. J. , vol.55 , pp. 21-28
    • Saxton, M.J.1
  • 53
    • 0025325763 scopus 로고
    • The membrane skeleton of erythrocytes. A percolation model
    • Saxton MJ. 1990. The membrane skeleton of erythrocytes. A percolation model. Biophys. J. 57:1167-77
    • (1990) Biophys. J. , vol.57 , pp. 1167-1177
    • Saxton, M.J.1
  • 54
    • 0028140412 scopus 로고
    • Anomalous diffusion due to obstacles: A Monte Carlo study
    • Saxton MJ. 1994. 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
  • 55
    • 0028170954 scopus 로고
    • Single-particle tracking: Models of directed transport
    • Saxton MJ. 1994. Single-particle tracking: models of directed transport. Biophys. J. 67:2110-19
    • (1994) Biophys. J. , vol.67 , pp. 2110-2119
    • Saxton, M.J.1
  • 56
    • 0029163176 scopus 로고
    • Single-particle tracking: Effects of corrals
    • Saxton MJ. 1995. Single-particle tracking: effects of corrals. Biophys. J. 69:389-98
    • (1995) Biophys. J. , vol.69 , pp. 389-398
    • Saxton, M.J.1
  • 57
    • 0030050141 scopus 로고    scopus 로고
    • Anomalous diffusion due to binding: A Monte Carlo study
    • Saxton MJ. 1996. Anomalous diffusion due to binding: a Monte Carlo study. Biophys. J. 70:1250-62
    • (1996) Biophys. J. , vol.70 , pp. 1250-1262
    • Saxton, M.J.1
  • 58
    • 0034805503 scopus 로고    scopus 로고
    • Anomalous subdiffusion in fluorescence photobleaching recovery: A Monte Carlo study
    • Saxton MJ. 2001. Anomalous subdiffusion in fluorescence photobleaching recovery: a Monte Carlo study. Biophys. J. 81:2226-40
    • (2001) Biophys. J. , vol.81 , pp. 2226-2240
    • Saxton, M.J.1
  • 59
  • 60
    • 2642575982 scopus 로고    scopus 로고
    • A barrier to lateral diffusion in the cleavage furrow of dividing mammalian cells
    • Schmidt K, Nichols BJ. 2004. A barrier to lateral diffusion in the cleavage furrow of dividing mammalian cells. Curr. Biol. 14:1002-6
    • (2004) Curr. Biol. , vol.14 , pp. 1002-1006
    • Schmidt, K.1    Nichols, B.J.2
  • 62
    • 0030863490 scopus 로고    scopus 로고
    • Transient confinement of a glycosylphosphatidylinositol-anchored protein in the plasma membrane
    • Sheets ED, Lee GM, Simson R, Jacobson K. 1997. Transient confinement of a glycosylphosphatidylinositol-anchored protein in the plasma membrane. Biochemistry 36:12449-58
    • (1997) Biochemistry , vol.36 , pp. 12449-12458
    • Sheets, E.D.1    Lee, G.M.2    Simson, R.3    Jacobson, K.4
  • 63
    • 0020790863 scopus 로고
    • Membrane skeletal dynamics-role in modulation of red-cell deformability, mobility of transmembrane proteins, and shape
    • Sheetz MP. 1983. Membrane skeletal dynamics-role in modulation of red-cell deformability, mobility of transmembrane proteins, and shape. Semin. Hematol. 20:175-88
    • (1983) Semin. Hematol. , vol.20 , pp. 175-188
    • Sheetz, M.P.1
  • 64
    • 0027232839 scopus 로고
    • Glycoprotein motility and dynamic domains in fluid plasma membranes
    • Sheetz MP. 1993. Glycoprotein motility and dynamic domains in fluid plasma membranes. Annu. Rev. Biophys. Biomol. Struct. 22:417-31
    • (1993) Annu. Rev. Biophys. Biomol. Struct. , vol.22 , pp. 417-431
    • Sheetz, M.P.1
  • 65
    • 0019304034 scopus 로고
    • Lateral mobility of integral membrane proteins is increased in spherocytic erythrocytes
    • Sheetz MP, Schindler M, Koppel DE. 1980. Lateral mobility of integral membrane proteins is increased in spherocytic erythrocytes. Nature 285:510-11
    • (1980) Nature , vol.285 , pp. 510-511
    • Sheetz, M.P.1    Schindler, M.2    Koppel, D.E.3
  • 66
    • 0024338987 scopus 로고
    • Nanometre-level analysis demonstrates that lipid flow does not drive membrane glycoprotein movements
    • Sheetz MP, Turney S, Qian H, Elson EL. 1989. Nanometre-level analysis demonstrates that lipid flow does not drive membrane glycoprotein movements. Nature 340:284-88
    • (1989) Nature , vol.340 , pp. 284-288
    • Sheetz, M.P.1    Turney, S.2    Qian, H.3    Elson, E.L.4
  • 67
    • 0345599000 scopus 로고    scopus 로고
    • Differently anchored influenza hemagglutinin mutants display distinct interaction dynamics with mutual rafts
    • Shvartsman DE, Kotler M, Tall RD, Roth MG, Henis YI. 2003. Differently anchored influenza hemagglutinin mutants display distinct interaction dynamics with mutual rafts. J. Cell Biol. 163:879-88
    • (2003) J. Cell Biol. , vol.163 , pp. 879-888
    • Shvartsman, D.E.1    Kotler, M.2    Tall, R.D.3    Roth, M.G.4    Henis, Y.I.5
  • 69
    • 0015514472 scopus 로고
    • The fluid mosaic model of the structure of cell membranes
    • Singer SJ, Nicolson GL. 1972. The fluid mosaic model of the structure of cell membranes. Science 175:720-31
    • (1972) Science , vol.175 , pp. 720-731
    • Singer, S.J.1    Nicolson, G.L.2
  • 70
    • 0034805172 scopus 로고    scopus 로고
    • Binding of cross-linked glycosylphosphatidylinositol-anchored proteins to discrete actin-associated sites and cholesterol-dependent domains
    • Suzuki K, Sheetz MP. 2001. Binding of cross-linked glycosylphosphatidylinositol-anchored proteins to discrete actin-associated sites and cholesterol-dependent domains. Biophys. J. 81:2181-89
    • (2001) Biophys. J. , vol.81 , pp. 2181-2189
    • Suzuki, K.1    Sheetz, M.P.2
  • 71
    • 0031958201 scopus 로고    scopus 로고
    • Structure of the erythrocyte membrane skeleton as observed by atomic force microscopy
    • Takeuchi M, Miyamoto H, Sako Y, Komizu H, Kusumi A. 1998. Structure of the erythrocyte membrane skeleton as observed by atomic force microscopy. Biophys. J. 74:2171-83
    • (1998) Biophys. J. , vol.74 , pp. 2171-2183
    • Takeuchi, M.1    Miyamoto, H.2    Sako, Y.3    Komizu, H.4    Kusumi, A.5
  • 72
    • 0020401953 scopus 로고
    • Lateral diffusion of gramicidin C in phospholipid multibilayers. Effects of cholesterol and high gramicidin concentration
    • Tank DW, Wu ES, Meers PR, Webb WW. 1982. Lateral diffusion of gramicidin C in phospholipid multibilayers. Effects of cholesterol and high gramicidin concentration. Biophys. J. 40:129-35
    • (1982) Biophys. J. , vol.40 , pp. 129-135
    • Tank, D.W.1    Wu, E.S.2    Meers, P.R.3    Webb, W.W.4
  • 73
    • 0020029509 scopus 로고
    • Enhanced molecular diffusibility in muscle membrane blebs: Release of lateral constraints
    • Tank DW, Wu ES, Webb WW. 1982. Enhanced molecular diffusibility in muscle membrane blebs: release of lateral constraints. J. Cell. Biol. 92:207-12
    • (1982) J. Cell. Biol. , vol.92 , pp. 207-212
    • Tank, D.W.1    Wu, E.S.2    Webb, W.W.3
  • 74
    • 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
  • 75
    • 0023688017 scopus 로고
    • Regulation of band 3 mobilities in erythrocyte ghost membranes by protein association and cytoskeletal mesh-work
    • Tsuji A, Kawasaki K, Ohnishi S, Merkle H, Kusumi A. 1988. Regulation of band 3 mobilities in erythrocyte ghost membranes by protein association and cytoskeletal mesh-work. Biochemistry 27:7447-52
    • (1988) Biochemistry , vol.27 , pp. 7447-7452
    • Tsuji, A.1    Kawasaki, K.2    Ohnishi, S.3    Merkle, H.4    Kusumi, A.5
  • 76
    • 0022966969 scopus 로고
    • Restriction of the lateral motion of band 3 in the erythrocyte membrane by the cytoskeletal network: Dependence on spectrin association state
    • Tsuji A, Ohnishi S. 1986. Restriction of the lateral motion of band 3 in the erythrocyte membrane by the cytoskeletal network: dependence on spectrin association state. Biochemistry 25:6133-39
    • (1986) Biochemistry , vol.25 , pp. 6133-6139
    • Tsuji, A.1    Ohnishi, S.2
  • 77
    • 0020491932 scopus 로고
    • Size dependence of the translational diffusion of large integral membrane proteins in liquid-crystalline phase lipid bilayers. A study using fluorescence recovery after photobleaching
    • Vaz WL, Criado M, Madeira VM, Schoellmann G, Jovin TM. 1982. Size dependence of the translational diffusion of large integral membrane proteins in liquid-crystalline phase lipid bilayers. A study using fluorescence recovery after photobleaching. Biochemistry 21:5608-12
    • (1982) Biochemistry , vol.21 , pp. 5608-5612
    • Vaz, W.L.1    Criado, M.2    Madeira, V.M.3    Schoellmann, G.4    Jovin, T.M.5
  • 78
    • 0019871853 scopus 로고
    • Translational mobility of glycophorin in bilayer membranes of dimyristoylphosphatidylcholine
    • Vaz WL, Kapitza HG, Stumpel J, Sackmann E, Jovin TM. 1981. Translational mobility of glycophorin in bilayer membranes of dimyristoylphosphatidylcholine. Biochemistry 20:1392-96
    • (1981) Biochemistry , vol.20 , pp. 1392-1396
    • Vaz, W.L.1    Kapitza, H.G.2    Stumpel, J.3    Sackmann, E.4    Jovin, T.M.5
  • 80
    • 0016862420 scopus 로고
    • Cholesterol is excluded from the phospholipid annulus surrounding an active calcium transport protein
    • Warren GB, Houslay MD, Metcalfe JC, Birdsall NJ. 1975. Cholesterol is excluded from the phospholipid annulus surrounding an active calcium transport protein. Nature 255:684-87
    • (1975) Nature , vol.255 , pp. 684-687
    • Warren, G.B.1    Houslay, M.D.2    Metcalfe, J.C.3    Birdsall, N.J.4
  • 81
    • 0020171652 scopus 로고
    • Unconstrained lateral diffusion of concanavalin a receptors on bulbous lymphocytes
    • Wu ES, Tank DW, Webb WW. 1982. Unconstrained lateral diffusion of concanavalin A receptors on bulbous lymphocytes. Proc. Natl. Acad. Sci. USA 79:4962-66
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 4962-4966
    • Wu, E.S.1    Tank, D.W.2    Webb, W.W.3
  • 82
    • 0026076574 scopus 로고
    • Lateral diffusion of membrane-spanning and glycosylphosphatidylinositol- linked proteins: Toward establishing rules governing the lateral mobility of membrane proteins
    • Zhang F, Crise B, Su B, Hou Y, Rose JK, et al. 1991. Lateral diffusion of membrane-spanning and glycosylphosphatidylinositol-linked proteins: toward establishing rules governing the lateral mobility of membrane proteins. J. Cell Biol. 115:75-84
    • (1991) J. Cell Biol. , vol.115 , pp. 75-84
    • Zhang, F.1    Crise, B.2    Su, B.3    Hou, Y.4    Rose, J.K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.