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Volumn 76, Issue 6, 1999, Pages 3331-3344

Anomalous diffusion of major histocompatibility complex class I molecules on HeLa cells determined by single particle tracking

Author keywords

[No Author keywords available]

Indexed keywords

IMMUNOGLOBULIN F(AB) FRAGMENT; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; MICROSPHERE; MONOCLONAL ANTIBODY;

EID: 0032998181     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(99)77486-2     Document Type: Article
Times cited : (162)

References (73)
  • 1
    • 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 4°C
    • Anderson, C. M., G. N. Georgiou, I. E. G. Morrison, G. V. W. Stevenson, and R. J. Cherry. 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 4°C. 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
  • 2
    • 0030566759 scopus 로고    scopus 로고
    • A photobleaching energy transfer analysis of CD8/MHC-I and LFA-1/ CAM-1 interaction in CTL-target cell conjugates
    • Bacsó, Z., L. Bene, A. Bodnár, J. Matkó, and S. Damjanovich. 1996. A photobleaching energy transfer analysis of CD8/MHC-I and LFA-1/ CAM-1 interaction in CTL-target cell conjugates. Immunol. Lett. 54: 151-156.
    • (1996) Immunol. Lett. , vol.54 , pp. 151-156
    • Bacsó, Z.1    Bene, L.2    Bodnár, A.3    Matkó, J.4    Damjanovich, S.5
  • 5
    • 0030566663 scopus 로고    scopus 로고
    • Modification of membrane cholesterol level affects expression and clustering of class I HLA molecules at the surface of JY lymphoblasts
    • Bodnár, A., A. Jenei, L. Bene, S. Damjanovich, and J. Matkó. 1996. Modification of membrane cholesterol level affects expression and clustering of class I HLA molecules at the surface of JY lymphoblasts. Immunol Lett. 54:221-226.
    • (1996) Immunol Lett. , vol.54 , pp. 221-226
    • Bodnár, A.1    Jenei, A.2    Bene, L.3    Damjanovich, S.4    Matkó, J.5
  • 6
    • 0026694442 scopus 로고
    • Intramembrane helix-helix association in oligomerisation and transmembrane signaling
    • Bormann, B. J., and D. M. Engelman. 1992. Intramembrane helix-helix association in oligomerisation and transmembrane signaling. Annu. Rev. Biophys. Biomol. Struct. 21:223-242.
    • (1992) Annu. Rev. Biophys. Biomol. Struct. , vol.21 , pp. 223-242
    • Bormann, B.J.1    Engelman, D.M.2
  • 7
    • 0003468328 scopus 로고
    • The physical mechanisms of anomalous diffusion
    • E. Guyon, J.-P. Nadal, and Y. Pomeau, editors. Kluwer Academic Publishers, Dordrecht, the Netherlands
    • Bouchaud, J.-P. A., and A. Georges. 1988. The physical mechanisms of anomalous diffusion. In Disorder and Mixing. E. Guyon, J.-P. Nadal, and Y. Pomeau, editors. Kluwer Academic Publishers, Dordrecht, the Netherlands. 19-29.
    • (1988) Disorder and Mixing , pp. 19-29
    • Bouchaud, J.-P.A.1    Georges, A.2
  • 8
    • 0040307478 scopus 로고
    • Anomalous diffusion in disordered media: Statistical mechanisms, models, and physical applications
    • Bouchaud, J.-P., and A. Georges. 1990. Anomalous diffusion in disordered media: statistical mechanisms, models, and physical applications. Phys. Rep. 195:127-193.
    • (1990) Phys. Rep. , vol.195 , pp. 127-193
    • Bouchaud, J.-P.1    Georges, A.2
  • 9
    • 0031032958 scopus 로고    scopus 로고
    • Characteristics of albumin binding to opossum kidney cells and identification of potential receptors
    • Brunskill, N. J., S. Nahorski, and J. Walls. 1997. Characteristics of albumin binding to opossum kidney cells and identification of potential receptors. Pflugers Arch. Eur. J. Physiol. 433:497-504.
    • (1997) Pflugers Arch. Eur. J. Physiol. , vol.433 , pp. 497-504
    • Brunskill, N.J.1    Nahorski, S.2    Walls, J.3
  • 10
    • 0027219916 scopus 로고
    • In vivo dimeric association of class I MHC heavy chains
    • Capps, G. G., B. E. Robinson, R. D. Lewis, and M. C. Zúñiga. 1993. In vivo dimeric association of class I MHC heavy chains. J. Immunol. 151:159-169.
    • (1993) J. Immunol. , vol.151 , pp. 159-169
    • Capps, G.G.1    Robinson, B.E.2    Lewis, R.D.3    Zúñiga, M.C.4
  • 11
    • 0027987216 scopus 로고
    • Analysis of the structure of empty and peptide-loaded major histocompatibility molecules at the cell surface
    • Catipovic, B., G. Talluri, J. Oh, T. Y. Wei, X. M. Su, T. E. Johansen, M. Edidin, and J. P. Schneck. 1994. Analysis of the structure of empty and peptide-loaded major histocompatibility molecules at the cell surface. J. Exp. Med. 180:1753-1761.
    • (1994) J. Exp. Med. , vol.180 , pp. 1753-1761
    • Catipovic, B.1    Talluri, G.2    Oh, J.3    Wei, T.Y.4    Su, X.M.5    Johansen, T.E.6    Edidin, M.7    Schneck, J.P.8
  • 12
    • 0026670158 scopus 로고
    • Self-association of class I major histocompatibility complex molecules in liposomes and cell-surface membranes
    • Chakrabarti, A., J. Matkó, N. A. Rahman, B. G. Barisas, and M. Edidin. 1992. Self-association of class I major histocompatibility complex molecules in liposomes and cell-surface membranes. Biochemistry. 31: 7182-7189.
    • (1992) Biochemistry. , vol.31 , pp. 7182-7189
    • Chakrabarti, A.1    Matkó, J.2    Rahman, N.A.3    Barisas, B.G.4    Edidin, M.5
  • 13
    • 0026683137 scopus 로고
    • Keeping track of cell surface receptors
    • Cherry, R. J. 1992. Keeping track of cell surface receptors. Trends Cell Biol. 2:242-244.
    • (1992) Trends Cell Biol. , vol.2 , pp. 242-244
    • Cherry, R.J.1
  • 18
    • 0026053736 scopus 로고
    • Lateral diffusion and retrograde movements of individual cell surface components on single motile cells observed with Nanovid microscopy
    • de Brabander, M., R. Nuydens, A. Ishihara, B. Holifield, K. Jacobson, and H. Geerts. 1991. Lateral diffusion and retrograde movements of individual cell surface components on single motile cells observed with Nanovid microscopy. J. Cell Biol. 112:1143-1150.
    • (1991) J. Cell Biol. , vol.112 , pp. 1143-1150
    • De Brabander, M.1    Nuydens, R.2    Ishihara, A.3    Holifield, B.4    Jacobson, K.5    Geerts, H.6
  • 19
    • 0030822255 scopus 로고    scopus 로고
    • Lipid microdomains in cell surface membranes
    • Edidin, M. 1997. Lipid microdomains in cell surface membranes. Curr. Opin. Struct. Biol. 7:528-532.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 528-532
    • Edidin, M.1
  • 20
    • 0026320864 scopus 로고
    • Lateral movements of membrane glycoproteins restricted by dynamic cyoplasmic barriers
    • Edidin, M., S. C. Kuo, and M. P. Sheetz. 1991. Lateral movements of membrane glycoproteins restricted by dynamic cyoplasmic barriers. Science. 254:1379-1382.
    • (1991) Science. , vol.254 , pp. 1379-1382
    • Edidin, M.1    Kuo, S.C.2    Sheetz, M.P.3
  • 21
    • 0026071833 scopus 로고
    • Differences between the lateral organisation of conventional and inositol phospholipid-anchored membrane proteins. a further definition of micrometer scale membrane domains
    • Edidin, M., and I. Stroynowski. 1991. Differences between the lateral organisation of conventional and inositol phospholipid-anchored membrane proteins. A further definition of micrometer scale membrane domains. J. Cell Biol. 112:1143-1150.
    • (1991) J. Cell Biol. , vol.112 , pp. 1143-1150
    • Edidin, M.1    Stroynowski, I.2
  • 22
    • 0028325756 scopus 로고
    • Truncation mutants define and locate cytoplasmic barriers to lateral mobility of membrane glycoproteins
    • Edidin, M., M. C. Zúñiga, and M. P. Sheetz. 1994. Truncation mutants define and locate cytoplasmic barriers to lateral mobility of membrane glycoproteins. Proc. Natl. Acad. Sci. USA. 91:3378-3382.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 3378-3382
    • Edidin, M.1    Zúñiga, M.C.2    Sheetz, M.P.3
  • 23
    • 0029946890 scopus 로고    scopus 로고
    • Constrained diffusion or immobile fraction on cell surfaces - A new interpretation
    • Feder, T. J., I. Brustmascher, J. B. Slattery, B. Baird, and W. W. Webb. 1996. Constrained diffusion or immobile fraction on cell surfaces - a new interpretation. Biophys. J. 70:2767-2773.
    • (1996) Biophys. J. , vol.70 , pp. 2767-2773
    • Feder, T.J.1    Brustmascher, I.2    Slattery, J.B.3    Baird, B.4    Webb, W.W.5
  • 24
    • 0026786531 scopus 로고
    • A ligand epitope in vitro analysis of major histocompatibility determinants expressed on B and T lymphocytes
    • Fernández, N., M. Kurpisz, M. Labeta, J. Sachs, and G. Pawelec. 1992. A ligand epitope in vitro analysis of major histocompatibility determinants expressed on B and T lymphocytes. Immunology. 77:116-122.
    • (1992) Immunology. , vol.77 , pp. 116-122
    • Fernández, N.1    Kurpisz, M.2    Labeta, M.3    Sachs, J.4    Pawelec, G.5
  • 26
    • 0942276922 scopus 로고
    • Evidence for intramembrane constraints to cell surface LDL receptor motion
    • 286a
    • Ghosh, R. N., and W. W. Webb. 1990. Evidence for intramembrane constraints to cell surface LDL receptor motion. Biophys. J. 57:286a.
    • (1990) Biophys. J. , vol.57
    • Ghosh, R.N.1    Webb, W.W.2
  • 27
    • 0028281482 scopus 로고
    • Automated detection and tracking of individual and clustered cell surface low density lipoprotein receptor molecules
    • Ghosh, R. N., and W. W. Webb. 1994. Automated detection and tracking of individual and clustered cell surface low density lipoprotein receptor molecules. Biophys. J. 66:1301-131.
    • (1994) Biophys. J. , vol.66 , pp. 1301-2131
    • Ghosh, R.N.1    Webb, W.W.2
  • 28
    • 0017354135 scopus 로고
    • The low-density lipoprotein pathway and its relation to atherosclerosis
    • Goldstein, J. L., and M. S. Brown. 1977. The low-density lipoprotein pathway and its relation to atherosclerosis. Annu. Rev. Biochem. 46: 897-930.
    • (1977) Annu. Rev. Biochem. , vol.46 , pp. 897-930
    • Goldstein, J.L.1    Brown, M.S.2
  • 29
    • 0008856154 scopus 로고
    • Cell surface clustering and mobility of the liganded LDL receptor measured by digital video fluorescence microscopy
    • L. M. Loew, editor. CRC Press, Boca Raton, FL.
    • Gross, D. J., and W. W. Webb. 1988. Cell surface clustering and mobility of the liganded LDL receptor measured by digital video fluorescence microscopy. In Spectroscopic Membrane Probes, Vol. II, L. M. Loew, editor. CRC Press, Boca Raton, FL. 9-45.
    • (1988) Spectroscopic Membrane Probes , vol.2 , pp. 9-45
    • Gross, D.J.1    Webb, W.W.2
  • 30
    • 0028838012 scopus 로고
    • Dimerisation of cell-surface receptors in signal transduction
    • Heldin, C. H. 1995. Dimerisation of cell-surface receptors in signal transduction. Cell. 80:213-223.
    • (1995) Cell. , vol.80 , pp. 213-223
    • Heldin, C.H.1
  • 31
    • 34249755873 scopus 로고
    • Tracking movements of lipids and Thy-1 molecules in the plasmalemma of living fibroblasts by fluorescence video microscopy with nanometer scale precision
    • Hicks, B. W., and K. J. Angelides. 1995. Tracking movements of lipids and Thy-1 molecules in the plasmalemma of living fibroblasts by fluorescence video microscopy with nanometer scale precision. J. Membr. Biol. 144:231-244.
    • (1995) J. Membr. Biol. , vol.144 , pp. 231-244
    • Hicks, B.W.1    Angelides, K.J.2
  • 32
    • 0024392570 scopus 로고
    • Rotational and translational diffusion in membranes measured by fluorescence and phosphorescence methods
    • Jovin, T., and W. L. C. Vaz. 1989. Rotational and translational diffusion in membranes measured by fluorescence and phosphorescence methods. Methods Enzymol. 172:471-573.
    • (1989) Methods Enzymol. , vol.172 , pp. 471-573
    • Jovin, T.1    Vaz, W.L.C.2
  • 34
    • 0030222116 scopus 로고    scopus 로고
    • Cell-surface organisation by the membrane skeleton
    • Kusumi, A., and Y. Sako. 1996. Cell-surface organisation by the membrane skeleton. Curr. Opin. Cell Biol. 8:566-574.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 566-574
    • Kusumi, A.1    Sako, Y.2
  • 35
    • 33845429870 scopus 로고    scopus 로고
    • Applications of laser tweezers to studies of fences and tethers of the membrane skeleton that regulate the movements of plasma membrane proteins
    • Kusumi, A., Y. Sako, T. Fujiwara, and M. Tomishige. 1998. Applications of laser tweezers to studies of fences and tethers of the membrane skeleton that regulate the movements of plasma membrane proteins. Methods Cell Biol. 55:173-194.
    • (1998) Methods Cell Biol. , vol.55 , pp. 173-194
    • Kusumi, A.1    Sako, Y.2    Fujiwara, T.3    Tomishige, M.4
  • 36
    • 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., Y. Sako, and M. Yamamoto. 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. 65:2021-2040.
    • (1993) Biophys. J. , vol.65 , pp. 2021-2040
    • Kusumi, A.1    Sako, Y.2    Yamamoto, M.3
  • 37
    • 0025823340 scopus 로고
    • Direct observation of Brownian motion of lipids in membranes
    • Lee, G. M., A. Ishihara, and K. A. Jacobson. 1991. Direct observation of Brownian motion of lipids in membranes. Proc. Natl. Acad. Sci. USA. 88:6274-7278.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 6274-7278
    • Lee, G.M.1    Ishihara, A.2    Jacobson, K.A.3
  • 38
    • 0342448200 scopus 로고
    • Microfilamemts in normal and transformed cells: Changes in the multiple forms of tropomysin
    • A. J. Levine, G. F. V. Woude, W. C. Topp, and J. D. Watson, editors. Cold Spring Harbor Laboratory, Cold Spring Harbor, New York.
    • Lin, J. J.-C., S. Yamashiro-Matsumura, and F. Matsumura. 1984. Microfilamemts in normal and transformed cells: changes in the multiple forms of tropomysin. In The Transformed Phenotype. A. J. Levine, G. F. V. Woude, W. C. Topp, and J. D. Watson, editors. Cold Spring Harbor Laboratory, Cold Spring Harbor, New York. 57-65.
    • (1984) The Transformed Phenotype , pp. 57-65
    • Lin, J.J.-C.1    Yamashiro-Matsumura, S.2    Matsumura, F.3
  • 39
    • 0028181870 scopus 로고
    • Clustering of class I HLA molecules on the surfaces of activated and transformed human cells
    • Matkó, J., Y. Bushkin, T. Wei, and M. Edidin. 1994. Clustering of class I HLA molecules on the surfaces of activated and transformed human cells. J. Immunol. 152:3353-3360.
    • (1994) J. Immunol. , vol.152 , pp. 3353-3360
    • Matkó, J.1    Bushkin, Y.2    Wei, T.3    Edidin, M.4
  • 40
    • 0026675654 scopus 로고
    • Transmembrane signaling - The joy of aggregation
    • Metzger, H. 1992. Transmembrane signaling - the joy of aggregation. J. Immunol. 149:1477-1487.
    • (1992) J. Immunol. , vol.149 , pp. 1477-1487
    • Metzger, H.1
  • 42
    • 0026783791 scopus 로고
    • Long-tail kinetics in biophysics?
    • Nagle, J. F. 1992. Long-tail kinetics in biophysics? Biophys. J. 63:366-370.
    • (1992) Biophys. J. , vol.63 , pp. 366-370
    • Nagle, J.F.1
  • 44
    • 0030273252 scopus 로고    scopus 로고
    • Lateral dynamics of major histocompatibility complex class II molecules bound with agonist peptide or altered peptide ligands
    • Qiu, Y., W. F. Wade, D. A. Roess, and B. G. Barisas. 1996. Lateral dynamics of major histocompatibility complex class II molecules bound with agonist peptide or altered peptide ligands. Immunol. Lett. 53:19-23.
    • (1996) Immunol. Lett. , vol.53 , pp. 19-23
    • Qiu, Y.1    Wade, W.F.2    Roess, D.A.3    Barisas, B.G.4
  • 45
    • 0028243194 scopus 로고
    • Compartmentalised structure of the plasma membrane for receptor movements as revealed by a nanometer-level motion analysis
    • Sako, Y., and A. Kusumi. 1994. Compartmentalised structure of the plasma membrane for receptor movements as revealed by a nanometer-level motion analysis. J. Cell Biol. 125:1251-1264.
    • (1994) J. Cell Biol. , vol.125 , pp. 1251-1264
    • Sako, Y.1    Kusumi, A.2
  • 46
    • 0029014265 scopus 로고
    • Barriers for lateral diffusion of transferrin receptor in the plasma membrane as characterised by receptor dragging by laser tweezers: Fence versus tether
    • Sako, Y., and A. Kusumi. 1995. Barriers for lateral diffusion of transferrin receptor in the plasma membrane as characterised by receptor dragging by laser tweezers: fence versus tether. J. Cell Biol. 129:1559-1574.
    • (1995) J. Cell Biol. , vol.129 , pp. 1559-1574
    • Sako, Y.1    Kusumi, A.2
  • 47
    • 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: Corraling and tethering by the membrane skeleton
    • Sako, Y., A. Nagafuchi, S. Tsukita, M. Takeichi, and A. Kusumi. 1998. Cytoplasmic regulation of the movement of E-cadherin on the free cell surface as studied by optical tweezers and single particle tracking: corraling and tethering by the membrane skeleton. J. Cell Biol. 140: 1227-1240.
    • (1998) J. Cell Biol. , vol.140 , pp. 1227-1240
    • Sako, Y.1    Nagafuchi, A.2    Tsukita, S.3    Takeichi, M.4    Kusumi, A.5
  • 48
    • 0027197103 scopus 로고
    • Lateral diffusion in an archipelago: Single particle diffusion
    • Saxton, M. J. 1993. Lateral diffusion in an archipelago: single particle diffusion. Biophys. J. 64:1766-1780.
    • (1993) Biophys. J. , vol.64 , pp. 1766-1780
    • Saxton, M.J.1
  • 49
    • 0028140412 scopus 로고
    • Anomalous diffusion due to obstacles: A Monte Carlo study
    • Saxton, M. 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.1
  • 50
    • 0029163176 scopus 로고
    • Single particle tracking - Effects of corrals
    • Saxton, M. 1995. Single particle tracking - effects of corrals. Biophys. J. 69:389-398.
    • (1995) Biophys. J. , vol.69 , pp. 389-398
    • Saxton, M.1
  • 51
    • 0030050141 scopus 로고    scopus 로고
    • Anomalous diffusion due to binding - a Monte Carlo study
    • Saxton, M. 1996. Anomalous diffusion due to binding - a Monte Carlo study. Biophys. J. 70:1250-1262.
    • (1996) Biophys. J. , vol.70 , pp. 1250-1262
    • Saxton, M.1
  • 52
    • 0030956033 scopus 로고    scopus 로고
    • Single-particle tracking: Applications to membrane dynamics
    • Saxton, M. J., and K. Jacobson. 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
  • 54
    • 0028584124 scopus 로고
    • Influence of obstacles on lipid lateral diffusion: Computer simulation of FRAP experiments and application to proteoliposomes and biomembranes
    • Schram, V., J.-F. Tocanne, and A. Lopez. 1994. Influence of obstacles on lipid lateral diffusion: computer simulation of FRAP experiments and application to proteoliposomes and biomembranes. Eur. Biophys. J. 23:337-348.
    • (1994) Eur. Biophys. J. , vol.23 , pp. 337-348
    • Schram, V.1    Tocanne, J.-F.2    Lopez, A.3
  • 56
    • 0039587949 scopus 로고    scopus 로고
    • Single-molecule microscopy on model membranes reveals anomalous diffusion
    • Schütz, G. J., H. Schindler, and T. Schmidt. 1997a. Single-molecule microscopy on model membranes reveals anomalous diffusion. Biophys. J. 73:1073-1080.
    • (1997) Biophys. J. , vol.73 , pp. 1073-1080
    • Schütz, G.J.1    Schindler, H.2    Schmidt, T.3
  • 57
    • 0030863490 scopus 로고    scopus 로고
    • Transient confinement of a glycosylphosphatidylinositol-anchored protein in the plasma membrane
    • Sheets, E. D., G. M. Lee, R. Simson, and K. Jacobson. 1997. Transient confinement of a glycosylphosphatidylinositol-anchored protein in the plasma membrane. Biochemistry. 36:12449-12458.
    • (1997) Biochemistry. , vol.36 , pp. 12449-12458
    • Sheets, E.D.1    Lee, G.M.2    Simson, R.3    Jacobson, K.4
  • 58
    • 0029126377 scopus 로고
    • New insights into membrane dynamics from the analysis of cell surface interactions by physical methods
    • Sheets, E. D., R. Simson, and K. Jacobson. 1995. New insights into membrane dynamics from the analysis of cell surface interactions by physical methods. Curr. Opin. Cell Biol. 7:707-714.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 707-714
    • Sheets, E.D.1    Simson, R.2    Jacobson, K.3
  • 59
    • 0024338987 scopus 로고
    • Nanometer-level analysis demonstrates that lipid flow does not drive membrane glycoprotein movement
    • Sheetz, M. P., S. Turney, H. Qian, and E. L. Elson. 1989. Nanometer-level analysis demonstrates that lipid flow does not drive membrane glycoprotein movement Nature. 340:284-288.
    • (1989) Nature , vol.340 , pp. 284-288
    • Sheetz, M.P.1    Turney, S.2    Qian, H.3    Elson, E.L.4
  • 61
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons, K., and E. Ikonen. 1997. Functional rafts in cell membranes. Nature. 387:569-572.
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 62
    • 0029162080 scopus 로고
    • Detection of temporary lateral confinement of membrane proteins using single-particle tracking analysis
    • Simson, R., E. D. Sheets, and K. Jacobson. 1995. Detection of temporary lateral confinement of membrane proteins using single-particle tracking analysis. Biophys. J. 69:989-993.
    • (1995) Biophys. J. , vol.69 , pp. 989-993
    • Simson, R.1    Sheets, E.D.2    Jacobson, K.3
  • 64
    • 0000566148 scopus 로고    scopus 로고
    • Imaging of individual cell surface MHC antigens using fluorescent particles
    • N. Fernández and G. Butcher, editors. Practical Approach Series, Oxford University Press, London
    • Smith, P. R., K. M. Wilson, I. E. G. Morrison, R. J. Cherry, and N. Fernández. 1998. Imaging of individual cell surface MHC antigens using fluorescent particles. In MHC: Biochemistry and Genetics. N. Fernández and G. Butcher, editors. Practical Approach Series, Oxford University Press, London. 131-151.
    • (1998) MHC: Biochemistry and Genetics , pp. 131-151
    • Smith, P.R.1    Wilson, K.M.2    Morrison, I.E.G.3    Cherry, R.J.4    Fernández, N.5
  • 65
    • 0030054163 scopus 로고    scopus 로고
    • ATP depletion causes translational immobilization of cell surface transferrin receptors in K562 cells
    • Thatte, S. T., K. R. Bridges, and D. E. Golan. 1996. ATP depletion causes translational immobilization of cell surface transferrin receptors in K562 cells. J Cell. Physiol. 166:446-452.
    • (1996) J Cell. Physiol. , vol.166 , pp. 446-452
    • Thatte, S.T.1    Bridges, K.R.2    Golan, D.E.3
  • 66
    • 0029331068 scopus 로고
    • Plasma-membrane-bound macromolecules are dynamically aggregated to form nonrandom codistribution patterns of selected functional elements - Do pattern-recognition processes govern antigen presentation and intercellular interactions?
    • Vereb, G., L. Mátyus, L. Bene, G. Panyi, Z. Bacsó, M. Balázs, J. Matkó, J Szöllösi, R. Gáspár, S. Damjanovich, R. E. Dale, C. Pieri, and M. Ameloot, M. 1995. Plasma-membrane-bound macromolecules are dynamically aggregated to form nonrandom codistribution patterns of selected functional elements - do pattern-recognition processes govern antigen presentation and intercellular interactions? J. Mol. Recognit. 8:237-246.
    • (1995) J. Mol. Recognit. , vol.8 , pp. 237-246
    • Vereb, G.1    Mátyus, L.2    Bene, L.3    Panyi, G.4    Bacsó, Z.5    Balázs, M.6    Matkó, J.7    Szöllösi, J.8    Gáspár, R.9    Damjanovich, S.10    Dale, R.E.11    Pieri, C.12    Ameloot, M.13
  • 67
    • 0024803851 scopus 로고
    • Translational diffusion of class II major histocompatibility complex molecules is constrained by their cytoplasmic domains
    • Wade, W. F., J. H. Freed, and M. Edidin. 1989. Translational diffusion of class II major histocompatibility complex molecules is constrained by their cytoplasmic domains. J. Cell Biol. 109:3325-3331.
    • (1989) J. Cell Biol. , vol.109 , pp. 3325-3331
    • Wade, W.F.1    Freed, J.H.2    Edidin, M.3
  • 68
    • 0027970208 scopus 로고
    • Single particle tracking of surface receptor movement during cell division
    • Wang, Y., J. D. Silverman, and L. Cao. 1994. Single particle tracking of surface receptor movement during cell division. J. Cell Biol. 127:963-971.
    • (1994) J. Cell Biol. , vol.127 , pp. 963-971
    • Wang, Y.1    Silverman, J.D.2    Cao, L.3
  • 69
    • 0028014460 scopus 로고
    • Signal transduction by lymphocyte antigen receptors
    • Weiss, A., and D. R. Littman. 1994. Signal transduction by lymphocyte antigen receptors. Cell. 76:263-274.
    • (1994) Cell. , vol.76 , pp. 263-274
    • Weiss, A.1    Littman, D.R.2
  • 70
    • 0031868557 scopus 로고    scopus 로고
    • Toward a predictive understanding of molecular recognition
    • Weng, Z., and C. DeLisi. 1998. Toward a predictive understanding of molecular recognition. Immunol. Rev. 163:251-266.
    • (1998) Immunol. Rev. , vol.163 , pp. 251-266
    • Weng, Z.1    Delisi, C.2
  • 71
    • 0029815535 scopus 로고    scopus 로고
    • Single particle tracking of cell-surface HLA-DR molecules using R-phycoerythrin labelled monoclonal antibodies and fluorescence digital imaging
    • Wilson, K. M., I. E. G. Morrison, P. R. Smith, N. Fernández, and R. J. Cherry. 1996. Single particle tracking of cell-surface HLA-DR molecules using R-phycoerythrin labelled monoclonal antibodies and fluorescence digital imaging. J. Cell Sci. 109:2101-2109.
    • (1996) J. Cell Sci. , vol.109 , pp. 2101-2109
    • Wilson, K.M.1    Morrison, I.E.G.2    Smith, P.R.3    Fernández, N.4    Cherry, R.J.5
  • 72
    • 0027661274 scopus 로고
    • Protein lateral mobility as a reflection of membrane microstructure
    • Zhang, F., G. M. Lee, and K. Jacobson. 1993. Protein lateral mobility as a reflection of membrane microstructure. Bioessays. 15:579-588.
    • (1993) Bioessays. , vol.15 , pp. 579-588
    • Zhang, F.1    Lee, G.M.2    Jacobson, K.3
  • 73
    • 0028870140 scopus 로고
    • Kinetics of bilirubin transfer between serum albumin and membrane vesicles-insight into the mechanism of organic anion delivery to the hepatocyte plasma membrane
    • Zucker, S. D., W. Goessling, and J. L. Gollan. 1995. Kinetics of bilirubin transfer between serum albumin and membrane vesicles-insight into the mechanism of organic anion delivery to the hepatocyte plasma membrane. J. Biol. Chem. 270:1074-1081.
    • (1995) J. Biol. Chem. , vol.270 , pp. 1074-1081
    • Zucker, S.D.1    Goessling, W.2    Gollan, J.L.3


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