메뉴 건너뛰기




Volumn 141, Issue 4, 1998, Pages 929-942

Lipid domain structure of the plasma membrane revealed by patching of membrane components

Author keywords

[No Author keywords available]

Indexed keywords

ALKALINE PHOSPHATASE PLACENTA ISOENZYME; CHOLERA TOXIN; GANGLIOSIDE GM1; GLYCOSYLPHOSPHATIDYLINOSITOL; INFLUENZA VIRUS HEMAGGLUTININ; LIPID; PHOSPHATIDYLINOSITOL;

EID: 0031750335     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.141.4.929     Document Type: Article
Times cited : (1065)

References (66)
  • 1
    • 0030774479 scopus 로고    scopus 로고
    • On the origin of sphingolipid/ cholesterol-rich detergent-insoluble cell membranes: Physiological concentrations of cholesterol and sphingolipid induce formation of a detergent insoluble, liquid ordered lipid phase in model membranes
    • Ahmed, S.N., D.A. Brown, and E. London. 1997. On the origin of sphingolipid/ cholesterol-rich detergent-insoluble cell membranes: physiological concentrations of cholesterol and sphingolipid induce formation of a detergent insoluble, liquid ordered lipid phase in model membranes. Biochemistry. 36: 10944-10953.
    • (1997) Biochemistry , vol.36 , pp. 10944-10953
    • Ahmed, S.N.1    Brown, D.A.2    London, E.3
  • 2
    • 0026717736 scopus 로고
    • Major histocompatibility complex restricted recognition of retroviral superantigens by V β 17+ T cells
    • Blackman, M.A., F.E. Lund, S. Surman, R.B. Corley, and D.L. Woodland. 1992. Major histocompatibility complex restricted recognition of retroviral superantigens by V β 17+ T cells. J. Exp. Med. 176:275-280.
    • (1992) J. Exp. Med. , vol.176 , pp. 275-280
    • Blackman, M.A.1    Lund, F.E.2    Surman, S.3    Corley, R.B.4    Woodland, D.L.5
  • 3
    • 0025913946 scopus 로고
    • A single amino acid change in the cytoplasmic domain alters the polarized delivery of influenza virus hemagglutinin
    • Brewer, C.B., and M.G. Roth. 1991. A single amino acid change in the cytoplasmic domain alters the polarized delivery of influenza virus hemagglutinin. J. Cell Biol. 114:413-421.
    • (1991) J. Cell Biol. , vol.114 , pp. 413-421
    • Brewer, C.B.1    Roth, M.G.2
  • 4
    • 0026667338 scopus 로고
    • Interactions between GPI-anchored proteins and membrane lipids
    • Brown, D.A. 1992. Interactions between GPI-anchored proteins and membrane lipids. Trends Cell Biol. 2:338-343.
    • (1992) Trends Cell Biol. , vol.2 , pp. 338-343
    • Brown, D.A.1
  • 5
    • 0027269661 scopus 로고
    • The tyrosine kinase connection: How GPI-anchored proteins activate T cells
    • Brown, D.A. 1993. The tyrosine kinase connection: how GPI-anchored proteins activate T cells. Curr. Opin. Immunol. 5:349-354.
    • (1993) Curr. Opin. Immunol. , vol.5 , pp. 349-354
    • Brown, D.A.1
  • 6
    • 0026512314 scopus 로고
    • Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the cell surface
    • Brown, D. A., and J.K. Rose. 1992. Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the cell surface. Cell. 68:533-544.
    • (1992) Cell , vol.68 , pp. 533-544
    • Brown, D.A.1    Rose, J.K.2
  • 7
    • 0024433592 scopus 로고
    • Mechanism of membrane anchoring affects polarized expression of two proteins in MDCK cells
    • Brown, D.A., B. Crise, and J.K. Rose. 1989. Mechanism of membrane anchoring affects polarized expression of two proteins in MDCK cells. Science. 245: 1499-1501.
    • (1989) Science , vol.245 , pp. 1499-1501
    • Brown, D.A.1    Crise, B.2    Rose, J.K.3
  • 8
    • 0031965054 scopus 로고    scopus 로고
    • Sphingolipid organisation in biomembranes: What physical studies of model membranes reveal
    • Brown, R.E. 1998. Sphingolipid organisation in biomembranes: what physical studies of model membranes reveal. J. Cell Sci. 111:1-9.
    • (1998) J. Cell Sci. , vol.111 , pp. 1-9
    • Brown, R.E.1
  • 9
    • 0020966332 scopus 로고
    • Specific selection of host cell glycoproteins during assembly of murine leukaemia virus and vesicular stomatitis virus: Presence of Thy-I glycoprotein and absence of H-2, Pgp1 and T-200 glycoproteins on the envelopes of these virus particles
    • Calafat, J., H. Janssen, P. Demant, J. Hilgers, and J. Zavada. 1983. Specific selection of host cell glycoproteins during assembly of murine leukaemia virus and vesicular stomatitis virus: presence of Thy-I glycoprotein and absence of H-2, Pgp1 and T-200 glycoproteins on the envelopes of these virus particles. J. Gen. Virol. 64:1241-1253.
    • (1983) J. Gen. Virol. , vol.64 , pp. 1241-1253
    • Calafat, J.1    Janssen, H.2    Demant, P.3    Hilgers, J.4    Zavada, J.5
  • 10
    • 0027468760 scopus 로고
    • Detergent insolubility of alkaline phosphatase during biosynthetic transport and endocytosis. Role of cholesterol
    • Cerneus, D.P., E. Ueffing, G. Posthuma, G.J. Strous, and A. van der Ende. 1993. Detergent insolubility of alkaline phosphatase during biosynthetic transport and endocytosis. Role of cholesterol. J. Biol Chem. 268:3150-3155.
    • (1993) J. Biol Chem. , vol.268 , pp. 3150-3155
    • Cerneus, D.P.1    Ueffing, E.2    Posthuma, G.3    Strous, G.J.4    Van Der Ende, A.5
  • 11
    • 0029994378 scopus 로고    scopus 로고
    • Endocytosis of GPI-anchored proteins in human lymphocytes: Role of glycolipid-based domains, actin cytoskeleton, and protein kinases
    • Deckert, M., M. Ticchioni, and A. Bernard. 1996. Endocytosis of GPI-anchored proteins in human lymphocytes: Role of glycolipid-based domains, actin cytoskeleton, and protein kinases. J. Cell Biol. 133:791-799.
    • (1996) J. Cell Biol. , vol.133 , pp. 791-799
    • Deckert, M.1    Ticchioni, M.2    Bernard, A.3
  • 12
    • 0028920139 scopus 로고
    • Caveolin is palmitoylated on multiple cysteine residues: Palmitoylation is not required for localization of caveolin to caveolae
    • Dietzen, D.J., W.R. Hastings, and D.M. Lublin. 1995. Caveolin is palmitoylated on multiple cysteine residues: Palmitoylation is not required for localization of caveolin to caveolae. J. Biol. Chem. 270:6838-6842.
    • (1995) J. Biol. Chem. , vol.270 , pp. 6838-6842
    • Dietzen, D.J.1    Hastings, W.R.2    Lublin, D.M.3
  • 13
    • 0028209329 scopus 로고
    • VIP36, a novel component of glycolipid rafts and exocytic carrier vesicles in epithelial cells
    • Fiedler, K., R.G. Parton, R. Kellner, T. Etzold, and K. Simons. 1994. VIP36, a novel component of glycolipid rafts and exocytic carrier vesicles in epithelial cells. EMBO (Eur. Mol. Biol. Organ.) J. 13:1729-1740.
    • (1994) EMBO (Eur. Mol. Biol. Organ.) J. , vol.13 , pp. 1729-1740
    • Fiedler, K.1    Parton, R.G.2    Kellner, R.3    Etzold, T.4    Simons, K.5
  • 14
    • 0031041581 scopus 로고    scopus 로고
    • Compartmentalized activation of the high affinity immunoglobulin E receptor within membrane domains
    • Field, K.A., D. Holowka, and B. Baird. 1997. Compartmentalized activation of the high affinity immunoglobulin E receptor within membrane domains. J. Biol. Chem. 272:4276-4280.
    • (1997) J. Biol. Chem. , vol.272 , pp. 4276-4280
    • Field, K.A.1    Holowka, D.2    Baird, B.3
  • 15
    • 0029086362 scopus 로고
    • De novo formation of caveolae in lymphocytes by expression of VIP21-caveolin
    • Fra, A.M., E. Williamson, K. Simons, and R.G. Parton. 1995. De novo formation of caveolae in lymphocytes by expression of VIP21-caveolin. Proc. Natl. Acad. Sci. USA. 92:8655-8659.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8655-8659
    • Fra, A.M.1    Williamson, E.2    Simons, K.3    Parton, R.G.4
  • 16
    • 0029757511 scopus 로고    scopus 로고
    • GPI-anchored proteins, glycosphingolipids, and sphingomyelin are sequestered to caveolae only after crosslinking
    • Fujimoto, T. 1996. GPI-anchored proteins, glycosphingolipids, and sphingomyelin are sequestered to caveolae only after crosslinking. J. Histochem. Cytochem. 44:929-941.
    • (1996) J. Histochem. Cytochem. , vol.44 , pp. 929-941
    • Fujimoto, T.1
  • 17
    • 0028947029 scopus 로고
    • Both sphingolipids and cholesterol participate in the detergent insolubility of alkaline phosphatase, a glycosylphosphatidylinositol-anchored protein, in mammalian membranes
    • Hanada, K., M. Nishijima, Y. Akamatsu, and R.E. Pagano. 1995. Both sphingolipids and cholesterol participate in the detergent insolubility of alkaline phosphatase, a glycosylphosphatidylinositol-anchored protein, in mammalian membranes. J. Biol. Chem. 270:6254-6260.
    • (1995) J. Biol. Chem. , vol.270 , pp. 6254-6260
    • Hanada, K.1    Nishijima, M.2    Akamatsu, Y.3    Pagano, R.E.4
  • 19
    • 0030878573 scopus 로고    scopus 로고
    • Caveolae, DIGs, and the dynamics of sphingolipid-cholesterol microdomains
    • Harder, T., and K. Simons. 1997. Caveolae, DIGs, and the dynamics of sphingolipid-cholesterol microdomains. Curr. Opin. Cell Biol. 9:534-542.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 534-542
    • Harder, T.1    Simons, K.2
  • 20
    • 0028965138 scopus 로고
    • Evidence for transbilayer, tail-to-tail cholesterol dimers in dipalmitoylglycerophosphocholine liposomes
    • Harris, J.S., D.E. Epps, S.R. Davio, and F.J. Kezdy. 1995. Evidence for transbilayer, tail-to-tail cholesterol dimers in dipalmitoylglycerophosphocholine liposomes. Biochemistry. 34:3851-3857.
    • (1995) Biochemistry , vol.34 , pp. 3851-3857
    • Harris, J.S.1    Epps, D.E.2    Davio, S.R.3    Kezdy, F.J.4
  • 21
    • 0029795488 scopus 로고    scopus 로고
    • Regulation mechanism of ERM protein/ plasma membrane association: Possible involvement of phosphatidyl inositol turnover and rho-dependent signaling pathway
    • Hirao, M., N. Sato, T. Kondo, S. Yonemura, M. Monden, T. Sasaki, Y. Takai, S. Tsukita, and S. Tsukita. 1996. Regulation mechanism of ERM protein/ plasma membrane association: possible involvement of phosphatidyl inositol turnover and rho-dependent signaling pathway. J. Cell Biol. 135:37-52.
    • (1996) J. Cell Biol. , vol.135 , pp. 37-52
    • Hirao, M.1    Sato, N.2    Kondo, T.3    Yonemura, S.4    Monden, M.5    Sasaki, T.6    Takai, Y.7    Tsukita, S.8    Tsukita, S.9
  • 22
    • 0029977729 scopus 로고    scopus 로고
    • Antigen-mediated IgE receptor aggregation and signaling: A window on cell surface structure and dynamics
    • Holowka, D., and B. Baird. 1996. Antigen-mediated IgE receptor aggregation and signaling: a window on cell surface structure and dynamics. Ann. Rev. Biophys. Biomol. Struct. 25:79-112.
    • (1996) Ann. Rev. Biophys. Biomol. Struct. , vol.25 , pp. 79-112
    • Holowka, D.1    Baird, B.2
  • 23
    • 0020587059 scopus 로고
    • Role of cholesterol in the capping of surface immunoglobulin receptors on murine lymphocytes
    • Hoover, R.L., E.A. Dawidowicz, J.M. Robinson, and M.J. Karnovsiky. 1983. Role of cholesterol in the capping of surface immunoglobulin receptors on murine lymphocytes. J. Cell Biol. 97:73-80.
    • (1983) J. Cell Biol. , vol.97 , pp. 73-80
    • Hoover, R.L.1    Dawidowicz, E.A.2    Robinson, J.M.3    Karnovsiky, M.J.4
  • 24
    • 0029062772 scopus 로고
    • Different requirements for NSF, SNAP, and Rab proteins in apical and basolateral transport in MDCK cells
    • Ikonen, E., M. Tagaya, O. Ullrich, C. Montecucco, and K. Simons. 1995. Different requirements for NSF, SNAP, and Rab proteins in apical and basolateral transport in MDCK cells. Cell. 81:571-580.
    • (1995) Cell , vol.81 , pp. 571-580
    • Ikonen, E.1    Tagaya, M.2    Ullrich, O.3    Montecucco, C.4    Simons, K.5
  • 26
    • 0032559854 scopus 로고    scopus 로고
    • Cholesterol is required for surface transport of Influenza virus hemagglutinin
    • Keller, P., and K. Simons. 1998a. Cholesterol is required for surface transport of Influenza virus hemagglutinin. J. Cell Biol. 140:1357-1367.
    • (1998) J. Cell Biol. , vol.140 , pp. 1357-1367
    • Keller, P.1    Simons, K.2
  • 27
    • 0031457805 scopus 로고    scopus 로고
    • Post-Golgi biosynthetic trafficking
    • Keller, P., and K. Simons. 1998b. Post-Golgi biosynthetic trafficking. J. Cell Sci. 110:3001-3009.
    • (1998) J. Cell Sci. , vol.110 , pp. 3001-3009
    • Keller, P.1    Simons, K.2
  • 28
    • 0028812541 scopus 로고
    • Alteration of the myometrial plasma membrane cholesterol content with β-cyclodextrin modulates the binding affinity of the oxytocin receptor
    • Klein, U., G. Gimpl, and F. Fahrenholz. 1995. Alteration of the myometrial plasma membrane cholesterol content with β-cyclodextrin modulates the binding affinity of the oxytocin receptor. Biochemistry. 34:13784-13793.
    • (1995) Biochemistry , vol.34 , pp. 13784-13793
    • Klein, U.1    Gimpl, G.2    Fahrenholz, F.3
  • 29
    • 0022721628 scopus 로고
    • Microinjected antibodies against the cytoplasmic domain of vesicular stomatitis virus glycoprotein block its transport to the cell surface
    • Kreis, T.E. 1986. Microinjected antibodies against the cytoplasmic domain of vesicular stomatitis virus glycoprotein block its transport to the cell surface. EMBO (Eur. Mol. Biol. Organ.) J. 5:931-941.
    • (1986) EMBO (Eur. Mol. Biol. Organ.) J. , vol.5 , pp. 931-941
    • Kreis, T.E.1
  • 30
    • 0028933450 scopus 로고
    • Guilt by insolubility - Does a protein's detergent insolubility reflect caveolar location?
    • Kurzchalia, T.V., E. Hartmann, and P. Dupree. 1995. Guilt by insolubility - does a protein's detergent insolubility reflect caveolar location? Trends Cell Biol. 5:187-189.
    • (1995) Trends Cell Biol. , vol.5 , pp. 187-189
    • Kurzchalia, T.V.1    Hartmann, E.2    Dupree, P.3
  • 31
    • 0024276904 scopus 로고
    • A single amino acid change in the cytoplasmic domain allows the influenza virus haemagglutinin to be endocytosed through coated pits
    • Lazarovits, J., and M. Roth. 1988. A single amino acid change in the cytoplasmic domain allows the influenza virus haemagglutinin to be endocytosed through coated pits. Cell. 53:743-752.
    • (1988) Cell , vol.53 , pp. 743-752
    • Lazarovits, J.1    Roth, M.2
  • 32
    • 0006773266 scopus 로고
    • Caveolae and human disease: Functional roles in transcytosis, potocytosis, signalling, and cell polarity
    • Lisanti, P.L., P.E. Scherer, Z. Tang, E. Kübler, A.J. Koleske, and M. Sargiacomo. 1995. Caveolae and human disease: functional roles in transcytosis, potocytosis, signalling, and cell polarity. Semin. Dev. Biol. 6:47-58.
    • (1995) Semin. Dev. Biol. , vol.6 , pp. 47-58
    • Lisanti, P.L.1    Scherer, P.E.2    Tang, Z.3    Kübler, E.4    Koleske, A.J.5    Sargiacomo, M.6
  • 33
    • 0028068273 scopus 로고
    • Mechanisms of cell polarity: Sorting and transport in epithelial cells
    • Matter, K., and I. Mellman. 1994. Mechanisms of cell polarity: sorting and transport in epithelial cells. Curr. Opin. Cell Biol. 6:545-554.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 545-554
    • Matter, K.1    Mellman, I.2
  • 34
    • 0026482992 scopus 로고
    • Basolateral sorting of LDL receptor in MDCK cells: The cytoplasmic domain contains two tyrosine-dependent targeting determinants
    • Matter, K., W. Hunziker, and I. Mellman. 1992. Basolateral sorting of LDL receptor in MDCK cells: the cytoplasmic domain contains two tyrosine-dependent targeting determinants. Cell. 71:741-753.
    • (1992) Cell , vol.71 , pp. 741-753
    • Matter, K.1    Hunziker, W.2    Mellman, I.3
  • 35
    • 0029044628 scopus 로고
    • Insolubility and redistribution of GPI-anchored proteins at the cell surface after detergent treatment
    • Mayor, S., and F.R. Maxfield. 1995. Insolubility and redistribution of GPI-anchored proteins at the cell surface after detergent treatment. Mol. Biol. Cell. 6:929-944.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 929-944
    • Mayor, S.1    Maxfield, F.R.2
  • 36
    • 0028000605 scopus 로고
    • Sequestration of GPI-anchored proteins in caveolae triggered by cross-linking
    • Mayor, S., K.G. Rothberg, and F.R. Maxfield. 1994. Sequestration of GPI-anchored proteins in caveolae triggered by cross-linking. Science. 264:1948-1951.
    • (1994) Science , vol.264 , pp. 1948-1951
    • Mayor, S.1    Rothberg, K.G.2    Maxfield, F.R.3
  • 39
    • 0030936823 scopus 로고    scopus 로고
    • Reversible palmitoylation of signaling proteins
    • Mumby, S.M. 1997. Reversible palmitoylation of signaling proteins. Curr. Opin. Cell Biol. 9:148-154.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 148-154
    • Mumby, S.M.1
  • 41
    • 0029943503 scopus 로고    scopus 로고
    • Transport of vesicular stomatitis virus G-protein to the cell surface is signal mediated in polarized and nonpolarized cells
    • Müsch, A., H. Xu, D. Shields, and E. Rodriguez-Boulan. 1996. Transport of vesicular stomatitis virus G-protein to the cell surface is signal mediated in polarized and nonpolarized cells. J. Cell Biol. 133:543-558.
    • (1996) J. Cell Biol. , vol.133 , pp. 543-558
    • Müsch, A.1    Xu, H.2    Shields, D.3    Rodriguez-Boulan, E.4
  • 42
    • 0030905888 scopus 로고    scopus 로고
    • Structural requirements for basolateral sorting of the human transferrin receptor in the biosynthetic and endocytic pathways of Madin-Darby canine kidney cells
    • Odorizzi, G., and I.S. Trowbridge. 1997. Structural requirements for basolateral sorting of the human transferrin receptor in the biosynthetic and endocytic pathways of Madin-Darby canine kidney cells. J. Cell Biol. 137:1255-1264.
    • (1997) J. Cell Biol. , vol.137 , pp. 1255-1264
    • Odorizzi, G.1    Trowbridge, I.S.2
  • 43
    • 0023897690 scopus 로고
    • The submembraneous location of p11 and its interaction with the p36 substrate of pp60 src kinase in situ
    • Osborn, M., N. Johnsson, J. Wehland, and K. Weber. 1988. The submembraneous location of p11 and its interaction with the p36 substrate of pp60 src kinase in situ. Exp. Cell Res. 175:81-96.
    • (1988) Exp. Cell Res. , vol.175 , pp. 81-96
    • Osborn, M.1    Johnsson, N.2    Wehland, J.3    Weber, K.4
  • 44
    • 0028057494 scopus 로고
    • Ultrastructural localization of gangliosides; GM1 is concentrated in caveolae
    • Parton, R.G. 1994. Ultrastructural localization of gangliosides; GM1 is concentrated in caveolae. J. Histochem. Cytochem. 42:155-166.
    • (1994) J. Histochem. Cytochem. , vol.42 , pp. 155-166
    • Parton, R.G.1
  • 45
  • 46
    • 0029147426 scopus 로고
    • Digging into caveolae
    • Parton, R.G., and K. Simons. 1995. Digging into caveolae. Science. 269:1398-1399.
    • (1995) Science , vol.269 , pp. 1398-1399
    • Parton, R.G.1    Simons, K.2
  • 47
    • 0029665631 scopus 로고    scopus 로고
    • Fc epsilon RI-mediated association of 6-micron beads with RBL-2H3 mast cells results in exclusion of signaling proteins from the forming phagosome and abrogation of normal downstream signaling
    • Pierini, L., D. Holowka, and B. Baird. 1996. Fc epsilon RI-mediated association of 6-micron beads with RBL-2H3 mast cells results in exclusion of signaling proteins from the forming phagosome and abrogation of normal downstream signaling. J. Cell Biol. 134:1427-1439.
    • (1996) J. Cell Biol. , vol.134 , pp. 1427-1439
    • Pierini, L.1    Holowka, D.2    Baird, B.3
  • 48
    • 0028145334 scopus 로고
    • Signals determining protein tyrosine kinase and glycosyl-phosphatidyl-anchored protein targeting to a glycolipid-enriched membrane fraction
    • Rodgers, W., B. Crise, and J.K. Rose. 1994. Signals determining protein tyrosine kinase and glycosyl-phosphatidyl-anchored protein targeting to a glycolipid-enriched membrane fraction. Mol. Cell. Biol. 14:5384-5391.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 5384-5391
    • Rodgers, W.1    Crise, B.2    Rose, J.K.3
  • 49
    • 0024315423 scopus 로고
    • Morphogenesis of the polarized epithelial cell phenotype
    • Rodriguez-Boulan, E., and W.J. Nelson. 1989. Morphogenesis of the polarized epithelial cell phenotype. Science. 245:718-725.
    • (1989) Science , vol.245 , pp. 718-725
    • Rodriguez-Boulan, E.1    Nelson, W.J.2
  • 50
    • 0030747392 scopus 로고    scopus 로고
    • The role of lipid signaling in constitutive membrane transport
    • Roth, M.G., and P.C. Sternweis. 1997. The role of lipid signaling in constitutive membrane transport. Curr. Opin. Cell Biol. 9:519-526.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 519-526
    • Roth, M.G.1    Sternweis, P.C.2
  • 51
    • 0347593587 scopus 로고    scopus 로고
    • Bone-resorbing osteoclasts reveal a dynamic division of basal plasma membrane into two different domains
    • Salo, J., K. Metsikkö, H. Palokangas, P. Lehenkari, and H.K. Väänänen. 1996. Bone-resorbing osteoclasts reveal a dynamic division of basal plasma membrane into two different domains. J. Cell Sci. 109:301-307.
    • (1996) J. Cell Sci. , vol.109 , pp. 301-307
    • Salo, J.1    Metsikkö, K.2    Palokangas, H.3    Lehenkari, P.4    Väänänen, H.K.5
  • 52
    • 0026058545 scopus 로고
    • Cholesterol-induced fluid-phase immiscibility in membranes
    • Sankaram, M.B., and T.E. Thompson. 1991. Cholesterol-induced fluid-phase immiscibility in membranes. Proc. Natl. Acad. Sci. USA. 88:8686-8690.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 8686-8690
    • Sankaram, M.B.1    Thompson, T.E.2
  • 53
    • 0030804183 scopus 로고    scopus 로고
    • Interaction of influenza virus hemagglutinin with sphingolipid-cholesterol membrane domains via its transmembrane domains
    • Scheiffele, P., M.G. Roth, and K. Simons. 1997. Interaction of influenza virus hemagglutinin with sphingolipid-cholesterol membrane domains via its transmembrane domains. EMBO (Eur. Mol. Biol. Organ.) J. 16:5501-5508.
    • (1997) EMBO (Eur. Mol. Biol. Organ.) J. , vol.16 , pp. 5501-5508
    • Scheiffele, P.1    Roth, M.G.2    Simons, K.3
  • 54
    • 0028151351 scopus 로고
    • Interactions between saturated acyl chains confer detergent resistance to lipids and glycosylphosphatidylinositol (GPI)-anchored proteins: GPI-anchored proteins in liposomes and cells show similar behavior
    • Schroeder, R., E. London, and D. Brown. 1994. Interactions between saturated acyl chains confer detergent resistance to lipids and glycosylphosphatidylinositol (GPI)-anchored proteins: GPI-anchored proteins in liposomes and cells show similar behavior. Proc. Natl. Acad. Sci. USA. 91:12130-12134.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12130-12134
    • Schroeder, R.1    London, E.2    Brown, D.3
  • 55
    • 0028175989 scopus 로고
    • Cysteine(3) of Src family protein tyrosine kinases determines palmitoylation and localization in caveolae
    • Shenoy-Scaria, A.M., D.J. Dietzen, J. Kwong, D.C. Link, and D.M. Lublin. 1994. Cysteine(3) of Src family protein tyrosine kinases determines palmitoylation and localization in caveolae. J. Cell Biol. 126:353-363.
    • (1994) J. Cell Biol. , vol.126 , pp. 353-363
    • Shenoy-Scaria, A.M.1    Dietzen, D.J.2    Kwong, J.3    Link, D.C.4    Lublin, D.M.5
  • 56
    • 0030949124 scopus 로고    scopus 로고
    • Sphingolipid-cholesterol rafts in membrane trafficking and signalling
    • Simons, K., and E. Ikonen. 1997. Sphingolipid-cholesterol rafts in membrane trafficking and signalling. Nature. 387:569-572.
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 57
    • 0024547523 scopus 로고
    • Differential extractability of influenza virus hemagglutinin during intracellular transport in polarized epithelial cells and nonpolar fibroblasts
    • Skibbens, J.E., M.G. Roth, and K.S. Matlin. 1989. Differential extractability of influenza virus hemagglutinin during intracellular transport in polarized epithelial cells and nonpolar fibroblasts. J. Cell Biol. 108:821-832.
    • (1989) J. Cell Biol. , vol.108 , pp. 821-832
    • Skibbens, J.E.1    Roth, M.G.2    Matlin, K.S.3
  • 58
    • 0021749841 scopus 로고
    • Direct visualization of redistribution and capping of fluorescent gangliosides on lymphocytes
    • Spiegel, S., S. Kassis, M. Wilchek, and P.H. Fishman. 1984. Direct visualization of redistribution and capping of fluorescent gangliosides on lymphocytes. J. Cell Biol. 99:1575-1581.
    • (1984) J. Cell Biol. , vol.99 , pp. 1575-1581
    • Spiegel, S.1    Kassis, S.2    Wilchek, M.3    Fishman, P.H.4
  • 59
    • 0028352175 scopus 로고
    • Large-scale co-aggregation of fluorescent lipid probes with cell surface proteins
    • Thomas, J.L., D. Holowka, B. Baird, and W.W. Webb. 1994. Large-scale co-aggregation of fluorescent lipid probes with cell surface proteins. J. Cell Biol. 125: 795-802.
    • (1994) J. Cell Biol. , vol.125 , pp. 795-802
    • Thomas, J.L.1    Holowka, D.2    Baird, B.3    Webb, W.W.4
  • 60
    • 0027180191 scopus 로고
    • Phase topology and percolation in multiphase bilayers: Is the biological membrane a domain mosaic?
    • Vaz, W.L., and P.F. Almeida. 1993. Phase topology and percolation in multiphase bilayers: is the biological membrane a domain mosaic? Curr. Opin. Struct. Biol. 3:482-488.
    • (1993) Curr. Opin. Struct. Biol. , vol.3 , pp. 482-488
    • Vaz, W.L.1    Almeida, P.F.2
  • 61
    • 0025153020 scopus 로고
    • Distinct transport vesicles mediate the delivery of plasma membrane proteins to the apical and basolateral domains of MDCK cells
    • Wandinger-Ness, A., M.K. Bennet, C. Antony, and K. Simons. 1990. Distinct transport vesicles mediate the delivery of plasma membrane proteins to the apical and basolateral domains of MDCK cells. J. Cell Biol. 111:987-1000.
    • (1990) J. Cell Biol. , vol.111 , pp. 987-1000
    • Wandinger-Ness, A.1    Bennet, M.K.2    Antony, C.3    Simons, K.4
  • 62
    • 0031034485 scopus 로고    scopus 로고
    • Saturation of the endocytic pathway for the transferrin receptor does not affect the endocytosis of the epidermal growth factor receptor
    • Warren, R.A., F.A. Green, and C.A. Enns. 1997. Saturation of the endocytic pathway for the transferrin receptor does not affect the endocytosis of the epidermal growth factor receptor. J. Biol. Chem. 272:2116-2121.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2116-2121
    • Warren, R.A.1    Green, F.A.2    Enns, C.A.3
  • 63
    • 0030774609 scopus 로고    scopus 로고
    • Apical targeting in polarised cells: There's more afloat than rafts
    • Weimbs, T., S.H. Low, S.J. Chapin, and K. Mostov. 1997. Apical targeting in polarised cells: there's more afloat than rafts. Trends Cell Biol. 7:393-399.
    • (1997) Trends Cell Biol. , vol.7 , pp. 393-399
    • Weimbs, T.1    Low, S.H.2    Chapin, S.J.3    Mostov, K.4
  • 64
    • 0027941253 scopus 로고
    • Lipid domains in model and biological membranes
    • Welti, R., and M. Glaser. 1994. Lipid domains in model and biological membranes. Chem. Phys. Lipids. 73:121-137.
    • (1994) Chem. Phys. Lipids , vol.73 , pp. 121-137
    • Welti, R.1    Glaser, M.2
  • 65
    • 0030613520 scopus 로고    scopus 로고
    • Pamitoylation of p59fyn is reversible and sufficient for plasma membrane association
    • Wolven, A., H. Okamura, Y. Rosenblatt, and M.D. Resh. 1997. Pamitoylation of p59fyn is reversible and sufficient for plasma membrane association. Mol. Biol. Cell. 8:1159-1173.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1159-1173
    • Wolven, A.1    Okamura, H.2    Rosenblatt, Y.3    Resh, M.D.4
  • 66
    • 0029879919 scopus 로고    scopus 로고
    • Different biosynthetic transport routes to the plasma membrane in BHK and CHO cells
    • Yoshimori, T., P. Keller, G.M. Roth, and K. Simons. 1996. Different biosynthetic transport routes to the plasma membrane in BHK and CHO cells. J. Cell Biol. 133:247-256.
    • (1996) J. Cell Biol. , vol.133 , pp. 247-256
    • Yoshimori, T.1    Keller, P.2    Roth, G.M.3    Simons, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.