메뉴 건너뛰기




Volumn 387, Issue 6633, 1997, Pages 569-572

Functional rafts in cell membranes

Author keywords

[No Author keywords available]

Indexed keywords

CHOLESTEROL; SPHINGOLIPID;

EID: 0030949124     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/42408     Document Type: Review
Times cited : (8446)

References (67)
  • 1
    • 0015514472 scopus 로고
    • The fluid mosaic model of the structure of cell membranes
    • Singer, S. J. & Nicolson, G. L. The fluid mosaic model of the structure of cell membranes. Science 175, 720-731 (1972).
    • (1972) Science , vol.175 , pp. 720-731
    • Singer, S.J.1    Nicolson, G.L.2
  • 2
    • 0024448087 scopus 로고
    • Lipid traffic in animal cells
    • van Meer, G. Lipid traffic in animal cells. Annu. Rev. Cell Biol. 5, 247-275 (1989).
    • (1989) Annu. Rev. Cell Biol. , vol.5 , pp. 247-275
    • Van Meer, G.1
  • 3
    • 0030222116 scopus 로고    scopus 로고
    • Cell surface organization by the membrane skeleton
    • Kusumi, A. & Sako, Y. Cell surface organization by the membrane skeleton. Curr. Opin. Cell Biol. 8, 566-574 (1996).
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 566-574
    • Kusumi, A.1    Sako, Y.2
  • 4
    • 0024315423 scopus 로고
    • Morphogenesis of the polarized epithelial cell phenotype
    • Rodriguez-Boulan, E. & Nelson, W. J. Morphogenesis of the polarized epithelial cell phenotype. Science 245, 718-725 (1989).
    • (1989) Science , vol.245 , pp. 718-725
    • Rodriguez-Boulan, E.1    Nelson, W.J.2
  • 5
    • 0023788823 scopus 로고
    • Lipid sorting in epithelial cells
    • Simons, K. & van Meer, G. Lipid sorting in epithelial cells. Biochemistry 27, 6197-6202 (1988).
    • (1988) Biochemistry , vol.27 , pp. 6197-6202
    • Simons, K.1    Van Meer, G.2
  • 6
    • 0007544439 scopus 로고    scopus 로고
    • MDR1 P-glycoprotein is a lipid translocase of broad specificity, while M P-glycoprotein specifically translocates phosphatidylcholine
    • van Helvoort, A. et al. MDR1 P-glycoprotein is a lipid translocase of broad specificity, while M P-glycoprotein specifically translocates phosphatidylcholine. Cell 87, 507-518 (1996).
    • (1996) Cell , vol.87 , pp. 507-518
    • Van Helvoort, A.1
  • 7
    • 0026512314 scopus 로고
    • Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface
    • Brown, D. & Rose, J. Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface. Cell 68, 533-544 (1992).
    • (1992) Cell , vol.68 , pp. 533-544
    • Brown, D.1    Rose, J.2
  • 8
    • 0030222108 scopus 로고    scopus 로고
    • Caveolae and caveolins
    • Parton, R. G. Caveolae and caveolins. Curr. Opin. Cell Biol. 8, 542-548 (1996).
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 542-548
    • Parton, R.G.1
  • 9
    • 0023449563 scopus 로고
    • Ligands internalized through coated or non-coated invaginations follow a common intracellular pathway
    • Tran, D. J., Carpentier, J. L., Sawano, F., Gorden, P. & Orci, L. Ligands internalized through coated or non-coated invaginations follow a common intracellular pathway. Proc. Natl Acad. Sci. USA 84, 7957-7961 (1987).
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 7957-7961
    • Tran, D.J.1    Carpentier, J.L.2    Sawano, F.3    Gorden, P.4    Orci, L.5
  • 10
    • 0025695634 scopus 로고
    • Cholesterol controls the clustering of the glycophospholipid-anchored membrane receptor for 5-methyltetrahydrofolate
    • Rothberg, K. G., Ying, Y. S., Kamen, B. A. & Anderson, R. G. W. Cholesterol controls the clustering of the glycophospholipid-anchored membrane receptor for 5-methyltetrahydrofolate. J. Cell Biol. 111, 2931-2938 (1990).
    • (1990) J. Cell Biol. , vol.111 , pp. 2931-2938
    • Rothberg, K.G.1    Ying, Y.S.2    Kamen, B.A.3    Anderson, R.G.W.4
  • 11
    • 0022551377 scopus 로고
    • Specific binding sites for albumin restricted to plasmalemmal vesicles of continuous capillary endothelium; receptor-mediated transcytosis
    • Ghitescu, L., Fixman, A., Simionescu, M. & Simionescu, N. Specific binding sites for albumin restricted to plasmalemmal vesicles of continuous capillary endothelium; receptor-mediated transcytosis. J. Cell Biol. 102, 1304-1311 (1986).
    • (1986) J. Cell Biol. , vol.102 , pp. 1304-1311
    • Ghitescu, L.1    Fixman, A.2    Simionescu, M.3    Simionescu, N.4
  • 12
    • 0027414646 scopus 로고
    • Caveolae and sorting in the Trans-Golgi network of epithelial cells
    • Dupree, P., Parton, R. G., Raposo, G., Kurzchalia, T. V. & Simons, K. Caveolae and sorting in the Trans-Golgi network of epithelial cells. EMBO J. 12, 1597-1605 (1993).
    • (1993) EMBO J. , vol.12 , pp. 1597-1605
    • Dupree, P.1    Parton, R.G.2    Raposo, G.3    Kurzchalia, T.V.4    Simons, K.5
  • 13
    • 0028837910 scopus 로고
    • Glycosphingolipid fatty acid arrangement in phospholipid bilayers: Cholesterol effects
    • Morrow, M. R., Singh, D., Lu, D. & Grant, C. W. M. Glycosphingolipid fatty acid arrangement in phospholipid bilayers: cholesterol effects. Biophysical J. 68, 179-186 (1995).
    • (1995) Biophysical J. , vol.68 , pp. 179-186
    • Morrow, M.R.1    Singh, D.2    Lu, D.3    Grant, C.W.M.4
  • 14
    • 0028009878 scopus 로고
    • Do the long fatty acid chains of sphingolipids interdigitate across the center of bilayer of shorter chain symmetric phospholipids?
    • Boggs, J. M. & Koshy, K. M. Do the long fatty acid chains of sphingolipids interdigitate across the center of bilayer of shorter chain symmetric phospholipids? Biochim. Biophys. Acta 1189, 233-241 (1994).
    • (1994) Biochim. Biophys. Acta , vol.1189 , pp. 233-241
    • Boggs, J.M.1    Koshy, K.M.2
  • 15
    • 0029147426 scopus 로고
    • Digging into caveolae
    • Parton, R. G. & Simons, K. Digging into caveolae. Science 269, 1398-1399 (1995).
    • (1995) Science , vol.269 , pp. 1398-1399
    • Parton, R.G.1    Simons, K.2
  • 16
    • 0028151351 scopus 로고
    • Interactions between saturated acyl chains confer detergent resistance on lipids and glycosylphosphatidylinositol(GPI)-anchored proteins: GPI-anchored proteins in liposomes and cells show similar behavior
    • Schroeder, R., London, E. & Brown, D. Interactions between saturated acyl chains confer detergent resistance on 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).
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 12130-12134
    • Schroeder, R.1    London, E.2    Brown, D.3
  • 17
    • 0024547523 scopus 로고
    • Differential extractibility of influenza virus hemagglutinin during intracellular transport in polarized epithelial cells and nonpolar fibroblasts
    • Skibbens, J. E., Roth, M. G. & Matlin, K. S. Differential extractibility of influenza virus hemagglutinin during intracellular transport in polarized epithelial cells and nonpolar fibroblasts. J. Cell Biol. 108, 821-832 (1989).
    • (1989) J. Cell Biol. , vol.108 , pp. 821-832
    • Skibbens, J.E.1    Roth, M.G.2    Matlin, K.S.3
  • 18
    • 0027275642 scopus 로고
    • Signal transducing molecules and GPI-linked proteins from a caveolin-rich insoluble complex in MDCK cells
    • Sargiacomo, M., Sudol, M., Tang, Z. & Lisanti, M. P. Signal transducing molecules and GPI-linked proteins from a caveolin-rich insoluble complex in MDCK cells. J. Cell Biol. 122, 789-807 (1993).
    • (1993) J. Cell Biol. , vol.122 , pp. 789-807
    • Sargiacomo, M.1    Sudol, M.2    Tang, Z.3    Lisanti, M.P.4
  • 19
    • 0027970448 scopus 로고
    • Detergent-insoluble glycolipid microdomains in lymphocytes in the absence of caveolae
    • Fra, A. M., Williamson, E., Simons, K. & Parton, R. G. Detergent-insoluble glycolipid microdomains in lymphocytes in the absence of caveolae. J. Biol. Chem. 269, 30745-30748 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 30745-30748
    • Fra, A.M.1    Williamson, E.2    Simons, K.3    Parton, R.G.4
  • 20
    • 0028955507 scopus 로고
    • A transferrin-like GPI-linked iron-binding protein in detergent-insoluble non-caveolar microdomains at the apical surface of fetal intestinal epithelial cells
    • Danielsen, E. M. A transferrin-like GPI-linked iron-binding protein in detergent-insoluble non-caveolar microdomains at the apical surface of fetal intestinal epithelial cells. Biochemistry 34, 1596-1605 (1995).
    • (1995) Biochemistry , vol.34 , pp. 1596-1605
    • Danielsen, E.M.1
  • 21
    • 0028935780 scopus 로고
    • Protein lipidation in cell signalling
    • Casey, P. J. Protein lipidation in cell signalling. Science 268, 221-225 (1995).
    • (1995) Science , vol.268 , pp. 221-225
    • Casey, P.J.1
  • 22
    • 0027468760 scopus 로고
    • Detergent insolubility of alkaline phosphatase during biosynthetic transport and endocytosis. Role of cholesterol
    • Cerneus, D. P., Ueffing, E., Posthuma, G., Strous, G. J. & van der Ende, A. Detergent insolubility of alkaline phosphatase during biosynthetic transport and endocytosis. Role of cholesterol. J. Biol. Chem. 268, 3150-3155 (1993).
    • (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
  • 23
    • 0028947029 scopus 로고
    • Both sphingolipids and cholesterol participate in the detergent-insolubility of alkaline phosphatase, a glycosyl-phosphatidylinositol anchored protein in mammalian cells
    • Hanada, K., Nishijima, M., Akamatsu, Y. & Pagano, R. E. Both sphingolipids and cholesterol participate in the detergent-insolubility of alkaline phosphatase, a glycosyl-phosphatidylinositol anchored protein in mammalian cells. J. Biol. Chem. 270, 6254-6260 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 6254-6260
    • Hanada, K.1    Nishijima, M.2    Akamatsu, Y.3    Pagano, R.E.4
  • 24
    • 0029894832 scopus 로고    scopus 로고
    • Glycosylphosphatidytinositol-anchored protein after LDL-deprivation of MDCK cells
    • Hannan, L. A. & Edidin, M. Glycosylphosphatidytinositol-anchored protein after LDL-deprivation of MDCK cells. J. Cell Biol. 133, 1265-1276 (1996).
    • (1996) J. Cell Biol. , vol.133 , pp. 1265-1276
    • Hannan, L.A.1    Edidin, M.2
  • 25
    • 0029839393 scopus 로고    scopus 로고
    • Transmembrane domain of influenza virus neuraminidase, a type II protein, possesses an apical sorting signal in polarized MDCK cells
    • Kundu, A., Avalos, R. T., Sanderson, C. M. & Nayak, D. P. Transmembrane domain of influenza virus neuraminidase, a type II protein, possesses an apical sorting signal in polarized MDCK cells. J. Virol. 70, 6508-6515 (1996).
    • (1996) J. Virol. , vol.70 , pp. 6508-6515
    • Kundu, A.1    Avalos, R.T.2    Sanderson, C.M.3    Nayak, D.P.4
  • 26
    • 0028885614 scopus 로고
    • VIP21-caveolin is a cholesterol-binding protein
    • Murata, M. et al. VIP21-caveolin is a cholesterol-binding protein. Proc. Natl Acad. Sci. USA 92, 10339-10343 (1995).
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 10339-10343
    • Murata, M.1
  • 27
    • 0000441994 scopus 로고
    • Polarized apical distribution of glycosyl-phosphatidylinositol-anchored proteins in a renal epithelial cell line
    • Lisanti, M. P., Sargiacomo, M., Graeve, L., Saltiel, A. & Rodriguez-Boulan, E. Polarized apical distribution of glycosyl-phosphatidylinositol-anchored proteins in a renal epithelial cell line. Proc. Natl Acad. Sci. USA 85, 9557-9561 (1989).
    • (1989) Proc. Natl Acad. Sci. USA , vol.85 , pp. 9557-9561
    • Lisanti, M.P.1    Sargiacomo, M.2    Graeve, L.3    Saltiel, A.4    Rodriguez-Boulan, E.5
  • 28
    • 0028810337 scopus 로고
    • N-glycans as apical sorting signals in epithelial cells
    • Scheiffele, P., Peränen, J. & Simons, K. N-glycans as apical sorting signals in epithelial cells. Nature 378, 96-98 (1995).
    • (1995) Nature , vol.378 , pp. 96-98
    • Scheiffele, P.1    Peränen, J.2    Simons, K.3
  • 29
    • 0028209329 scopus 로고
    • VIP36, a novel component of glycolipid rafts and exocytic carrier vesicles in epithelial cells
    • Fiedler, K., Parton, R. G., Kellner, R., Etzold, T. & Simons, K. VIP36, a novel component of glycolipid rafts and exocytic carrier vesicles in epithelial cells. EMBO J. 13, 1729-1740 (1994).
    • (1994) EMBO J. , vol.13 , pp. 1729-1740
    • Fiedler, K.1    Parton, R.G.2    Kellner, R.3    Etzold, T.4    Simons, K.5
  • 30
    • 0028068273 scopus 로고
    • Mechanisms of cell polarity: Sorting and transport in epithelial cells
    • Matter, K. & Mellman, I. Mechanisms of cell polarity: Sorting and transport in epithelial cells. Curr. Opin. Cell. Biol. 6, 545-554 (1994).
    • (1994) Curr. Opin. Cell. Biol. , vol.6 , pp. 545-554
    • Matter, K.1    Mellman, I.2
  • 31
    • 0029062772 scopus 로고
    • Different requirements for NSF, SNAP, and Rab proteins in apical and basolateral transport in MDCK cells
    • Ikonen, E., Tagaya, M., Ullrich, O., Montecucco, C. & Simons, K. Different requirements for NSF, SNAP, and Rab proteins in apical and basolateral transport in MDCK cells. Cell 81, 1-20 (1995).
    • (1995) Cell , vol.81 , pp. 1-20
    • Ikonen, E.1    Tagaya, M.2    Ullrich, O.3    Montecucco, C.4    Simons, K.5
  • 32
    • 0029670289 scopus 로고    scopus 로고
    • Protein sorting by transport vesicles
    • Rothman, J. E. & Wieland, F. T. Protein sorting by transport vesicles. Science 272, 227-234 (1996).
    • (1996) Science , vol.272 , pp. 227-234
    • Rothman, J.E.1    Wieland, F.T.2
  • 33
    • 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., Xu, H., Shield, D. & Rodriguez-Boulan, E. 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).
    • (1996) J. Cell Biol. , vol.133 , pp. 543-558
    • Müsch, A.1    Xu, H.2    Shield, D.3    Rodriguez-Boulan, E.4
  • 34
    • 0029879919 scopus 로고    scopus 로고
    • Different biosynthetic transport routes to the plasma membrane in BHK and CHO cells
    • Yoshimori, T., Keller, P., Roth, M. G. & Simons, K. Different biosynthetic transport routes to the plasma membrane in BHK and CHO cells. J. Cell Biol. 133, 247-256 (1996).
    • (1996) J. Cell Biol. , vol.133 , pp. 247-256
    • Yoshimori, T.1    Keller, P.2    Roth, M.G.3    Simons, K.4
  • 35
    • 0028809826 scopus 로고
    • Involvement of detergent-insoluble complexes in the intracellular transport of intestinal brush border enzymes
    • Danielsen, E. M. & van Deurs, B. Involvement of detergent-insoluble complexes in the intracellular transport of intestinal brush border enzymes. J. Cell Biol. 131, 939-950 (1995).
    • (1995) J. Cell Biol. , vol.131 , pp. 939-950
    • Danielsen, E.M.1    Van Deurs, B.2
  • 36
    • 0027997787 scopus 로고
    • Filipin-sensitive caveolae-mediated transport in endothelium: Reduced transcytosis, scavenger endocytosis, and capillary permeability of select macromolecules
    • Schnitzer, J. E., Oh, P., Pinney, E. & Allard, J. Filipin-sensitive caveolae-mediated transport in endothelium: reduced transcytosis, scavenger endocytosis, and capillary permeability of select macromolecules. J. Cell Biol. 127, 1217-1232 (1994).
    • (1994) J. Cell Biol. , vol.127 , pp. 1217-1232
    • Schnitzer, J.E.1    Oh, P.2    Pinney, E.3    Allard, J.4
  • 37
    • 0026545612 scopus 로고
    • Potocytosis: Sequestration and transport of small molecules by caveolae
    • Anderson, R. G. W., Kamen, B. A., Rothberg, K. G. & Lacey, S. W. Potocytosis: sequestration and transport of small molecules by caveolae. Science 255, 410-411 (1992).
    • (1992) Science , vol.255 , pp. 410-411
    • Anderson, R.G.W.1    Kamen, B.A.2    Rothberg, K.G.3    Lacey, S.W.4
  • 38
    • 0029987340 scopus 로고    scopus 로고
    • Bound simian virus 40 translocates to caveolin-enriched membrane domains, and its entry is inhibited by drugs that selectively disrupt caveolae
    • Anderson, H. A., Chen, Y. & Norkin, L. C. Bound simian virus 40 translocates to caveolin-enriched membrane domains, and its entry is inhibited by drugs that selectively disrupt caveolae, Mol. Biol. Cell 7, 1825-1834 (1996).
    • (1996) Mol. Biol. Cell , vol.7 , pp. 1825-1834
    • Anderson, H.A.1    Chen, Y.2    Norkin, L.C.3
  • 39
    • 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. et al. 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).
    • (1996) J. Cell Biol. , vol.133 , pp. 791-799
    • Deckert, M.1
  • 40
    • 0026531638 scopus 로고
    • Plasma membrane protein sorting in polarized epithelial cells
    • Mostov, K. E., Apodaca, G., Aroeti, B. & Okamoto, C. Plasma membrane protein sorting in polarized epithelial cells. J. Cell Biol. 116, 577-583 (1992).
    • (1992) J. Cell Biol. , vol.116 , pp. 577-583
    • Mostov, K.E.1    Apodaca, G.2    Aroeti, B.3    Okamoto, C.4
  • 41
    • 0026979979 scopus 로고
    • The biogenesis of cell surface polarity in epithelial cells and neurons
    • Simons, K, et al. The biogenesis of cell surface polarity in epithelial cells and neurons. Cold Spring Harbor Symp. Quant. Biol. LVII, 611-619 (1992).
    • (1992) Cold Spring Harbor Symp. Quant. Biol. , vol.57 , pp. 611-619
    • Simons, K.1
  • 42
    • 0027193569 scopus 로고
    • The oligodendrocyte and its many cellular processes
    • Pfeiffer, S. E., Warrington, A. E. & Bansal, R. The oligodendrocyte and its many cellular processes. Trends Cell Biol. 3, 191-197 (1993).
    • (1993) Trends Cell Biol. , vol.3 , pp. 191-197
    • Pfeiffer, S.E.1    Warrington, A.E.2    Bansal, R.3
  • 43
    • 0029819793 scopus 로고    scopus 로고
    • Rab8 promotes polarized membrane transport through reorganization of actin and microtubules in fibroblasts
    • Peranen, J., Auvinen, P., Virta, H., Wepf, R. & Simons, K. Rab8 promotes polarized membrane transport through reorganization of actin and microtubules in fibroblasts. J. Cell Biol. 135, 153-167 (1996).
    • (1996) J. Cell Biol. , vol.135 , pp. 153-167
    • Peranen, J.1    Auvinen, P.2    Virta, H.3    Wepf, R.4    Simons, K.5
  • 44
    • 0027443234 scopus 로고
    • Caveolae: Where incoming and outgoing messengers meet
    • Anderson, R. G. W. Caveolae: where incoming and outgoing messengers meet. Proc. Natl Acad. Sci. USA 90, 10909-10913 (1993).
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 10909-10913
    • Anderson, R.G.W.1
  • 45
    • 0028285191 scopus 로고
    • Caveolaer, caveolin and caveolin-rich membrane domains: A signalling hypothesis
    • Lisanti, M. P., Scherer, P. E., Tang, Z. L. & Sargiacomo, M. Caveolaer, caveolin and caveolin-rich membrane domains: a signalling hypothesis. Trends Cell Biol. 4, 231-235 (1994).
    • (1994) Trends Cell Biol. , vol.4 , pp. 231-235
    • Lisanti, M.P.1    Scherer, P.E.2    Tang, Z.L.3    Sargiacomo, M.4
  • 46
    • 0029130692 scopus 로고
    • Isolation of phosphooligosaccharide/phosphoinositol glycan from caveolae and cytosol of insulin-stimulated cells
    • Parpal, S., Gustavsson, J. & Strålfors, P. Isolation of phosphooligosaccharide/phosphoinositol glycan from caveolae and cytosol of insulin-stimulated cells. J. Cell Biol. 131, 125-135 (1995).
    • (1995) J. Cell Biol. , vol.131 , pp. 125-135
    • Parpal, S.1    Gustavsson, J.2    Strålfors, P.3
  • 47
    • 0029075372 scopus 로고
    • Evidence for a regulated interaction between heterotrimeric G proteins and caveolin
    • Li, S. et al. Evidence for a regulated interaction between heterotrimeric G proteins and caveolin. J. Biol. Chem. 270, 15693-15701 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 15693-15701
    • Li, S.1
  • 48
    • 0029912981 scopus 로고    scopus 로고
    • Co-purification and direct interaciton of Ras with caveolin, an integral membrane protein of caveolae microdomains
    • Song, K. S. et al. Co-purification and direct interaciton of Ras with caveolin, an integral membrane protein of caveolae microdomains. J. Biol. Chem. 271, 9690-9697 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 9690-9697
    • Song, K.S.1
  • 49
    • 15844431258 scopus 로고    scopus 로고
    • Localization of epidermal growth factor-stimulated Ras/Raf-1 interaction to caveolae membrane
    • Mineo, C., James, G. L., Smart, E. J. & Anderson, R. G. Localization of epidermal growth factor-stimulated Ras/Raf-1 interaction to caveolae membrane. J. Biol. Chem. 217, 11930-11935 (1996).
    • (1996) J. Biol. Chem. , vol.217 , pp. 11930-11935
    • Mineo, C.1    James, G.L.2    Smart, E.J.3    Anderson, R.G.4
  • 50
    • 0029899011 scopus 로고    scopus 로고
    • Phosphoinositides and phosphoinositide-utilizing enzymes in detergent-insoluble lipid domains
    • Hope, H. R. & Pike, L. J. Phosphoinositides and phosphoinositide-utilizing enzymes in detergent-insoluble lipid domains. Mol. Biol. Cell 7, 843-851 (1996).
    • (1996) Mol. Biol. Cell , vol.7 , pp. 843-851
    • Hope, H.R.1    Pike, L.J.2
  • 51
    • 0027978352 scopus 로고
    • Identification of a distinct pool of sphingomyelin involved in the sphingomyelin cycle
    • Linardic, C. M. & Hannun, Y. A. Identification of a distinct pool of sphingomyelin involved in the sphingomyelin cycle. J. Biol. Chem. 269, 23530-23537 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 23530-23537
    • Linardic, C.M.1    Hannun, Y.A.2
  • 52
    • 0028784298 scopus 로고
    • Compartmentalized production of ceramide at the cell surface
    • Liu, P. & Anderson, R. G. W. Compartmentalized production of ceramide at the cell surface. J. Biol. Chem. 270, 27179-27185 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 27179-27185
    • Liu, P.1    Anderson, R.G.W.2
  • 53
    • 0028000605 scopus 로고
    • Sequestration of GPI-anchored proteins in caveolae triggered by cross-linking
    • Mayor, S., Rothberg, K. G. & Maxfield, F. R. Sequestration of GPI-anchored proteins in caveolae triggered by cross-linking. Science 264, 1948-1951 (1994).
    • (1994) Science , vol.264 , pp. 1948-1951
    • Mayor, S.1    Rothberg, K.G.2    Maxfield, F.R.3
  • 54
    • 0027999481 scopus 로고
    • 2-macroglobulin receptor/low density lipoprotein receptor-related protein
    • 2-macroglobulin receptor/low density lipoprotein receptor-related protein. J. Biol. Chem. 269, 25668-25676 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 25668-25676
    • Nykjaer, A.1
  • 55
    • 0028981284 scopus 로고
    • FcεRI-mediated recruitment of p53/56lyn to detergent-resistant membrane domains accompanies cellular signaling
    • Field, K. A., Holowka, D. & Baird, B. FcεRI-mediated recruitment of p53/56lyn to detergent-resistant membrane domains accompanies cellular signaling. Proc. Natl Acad. Sci. USA 92, 9201-9205 (1995).
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 9201-9205
    • Field, K.A.1    Holowka, D.2    Baird, B.3
  • 56
    • 0028812541 scopus 로고
    • Alteration of myometrial plasma membrane cholesterol content with β-cyclodextrin modulates the binding affinity of the oxytocin receptor
    • Klein, U., Gimpl, G. & Fahrenholz, F. Alteration of myometrial plasma membrane cholesterol content with β-cyclodextrin modulates the binding affinity of the oxytocin receptor. Biochemistry 34, 13784-13793 (1995).
    • (1995) Biochemistry , vol.34 , pp. 13784-13793
    • Klein, U.1    Gimpl, G.2    Fahrenholz, F.3
  • 58
    • 0027892019 scopus 로고
    • Cholesterol and the Golgi apparatus
    • Bretscher, M. S. & Munro, S. Cholesterol and the Golgi apparatus. Science 261, 1280-1281 (1993).
    • (1993) Science , vol.261 , pp. 1280-1281
    • Bretscher, M.S.1    Munro, S.2
  • 59
    • 0025118707 scopus 로고
    • Organization of glycosphingolipids in phosphatidylcholine bilayers: Use of antibody molecules and Fab fragments as morphologic markers
    • Rock, P., Allietta, M., Young, W. W. Jr, Thompson, T. E. & Tillack, T. W. Organization of glycosphingolipids in phosphatidylcholine bilayers: use of antibody molecules and Fab fragments as morphologic markers. Biochemistry 29, 8484-8490 (1990).
    • (1990) Biochemistry , vol.29 , pp. 8484-8490
    • Rock, P.1    Allietta, M.2    Young Jr., W.W.3    Thompson, T.E.4    Tillack, T.W.5
  • 60
    • 0021749841 scopus 로고
    • Direct visualization of redistribution and cappiang of fluorescent gangliosides on lymphocytes
    • Spiegel, S., Kassis, S., Wilchek, M. & Fishman, P. H. Direct visualization of redistribution and cappiang of fluorescent gangliosides on lymphocytes. J. Cell Biol. 99, 1575-1581 (1984).
    • (1984) J. Cell Biol. , vol.99 , pp. 1575-1581
    • Spiegel, S.1    Kassis, S.2    Wilchek, M.3    Fishman, P.H.4
  • 61
    • 0023239664 scopus 로고
    • Lipid intermolecular hydrogen bonding: Influence on structural organization and membrane function
    • Boggs, J. M. Lipid intermolecular hydrogen bonding: influence on structural organization and membrane function. Biochim. Biophys. Acta 906, 353-404 (1987).
    • (1987) Biochim. Biophys. Acta , vol.906 , pp. 353-404
    • Boggs, J.M.1
  • 62
    • 0029945751 scopus 로고    scopus 로고
    • Cholesterol-induced interfacial area condensations of galactosylceramides and sphingomyelins with identical acyl chains
    • Smaby, J. M., Momsen, M., Kulkarni, V. S. & Brown, R. E. Cholesterol-induced interfacial area condensations of galactosylceramides and sphingomyelins with identical acyl chains. Biochemistry 35, 5696-5704 (1996).
    • (1996) Biochemistry , vol.35 , pp. 5696-5704
    • Smaby, J.M.1    Momsen, M.2    Kulkarni, V.S.3    Brown, R.E.4
  • 63
    • 0026511732 scopus 로고
    • Cholesterol modulation of lipid intermixing in phospholipid and glycosphingolipid mixtures. Evaluation using fluorescent lipid probes and brominated lipid quenchers
    • Silvius, J. R. Cholesterol modulation of lipid intermixing in phospholipid and glycosphingolipid mixtures. Evaluation using fluorescent lipid probes and brominated lipid quenchers. Biochemistry 31, 3398-3408 (1992).
    • (1992) Biochemistry , vol.31 , pp. 3398-3408
    • Silvius, J.R.1
  • 64
    • 0025602953 scopus 로고
    • Interaction of cholesterol with various glycerophospholipids and sphingomyelin
    • Sankaram, M. B. & Thompson, T. E. Interaction of cholesterol with various glycerophospholipids and sphingomyelin. Biochemistry 29, 10670-10675 (1990).
    • (1990) Biochemistry , vol.29 , pp. 10670-10675
    • Sankaram, M.B.1    Thompson, T.E.2
  • 65
    • 0018632835 scopus 로고
    • Deuterium NMR studies of cerebroside-phospholipid bilayers
    • Neuringer, L. J., Sears, B. & Jungalwala, F. B. Deuterium NMR studies of cerebroside-phospholipid bilayers. Biochim. Biophys. Acta 558, 325-329 (1979).
    • (1979) Biochim. Biophys. Acta , vol.558 , pp. 325-329
    • Neuringer, L.J.1    Sears, B.2    Jungalwala, F.B.3
  • 66
    • 0028131711 scopus 로고
    • Evidence for regular distribution of sterols in liquid crystalline phosphatidylcholine bilayers
    • Chong, P.-L. Evidence for regular distribution of sterols in liquid crystalline phosphatidylcholine bilayers. Proc. Natl Acad. Sci. USA 91, 10069-10073 (1994).
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 10069-10073
    • Chong, P.-L.1
  • 67
    • 0028921025 scopus 로고
    • Annexin XIIIb: A novel epithelial specific annexin is implicated in vesicular traffic to the apical plasma membrane
    • Fiedler, K., Lafont, F., Parton, R. G. & Simons, K. Annexin XIIIb: A novel epithelial specific annexin is implicated in vesicular traffic to the apical plasma membrane. J. Cell Biol. 128, 1043-1053 (1995).
    • (1995) J. Cell Biol. , vol.128 , pp. 1043-1053
    • Fiedler, K.1    Lafont, F.2    Parton, R.G.3    Simons, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.