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Volumn 23, Issue 3, 2012, Pages 573-586

Lipid Sorting by Ceramide Structure from Plasma Membrane to ER for the Cholera Toxin Receptor Ganglioside GM1

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; CERAMIDE; CHOLESTEROL; FLOTILLIN PROTEIN; GANGLIOSIDE GM1; LIPID; MEMBRANE LIPID; MEMBRANE PROTEIN; UNCLASSIFIED DRUG;

EID: 84866034926     PISSN: 15345807     EISSN: 18781551     Source Type: Journal    
DOI: 10.1016/j.devcel.2012.08.002     Document Type: Article
Times cited : (111)

References (70)
  • 1
    • 0029923621 scopus 로고    scopus 로고
    • Influence of phospholipid chain length on verotoxin/globotriaosyl ceramide binding in model membranes: comparison of a supported bilayer film and liposomes
    • Arab S., Lingwood C.A. Influence of phospholipid chain length on verotoxin/globotriaosyl ceramide binding in model membranes: comparison of a supported bilayer film and liposomes. Glycoconj. J. 1996, 13:159-166.
    • (1996) Glycoconj. J. , vol.13 , pp. 159-166
    • Arab, S.1    Lingwood, C.A.2
  • 2
    • 6044235526 scopus 로고    scopus 로고
    • Trafficking of cholera toxin-ganglioside GM1 complex into Golgi and induction of toxicity depend on actin cytoskeleton
    • Badizadegan K., Wheeler H.E., Fujinaga Y., Lencer W.I. Trafficking of cholera toxin-ganglioside GM1 complex into Golgi and induction of toxicity depend on actin cytoskeleton. Am. J. Physiol. Cell Physiol. 2004, 287:C1453-C1462.
    • (2004) Am. J. Physiol. Cell Physiol. , vol.287
    • Badizadegan, K.1    Wheeler, H.E.2    Fujinaga, Y.3    Lencer, W.I.4
  • 4
    • 69449093833 scopus 로고    scopus 로고
    • Steric and not structure-specific factors dictate the endocytic mechanism of glycosylphosphatidylinositol-anchored proteins
    • Bhagatji P., Leventis R., Comeau J., Refaei M., Silvius J.R. Steric and not structure-specific factors dictate the endocytic mechanism of glycosylphosphatidylinositol-anchored proteins. J. Cell Biol. 2009, 186:615-628.
    • (2009) J. Cell Biol. , vol.186 , pp. 615-628
    • Bhagatji, P.1    Leventis, R.2    Comeau, J.3    Refaei, M.4    Silvius, J.R.5
  • 5
    • 0034063441 scopus 로고    scopus 로고
    • Lateral diffusion of membrane proteins in the presence of static and dynamic corrals: suggestions for appropriate observables
    • Brown F.L., Leitner D.M., McCammon J.A., Wilson K.R. Lateral diffusion of membrane proteins in the presence of static and dynamic corrals: suggestions for appropriate observables. Biophys. J. 2000, 78:2257-2269.
    • (2000) Biophys. J. , vol.78 , pp. 2257-2269
    • Brown, F.L.1    Leitner, D.M.2    McCammon, J.A.3    Wilson, K.R.4
  • 7
    • 80053634217 scopus 로고    scopus 로고
    • Gangliosides and the multiscale modulation of membrane structure
    • Cantù L., Del Favero E., Sonnino S., Prinetti A. Gangliosides and the multiscale modulation of membrane structure. Chem. Phys. Lipids 2011, 164:796-810.
    • (2011) Chem. Phys. Lipids , vol.164 , pp. 796-810
    • Cantù, L.1    Del Favero, E.2    Sonnino, S.3    Prinetti, A.4
  • 8
    • 34249090252 scopus 로고    scopus 로고
    • Cholesterol-sensitive Cdc42 activation regulates actin polymerization for endocytosis via the GEEC pathway
    • Chadda R., Howes M.T., Plowman S.J., Hancock J.F., Parton R.G., Mayor S. Cholesterol-sensitive Cdc42 activation regulates actin polymerization for endocytosis via the GEEC pathway. Traffic 2007, 8:702-717.
    • (2007) Traffic , vol.8 , pp. 702-717
    • Chadda, R.1    Howes, M.T.2    Plowman, S.J.3    Hancock, J.F.4    Parton, R.G.5    Mayor, S.6
  • 9
    • 0015795679 scopus 로고
    • Gangliosides and membrane receptors for cholera toxin
    • Cuatrecasas P. Gangliosides and membrane receptors for cholera toxin. Biochemistry 1973, 12:3558-3566.
    • (1973) Biochemistry , vol.12 , pp. 3558-3566
    • Cuatrecasas, P.1
  • 12
    • 0035168061 scopus 로고    scopus 로고
    • Targeting of Shiga toxin B-subunit to retrograde transport route in association with detergent-resistant membranes
    • Falguières T., Mallard F., Baron C., Hanau D., Lingwood C., Goud B., Salamero J., Johannes L. Targeting of Shiga toxin B-subunit to retrograde transport route in association with detergent-resistant membranes. Mol. Biol. Cell 2001, 12:2453-2468.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2453-2468
    • Falguières, T.1    Mallard, F.2    Baron, C.3    Hanau, D.4    Lingwood, C.5    Goud, B.6    Salamero, J.7    Johannes, L.8
  • 14
    • 38349014268 scopus 로고    scopus 로고
    • A syntaxin 10-SNARE complex distinguishes two distinct transport routes from endosomes to the trans-Golgi in human cells
    • Ganley I.G., Espinosa E., Pfeffer S.R. A syntaxin 10-SNARE complex distinguishes two distinct transport routes from endosomes to the trans-Golgi in human cells. J. Cell Biol. 2008, 180:159-172.
    • (2008) J. Cell Biol. , vol.180 , pp. 159-172
    • Ganley, I.G.1    Espinosa, E.2    Pfeffer, S.R.3
  • 15
    • 30344486984 scopus 로고    scopus 로고
    • Flotillin-1 defines a clathrin-independent endocytic pathway in mammalian cells
    • Glebov O.O., Bright N.A., Nichols B.J. Flotillin-1 defines a clathrin-independent endocytic pathway in mammalian cells. Nat. Cell Biol. 2006, 8:46-54.
    • (2006) Nat. Cell Biol. , vol.8 , pp. 46-54
    • Glebov, O.O.1    Bright, N.A.2    Nichols, B.J.3
  • 17
    • 78249272018 scopus 로고    scopus 로고
    • Sphingomyelin is important for the cellular entry and intracellular localization of Helicobacter pylori VacA
    • Gupta V.R., Wilson B.A., Blanke S.R. Sphingomyelin is important for the cellular entry and intracellular localization of Helicobacter pylori VacA. Cell. Microbiol. 2010, 12:1517-1533.
    • (2010) Cell. Microbiol. , vol.12 , pp. 1517-1533
    • Gupta, V.R.1    Wilson, B.A.2    Blanke, S.R.3
  • 18
    • 0037215494 scopus 로고    scopus 로고
    • Structure, organization, and function of glycosphingolipids in membrane
    • Hakomori S. Structure, organization, and function of glycosphingolipids in membrane. Curr. Opin. Hematol. 2003, 10:16-24.
    • (2003) Curr. Opin. Hematol. , vol.10 , pp. 16-24
    • Hakomori, S.1
  • 19
    • 18144417503 scopus 로고    scopus 로고
    • Crosslinking a lipid raft component triggers liquid ordered-liquid disordered phase separation in model plasma membranes
    • Hammond A.T., Heberle F.A., Baumgart T., Holowka D., Baird B., Feigenson G.W. Crosslinking a lipid raft component triggers liquid ordered-liquid disordered phase separation in model plasma membranes. Proc. Natl. Acad. Sci. USA 2005, 102:6320-6325.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 6320-6325
    • Hammond, A.T.1    Heberle, F.A.2    Baumgart, T.3    Holowka, D.4    Baird, B.5    Feigenson, G.W.6
  • 20
    • 77952132277 scopus 로고    scopus 로고
    • Dynamic sorting of lipids and proteins in membrane tubes with a moving phase boundary
    • Heinrich M., Tian A., Esposito C., Baumgart T. Dynamic sorting of lipids and proteins in membrane tubes with a moving phase boundary. Proc. Natl. Acad. Sci. USA 2010, 107:7208-7213.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 7208-7213
    • Heinrich, M.1    Tian, A.2    Esposito, C.3    Baumgart, T.4
  • 21
    • 58149201118 scopus 로고    scopus 로고
    • An introduction to critical points for biophysicists; observations of compositional heterogeneity in lipid membranes
    • Honerkamp-Smith A.R., Veatch S.L., Keller S.L. An introduction to critical points for biophysicists; observations of compositional heterogeneity in lipid membranes. Biochim. Biophys. Acta 2009, 1788:53-63.
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 53-63
    • Honerkamp-Smith, A.R.1    Veatch, S.L.2    Keller, S.L.3
  • 22
    • 33845901815 scopus 로고    scopus 로고
    • Lipid rafts: at a crossroad between cell biology and physics
    • Jacobson K., Mouritsen O.G., Anderson R.G. Lipid rafts: at a crossroad between cell biology and physics. Nat. Cell Biol. 2007, 9:7-14.
    • (2007) Nat. Cell Biol. , vol.9 , pp. 7-14
    • Jacobson, K.1    Mouritsen, O.G.2    Anderson, R.G.3
  • 23
    • 57749196733 scopus 로고    scopus 로고
    • Tracing the retrograde route in protein trafficking
    • Johannes L., Popoff V. Tracing the retrograde route in protein trafficking. Cell 2008, 135:1175-1187.
    • (2008) Cell , vol.135 , pp. 1175-1187
    • Johannes, L.1    Popoff, V.2
  • 24
    • 77955646459 scopus 로고    scopus 로고
    • Induced domain formation in endocytic invagination, lipid sorting, and scission
    • Johannes L., Mayor S. Induced domain formation in endocytic invagination, lipid sorting, and scission. Cell 2010, 142:507-510.
    • (2010) Cell , vol.142 , pp. 507-510
    • Johannes, L.1    Mayor, S.2
  • 28
    • 37049019270 scopus 로고    scopus 로고
    • Endocytic trafficking of sphingomyelin depends on its acyl chain length
    • Koivusalo M., Jansen M., Somerharju P., Ikonen E. Endocytic trafficking of sphingomyelin depends on its acyl chain length. Mol. Biol. Cell 2007, 18:5113-5123.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 5113-5123
    • Koivusalo, M.1    Jansen, M.2    Somerharju, P.3    Ikonen, E.4
  • 29
    • 0345490781 scopus 로고    scopus 로고
    • The intracellular voyage of cholera toxin: going retro
    • Lencer W.I., Tsai B. The intracellular voyage of cholera toxin: going retro. Trends Biochem. Sci. 2003, 28:639-645.
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 639-645
    • Lencer, W.I.1    Tsai, B.2
  • 31
    • 74849118341 scopus 로고    scopus 로고
    • Lipid rafts as a membrane-organizing principle
    • Lingwood D., Simons K. Lipid rafts as a membrane-organizing principle. Science 2010, 327:46-50.
    • (2010) Science , vol.327 , pp. 46-50
    • Lingwood, D.1    Simons, K.2
  • 32
    • 48249097851 scopus 로고    scopus 로고
    • Plasma membranes are poised for activation of raft phase coalescence at physiological temperature
    • Lingwood D., Ries J., Schwille P., Simons K. Plasma membranes are poised for activation of raft phase coalescence at physiological temperature. Proc. Natl. Acad. Sci. USA 2008, 105:10005-10010.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 10005-10010
    • Lingwood, D.1    Ries, J.2    Schwille, P.3    Simons, K.4
  • 35
    • 0033037483 scopus 로고    scopus 로고
    • Sphingolipid metabolism in the regulation of bioactive molecules
    • Luberto C., Hannun Y.A. Sphingolipid metabolism in the regulation of bioactive molecules. Lipids 1999, 34(Suppl):S5-S11.
    • (1999) Lipids , vol.34 , Issue.SUPPL.
    • Luberto, C.1    Hannun, Y.A.2
  • 36
    • 0032538927 scopus 로고    scopus 로고
    • Direct pathway from early/recycling endosomes to the Golgi apparatus revealed through the study of shiga toxin B-fragment transport
    • Mallard F., Antony C., Tenza D., Salamero J., Goud B., Johannes L. Direct pathway from early/recycling endosomes to the Golgi apparatus revealed through the study of shiga toxin B-fragment transport. J. Cell Biol. 1998, 143:973-990.
    • (1998) J. Cell Biol. , vol.143 , pp. 973-990
    • Mallard, F.1    Antony, C.2    Tenza, D.3    Salamero, J.4    Goud, B.5    Johannes, L.6
  • 37
    • 0025134695 scopus 로고
    • Cyclic AMP accumulation in HeLa cells induced by cholera toxin. Involvement of the ceramide moiety of GM1 ganglioside
    • Masserini M., Palestini P., Pitto M., Chigorno V., Tomasi M., Tettamanti G. Cyclic AMP accumulation in HeLa cells induced by cholera toxin. Involvement of the ceramide moiety of GM1 ganglioside. Biochem. J. 1990, 271:107-111.
    • (1990) Biochem. J. , vol.271 , pp. 107-111
    • Masserini, M.1    Palestini, P.2    Pitto, M.3    Chigorno, V.4    Tomasi, M.5    Tettamanti, G.6
  • 38
    • 3343011405 scopus 로고    scopus 로고
    • Cholera toxin toxicity does not require functional Arf6- and dynamin-dependent endocytic pathways
    • Massol R.H., Larsen J.E., Fujinaga Y., Lencer W.I., Kirchhausen T. Cholera toxin toxicity does not require functional Arf6- and dynamin-dependent endocytic pathways. Mol. Biol. Cell 2004, 15:3631-3641.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 3631-3641
    • Massol, R.H.1    Larsen, J.E.2    Fujinaga, Y.3    Lencer, W.I.4    Kirchhausen, T.5
  • 39
    • 0344791683 scopus 로고    scopus 로고
    • Endocytic sorting of lipid analogues differing solely in the chemistry of their hydrophobic tails
    • Mukherjee S., Soe T.T., Maxfield F.R. Endocytic sorting of lipid analogues differing solely in the chemistry of their hydrophobic tails. J. Cell Biol. 1999, 144:1271-1284.
    • (1999) J. Cell Biol. , vol.144 , pp. 1271-1284
    • Mukherjee, S.1    Soe, T.T.2    Maxfield, F.R.3
  • 40
    • 84856074275 scopus 로고    scopus 로고
    • Manganese blocks intracellular trafficking of Shiga toxin and protects against Shiga toxicosis
    • Mukhopadhyay S., Linstedt A.D. Manganese blocks intracellular trafficking of Shiga toxin and protects against Shiga toxicosis. Science 2012, 335:332-335.
    • (2012) Science , vol.335 , pp. 332-335
    • Mukhopadhyay, S.1    Linstedt, A.D.2
  • 41
    • 56549123103 scopus 로고    scopus 로고
    • Sphingolipid management by an orchestra of lipid transfer proteins
    • Neumann S., van Meer G. Sphingolipid management by an orchestra of lipid transfer proteins. Biol. Chem. 2008, 389:1349-1360.
    • (2008) Biol. Chem. , vol.389 , pp. 1349-1360
    • Neumann, S.1    van Meer, G.2
  • 42
    • 0020047904 scopus 로고
    • Characterization and quantitative determination of gangliosides and neutral glycosphingolipids in human liver
    • Nilsson O., Svennerholm L. Characterization and quantitative determination of gangliosides and neutral glycosphingolipids in human liver. J. Lipid Res. 1982, 23:327-334.
    • (1982) J. Lipid Res. , vol.23 , pp. 327-334
    • Nilsson, O.1    Svennerholm, L.2
  • 43
    • 0031750101 scopus 로고    scopus 로고
    • Filipin-dependent inhibition of cholera toxin: evidence for toxin internalization and activation through caveolae-like domains
    • Orlandi P.A., Fishman P.H. Filipin-dependent inhibition of cholera toxin: evidence for toxin internalization and activation through caveolae-like domains. J. Cell Biol. 1998, 141:905-915.
    • (1998) J. Cell Biol. , vol.141 , pp. 905-915
    • Orlandi, P.A.1    Fishman, P.H.2
  • 44
    • 0038728628 scopus 로고    scopus 로고
    • Structure of the ceramide moiety of GM1 ganglioside determines its occurrence in different detergent-resistant membrane domains in HL-60 cells
    • Panasiewicz M., Domek H., Hoser G., Kawalec M., Pacuszka T. Structure of the ceramide moiety of GM1 ganglioside determines its occurrence in different detergent-resistant membrane domains in HL-60 cells. Biochemistry 2003, 42:6608-6619.
    • (2003) Biochemistry , vol.42 , pp. 6608-6619
    • Panasiewicz, M.1    Domek, H.2    Hoser, G.3    Kawalec, M.4    Pacuszka, T.5
  • 45
    • 0028057494 scopus 로고
    • Ultrastructural localization of gangliosides; GM1 is concentrated in caveolae
    • Parton R.G. Ultrastructural localization of gangliosides; GM1 is concentrated in caveolae. J. Histochem. Cytochem. 1994, 42:155-166.
    • (1994) J. Histochem. Cytochem. , vol.42 , pp. 155-166
    • Parton, R.G.1
  • 47
    • 79960197420 scopus 로고    scopus 로고
    • Assessment of the roles of ordered lipid microdomains in post-endocytic trafficking of glycosyl-phosphatidylinositol-anchored proteins in mammalian fibroblasts
    • Refaei M., Leventis R., Silvius J.R. Assessment of the roles of ordered lipid microdomains in post-endocytic trafficking of glycosyl-phosphatidylinositol-anchored proteins in mammalian fibroblasts. Traffic 2011, 12:1012-1024.
    • (2011) Traffic , vol.12 , pp. 1012-1024
    • Refaei, M.1    Leventis, R.2    Silvius, J.R.3
  • 52
    • 0028352977 scopus 로고
    • Retrograde transport from the Golgi complex to the ER of both Shiga toxin and the nontoxic Shiga B-fragment is regulated by butyric acid and cAMP
    • Sandvig K., Ryd M., Garred O., Schweda E., Holm P.K., van Deurs B. Retrograde transport from the Golgi complex to the ER of both Shiga toxin and the nontoxic Shiga B-fragment is regulated by butyric acid and cAMP. J. Cell Biol. 1994, 126:53-64.
    • (1994) J. Cell Biol. , vol.126 , pp. 53-64
    • Sandvig, K.1    Ryd, M.2    Garred, O.3    Schweda, E.4    Holm, P.K.5    van Deurs, B.6
  • 53
    • 0027179047 scopus 로고
    • A review and predictive models of ganglioside uptake by biological membranes
    • Saqr H.E., Pearl D.K., Yates A.J. A review and predictive models of ganglioside uptake by biological membranes. J. Neurochem. 1993, 61:395-411.
    • (1993) J. Neurochem. , vol.61 , pp. 395-411
    • Saqr, H.E.1    Pearl, D.K.2    Yates, A.J.3
  • 55
    • 0022400196 scopus 로고
    • The influence of ganglioside insertion into brain membranes on the rate of ganglioside degradation by membrane-bound sialidase
    • Scheel G., Schwarzmann G., Hoffmann-Bleihauer P., Sandhoff K. The influence of ganglioside insertion into brain membranes on the rate of ganglioside degradation by membrane-bound sialidase. Eur. J. Biochem. 1985, 153:29-35.
    • (1985) Eur. J. Biochem. , vol.153 , pp. 29-35
    • Scheel, G.1    Schwarzmann, G.2    Hoffmann-Bleihauer, P.3    Sandhoff, K.4
  • 56
    • 0035783078 scopus 로고    scopus 로고
    • Uptake and metabolism of exogenous glycosphingolipids by cultured cells
    • Schwarzmann G. Uptake and metabolism of exogenous glycosphingolipids by cultured cells. Semin. Cell Dev. Biol. 2001, 12:163-171.
    • (2001) Semin. Cell Dev. Biol. , vol.12 , pp. 163-171
    • Schwarzmann, G.1
  • 58
    • 77957167810 scopus 로고    scopus 로고
    • Revitalizing membrane rafts: new tools and insights
    • Simons K., Gerl M.J. Revitalizing membrane rafts: new tools and insights. Nat. Rev. Mol. Cell Biol. 2010, 11:688-699.
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 688-699
    • Simons, K.1    Gerl, M.J.2
  • 59
    • 33644867725 scopus 로고    scopus 로고
    • The association of Shiga-like toxin with detergent-resistant membranes is modulated by glucosylceramide and is an essential requirement in the endoplasmic reticulum for a cytotoxic effect
    • Smith D.C., Sillence D.J., Falguières T., Jarvis R.M., Johannes L., Lord J.M., Platt F.M., Roberts L.M. The association of Shiga-like toxin with detergent-resistant membranes is modulated by glucosylceramide and is an essential requirement in the endoplasmic reticulum for a cytotoxic effect. Mol. Biol. Cell 2006, 17:1375-1387.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 1375-1387
    • Smith, D.C.1    Sillence, D.J.2    Falguières, T.3    Jarvis, R.M.4    Johannes, L.5    Lord, J.M.6    Platt, F.M.7    Roberts, L.M.8
  • 62
    • 84857880542 scopus 로고    scopus 로고
    • How ricin and Shiga toxin reach the cytosol of target cells: retrotranslocation from the endoplasmic reticulum
    • Spooner R.A., Lord J.M. How ricin and Shiga toxin reach the cytosol of target cells: retrotranslocation from the endoplasmic reticulum. Curr. Top. Microbiol. Immunol. 2012, 357:19-40.
    • (2012) Curr. Top. Microbiol. Immunol. , vol.357 , pp. 19-40
    • Spooner, R.A.1    Lord, J.M.2
  • 63
    • 66249127141 scopus 로고    scopus 로고
    • Sorting of lipids and proteins in membrane curvature gradients
    • Tian A., Baumgart T. Sorting of lipids and proteins in membrane curvature gradients. Biophys. J. 2009, 96:2676-2688.
    • (2009) Biophys. J. , vol.96 , pp. 2676-2688
    • Tian, A.1    Baumgart, T.2
  • 64
    • 70350025168 scopus 로고    scopus 로고
    • Bending stiffness depends on curvature of ternary lipid mixture tubular membranes
    • Tian A., Capraro B.R., Esposito C., Baumgart T. Bending stiffness depends on curvature of ternary lipid mixture tubular membranes. Biophys. J. 2009, 97:1636-1646.
    • (2009) Biophys. J. , vol.97 , pp. 1636-1646
    • Tian, A.1    Capraro, B.R.2    Esposito, C.3    Baumgart, T.4
  • 65
    • 0034762332 scopus 로고    scopus 로고
    • Internalization of cholera toxin by different endocytic mechanisms
    • Torgersen M.L., Skretting G., van Deurs B., Sandvig K. Internalization of cholera toxin by different endocytic mechanisms. J. Cell Sci. 2001, 114:3737-3747.
    • (2001) J. Cell Sci. , vol.114 , pp. 3737-3747
    • Torgersen, M.L.1    Skretting, G.2    van Deurs, B.3    Sandvig, K.4
  • 67
    • 0242385346 scopus 로고    scopus 로고
    • Separation of liquid phases in giant vesicles of ternary mixtures of phospholipids and cholesterol
    • Veatch S.L., Keller S.L. Separation of liquid phases in giant vesicles of ternary mixtures of phospholipids and cholesterol. Biophys. J. 2003, 85:3074-3083.
    • (2003) Biophys. J. , vol.85 , pp. 3074-3083
    • Veatch, S.L.1    Keller, S.L.2
  • 68
    • 0031802210 scopus 로고    scopus 로고
    • Ganglioside structure dictates signal transduction by cholera toxin and association with caveolae-like membrane domains in polarized epithelia
    • Wolf A.A., Jobling M.G., Wimer-Mackin S., Ferguson-Maltzman M., Madara J.L., Holmes R.K., Lencer W.I. Ganglioside structure dictates signal transduction by cholera toxin and association with caveolae-like membrane domains in polarized epithelia. J. Cell Biol. 1998, 141:917-927.
    • (1998) J. Cell Biol. , vol.141 , pp. 917-927
    • Wolf, A.A.1    Jobling, M.G.2    Wimer-Mackin, S.3    Ferguson-Maltzman, M.4    Madara, J.L.5    Holmes, R.K.6    Lencer, W.I.7
  • 70
    • 2642537895 scopus 로고    scopus 로고
    • Alteration in the metastatic potential of ovarian cancer cells by transfection of the antisense gene of beta-1,4-galactosyltransferase
    • Yamashita H., Kubushiro K., Ma J., Fujii T., Tsukazaki K., Iwamori M., Nozawa S. Alteration in the metastatic potential of ovarian cancer cells by transfection of the antisense gene of beta-1,4-galactosyltransferase. Oncol. Rep. 2003, 10:1857-1862.
    • (2003) Oncol. Rep. , vol.10 , pp. 1857-1862
    • Yamashita, H.1    Kubushiro, K.2    Ma, J.3    Fujii, T.4    Tsukazaki, K.5    Iwamori, M.6    Nozawa, S.7


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