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Volumn 42, Issue 45, 2003, Pages 13250-13259

Exposure of Phosphatidylinositol Transfer Proteins to Sphingomyelin-Cholesterol Membranes Suggests Transient but Productive Interactions with Raft-Like, Liquid-Ordered Domains

Author keywords

[No Author keywords available]

Indexed keywords

PLASMA MEMBRANES;

EID: 0242653610     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi034616n     Document Type: Article
Times cited : (5)

References (66)
  • 1
    • 0014409392 scopus 로고
    • Exchange of phospholipids between liver mitochondria and microsomes in vitro
    • Wirtz, K. W. A., and Zilversmit, D. B. (1968) Exchange of phospholipids between liver mitochondria and microsomes in vitro, J. Biol. Chem. 243, 3596-3602.
    • (1968) J. Biol. Chem. , vol.243 , pp. 3596-3602
    • Wirtz, K.W.A.1    Zilversmit, D.B.2
  • 2
    • 0015810355 scopus 로고
    • Some properties of phosphatidylcholine exchange protein purified from beef liver
    • Kamp, H. H., Wirtz, K. W. A., and van Deenen, L. L. M. (1973) Some properties of phosphatidylcholine exchange protein purified from beef liver, Biochim. Biophys. Acta 318, 313-325.
    • (1973) Biochim. Biophys. Acta , vol.318 , pp. 313-325
    • Kamp, H.H.1    Wirtz, K.W.A.2    Van Deenen, L.L.M.3
  • 3
    • 0016302040 scopus 로고
    • Phospholipid exchange between membranes: Purification of bovine brain proteins that preferentially catalyze the transfer of phosphatidylinositol
    • Helmkamp, G. M., Jr., Harvey, M. S., Wirtz, K. W. A., and van Deenen, L. L. M. (1974) Phospholipid exchange between membranes: purification of bovine brain proteins that preferentially catalyze the transfer of phosphatidylinositol, J. Biol. Chem. 249, 6382-6389.
    • (1974) J. Biol. Chem. , vol.249 , pp. 6382-6389
    • Helmkamp Jr., G.M.1    Harvey, M.S.2    Wirtz, K.W.A.3    Van Deenen, L.L.M.4
  • 4
    • 0018733323 scopus 로고
    • Purification and characterization of two phospholipid exchange proteins from bovine heart
    • DiCorleto, P. E., Warach, J. B., and Zilversmit, D. B. (1979) Purification and characterization of two phospholipid exchange proteins from bovine heart, J. Biol. Chem. 254, 7795-7802.
    • (1979) J. Biol. Chem. , vol.254 , pp. 7795-7802
    • DiCorleto, P.E.1    Warach, J.B.2    Zilversmit, D.B.3
  • 5
    • 0034064138 scopus 로고    scopus 로고
    • Structure and lipid transport mechanism of a StAR-related domain
    • Tsujishata, Y., and Hurley J. H. (2000) Structure and lipid transport mechanism of a StAR-related domain, Nat. Struct. Biol. 7, 408-414.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 408-414
    • Tsujishata, Y.1    Hurley, J.H.2
  • 6
    • 0035937732 scopus 로고    scopus 로고
    • Structure of a multifunctional protein: Mammalian phosphatidylinositol transfer protein complexed with phosphatidylcholine
    • Yoder, M. D., Thomas, L. M., Tremblay, J. M., Oliver, R. L., Yarbrough, L. R., and Helmkamp, G. M., Jr. (2001) Structure of a multifunctional protein: Mammalian phosphatidylinositol transfer protein complexed with phosphatidylcholine, J. Biol. Chem. 276, 9246-9252.
    • (2001) J. Biol. Chem. , vol.276 , pp. 9246-9252
    • Yoder, M.D.1    Thomas, L.M.2    Tremblay, J.M.3    Oliver, R.L.4    Yarbrough, L.R.5    Helmkamp Jr., G.M.6
  • 7
    • 0037076327 scopus 로고    scopus 로고
    • Crystal structure of the Mus musculus cholesterol-regulated START protein 4 (StarD4) containing a StAR-related lipid transfer domain
    • Romanowski, M. J., Soccio, R. E., Breslow, J. L., and Burley, S. K. (2002) Crystal structure of the Mus musculus cholesterol-regulated START protein 4 (StarD4) containing a StAR-related lipid transfer domain, Proc. Natl. Acad. Sci. U.S.A. 99, 6949-6954.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 6949-6954
    • Romanowski, M.J.1    Soccio, R.E.2    Breslow, J.L.3    Burley, S.K.4
  • 9
    • 0037201934 scopus 로고    scopus 로고
    • Current thoughts on the phosphatidylinositol transfer protein family
    • Allen-Baume, V., Ségui, B., and Cockcroft, S. (2002) Current thoughts on the phosphatidylinositol transfer protein family, FEBS Lett. 531, 74-80.
    • (2002) FEBS Lett. , vol.531 , pp. 74-80
    • Allen-Baume, V.1    Ségui, B.2    Cockcroft, S.3
  • 10
    • 0030601310 scopus 로고    scopus 로고
    • Fluorescently labeled phosphatidylinositol transfer protein isoforms (α and β), microinjected into fetal bovine heart endothelial cells, are targeted to distinct intracellular sites
    • de Vries, K. J., Westerman, J., Bastiaens, P. I. H., Jovin, T. M., Wirtz, K. W. A., and Snoek, G. T. (1996) Fluorescently labeled phosphatidylinositol transfer protein isoforms (α and β), microinjected into fetal bovine heart endothelial cells, are targeted to distinct intracellular sites, Exp. Cell Res. 227, 33-39.
    • (1996) Exp. Cell Res. , vol.227 , pp. 33-39
    • De Vries, K.J.1    Westerman, J.2    Bastiaens, P.I.H.3    Jovin, T.M.4    Wirtz, K.W.A.5    Snoek, G.T.6
  • 11
    • 0037196575 scopus 로고    scopus 로고
    • Both isoforms of mammalian phosphatidylinositol transfer protein are capable of binding and transporting sphingomyelin
    • Li, H., Tremblay, J. M., Yarbrough, L. R., and Helmkamp, G. M., Jr. (2002) Both isoforms of mammalian phosphatidylinositol transfer protein are capable of binding and transporting sphingomyelin, Biochim. Biophys. Acta 1580, 67-76.
    • (2002) Biochim. Biophys. Acta , vol.1580 , pp. 67-76
    • Li, H.1    Tremblay, J.M.2    Yarbrough, L.R.3    Helmkamp Jr., G.M.4
  • 12
    • 0037103783 scopus 로고    scopus 로고
    • Phosphatidylinositol transfer protein β displays minimal sphingomyelin transfer activity and is not required for biosynthesis and trafficking of sphingomyelin
    • Ségui, B., Allen-Baume, V., and Cockcroft, S. (2002) Phosphatidylinositol transfer protein β displays minimal sphingomyelin transfer activity and is not required for biosynthesis and trafficking of sphingomyelin, Biochem. J. 366, 23-34.
    • (2002) Biochem. J. , vol.366 , pp. 23-34
    • Ségui, B.1    Allen-Baume, V.2    Cockcroft, S.3
  • 13
    • 0035047848 scopus 로고    scopus 로고
    • StAR protein and the regulation of steroid hormone biosynthesis
    • Stocco, D. M. (2001) StAR protein and the regulation of steroid hormone biosynthesis, Annu. Rev. Physiol. 63, 193-213.
    • (2001) Annu. Rev. Physiol. , vol.63 , pp. 193-213
    • Stocco, D.M.1
  • 14
    • 0034130649 scopus 로고    scopus 로고
    • Priming in exocytosis, attaining fusion-competence after vesicle docking
    • Klenchin, V. A., and Martin, T. F. J. (2000) Priming in exocytosis, attaining fusion-competence after vesicle docking, Biochimie 82, 399-407.
    • (2000) Biochimie , vol.82 , pp. 399-407
    • Klenchin, V.A.1    Martin, T.F.J.2
  • 15
    • 0035782882 scopus 로고    scopus 로고
    • Phosphatidylinositol transfer proteins couple lipid transport to phosphoinositide synthesis
    • Cockcroft, S. (2001) Phosphatidylinositol transfer proteins couple lipid transport to phosphoinositide synthesis, Semin. Cell Dev. Biol. 12, 183-191.
    • (2001) Semin. Cell Dev. Biol. , vol.12 , pp. 183-191
    • Cockcroft, S.1
  • 16
    • 0037201969 scopus 로고    scopus 로고
    • The structure of phosphatidylinositol transfer protein α reveals sites for phospholipid binding and membrane association with major implications for its function
    • van Tiel, C. M., Schouten, A., Snoek, G. T., Gros, P., and Wirtz, K. W. A. (2002) The structure of phosphatidylinositol transfer protein α reveals sites for phospholipid binding and membrane association with major implications for its function, FEBS Lett. 531, 69-73.
    • (2002) FEBS Lett. , vol.531 , pp. 69-73
    • Van Tiel, C.M.1    Schouten, A.2    Snoek, G.T.3    Gros, P.4    Wirtz, K.W.A.5
  • 17
    • 0036349207 scopus 로고    scopus 로고
    • Clofibrate-induced relocation of phosphatidylcholine transfer protein to mitochondria in endothelial cells
    • de Brouwer, A. P. M., Westerman, J., Kleinnijenhuis, A., Bevers, L. E., Roelofsen, B., and Wirtz, K. W. A. (2002) Clofibrate-induced relocation of phosphatidylcholine transfer protein to mitochondria in endothelial cells, Exp. Cell Res. 274, 100-111.
    • (2002) Exp. Cell Res. , vol.274 , pp. 100-111
    • De Brouwer, A.P.M.1    Westerman, J.2    Kleinnijenhuis, A.3    Bevers, L.E.4    Roelofsen, B.5    Wirtz, K.W.A.6
  • 18
    • 0034789931 scopus 로고    scopus 로고
    • The organizing potential of sphingolipids in intracellular membrane transport
    • Holthuis, J. C. M., Pomorski, T., Raggers, R. J., Sprong, H., and van Meer, G. (2001) The organizing potential of sphingolipids in intracellular membrane transport, Physiol. Rev. 81, 1689-1723.
    • (2001) Physiol. Rev. , vol.81 , pp. 1689-1723
    • Holthuis, J.C.M.1    Pomorski, T.2    Raggers, R.J.3    Sprong, H.4    Van Meer, G.5
  • 19
    • 0037010173 scopus 로고    scopus 로고
    • Sphingolipid trafficking and protein sorting in epithelial cells
    • Aï t Slimane, T., and Hoekstra, D. (2002) Sphingolipid trafficking and protein sorting in epithelial cells. FEBS Lett. 529, 54-59.
    • (2002) FEBS Lett. , vol.529 , pp. 54-59
    • Aï T Slimane, T.1    Hoekstra, D.2
  • 20
    • 0030893370 scopus 로고    scopus 로고
    • Expression of neutral sphingomyelinase identifies a distinct pool of sphingomyelin involved in apoptosis
    • Zhang, P., Liu, B., Jenkins, G. M., Hannun, Y. A., and Obeid, L. M. (1997) Expression of neutral sphingomyelinase identifies a distinct pool of sphingomyelin involved in apoptosis, J. Biol. Chem. 272, 9609-9612.
    • (1997) J. Biol. Chem. , vol.272 , pp. 9609-9612
    • Zhang, P.1    Liu, B.2    Jenkins, G.M.3    Hannun, Y.A.4    Obeid, L.M.5
  • 21
    • 0034625373 scopus 로고    scopus 로고
    • Structure and function of sphingolipid- and cholesterol-rich membrane rafts
    • Brown, D. A., and London, E. (2000) Structure and function of sphingolipid- and cholesterol-rich membrane rafts, J. Biol. Chem. 275, 17221-17224.
    • (2000) J. Biol. Chem. , vol.275 , pp. 17221-17224
    • Brown, D.A.1    London, E.2
  • 22
    • 0037135518 scopus 로고    scopus 로고
    • Sphingolipid transport: Rafts and translocators
    • van Meer, G., and Lisman, Q. (2002) Sphingolipid transport: rafts and translocators, J. Biol. Chem. 277, 25855-25858.
    • (2002) J. Biol. Chem. , vol.277 , pp. 25855-25858
    • Van Meer, G.1    Lisman, Q.2
  • 23
    • 0020580252 scopus 로고
    • Sterol partitioning among intracellular membranes. Testing a model for cellular sterol distribution
    • Wattenberg, B. W., and Silbert, D. F. (1983) Sterol partitioning among intracellular membranes. Testing a model for cellular sterol distribution, J. Biol. Chem. 258, 2284-2289.
    • (1983) J. Biol. Chem. , vol.258 , pp. 2284-2289
    • Wattenberg, B.W.1    Silbert, D.F.2
  • 24
    • 0024509922 scopus 로고
    • Plasma membranes contain half the phospholipid and 90% of the cholesterol and sphingomyelin in cultured human fibroblasts
    • Lange, Y., Swaisgood, M. H., Ramos, B. V., and Steck, T. L. (1989) Plasma membranes contain half the phospholipid and 90% of the cholesterol and sphingomyelin in cultured human fibroblasts, J. Biol. Chem. 264, 3786-3793.
    • (1989) J. Biol. Chem. , vol.264 , pp. 3786-3793
    • Lange, Y.1    Swaisgood, M.H.2    Ramos, B.V.3    Steck, T.L.4
  • 25
    • 0041494100 scopus 로고    scopus 로고
    • Lipid rafts: Bringing order to chaos
    • Pike, L. J. (2003) Lipid rafts: bringing order to chaos, J. Lipid Res. 44, 655-667.
    • (2003) J. Lipid Res. , vol.44 , pp. 655-667
    • Pike, L.J.1
  • 26
    • 0030591476 scopus 로고    scopus 로고
    • Does cholesterol discriminate between sphingomyelin and phosphatidylcholine in mixed monolayers containing both phospholipids?
    • Mattjus, P., and Slotte, J. P. (1996) Does cholesterol discriminate between sphingomyelin and phosphatidylcholine in mixed monolayers containing both phospholipids? Chem. Phys. Lipids 81, 69-80.
    • (1996) Chem. Phys. Lipids , vol.81 , pp. 69-80
    • Mattjus, P.1    Slotte, J.P.2
  • 27
    • 0019886821 scopus 로고
    • Intermembrane phospholipid fluxes catalyzed by bovine brain phospholipid exchange protein
    • Kasper, A. M., and Helmkamp, G. M., Jr. (1981) Intermembrane phospholipid fluxes catalyzed by bovine brain phospholipid exchange protein, Biochim. Biophys. Acta 664, 22-32.
    • (1981) Biochim. Biophys. Acta , vol.664 , pp. 22-32
    • Kasper, A.M.1    Helmkamp Jr., G.M.2
  • 29
    • 0018185821 scopus 로고
    • Homology between ricin and Ricinus communis agglutinin: Amino terminal sequence analysis and protein synthesis inhibition studies
    • Cawley, D. B., Hedblom, M. L., and Houston, L. L. (1978) Homology between ricin and Ricinus communis agglutinin: amino terminal sequence analysis and protein synthesis inhibition studies, Arch. Biochem. Biophys. 190, 744-755.
    • (1978) Arch. Biochem. Biophys. , vol.190 , pp. 744-755
    • Cawley, D.B.1    Hedblom, M.L.2    Houston, L.L.3
  • 30
    • 0029831653 scopus 로고    scopus 로고
    • Limited proteolysis of rat phosphatidylinositol transfer protein by trypsin cleaves the C terminus, enhances binding to lipid vesicles, and reduces phospholipid transfer activity
    • Tremblay, J. M., Helmkamp, G. M., Jr., and Yarbrough, L. R. (1996) Limited proteolysis of rat phosphatidylinositol transfer protein by trypsin cleaves the C terminus, enhances binding to lipid vesicles, and reduces phospholipid transfer activity, J. Biol. Chem. 271, 21075-21080.
    • (1996) J. Biol. Chem. , vol.271 , pp. 21075-21080
    • Tremblay, J.M.1    Helmkamp Jr., G.M.2    Yarbrough, L.R.3
  • 31
    • 0029822208 scopus 로고    scopus 로고
    • Truncations of the C terminus have different effects on the conformation and activity of phosphatidylinositol transfer protein
    • Voziyan, P. A., Tremblay, J. M., Yarbrough, L. R., and Helmkamp, G. M., Jr. (1996) Truncations of the C terminus have different effects on the conformation and activity of phosphatidylinositol transfer protein, Biochemistry 35, 12526-12531.
    • (1996) Biochemistry , vol.35 , pp. 12526-12531
    • Voziyan, P.A.1    Tremblay, J.M.2    Yarbrough, L.R.3    Helmkamp Jr., G.M.4
  • 32
    • 0019873818 scopus 로고
    • Protein-catalyzed phospholipid exchange between gel and liquid-crystalline phospholipid vesicles
    • Kasper, A. M., and Helmkamp, G. M., Jr. (1981) Protein-catalyzed phospholipid exchange between gel and liquid-crystalline phospholipid vesicles, Biochemistry 20, 146-151.
    • (1981) Biochemistry , vol.20 , pp. 146-151
    • Kasper, A.M.1    Helmkamp Jr., G.M.2
  • 33
    • 0023807967 scopus 로고
    • General kinetic model for protein-mediated phospholipid transfer between membranes
    • Yoshimura, T., Welti, R., and Helmkamp, G. M., Jr. (1988) General kinetic model for protein-mediated phospholipid transfer between membranes, Arch. Biochem. Biophys. 266, 299-312.
    • (1988) Arch. Biochem. Biophys. , vol.266 , pp. 299-312
    • Yoshimura, T.1    Welti, R.2    Helmkamp Jr., G.M.3
  • 34
    • 0023735287 scopus 로고
    • Properties of the binding sites for the sn-1 and sn-2 acyl chains on the phosphatidylinositol transfer protein from bovine brain
    • van Paridon, P. A., Gadella, T. W. J., Jr., Somerharju, P. J., and Wirtz, K. W. A. (1988) Properties of the binding sites for the sn-1 and sn-2 acyl chains on the phosphatidylinositol transfer protein from bovine brain, Biochemistry 27, 6208-6214.
    • (1988) Biochemistry , vol.27 , pp. 6208-6214
    • Van Paridon, P.A.1    Gadella Jr., T.W.J.2    Somerharju, P.J.3    Wirtz, K.W.A.4
  • 35
    • 0037172782 scopus 로고    scopus 로고
    • Determination of the stability of the noncovalent phospholipid transfer protein-lipid complex by electrospray time-of-flight mass spectrometry
    • de Brouwer, A. P. M., Versluis, C., Westerman, J., Roelofson, B., Heck, A. J. R., and Wirtz, K. W. A. (2002) Determination of the stability of the noncovalent phospholipid transfer protein-lipid complex by electrospray time-of-flight mass spectrometry, Biochemistry 41, 8013-8018.
    • (2002) Biochemistry , vol.41 , pp. 8013-8018
    • De Brouwer, A.P.M.1    Versluis, C.2    Westerman, J.3    Roelofson, B.4    Heck, A.J.R.5    Wirtz, K.W.A.6
  • 36
    • 0018225465 scopus 로고
    • Fluidity parameters of lipid regions determined by fluorescence polarization
    • Shinitzky, M., and Barenholz, Y. (1978) Fluidity parameters of lipid regions determined by fluorescence polarization, Biochim. Biophys. Acta 515, 367-394.
    • (1978) Biochim. Biophys. Acta , vol.515 , pp. 367-394
    • Shinitzky, M.1    Barenholz, Y.2
  • 37
    • 0032518761 scopus 로고    scopus 로고
    • The C terminus of phosphatidylinositol transfer protein modulates membrane interactions and transfer activity but not phospholipid binding
    • Tremblay, J. M., Voziyan, P. A., Helmkamp, G. M., Jr., and Yarbrough, L. R. (1998) The C terminus of phosphatidylinositol transfer protein modulates membrane interactions and transfer activity but not phospholipid binding, Biochim. Biophys. Acta 1389, 91-100.
    • (1998) Biochim. Biophys. Acta , vol.1389 , pp. 91-100
    • Tremblay, J.M.1    Voziyan, P.A.2    Helmkamp Jr., G.M.3    Yarbrough, L.R.4
  • 38
    • 0040001800 scopus 로고
    • Physical properties and functional roles of lipids membranes
    • (Vance, D. E., and Vance, J. E., Eds.), Elsevier, Amsterdam
    • Cullis, P. R, and Hope, M. J. (1991) Physical properties and functional roles of lipids in membranes, in Biochemistry of Lipids, Lipoproteins and Membranes (Vance, D. E., and Vance, J. E., Eds.) pp 1-41, Elsevier, Amsterdam.
    • (1991) Biochemistry of Lipids, Lipoproteins and Membranes , pp. 1-41
    • Cullis, P.R.1    Hope, M.J.2
  • 40
    • 0032119526 scopus 로고    scopus 로고
    • Cyclodextrin drug carrier systems
    • Uekama, K., Hirayama, F., and Irie, T. (1998) Cyclodextrin drug carrier systems, Chem. Rev. 98, 2045-2076.
    • (1998) Chem. Rev. , vol.98 , pp. 2045-2076
    • Uekama, K.1    Hirayama, F.2    Irie, T.3
  • 41
    • 0025602953 scopus 로고
    • Interaction of cholesterol with various glycerophospholipids and sphingomyelin
    • Sankaram, M. B., and Thompson, T. E. (1990) Interaction of cholesterol with various glycerophospholipids and sphingomyelin, Biochemistry 29, 10670-10675.
    • (1990) Biochemistry , vol.29 , pp. 10670-10675
    • Sankaram, M.B.1    Thompson, T.E.2
  • 42
    • 0028034850 scopus 로고
    • Interaction of cholesterol with sphingomyelin in monolayers and vesicles
    • Bittman, R., Kasireddy, C. R., Mattjus, P., and Slotte, J. P. (1994) Interaction of cholesterol with sphingomyelin in monolayers and vesicles, Biochemistry 33, 11776-11781.
    • (1994) Biochemistry , vol.33 , pp. 11776-11781
    • Bittman, R.1    Kasireddy, C.R.2    Mattjus, P.3    Slotte, J.P.4
  • 43
    • 0034682556 scopus 로고    scopus 로고
    • Chemical activity of cholesterol in membranes
    • Radhakrishnan, A., and McConnell, H. M. (2000) Chemical activity of cholesterol in membranes, Biochemistry 39, 8119-8124.
    • (2000) Biochemistry , vol.39 , pp. 8119-8124
    • Radhakrishnan, A.1    McConnell, H.M.2
  • 44
    • 0035957101 scopus 로고    scopus 로고
    • Interaction of cholesterol with sphingomyelin in mixed membranes containing phosphatidylcholine, studied by spin-label ESR and IR spectroscopies. A possible stabilization of gel-phase sphingolipid domains by cholesterol
    • Veiga, M. P., Arrondo, J. L. R., Goñi, F. M., Alonso, A., and Marsh, D. (2001) Interaction of cholesterol with sphingomyelin in mixed membranes containing phosphatidylcholine, studied by spin-label ESR and IR spectroscopies. A possible stabilization of gel-phase sphingolipid domains by cholesterol, Biochemistry 40, 2614-2622.
    • (2001) Biochemistry , vol.40 , pp. 2614-2622
    • Veiga, M.P.1    Arrondo, J.L.R.2    Goñi, F.M.3    Alonso, A.4    Marsh, D.5
  • 45
    • 0034659876 scopus 로고    scopus 로고
    • Activity of phosphatidylinositol transfer protein is sensitive to ethanol and membrane curvature
    • Komatsu, H., Bouma, B., Wirtz, K. W. A., Taraschi, T. F., and Janes, N. (2000) Activity of phosphatidylinositol transfer protein is sensitive to ethanol and membrane curvature, Biochem. J. 348, 667-673.
    • (2000) Biochem. J. , vol.348 , pp. 667-673
    • Komatsu, H.1    Bouma, B.2    Wirtz, K.W.A.3    Taraschi, T.F.4    Janes, N.5
  • 47
    • 0032532271 scopus 로고    scopus 로고
    • Effects of cholesterol depletion by cyclodextrin on the sphingolipid microdomains of the plasma membrane
    • Ilangumaran, S., and Hoessli, D. C. (1998) Effects of cholesterol depletion by cyclodextrin on the sphingolipid microdomains of the plasma membrane, Biochem. J. 335, 433-440.
    • (1998) Biochem. J. , vol.335 , pp. 433-440
    • Ilangumaran, S.1    Hoessli, D.C.2
  • 48
    • 0034815625 scopus 로고    scopus 로고
    • Use of cyclodextrins to monitor transbilayer movement and differential lipid affinities of cholesterol
    • Leventis, R., and Silvius, J. R. (2001) Use of cyclodextrins to monitor transbilayer movement and differential lipid affinities of cholesterol, Biophys. J. 81, 2257-2267.
    • (2001) Biophys. J. , vol.81 , pp. 2257-2267
    • Leventis, R.1    Silvius, J.R.2
  • 49
    • 0032816939 scopus 로고    scopus 로고
    • Condensed complexes of cholesterol and phospholipids
    • Radhakrishnan, A., and McConnell, H. M. (1999) Condensed complexes of cholesterol and phospholipids, Biophys. J. 77, 1507-1517.
    • (1999) Biophys. J. , vol.77 , pp. 1507-1517
    • Radhakrishnan, A.1    McConnell, H.M.2
  • 50
    • 0017175076 scopus 로고
    • Phosphatidylinositol exchange protein: Effects of membrane structure and evidence for a ping-pong mechanism
    • Helmkamp, G. M., Jr., Wirtz, K. W. A., and van Deenen, L. L. M. (1976) Phosphatidylinositol exchange protein: effects of membrane structure and evidence for a ping-pong mechanism, Arch. Biochem. Biophys. 174, 592-602.
    • (1976) Arch. Biochem. Biophys. , vol.174 , pp. 592-602
    • Helmkamp Jr., G.M.1    Wirtz, K.W.A.2    Van Deenen, L.L.M.3
  • 51
  • 52
    • 0017118712 scopus 로고
    • Distribution of positional isomers of monoenoic fatty acids in pig-brain white matter sphingomyelin
    • Pullarat, R. K., and Reha, H. (1976) Distribution of positional isomers of monoenoic fatty acids in pig-brain white matter sphingomyelin, J. Neurochem. 27, 321-322.
    • (1976) J. Neurochem. , vol.27 , pp. 321-322
    • Pullarat, R.K.1    Reha, H.2
  • 53
    • 0018799289 scopus 로고
    • Fatty acid composition and thermal behavior of natural sphingomyelins
    • Calhoun, W. L., and Shipley, G. G. (1979) Fatty acid composition and thermal behavior of natural sphingomyelins, Biochim. Biophys. Acta 555, 436-441.
    • (1979) Biochim. Biophys. Acta , vol.555 , pp. 436-441
    • Calhoun, W.L.1    Shipley, G.G.2
  • 54
    • 0019061208 scopus 로고
    • Mild alkali-stable phospholipids in chicken egg yolks: Characterization of 1-alkenyl and 1-alkyl-sn-glycero-3-phosphoethanolamine, sphingomyelin, and 1-alkyl-sn-glycero-3-phosphocholine
    • Do, U. H., and Ramachandran, S. (1980) Mild alkali-stable phospholipids in chicken egg yolks: characterization of 1-alkenyl and 1-alkyl-sn-glycero-3-phosphoethanolamine, sphingomyelin, and 1-alkyl-sn-glycero-3-phosphocholine, J. Lipid Res. 21, 888-894.
    • (1980) J. Lipid Res. , vol.21 , pp. 888-894
    • Do, U.H.1    Ramachandran, S.2
  • 55
    • 0035831212 scopus 로고    scopus 로고
    • Stoichiometry of cholesterol-sphingomyelin condensed complexes in monolayers
    • Radhakrishnan, A., Li, X.-M., Brown, R. E., and McConnell, H. M. (2001) Stoichiometry of cholesterol-sphingomyelin condensed complexes in monolayers, Biochim. Biophys. Acta 1511, 1-6.
    • (2001) Biochim. Biophys. Acta , vol.1511 , pp. 1-6
    • Radhakrishnan, A.1    Li, X.-M.2    Brown, R.E.3    McConnell, H.M.4
  • 57
    • 0029945129 scopus 로고    scopus 로고
    • N-Palmitoyl sphingo-myelin bilayers: Structure and interactions with cholesterol and dipalmitoylphosphatidylcholine
    • Maulik, P. R., and Shipley, G. G. (1996) N-Palmitoyl sphingo-myelin bilayers: structure and interactions with cholesterol and dipalmitoylphosphatidylcholine, Biochemistry 35, 8025-8034.
    • (1996) Biochemistry , vol.35 , pp. 8025-8034
    • Maulik, P.R.1    Shipley, G.G.2
  • 58
    • 0035830645 scopus 로고    scopus 로고
    • Interaction of ceramides with phosphatidylcholine, sphingomyelin, and sphingomyelin/cholesterol bilayers
    • Massey, J. B. (2001) Interaction of ceramides with phosphatidylcholine, sphingomyelin, and sphingomyelin/cholesterol bilayers, Biochim. Biophys. Acta 1510, 167-184.
    • (2001) Biochim. Biophys. Acta , vol.1510 , pp. 167-184
    • Massey, J.B.1
  • 59
    • 0034663853 scopus 로고    scopus 로고
    • Mixed membranes of sphingolipids and glycerolipids as studied by spinlabel ESR spectroscopy. A search for domain formation
    • Veiga, M. P., Goñi, F. M., Alonso, A., and Marsh, D. (2000) Mixed membranes of sphingolipids and glycerolipids as studied by spinlabel ESR spectroscopy, A search for domain formation, Biochemistry 39, 9876-9883.
    • (2000) Biochemistry , vol.39 , pp. 9876-9883
    • Veiga, M.P.1    Goñi, F.M.2    Alonso, A.3    Marsh, D.4
  • 60
    • 0036830114 scopus 로고    scopus 로고
    • Multiple functions of caveolin-1
    • Liu, P., Rudick, M., and Anderson, R. G. W. (2002) Multiple functions of caveolin-1, J. Biol. Chem. 277, 41295-41298.
    • (2002) J. Biol. Chem. , vol.277 , pp. 41295-41298
    • Liu, P.1    Rudick, M.2    Anderson, R.G.W.3
  • 61
    • 0023748596 scopus 로고
    • Resynthesis of sphingomyelin from plasma membrane phosphatidylcholine in BHK cells treated with Staphylococcus aureus sphingomyelinase
    • Allan, D., and Quinn, P. (1988) Resynthesis of sphingomyelin from plasma membrane phosphatidylcholine in BHK cells treated with Staphylococcus aureus sphingomyelinase, Biochem. J. 254, 765-771.
    • (1988) Biochem. J. , vol.254 , pp. 765-771
    • Allan, D.1    Quinn, P.2
  • 62
    • 0034717903 scopus 로고    scopus 로고
    • Sphingolipid transport in eukaryotic cells
    • van Meer, G., and Holthuis, J. C. M. (2000) Sphingolipid transport in eukaryotic cells, Biochim. Biophys. Acta 1486, 145-170.
    • (2000) Biochim. Biophys. Acta , vol.1486 , pp. 145-170
    • Van Meer, G.1    Holthuis, J.C.M.2
  • 63
    • 0020432891 scopus 로고
    • Interaction of cholesterol and lysophosphatidylcholine in determining red cell shape
    • Lange, Y., and Slayton, J. M. (1982) Interaction of cholesterol and lysophosphatidylcholine in determining red cell shape, J. Lipid Res. 23, 1121-1127.
    • (1982) J. Lipid Res. , vol.23 , pp. 1121-1127
    • Lange, Y.1    Slayton, J.M.2
  • 64
    • 0035340071 scopus 로고    scopus 로고
    • A neutral sphingomyelinase resides in sphingolipid-enriched microdomains and is inhibited by the caveolin-scaffolding domain: Potential implications in tumor necrosis factor signaling
    • Veldman, R. J., Maestre, N., Aduib, O. M., Medin, J. A., Salvayre, R., and Levade, T. (2001) A neutral sphingomyelinase resides in sphingolipid-enriched microdomains and is inhibited by the caveolin-scaffolding domain: potential implications in tumor necrosis factor signaling, Biochem. J. 355, 859-868.
    • (2001) Biochem. J. , vol.355 , pp. 859-868
    • Veldman, R.J.1    Maestre, N.2    Aduib, O.M.3    Medin, J.A.4    Salvayre, R.5    Levade, T.6
  • 65
    • 0037135626 scopus 로고    scopus 로고
    • The ceramide-centric universe of lipid-mediated cell regulation: Stress encounters of the lipid kind
    • Hannun, Y., and Obeid, L. M. (2002) The ceramide-centric universe of lipid-mediated cell regulation: stress encounters of the lipid kind, J. Biol. Chem. 277, 25847-25850.
    • (2002) J. Biol. Chem. , vol.277 , pp. 25847-25850
    • Hannun, Y.1    Obeid, L.M.2
  • 66
    • 0033945943 scopus 로고    scopus 로고
    • Caveolin proteins in signaling, oncogenic transformation, and muscular dystrophy
    • Razani, B., Schlegel, A., and Lisanti, M. P. (2000) Caveolin proteins in signaling, oncogenic transformation, and muscular dystrophy, J. Cell Sci. 113, 2103-2109.
    • (2000) J. Cell Sci. , vol.113 , pp. 2103-2109
    • Razani, B.1    Schlegel, A.2    Lisanti, M.P.3


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