메뉴 건너뛰기




Volumn 11, Issue 7, 2000, Pages 2267-2281

Inositol phosphorylceramide synthase is located in the Golgi apparatus of Saccharomyces cerevisiae

Author keywords

[No Author keywords available]

Indexed keywords

CERAMIDE DERIVATIVE; SPHINGOLIPID; SPHINGOSINE ACYLTRANSFERASE;

EID: 0033944545     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.11.7.2267     Document Type: Article
Times cited : (142)

References (95)
  • 1
    • 0027097849 scopus 로고
    • 2+-ATPase homologue, PMR1, is required for normal Golgi function and localizes in a novel Golgi-like distribution
    • 2+-ATPase homologue, PMR1, is required for normal Golgi function and localizes in a novel Golgi-like distribution. Mol. Biol. Cell 3, 633-654.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 633-654
    • Antebi, A.1    Fink, G.R.2
  • 2
    • 0024299523 scopus 로고
    • Reconstitution of SEC gene product-dependent intercompartmental protein transport
    • Baker, D., Hicke, L., Rexach, M., Schleyer, M., and Schekman, R. (1988). Reconstitution of SEC gene product-dependent intercompartmental protein transport. Cell 54, 335-344.
    • (1988) Cell , vol.54 , pp. 335-344
    • Baker, D.1    Hicke, L.2    Rexach, M.3    Schleyer, M.4    Schekman, R.5
  • 3
    • 0029910301 scopus 로고    scopus 로고
    • The Dri 42 gene, whose expression is up-regulated during epithelial differentiation, encodes a novel endoplasmic reticulum resident transmembrane protein
    • Barila, D., Plateroti, M., Nobili, F., Muda, A.O., Xie, Y., Morimoto, T., and Perozzi, G. (1996). The Dri 42 gene, whose expression is up-regulated during epithelial differentiation, encodes a novel endoplasmic reticulum resident transmembrane protein. J. Biol. Chem. 271, 29928-29936.
    • (1996) J. Biol. Chem. , vol.271 , pp. 29928-29936
    • Barila, D.1    Plateroti, M.2    Nobili, F.3    Muda, A.O.4    Xie, Y.5    Morimoto, T.6    Perozzi, G.7
  • 4
    • 0019205160 scopus 로고
    • Biosynthesis of phosphoinositol-containing sphingolipids from phosphatidylinositol by a membrane preparation from Saccharomyces cerevisiae
    • Becker, G.W., and Lester, R.L. (1980). Biosynthesis of phosphoinositol-containing sphingolipids from phosphatidylinositol by a membrane preparation from Saccharomyces cerevisiae. J. Bacteriol. 142, 747-754.
    • (1980) J. Bacteriol. , vol.142 , pp. 747-754
    • Becker, G.W.1    Lester, R.L.2
  • 6
    • 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
  • 7
    • 0027892019 scopus 로고
    • Cholesterol and the Golgi apparatus
    • Bretscher, M.S., and Munro, S. (1993). Cholesterol and the Golgi apparatus. Science 261, 1280-1281.
    • (1993) Science , vol.261 , pp. 1280-1281
    • Bretscher, M.S.1    Munro, S.2
  • 8
    • 0032544691 scopus 로고    scopus 로고
    • Mammalian lipid phosphate phosphohydrolases
    • Brindley, D.M., and Waggoner, D.W. (1998). Mammalian lipid phosphate phosphohydrolases. J. Biol. Chem. 273, 24281-24284.
    • (1998) J. Biol. Chem. , vol.273 , pp. 24281-24284
    • Brindley, D.M.1    Waggoner, D.W.2
  • 9
    • 0032421354 scopus 로고    scopus 로고
    • Functions of lipid rafts in biological membranes
    • Brown, D.A., and London, E. (1998). Functions of lipid rafts in biological membranes. Annu. Rev. Cell Dev. Biol. 14, 111-136.
    • (1998) Annu. Rev. Cell Dev. Biol. , vol.14 , pp. 111-136
    • Brown, D.A.1    London, E.2
  • 10
    • 0031965054 scopus 로고    scopus 로고
    • Sphingolipid organization in biomembranes: What physical studies of model membranes reveal
    • Brown, R.E. (1998). Sphingolipid organization 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
  • 11
    • 0028203898 scopus 로고
    • Effects of membrane thickness on the molecular dynamics and enzymatic activity of reconstituted Ca-ATPase
    • Cornea, R.L., and Thomas, D.D. (1994). Effects of membrane thickness on the molecular dynamics and enzymatic activity of reconstituted Ca-ATPase. Biochemistry 33, 2912-2920.
    • (1994) Biochemistry , vol.33 , pp. 2912-2920
    • Cornea, R.L.1    Thomas, D.D.2
  • 12
    • 0032412784 scopus 로고    scopus 로고
    • Biochemistry, cell biology and molecular biology of lipids of Saccharomyces cerevisiae
    • Daum, G., Lees, N.D., Bard, M., and Dickson, R. (1998). Biochemistry, cell biology and molecular biology of lipids of Saccharomyces cerevisiae. Yeast 14, 1471-1510.
    • (1998) Yeast , vol.14 , pp. 1471-1510
    • Daum, G.1    Lees, N.D.2    Bard, M.3    Dickson, R.4
  • 13
    • 0032583117 scopus 로고    scopus 로고
    • Involvement of long chain fatty acid elongation in the trafficking of secretory vesicles in yeast
    • David, D., Sundarababu, S., and Gerst, J.E. (1998). Involvement of long chain fatty acid elongation in the trafficking of secretory vesicles in yeast. J. Cell Biol. 143, 1167-1182.
    • (1998) J. Cell Biol. , vol.143 , pp. 1167-1182
    • David, D.1    Sundarababu, S.2    Gerst, J.E.3
  • 14
    • 0031662853 scopus 로고    scopus 로고
    • Sphingolipid functions in Saccharomyces cerevisiae: Comparison to mammals
    • Dickson, R.C. (1998). Sphingolipid functions in Saccharomyces cerevisiae: comparison to mammals. Annu. Rev. Biochem. 67, 27-48.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 27-48
    • Dickson, R.C.1
  • 16
    • 0032877355 scopus 로고    scopus 로고
    • Is the protein/ lipid hydrophobic mismatching principle relevant to membrane organization and functions?
    • Dumas, F., Lebrun, M.C., and Tocanne, J.F. (1999). Is the protein/ lipid hydrophobic mismatching principle relevant to membrane organization and functions? FEBS Lett. 458, 271-277.
    • (1999) FEBS Lett. , vol.458 , pp. 271-277
    • Dumas, F.1    Lebrun, M.C.2    Tocanne, J.F.3
  • 17
    • 0022510143 scopus 로고
    • Identifying nonpolar transbilayer helices in amino acid sequences of membrane proteins
    • Engelman, D.M., Steitz, T.A., and Goldman, A. (1986). Identifying nonpolar transbilayer helices in amino acid sequences of membrane proteins. Annu. Rev. Biophys. Biophys. Chem. 15, 321-353.
    • (1986) Annu. Rev. Biophys. Biophys. Chem. , vol.15 , pp. 321-353
    • Engelman, D.M.1    Steitz, T.A.2    Goldman, A.3
  • 18
    • 0026097957 scopus 로고
    • Localization of components involved in protein transport and processing through the yeast Golgi apparatus
    • Franzusoff, A., Redding, K., Crosby, J., Fuller, R.S., and Schekman, R. (1991). Localization of components involved in protein transport and processing through the yeast Golgi apparatus. J. Cell Biol. 112, 27-37.
    • (1991) J. Cell Biol. , vol.112 , pp. 27-37
    • Franzusoff, A.1    Redding, K.2    Crosby, J.3    Fuller, R.S.4    Schekman, R.5
  • 19
    • 0033593788 scopus 로고    scopus 로고
    • Genetic evidence for ATP-dependent endoplasmic reticulum-to-Golgi apparatus trafficking of ceramide for sphingomyelin synthesis in chinese hamster ovary cells
    • Fukasawa, M., Nishijima, M., and Hanada, K. (1999). Genetic evidence for ATP-dependent endoplasmic reticulum-to-Golgi apparatus trafficking of ceramide for sphingomyelin synthesis in Chinese hamster ovary cells. J. Cell Biol. 144, 673-685.
    • (1999) J. Cell Biol. , vol.144 , pp. 673-685
    • Fukasawa, M.1    Nishijima, M.2    Hanada, K.3
  • 20
    • 0029142888 scopus 로고
    • Inhibition of sphingolipid synthesis: Effects on glycosphingolipid-GPI-anchored protein microdomains
    • Futerman, A.M. (1995). Inhibition of sphingolipid synthesis: effects on glycosphingolipid-GPI-anchored protein microdomains. Trends Cell Biol. 5, 377-380.
    • (1995) Trends Cell Biol. , vol.5 , pp. 377-380
    • Futerman, A.M.1
  • 21
    • 0025323167 scopus 로고
    • Sphingomyelin synthesis in rat liver occurs predominantly at the cis and medial cisternae of the Golgi apparatus
    • Futerman, A.H., Stieger, B., Hubbard, A.L., and Pagano, R.E. (1990). Sphingomyelin synthesis in rat liver occurs predominantly at the cis and medial cisternae of the Golgi apparatus. J. Biol. Chem. 265, 8650-8657.
    • (1990) J. Biol. Chem. , vol.265 , pp. 8650-8657
    • Futerman, A.H.1    Stieger, B.2    Hubbard, A.L.3    Pagano, R.E.4
  • 22
    • 0028171094 scopus 로고
    • Clathrin-dependent localization of α 1,3 mannosyltransferase to the Golgi complex of Saccharomyces cerevisiae
    • Graham, T.R., Seeger, M., Payne, G.S., Mackay, V.L., and Emr, S.D. (1994). Clathrin-dependent localization of α 1,3 mannosyltransferase to the Golgi complex of Saccharomyces cerevisiae. J. Cell Biol. 127, 667-678.
    • (1994) J. Cell Biol. , vol.127 , pp. 667-678
    • Graham, T.R.1    Seeger, M.2    Payne, G.S.3    Mackay, V.L.4    Emr, S.D.5
  • 23
    • 0014411770 scopus 로고
    • Cytomembrane differentiation in the endoplasmic reticulum-Golgi apparatus-vesicle complex
    • Grove, S.N., Bracker, C.E., and Morre, D.J. (1968). Cytomembrane differentiation in the endoplasmic reticulum-Golgi apparatus-vesicle complex. Science 161, 171-173.
    • (1968) Science , vol.161 , pp. 171-173
    • Grove, S.N.1    Bracker, C.E.2    Morre, D.J.3
  • 24
    • 0029032146 scopus 로고
    • Intracellular transport of inositol-containing sphingolipids in the yeast, Saccharomyces cerevisiae
    • Hechtberger, P., and Daum, G. (1995). Intracellular transport of inositol-containing sphingolipids in the yeast, Saccharomyces cerevisiae. FEBS Lett. 367, 201-204.
    • (1995) FEBS Lett. , vol.367 , pp. 201-204
    • Hechtberger, P.1    Daum, G.2
  • 25
    • 0028115977 scopus 로고
    • Characterization, quantification and subcellular localization of inositol-containing sphingolipids of the yeast, Saccharomyces cerevisiae
    • Hechtberger, P., Zinser, E., Saf, R., Hummel, K., Paltauf, F., and Daum, G. (1994). Characterization, quantification and subcellular localization of inositol-containing sphingolipids of the yeast, Saccharomyces cerevisiae. Eur. J. Biochem. 225, 641-649.
    • (1994) Eur. J. Biochem. , vol.225 , pp. 641-649
    • Hechtberger, P.1    Zinser, E.2    Saf, R.3    Hummel, K.4    Paltauf, F.5    Daum, G.6
  • 26
    • 0033991515 scopus 로고    scopus 로고
    • Inositol phosphoryl transferases from human pathogenic fungi
    • Heidler, S.A., and Radding, J.A. (2000). Inositol phosphoryl transferases from human pathogenic fungi. Biochim. Biophys. Acta 1500, 147-152.
    • (2000) Biochim. Biophys. Acta , vol.1500 , pp. 147-152
    • Heidler, S.A.1    Radding, J.A.2
  • 27
    • 0030938579 scopus 로고    scopus 로고
    • From phosphatases to vanadium peroxidases: A similar architecture of the active site
    • Hemrika, W., Renirie, R., Dekker, H.L., Barnett, P., and Wever, R. (1997). From phosphatases to vanadium peroxidases: a similar architecture of the active site. Proc. Natl. Acad. Sci. USA 94, 2145-2149.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 2145-2149
    • Hemrika, W.1    Renirie, R.2    Dekker, H.L.3    Barnett, P.4    Wever, R.5
  • 28
    • 0027413499 scopus 로고
    • The long-chain sphingoid base of sphingolipids is acylated at the cytosolic surface of the endoplasmic reticulum in rat liver
    • Hirschberg, K., Rodger, J., and Futerman, A.H. (1993). The long-chain sphingoid base of sphingolipids is acylated at the cytosolic surface of the endoplasmic reticulum in rat liver. Biochem. J. 290, 751-757.
    • (1993) Biochem. J. , vol.290 , pp. 751-757
    • Hirschberg, K.1    Rodger, J.2    Futerman, A.H.3
  • 29
    • 0032894060 scopus 로고    scopus 로고
    • The yeast proteome database (YPD): A model for the organization and presentation of genome-wide functional data
    • Hodges, P.E., McKee, A.H., Davis, B.P., Payne, W.E., and Garrels, J.I. (1999). The Yeast Proteome Database (YPD): a model for the organization and presentation of genome-wide functional data. Nucleic Acids Res. 27, 69-73.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 69-73
    • Hodges, P.E.1    McKee, A.H.2    Davis, B.P.3    Payne, W.E.4    Garrels, J.I.5
  • 30
    • 0032472324 scopus 로고    scopus 로고
    • Two syntaxin homologues in the TGN/endosomal system of yeast
    • Holthuis, J.C.M., Nichols, B.J., Dhruvakumar, S., and Pelham, H.R.B. (1998). Two syntaxin homologues in the TGN/endosomal system of yeast. EMBO J. 17, 113-126.
    • (1998) EMBO J. , vol.17 , pp. 113-126
    • Holthuis, J.C.M.1    Nichols, B.J.2    Dhruvakumar, S.3    Pelham, H.R.B.4
  • 32
    • 0026552908 scopus 로고
    • Glucosylceramide is synthesized at the cytosolic surface of various Golgi subfractions
    • Jeckel, D., Karrenbauer, A., Burger, K.N., van Meer, G., and Wieland, F. (1992). Glucosylceramide is synthesized at the cytosolic surface of various Golgi subfractions. J. Cell Biol. 117, 259-267.
    • (1992) J. Cell Biol. , vol.117 , pp. 259-267
    • Jeckel, D.1    Karrenbauer, A.2    Burger, K.N.3    Van Meer, G.A.4    Wieland, F.5
  • 33
    • 0032518685 scopus 로고    scopus 로고
    • Multi-protein complexes in the cis Golgi of Saccharomyces cerevisiae with α-1,6-mannosyltransferase activity
    • Jungmann, J., and Munro, S. (1998). Multi-protein complexes in the cis Golgi of Saccharomyces cerevisiae with α-1,6-mannosyltransferase activity. EMBO J. 17, 423-434.
    • (1998) EMBO J. , vol.17 , pp. 423-434
    • Jungmann, J.1    Munro, S.2
  • 34
    • 0033525512 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae protein Mnn10p/Bed1p is a subunit of a Golgi mannosyltransferase complex
    • Jungmann, J., Rayner, J.C., and Munro, S. (1999). The Saccharomyces cerevisiae protein Mnn10p/Bed1p is a subunit of a Golgi mannosyltransferase complex. J. Biol. Chem. 274, 6579-6585.
    • (1999) J. Biol. Chem. , vol.274 , pp. 6579-6585
    • Jungmann, J.1    Rayner, J.C.2    Munro, S.3
  • 35
    • 0029026637 scopus 로고
    • Eukaryotic phospholipid biosynthesis
    • Kent, C. (1995). Eukaryotic phospholipid biosynthesis. Annu. Rev. Biochem. 64, 315-343.
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 315-343
    • Kent, C.1
  • 36
    • 0031740415 scopus 로고    scopus 로고
    • Hydrophobic mismatch between proteins and lipids in membranes
    • Killian, J.A. (1998). Hydrophobic mismatch between proteins and lipids in membranes. Biochim. Biophys. Acta 1376, 401-415.
    • (1998) Biochim. Biophys. Acta , vol.1376 , pp. 401-415
    • Killian, J.A.1
  • 37
    • 0027936188 scopus 로고
    • Regulation of phosphatidylinositol:Ceramide phosphoinositol transferase in Saccharomyces cerevisiae
    • Ko, J., Cheah, S., and Fischl, A.S. (1994). Regulation of phosphatidylinositol:ceramide phosphoinositol transferase in Saccharomyces cerevisiae. J. Bacteriol. 176, 5181-5183.
    • (1994) J. Bacteriol. , vol.176 , pp. 5181-5183
    • Ko, J.1    Cheah, S.2    Fischl, A.S.3
  • 38
    • 0032510559 scopus 로고    scopus 로고
    • A lipid associated with the antiphospholipid syndrome regulates endosome structure and function
    • Kobayashi, T., Stang, E., Fang, K.S., de Moerloose, P., Parton, R.G., and Gruenberg, J. (1998). A lipid associated with the antiphospholipid syndrome regulates endosome structure and function. Nature 392, 193-197.
    • (1998) Nature , vol.392 , pp. 193-197
    • Kobayashi, T.1    Stang, E.2    Fang, K.S.3    De Moerloose, P.4    Parton, R.G.5    Gruenberg, J.6
  • 39
    • 0030000892 scopus 로고    scopus 로고
    • Phospholipids: Synthesis, sorting, subcellular traffic. The yeast approach
    • Kohlwein, S.D., Daum, G., Schneiter, R., and Paltauf, F. (1996). Phospholipids: synthesis, sorting, subcellular traffic. The yeast approach. Trends Cell Biol. 6, 260-266.
    • (1996) Trends Cell Biol. , vol.6 , pp. 260-266
    • Kohlwein, S.D.1    Daum, G.2    Schneiter, R.3    Paltauf, F.4
  • 40
    • 0032143958 scopus 로고    scopus 로고
    • Ceramide transport from endoplasmic reticulum to Golgi apparatus is not vesicle-mediated
    • Kok, J.W., Babia, T., Klappe, K., Egea, G., and Hoekstra, D. (1998). Ceramide transport from endoplasmic reticulum to Golgi apparatus is not vesicle-mediated. Biochem. J. 333, 779-786.
    • (1998) Biochem. J. , vol.333 , pp. 779-786
    • Kok, J.W.1    Babia, T.2    Klappe, K.3    Egea, G.4    Hoekstra, D.5
  • 41
    • 0027499143 scopus 로고
    • Non-random distribution of amino acids in the transmembrane segments of human type I single span membrane proteins
    • Landolt-Marticorena, C., Williams, K.A., Deber, C.M., and Reithmeier, R.A. (1993). Non-random distribution of amino acids in the transmembrane segments of human type I single span membrane proteins. J. Mol. Biol. 229, 602-608.
    • (1993) J. Mol. Biol. , vol.229 , pp. 602-608
    • Landolt-Marticorena, C.1    Williams, K.A.2    Deber, C.M.3    Reithmeier, R.A.4
  • 42
    • 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
  • 43
    • 0027404090 scopus 로고
    • Mutant strains of Saccharomyces cerevisiae lacking sphingolipids synthesize novel inositol glycerophospholipids that mimic sphingolipid structures
    • Lester, R.L., Wells, G.B., Oxford, G., and Dickson, R.C. (1993). Mutant strains of Saccharomyces cerevisiae lacking sphingolipids synthesize novel inositol glycerophospholipids that mimic sphingolipid structures. J. Biol. Chem. 268, 845-856.
    • (1993) J. Biol. Chem. , vol.268 , pp. 845-856
    • Lester, R.L.1    Wells, G.B.2    Oxford, G.3    Dickson, R.C.4
  • 44
    • 0021104115 scopus 로고
    • Bacteriorhodopsin remains dispersed in fluid phospholipid bilayers over a wide range of bilayer thicknesses
    • Lewis, B.A., and Engelman, D.M. (1983a). Bacteriorhodopsin remains dispersed in fluid phospholipid bilayers over a wide range of bilayer thicknesses. J. Mol. Biol. 166, 203-210.
    • (1983) J. Mol. Biol. , vol.166 , pp. 203-210
    • Lewis, B.A.1    Engelman, D.M.2
  • 45
    • 0021104058 scopus 로고
    • Lipid bilayer thickness varies linearly with acyl chain length in fluid phosphatidylcholine vesicles
    • Lewis, B.A., and Engelman, D.M. (1983b). Lipid bilayer thickness varies linearly with acyl chain length in fluid phosphatidylcholine vesicles. J. Mol. Biol. 166, 211-217.
    • (1983) J. Mol. Biol. , vol.166 , pp. 211-217
    • Lewis, B.A.1    Engelman, D.M.2
  • 46
    • 0029932226 scopus 로고    scopus 로고
    • Snare-mediated retrograde traffic from the Golgi complex to the endoplasmic reticulum
    • Lewis, M.J., and Pelham, H.R.B. (1996). SNARE-mediated retrograde traffic from the Golgi complex to the endoplasmic reticulum. Cell 85, 205-215.
    • (1996) Cell , vol.85 , pp. 205-215
    • Lewis, M.J.1    Pelham, H.R.B.2
  • 47
    • 0007712633 scopus 로고
    • Sphingolipid metabolism in cultured fibroblasts: Microscopic and biochemical studies employing a fluorescent ceramide analogue
    • Lipsky, N.G., and Pagano, R.E. (1983). Sphingolipid metabolism in cultured fibroblasts: microscopic and biochemical studies employing a fluorescent ceramide analogue. Proc. Natl. Acad. Sci. USA 80, 2608-2612.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 2608-2612
    • Lipsky, N.G.1    Pagano, R.E.2
  • 48
    • 0021958898 scopus 로고
    • Intracellular translocation of fluorescent sphingolipids in cultured fibroblasts: Endogenously synthesized sphingomyelin and glucocerebroside analogues pass through the Golgi apparatus en route to the plasma membrane
    • Lipsky, N.G., and Pagano, R.E. (1985). Intracellular translocation of fluorescent sphingolipids in cultured fibroblasts: endogenously synthesized sphingomyelin and glucocerebroside analogues pass through the Golgi apparatus en route to the plasma membrane. J. Cell Biol. 100, 27-34.
    • (1985) J. Cell Biol. , vol.100 , pp. 27-34
    • Lipsky, N.G.1    Pagano, R.E.2
  • 49
    • 0029034940 scopus 로고
    • Intracellular cholesterol transport and compartmentation
    • Liscum, L., and Underwood, K.W. (1995). Intracellular cholesterol transport and compartmentation. J. Biol. Chem. 270, 15443-15446.
    • (1995) J. Biol. Chem. , vol.270 , pp. 15443-15446
    • Liscum, L.1    Underwood, K.W.2
  • 50
    • 0026446549 scopus 로고
    • SHR3: A novel component of the secretory pathway specifically required for localization of amino acid permeases in yeast
    • Ljungdahl, P.O., Gimeno, C.J., Styles, C.A., and Fink, G.R. (1992). SHR3: a novel component of the secretory pathway specifically required for localization of amino acid permeases in yeast. Cell 71, 463-478.
    • (1992) Cell , vol.71 , pp. 463-478
    • Ljungdahl, P.O.1    Gimeno, C.J.2    Styles, C.A.3    Fink, G.R.4
  • 51
    • 0028832626 scopus 로고
    • Localization and targeting of the Saccharomyces cerevisiae Kre2p/Mnt1p α1,2-mannosyltransferase to a medial-Golgi compartment
    • Lussier, M., Sdicu, A.M., Ketela, T., and Bussey, H. (1995). Localization and targeting of the Saccharomyces cerevisiae Kre2p/Mnt1p α1,2-mannosyltransferase to a medial-Golgi compartment. J. Cell Biol. 131, 913-927.
    • (1995) J. Cell Biol. , vol.131 , pp. 913-927
    • Lussier, M.1    Sdicu, A.M.2    Ketela, T.3    Bussey, H.4
  • 52
    • 0026712872 scopus 로고
    • Subcellular localization and membrane topology of serine palmitoyltransferase, 3-dehydrosphinganine reductase, and sphinganine N-acyltransferase in mouse liver
    • Mandon, E.C., Ehses, I., Rother, J., van Echten, G., and Sandhoff, K. (1992). Subcellular localization and membrane topology of serine palmitoyltransferase, 3-dehydrosphinganine reductase, and sphinganine N-acyltransferase in mouse liver. J. Biol. Chem. 267, 11144-11148.
    • (1992) J. Biol. Chem. , vol.267 , pp. 11144-11148
    • Mandon, E.C.1    Ehses, I.2    Rother, J.3    Van Echten, G.A.4    Sandhoff, K.5
  • 53
    • 0027533511 scopus 로고
    • Cholesterol deprivation affects the fluorescence properties of a ceramide analog at the Golgi apparatus of living cells
    • Martin, O.C., Comly, M.E., Blanchette-Mackie, E.J., Pentchev, P.G., and Pagano, R.E. (1993). Cholesterol deprivation affects the fluorescence properties of a ceramide analog at the Golgi apparatus of living cells. Proc. Natl. Acad. Sci. USA 90, 2661-2665.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 2661-2665
    • Martin, O.C.1    Comly, M.E.2    Blanchette-Mackie, E.J.3    Pentchev, P.G.4    Pagano, R.E.5
  • 54
    • 0029133322 scopus 로고
    • A comparison of the transmembrane domains of Golgi and plasma membrane proteins
    • Munro, S. (1995). A comparison of the transmembrane domains of Golgi and plasma membrane proteins. Biochem. Soc. Trans. 23, 527-530.
    • (1995) Biochem. Soc. Trans. , vol.23 , pp. 527-530
    • Munro, S.1
  • 55
    • 0030970048 scopus 로고    scopus 로고
    • Sphingolipid synthesis as a target for antifungal drugs: Complementation of the inositol phosphorylceramide synthase defect in a mutant strain of Saccharomyces cerevisiae by the AUR1 gene
    • Nagiec, M.M., Nagiec, E.E., Baltisberger, J.A., Wells, G.B., Lester, R.L., and Dickson, R.C. (1997). Sphingolipid synthesis as a target for antifungal drugs: complementation of the inositol phosphorylceramide synthase defect in a mutant strain of Saccharomyces cerevisiae by the AUR1 gene. J. Biol. Chem. 272, 9809-9817.
    • (1997) J. Biol. Chem. , vol.272 , pp. 9809-9817
    • Nagiec, M.M.1    Nagiec, E.E.2    Baltisberger, J.A.3    Wells, G.B.4    Lester, R.L.5    Dickson, R.C.6
  • 56
    • 0027438892 scopus 로고
    • A suppressor gene that enables Saccharomyces cerevisiae to grow without making sphingolipids encodes a protein that resembles an Escherichia coli fatty acyltransferase
    • Nagiec, M.M., Wells, G.B., Lester, R.L., and Dickson, R.C. (1993). A suppressor gene that enables Saccharomyces cerevisiae to grow without making sphingolipids encodes a protein that resembles an Escherichia coli fatty acyltransferase. J. Biol. Chem. 268, 22156-22163.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22156-22163
    • Nagiec, M.M.1    Wells, G.B.2    Lester, R.L.3    Dickson, R.C.4
  • 57
    • 0026752711 scopus 로고
    • Immunological evidence that plants use both HDEL and KDEL for targeting proteins to the endoplasmic reticulum
    • Napier, R.M., Fowke, L.C., Hawes, C., Lewis, M., and Pelham, H.R.B. (1992). Immunological evidence that plants use both HDEL and KDEL for targeting proteins to the endoplasmic reticulum. J. Cell Sci. 102, 261-271.
    • (1992) J. Cell Sci. , vol.102 , pp. 261-271
    • Napier, R.M.1    Fowke, L.C.2    Hawes, C.3    Lewis, M.4    Pelham, H.R.B.5
  • 58
    • 0030753213 scopus 로고    scopus 로고
    • An unexpected structural relationship between integral membrane phosphatases and soluble haloperoxidases
    • Neuwald, A.F. (1997). An unexpected structural relationship between integral membrane phosphatases and soluble haloperoxidases. Protein Sci. 6, 1764-1767.
    • (1997) Protein Sci. , vol.6 , pp. 1764-1767
    • Neuwald, A.F.1
  • 59
    • 0026704101 scopus 로고
    • Combined influence of cholesterol and synthetic amphiphilic peptides upon bilayer thickness in model membranes
    • Nezil, F.A., and Bloom, M. (1992). Combined influence of cholesterol and synthetic amphiphilic peptides upon bilayer thickness in model membranes. Biophys. J. 61, 1176-1183.
    • (1992) Biophys. J. , vol.61 , pp. 1176-1183
    • Nezil, F.A.1    Bloom, M.2
  • 60
    • 0029834675 scopus 로고    scopus 로고
    • Interleaflet clear space is reduced in the membrane of COP I and COP II-coated buds/vesicles
    • Orci, L., Schekman, R., and Perrelet, A. (1996). Interleaflet clear space is reduced in the membrane of COP I and COP II-coated buds/vesicles. Proc. Natl. Acad. Sci. USA 93, 8968-8970.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 8968-8970
    • Orci, L.1    Schekman, R.2    Perrelet, A.3
  • 61
    • 0025744372 scopus 로고
    • A novel fluorescent ceramide analogue for studying membrane traffic in animal cells: Accumulation at the Golgi apparatus results in altered spectral properties of the sphingolipid precursor
    • Pagano, R.E., Martin, O.C., Kang, H.C., and Haugland, R.P. (1991). A novel fluorescent ceramide analogue for studying membrane traffic in animal cells: accumulation at the Golgi apparatus results in altered spectral properties of the sphingolipid precursor. J. Cell Biol. 113, 1267-1279.
    • (1991) J. Cell Biol. , vol.113 , pp. 1267-1279
    • Pagano, R.E.1    Martin, O.C.2    Kang, H.C.3    Haugland, R.P.4
  • 62
    • 0024470450 scopus 로고
    • Molecular trapping of a fluorescent ceramide analogue at the Golgi apparatus of fixed cells: Interaction with endogenous lipids provides a trans-Golgi marker for both light and electron microscopy
    • Pagano, R.E., Sepanski, M.A., and Martin, O.C. (1989). Molecular trapping of a fluorescent ceramide analogue at the Golgi apparatus of fixed cells: interaction with endogenous lipids provides a trans-Golgi marker for both light and electron microscopy. J. Cell Biol. 109, 2067-2079.
    • (1989) J. Cell Biol. , vol.109 , pp. 2067-2079
    • Pagano, R.E.1    Sepanski, M.A.2    Martin, O.C.3
  • 63
    • 0025760201 scopus 로고
    • The phosphoinositol sphingolipids of Saccharomyces cerevisiae are highly localized in the plasma membrane
    • Patton, J.L., and Lester, R.L. (1991). The phosphoinositol sphingolipids of Saccharomyces cerevisiae are highly localized in the plasma membrane. J. Bacteriol. 173, 3101-3108.
    • (1991) J. Bacteriol. , vol.173 , pp. 3101-3108
    • Patton, J.L.1    Lester, R.L.2
  • 64
    • 0014900757 scopus 로고
    • Correlative relationship of cholesterol and sphingomyelin in cell membranes
    • Patton, S. (1970). Correlative relationship of cholesterol and sphingomyelin in cell membranes. J. Theor. Biol. 29, 489-491.
    • (1970) J. Theor. Biol. , vol.29 , pp. 489-491
    • Patton, S.1
  • 65
    • 0032493933 scopus 로고    scopus 로고
    • Transport of ax12p depends on erv14p, an ER-vesicle protein related to the Drosophila cornichon gene product
    • Powers, J., and Barlowe, C. (1998). Transport of ax12p depends on erv14p, an ER-vesicle protein related to the Drosophila cornichon gene product. J. Cell Biol. 142, 1209-1222.
    • (1998) J. Cell Biol. , vol.142 , pp. 1209-1222
    • Powers, J.1    Barlowe, C.2
  • 66
    • 0025844928 scopus 로고
    • Biosynthesis of mannosylinositolphosphoceramide in Saccharomyces cerevisiae is dependent on genes controlling the flow of secretory vesicles from the endoplasmic reticulum to the Golgi
    • Puoti, A., Desponds, C., and Conzelmann, A. (1991). Biosynthesis of mannosylinositolphosphoceramide in Saccharomyces cerevisiae is dependent on genes controlling the flow of secretory vesicles from the endoplasmic reticulum to the Golgi. J. Cell Biol. 113, 515-525.
    • (1991) J. Cell Biol. , vol.113 , pp. 515-525
    • Puoti, A.1    Desponds, C.2    Conzelmann, A.3
  • 67
    • 0033031744 scopus 로고    scopus 로고
    • Interaction of cholesterol with sphingomyelins and acyl-chain-matched phosphatidylcholines: A comparative study of the effect of the chain length
    • Ramstedt, B., and Slotte, J.P. (1999). Interaction of cholesterol with sphingomyelins and acyl-chain-matched phosphatidylcholines: a comparative study of the effect of the chain length. Biophys. J. 76, 908-915.
    • (1999) Biophys. J. , vol.76 , pp. 908-915
    • Ramstedt, B.1    Slotte, J.P.2
  • 68
    • 0032500541 scopus 로고    scopus 로고
    • Identification of the MNN2 and MNN5 mannosyltransferases required for forming and extending the mannose branches of the outer chain mannans of Saccharomyces cerevisiae
    • Rayner, J.C., and Munro, S. (1998). Identification of the MNN2 and MNN5 mannosyltransferases required for forming and extending the mannose branches of the outer chain mannans of Saccharomyces cerevisiae. J. Biol. Chem. 273, 26836-26843.
    • (1998) J. Biol. Chem. , vol.273 , pp. 26836-26843
    • Rayner, J.C.1    Munro, S.2
  • 69
    • 0019885883 scopus 로고
    • Phase equilibria in binary mixtures of phosphatidykholine and cholesterol
    • Recktenwald, D.J., and McConnell, H.M. (1981). Phase equilibria in binary mixtures of phosphatidykholine and cholesterol. Biochemistry 20, 4505-4510.
    • (1981) Biochemistry , vol.20 , pp. 4505-4510
    • Recktenwald, D.J.1    McConnell, H.M.2
  • 70
    • 0023739386 scopus 로고
    • Protein sorting in Saccharomyces cerevisiae: Isolation of mutants defective in the delivery and processing of multiple vacuolar hydrolases
    • Robinson, J.S., Klionsky, D.J., Banta, L.M., and Emr, S.D. (1988). Protein sorting in Saccharomyces cerevisiae: isolation of mutants defective in the delivery and processing of multiple vacuolar hydrolases. Mol. Cell. Biol. 8, 4936-4948.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 4936-4948
    • Robinson, J.S.1    Klionsky, D.J.2    Banta, L.M.3    Emr, S.D.4
  • 71
    • 0033526048 scopus 로고    scopus 로고
    • Golgi structure correlates with transitional endoplasmic reticulum organization in Pichia pastoris and Saccharomyces cerevisiae
    • Rossanese, O.W., Soderholm, J., Bevis, B.J., Sears, I.B., O'Connor, J., Williamson, E.K., and Click, B.S. (1999). Golgi structure correlates with transitional endoplasmic reticulum organization in Pichia pastoris and Saccharomyces cerevisiae. J. Cell Biol. 145, 69-81.
    • (1999) J. Cell Biol. , vol.145 , pp. 69-81
    • Rossanese, O.W.1    Soderholm, J.2    Bevis, B.J.3    Sears, I.B.4    O'Connor, J.5    Williamson, E.K.6    Click, B.S.7
  • 72
    • 0030038634 scopus 로고    scopus 로고
    • Topology prediction for helical transmembrane proteins at 86% accuracy
    • Rost, B., Fariselli, P., and Casadio, R. (1996). Topology prediction for helical transmembrane proteins at 86% accuracy. Protein Sci. 5, 1704-1718.
    • (1996) Protein Sci. , vol.5 , pp. 1704-1718
    • Rost, B.1    Fariselli, P.2    Casadio, R.3
  • 73
    • 0026795003 scopus 로고
    • Protein rotational diffusion and lipid/protein interactions in recombinants of bovine rhodopsin with saturated diacylphosphatidylcholines of different chain lengths studied by conventional and saturation-transfer electron spin resonance
    • Ryba, N.J.P., and Marsh, D. (1992). Protein rotational diffusion and lipid/protein interactions in recombinants of bovine rhodopsin with saturated diacylphosphatidylcholines of different chain lengths studied by conventional and saturation-transfer electron spin resonance. Biochemistry 31, 7511-7518.
    • (1992) Biochemistry , vol.31 , pp. 7511-7518
    • Ryba, N.J.P.1    Marsh, D.2
  • 74
    • 0345363228 scopus 로고    scopus 로고
    • Electrospray ionization tandem mass spectrometry (ESI-MS/MS) analysis of the lipid molecular species composition of yeast subcellular membranes reveals acyl chain-based sorting/remodeling of distinct molecular species en route to the plasma membrane
    • Schneiter, R., et al. (1999). Electrospray ionization tandem mass spectrometry (ESI-MS/MS) analysis of the lipid molecular species composition of yeast subcellular membranes reveals acyl chain-based sorting/remodeling of distinct molecular species en route to the plasma membrane. J. Cell Biol. 146, 741-754.
    • (1999) J. Cell Biol. , vol.146 , pp. 741-754
    • Schneiter, R.1
  • 75
    • 0028840671 scopus 로고
    • The Golgi-localization of yeast Emp47p depends on its dilysine motif but is not affected by the ret1-1 mutation in α-COP
    • Schröder, S., Schimmöller, F., Singer-Krüger, B., and Riezman, H. (1995). The Golgi-localization of yeast Emp47p depends on its dilysine motif but is not affected by the ret1-1 mutation in α-COP. J. Cell Biol. 131, 895-912.
    • (1995) J. Cell Biol. , vol.131 , pp. 895-912
    • Schröder, S.1    Schimmöller, F.2    Singer-Krüger, B.3    Riezman, H.4
  • 76
    • 0031694848 scopus 로고    scopus 로고
    • A yeast t-SNARE involved in endocytosis
    • Seron, K., et al. (1998). A yeast t-SNARE involved in endocytosis. Mol. Biol. Cell 9, 2873-2889.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 2873-2889
    • Seron, K.1
  • 77
    • 0033594914 scopus 로고    scopus 로고
    • Efficient export of the glucose transporter Hxt1p from the endoplasmic reticulum requires Gsf2p
    • Sherwood, P.W., and Carlson, M. (1999). Efficient export of the glucose transporter Hxt1p from the endoplasmic reticulum requires Gsf2p. Proc. Natl. Acad. Sci. USA 96, 7415-7420.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 7415-7420
    • Sherwood, P.W.1    Carlson, M.2
  • 78
    • 0023788823 scopus 로고
    • Lipid sorting in epithelial cells
    • Simons, K., and van Meer, G. (1988). Lipid sorting in epithelial cells. Biochemistry 27, 6197-6202.
    • (1988) Biochemistry , vol.27 , pp. 6197-6202
    • Simons, K.1    Van Meer, G.2
  • 79
    • 0031614678 scopus 로고    scopus 로고
    • A hidden markov model for predicting transmembrane helices in protein sequences
    • Sonnhammer, E.L., von Heijne, G., and Krogh, A. (1998). A hidden Markov model for predicting transmembrane helices in protein sequences. Ismb 6, 175-182.
    • (1998) Ismb , vol.6 , pp. 175-182
    • Sonnhammer, E.L.1    Von Heijne, G.A.2    Krogh, A.3
  • 80
    • 0031048876 scopus 로고    scopus 로고
    • Identification of a novel phosphatase sequence motif
    • Stukey, J., and Carman, G.M. (1997). Identification of a novel phosphatase sequence motif. Protein Sci. 6, 469-472.
    • (1997) Protein Sci. , vol.6 , pp. 469-472
    • Stukey, J.1    Carman, G.M.2
  • 81
    • 0030665269 scopus 로고    scopus 로고
    • Specific requirements for the ER to Golgi transport of GPI-anchored proteins in yeast
    • Sutterlin, C., Doering, T.L., Schimmoller, F., Schroder, S., and Riezman, H. (1997). Specific requirements for the ER to Golgi transport of GPI-anchored proteins in yeast. J. Cell Sci. 110, 2703-2714.
    • (1997) J. Cell Sci. , vol.110 , pp. 2703-2714
    • Sutterlin, C.1    Doering, T.L.2    Schimmoller, F.3    Schroder, S.4    Riezman, H.5
  • 82
    • 0033553884 scopus 로고    scopus 로고
    • Chs7p, a new protein involved in the control of protein export from the endoplasmic reticulum that is specifically engaged in the regulation of chitin synthesis in Saccharomyces cerevisiae
    • Trilla, J.A., Duran, A., and Roncero, C. (1999). Chs7p, a new protein involved in the control of protein export from the endoplasmic reticulum that is specifically engaged in the regulation of chitin synthesis in Saccharomyces cerevisiae. J. Cell Biol. 145, 1153-1163.
    • (1999) J. Cell Biol. , vol.145 , pp. 1153-1163
    • Trilla, J.A.1    Duran, A.2    Roncero, C.3
  • 83
    • 0031738656 scopus 로고    scopus 로고
    • Eukaryotic lipid-biosynthetic enzymes: The same but not the same
    • Vance, J.E. (1998). Eukaryotic lipid-biosynthetic enzymes: the same but not the same. Trends Biochem. Sci. 23, 423-428.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 423-428
    • Vance, J.E.1
  • 84
    • 0031034056 scopus 로고    scopus 로고
    • 6-NBD-sphingomyelin is translocated across the plasma membrane by a multidrug transporter activity
    • 6-NBD-sphingomyelin is translocated across the plasma membrane by a multidrug transporter activity. J. Cell Sci. 110, 75-83.
    • (1997) J. Cell Sci. , vol.110 , pp. 75-83
    • Helvoort, A.1    Giudici, M.L.2    Thielemans, M.3    Van Meer, G.4
  • 85
    • 0007544439 scopus 로고    scopus 로고
    • MDR1 P-glycoprotein is a lipid translocase of broad specificity, while MDR3 P-glycoprotein specifically translocates phosphatidylcholine
    • van Helvoort, A., Smith, A.J., Sprong, H., Fritzsche, I., Schinkel, A.H., Borst, P., and van Meer, G. (1996). MDR1 P-glycoprotein is a lipid translocase of broad specificity, while MDR3 P-glycoprotein specifically translocates phosphatidylcholine. Cell 87, 507-517.
    • (1996) Cell , vol.87 , pp. 507-517
    • Van Helvoort, A.1    Smith, A.J.2    Sprong, H.3    Fritzsche, I.4    Schinkel, A.H.5    Borst, P.6    Van Meer, G.7
  • 86
    • 0024448087 scopus 로고
    • Lipid traffic in animal cells
    • van Meer, G. (1989). Lipid traffic in animal cells. Annu. Rev. Cell Biol. 5, 247-275.
    • (1989) Annu. Rev. Cell Biol. , vol.5 , pp. 247-275
    • Van Meer, G.1
  • 87
    • 0031985361 scopus 로고    scopus 로고
    • Lipids of the Golgi membrane
    • van Meer, G. (1998). Lipids of the Golgi membrane. Trends Cell Biol. 8, 29-33.
    • (1998) Trends Cell Biol. , vol.8 , pp. 29-33
    • Van Meer, G.1
  • 88
    • 0023432865 scopus 로고
    • Sorting of sphingolipids in epithelial (Madin-Darby canine kidney) cells
    • van Meer, G., Stelzer, E.H., Wijnaendts-van-Resandt, R.W., and Simons, K. (1987). Sorting of sphingolipids in epithelial (Madin-Darby canine kidney) cells. J. Cell Biol. 105, 1623-1635.
    • (1987) J. Cell Biol. , vol.105 , pp. 1623-1635
    • Meer, G.1    Stelzer, E.H.2    Wijnaendts-Van-Resandt, R.W.3    Simons, K.4
  • 89
    • 0023676242 scopus 로고
    • Topogenic signals in integral membrane proteins
    • von Heijne, G., and Gavel, Y. (1988). Topogenic signals in integral membrane proteins. Eur. J. Biochem. 174, 671-678.
    • (1988) Eur. J. Biochem. , vol.174 , pp. 671-678
    • Von Heijne, G.A.1    Gavel, Y.2
  • 90
    • 0030840519 scopus 로고    scopus 로고
    • Heterologous H1S3 marker and GFP reporter modules for PCR-targeting in Saccharomyces cerevisiae
    • Wach, A., Brachat, A., AlbertiSegui, C., Rebischung, C., and Philippsen, P. (1997). Heterologous H1S3 marker and GFP reporter modules for PCR-targeting in Saccharomyces cerevisiae. Yeast 13, 1065-1075.
    • (1997) Yeast , vol.13 , pp. 1065-1075
    • Wach, A.1    Brachat, A.2    Albertisegui, C.3    Rebischung, C.4    Philippsen, P.5
  • 91
    • 0032775582 scopus 로고    scopus 로고
    • Structural organization of mammalian lipid phosphate phosphatases: Implications for signal transduction
    • Waggoner, D.W., Xu, J., Singh, I., Jasinska, R., Zhang, Q.X., and Brindley, D.N. (1999). Structural organization of mammalian lipid phosphate phosphatases: implications for signal transduction. Biochim. Biophys. Acta 1439, 299-316.
    • (1999) Biochim. Biophys. Acta , vol.1439 , pp. 299-316
    • Waggoner, D.W.1    Xu, J.2    Singh, I.3    Jasinska, R.4    Zhang, Q.X.5    Brindley, D.N.6
  • 92
    • 0032512417 scopus 로고    scopus 로고
    • Hydrophobic mismatch and the incorporation of peptides into lipid bilayers: A possible mechanism for retention in the Golgi
    • Webb, K.J., East, J.M., Sharma, R.P., and Lee, A.G. (1998). Hydrophobic mismatch and the incorporation of peptides into lipid bilayers: a possible mechanism for retention in the Golgi. Biochemistry 37, 673-679.
    • (1998) Biochemistry , vol.37 , pp. 673-679
    • Webb, K.J.1    East, J.M.2    Sharma, R.P.3    Lee, A.G.4
  • 93
    • 0031665836 scopus 로고    scopus 로고
    • The dynamics of Golgi protein traffic visualized in living yeast cells
    • Wooding, S., and Pelham, H.R. (1998). The dynamics of Golgi protein traffic visualized in living yeast cells. Mol. Biol. Cell 9, 2667-2680.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 2667-2680
    • Wooding, S.1    Pelham, H.R.2
  • 94
    • 0033406057 scopus 로고    scopus 로고
    • Inhibition of yeast inositol phosphorylceramide synthase by aureobasidin A measured by a fluorometric assay
    • Zhong, W., Murphy, D.J., and Georgopapadakou, N.H. (1999). Inhibition of yeast inositol phosphorylceramide synthase by aureobasidin A measured by a fluorometric assay. FEBS Lett. 463, 241-244.
    • (1999) FEBS Lett. , vol.463 , pp. 241-244
    • Zhong, W.1    Murphy, D.J.2    Georgopapadakou, N.H.3
  • 95
    • 0027231368 scopus 로고
    • Sterol composition of yeast organelle membranes and subcellular distribution of enzymes involved in sterol metabolism
    • Zinser, E., Paltauf, F., and Daum, G. (1993). Sterol composition of yeast organelle membranes and subcellular distribution of enzymes involved in sterol metabolism. J. Bacteriol. 175, 2853-2858.
    • (1993) J. Bacteriol. , vol.175 , pp. 2853-2858
    • Zinser, E.1    Paltauf, F.2    Daum, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.