메뉴 건너뛰기




Volumn 18, Issue 6, 1999, Pages 1506-1515

Sac1p plays a crucial role in microsomal ATP transport, which is distinct from its function in Golgi phospholipid metabolism

Author keywords

Inositol; Microsomal ATP transport; Phospholipid metabolism; Protein trafficking; Sac1p

Indexed keywords

ADENOSINE TRIPHOSPHATE; CARRIER PROTEIN; PHOSPHATASE; PROTEIN; PROTEIN SAC1P; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

EID: 0038832051     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/18.6.1506     Document Type: Article
Times cited : (54)

References (51)
  • 1
    • 0031010772 scopus 로고    scopus 로고
    • Transporters of nucleotide sugars, nucleotide sulfate and ATP in the Golgi apparatus
    • Abeijon, C., Mandon, E.C. and Hirschberg, C.B. (1997) Transporters of nucleotide sugars, nucleotide sulfate and ATP in the Golgi apparatus. Trends Biochem. Sci. 22, 203-207.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 203-207
    • Abeijon, C.1    Mandon, E.C.2    Hirschberg, C.B.3
  • 4
    • 0025094319 scopus 로고
    • An essential role for a phospholipid transfer protein in yeast Golgi function
    • Bankaitis, V.A., Aitken, J.R., Cleves, A.E. and Dowhan, W. (1990) An essential role for a phospholipid transfer protein in yeast Golgi function. Nature, 347, 561-562.
    • (1990) Nature , vol.347 , pp. 561-562
    • Bankaitis, V.A.1    Aitken, J.R.2    Cleves, A.E.3    Dowhan, W.4
  • 5
    • 0029802682 scopus 로고    scopus 로고
    • SSI1 encodes a novel Hsp70 of the saccharomyces cerevisiae endoplasmic reticulum
    • Baxter, B.K., James, P., Evans, T. and Craig, E.A. (1996) SSI1 encodes a novel Hsp70 of the Saccharomyces cerevisiae endoplasmic reticulum. Mol. Cell. Biol., 16, 6444-6456.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6444-6456
    • Baxter, B.K.1    James, P.2    Evans, T.3    Craig, E.A.4
  • 6
    • 0023484186 scopus 로고
    • 5-Fluoroorotic acid as a selective agent in yeast molecular genetics
    • Boeke, J.D., Trueheart, J., Natsoulis, G. and Fink, G.R. (1987) 5-Fluoroorotic acid as a selective agent in yeast molecular genetics. Methods Enzymol., 154, 164-175.
    • (1987) Methods Enzymol. , vol.154 , pp. 164-175
    • Boeke, J.D.1    Trueheart, J.2    Natsoulis, G.3    Fink, G.R.4
  • 7
    • 0031561105 scopus 로고    scopus 로고
    • Sac1p of Saccharomyces cerevisiae is not involved in ATP release to the extracellular fluid
    • Boyum, R. and Guidotti, G. (1997) Sac1p of Saccharomyces cerevisiae is not involved in ATP release to the extracellular fluid. Biochem. Biophys. Res. Commun., 236, 50-53.
    • (1997) Biochem. Biophys. Res. Commun. , vol.236 , pp. 50-53
    • Boyum, R.1    Guidotti, G.2
  • 9
    • 0026665249 scopus 로고
    • Translocation of ATP into the lumen of rough endoplasmic reticulum-derived vesicles and its binding to luminal proteins including BiP (GRP 78) and GRP 94
    • Clairmont, C.A., De-Maio, A. and Hirschberg, C.B. (1992) Translocation of ATP into the lumen of rough endoplasmic reticulum-derived vesicles and its binding to luminal proteins including BiP (GRP 78) and GRP 94. J. Biol. Chem., 267, 3983-3990.
    • (1992) J. Biol. Chem. , vol.267 , pp. 3983-3990
    • Clairmont, C.A.1    De-Maio, A.2    Hirschberg, C.B.3
  • 10
    • 0024828304 scopus 로고
    • Mutations in the SAC1 gene suppress defects in yeast Golgi and yeast actin function
    • Cleves, A.E., Novick, P.J. and Bankaitis, V.A. (1989) Mutations in the SAC1 gene suppress defects in yeast Golgi and yeast actin function. J. Cell Biol., 109, 2939-2950.
    • (1989) J. Cell Biol. , vol.109 , pp. 2939-2950
    • Cleves, A.E.1    Novick, P.J.2    Bankaitis, V.A.3
  • 11
    • 0025831816 scopus 로고
    • Phospholipid transfer proteins: A biological debut
    • Cleves, A.E., McGee, T.P. and Bankaitis, V.A. (1991a) Phospholipid transfer proteins: a biological debut. Trends Cell Biol., 1, 30-34.
    • (1991) Trends Cell Biol. , vol.1 , pp. 30-34
    • Cleves, A.E.1    McGee, T.P.2    Bankaitis, V.A.3
  • 12
    • 0026073075 scopus 로고
    • Mutations in the CDP-choline pathway for phospholipid biosynthesis bypass the requirement for an essential phospholipid transfer protein
    • Cleves, A.E., McGee, T.P., Whitters, E.A., Champion, J.R., Aitken, J.R., Dowhan, W., Goebl, M. and Bankaitis, V.A. (1991b) Mutations in the CDP-choline pathway for phospholipid biosynthesis bypass the requirement for an essential phospholipid transfer protein. Cell, 64, 789-800.
    • (1991) Cell , vol.64 , pp. 789-800
    • Cleves, A.E.1    McGee, T.P.2    Whitters, E.A.3    Champion, J.R.4    Aitken, J.R.5    Dowhan, W.6    Goebl, M.7    Bankaitis, V.A.8
  • 13
    • 0030297537 scopus 로고    scopus 로고
    • A novel mechanism for regulating activity of a transcription factor that controls the unfolded protein response
    • Cox, J.S. and Walter, P. (1996) A novel mechanism for regulating activity of a transcription factor that controls the unfolded protein response. Cell, 87, 357-359.
    • (1996) Cell , vol.87 , pp. 357-359
    • Cox, J.S.1    Walter, P.2
  • 14
    • 0027324844 scopus 로고
    • Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase
    • Cox, J.S., Shamu, C.E. and Walter, P. (1993) Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase. Cell, 73, 1197-1206.
    • (1993) Cell , vol.73 , pp. 1197-1206
    • Cox, J.S.1    Shamu, C.E.2    Walter, P.3
  • 15
    • 0030879870 scopus 로고    scopus 로고
    • The unfolded protein response coordinates the production of endoplasmic reticulum protein and endoplasmic reticulum membrane
    • Cox, J.S., Chapman, R.E. and Walter, P. (1997) The unfolded protein response coordinates the production of endoplasmic reticulum protein and endoplasmic reticulum membrane. Mol. Biol. Cell. 8, 1805-1814.
    • (1997) Mol. Biol. Cell. , vol.8 , pp. 1805-1814
    • Cox, J.S.1    Chapman, R.E.2    Walter, P.3
  • 16
    • 0029968296 scopus 로고    scopus 로고
    • Phosphoinositides as regulators in membrane traffic
    • De Camilli, P., Emr, S.D., McPherson, P.S. and Novick, P. (1996) Phosphoinositides as regulators in membrane traffic. Science, 271, 1533-1539.
    • (1996) Science , vol.271 , pp. 1533-1539
    • De Camilli, P.1    Emr, S.D.2    McPherson, P.S.3    Novick, P.4
  • 17
    • 0026584271 scopus 로고
    • Protein folding in the cell
    • Gething, M.-J. and Sambrook, J.F. (1992) Protein folding in the cell. Nature, 355, 33-45.
    • (1992) Nature , vol.355 , pp. 33-45
    • Gething, M.-J.1    Sambrook, J.F.2
  • 18
    • 0024266139 scopus 로고
    • New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites
    • Gietz, R.D. and Sugino, A. (1988) New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites. Gene, 74, 527-534.
    • (1988) Gene , vol.74 , pp. 527-534
    • Gietz, R.D.1    Sugino, A.2
  • 19
    • 0029001112 scopus 로고
    • Transport of adenosine-triphosphate into endoplasmic-reticulum proteoliposomes
    • Guillen, E. and Hirschberg, C.B. (1995) Transport of adenosine-triphosphate into endoplasmic-reticulum proteoliposomes. Biochemistry, 34, 5472-5476.
    • (1995) Biochemistry , vol.34 , pp. 5472-5476
    • Guillen, E.1    Hirschberg, C.B.2
  • 20
    • 16144363243 scopus 로고    scopus 로고
    • Cer1p, a novel Hsp70-related protein required for posttranslational endoplasmic reticulum translocation in yeast
    • Hamilton, T.G. and Flynn, G.C. (1996) Cer1p, a novel Hsp70-related protein required for posttranslational endoplasmic reticulum translocation in yeast. J. Biol. Chem., 271, 30610-30613.
    • (1996) J. Biol. Chem. , vol.271 , pp. 30610-30613
    • Hamilton, T.G.1    Flynn, G.C.2
  • 21
    • 0024440559 scopus 로고
    • Galactose as gratuitous inducer of GAL gene expression in yeasts growing on glucose
    • Hovland, P., Flick, J., Johnston, M. and Sclafani, R.A. (1989) Galactose as gratuitous inducer of GAL gene expression in yeasts growing on glucose. Gene, 83, 57-64.
    • (1989) Gene , vol.83 , pp. 57-64
    • Hovland, P.1    Flick, J.2    Johnston, M.3    Sclafani, R.A.4
  • 23
    • 0021848614 scopus 로고
    • Coordinate regulation of phospholipid biosynthesis in saccharomyces cerevisicie: Pleiotropically constitutive opi1 mutant
    • Klig, L.S., Homann, M.J., Carman, G.M. and Henry, S.A. (1985) Coordinate regulation of phospholipid biosynthesis in Saccharomyces cerevisicie: pleiotropically constitutive opi1 mutant. J. Bacteriol., 162, 1135-1141.
    • (1985) J. Bacteriol. , vol.162 , pp. 1135-1141
    • Klig, L.S.1    Homann, M.J.2    Carman, G.M.3    Henry, S.A.4
  • 24
    • 0027465942 scopus 로고
    • The promoter region of the yeast KAR2 (BiP) gene contains a regulatory domain that responds to the presence of unfolded proteins in the endoplasmic reticulum
    • Kohno, O., Normington, K., Sambrook, J., Gething, M.J. and Mori, K. (1993) The promoter region of the yeast KAR2 (BiP) gene contains a regulatory domain that responds to the presence of unfolded proteins in the endoplasmic reticulum. Mol. Cell. Biol., 13, 877-890.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 877-890
    • Kohno, O.1    Normington, K.2    Sambrook, J.3    Gething, M.J.4    Mori, K.5
  • 25
    • 0029926584 scopus 로고    scopus 로고
    • Different subcellular localization of saccharomyces cerevisiae HMG-CoA reductase isozymes at elevated levels corresponds to distinct endoplasmic reticulum membrane proliferations
    • Koning, A.J., Roberts, C.J. and Wright, R.L. (1996) Different subcellular localization of Saccharomyces cerevisiae HMG-CoA reductase isozymes at elevated levels corresponds to distinct endoplasmic reticulum membrane proliferations. Mol. Biol. Cell, 7, 769-789.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 769-789
    • Koning, A.J.1    Roberts, C.J.2    Wright, R.L.3
  • 26
    • 0030013233 scopus 로고    scopus 로고
    • Evidence that phospholipase-D mediates ADP-ribosylation factor-dependent formation of Golgi coated vesicles
    • Ktistakis, N.T. Brown, H.A., Waters, M.G., Sternweis, P.C. and Roth, M.G. (1996) Evidence that phospholipase-D mediates ADP-ribosylation factor-dependent formation of Golgi coated vesicles. J. Cell Biol., 134, 295-306.
    • (1996) J. Cell Biol. , vol.134 , pp. 295-306
    • Ktistakis, N.T.1    Brown, H.A.2    Waters, M.G.3    Sternweis, P.C.4    Roth, M.G.5
  • 27
    • 0030970268 scopus 로고    scopus 로고
    • Binding of secretory precursor polypeptides to a translocon subcomplex regulated by BiP
    • Lyman, S.K. and Schekman, R. (1997) Binding of secretory precursor polypeptides to a translocon subcomplex regulated by BiP Cell, 88, 85-96.
    • (1997) Cell , vol.88 , pp. 85-96
    • Lyman, S.K.1    Schekman, R.2
  • 28
    • 0029881416 scopus 로고    scopus 로고
    • Inositols do it all
    • Majerus, P.W. (1996) Inositols do it all. Genes Dev., 10, 1051-1053.
    • (1996) Genes Dev. , vol.10 , pp. 1051-1053
    • Majerus, P.W.1
  • 29
    • 0027472178 scopus 로고
    • An ATP transporter is required for protein translocation into the yeast endoplasmic reticulum
    • Mayinger, P. and Meyer, D.I. (1993) An ATP transporter is required for protein translocation into the yeast endoplasmic reticulum. EMBO J., 12, 659-666.
    • (1993) EMBO J. , vol.12 , pp. 659-666
    • Mayinger, P.1    Meyer, D.I.2
  • 30
    • 0029620936 scopus 로고
    • Sac1p mediates the adenosine-triphosphate transport into yeast endoplasmic-reticulum that is required for protein translocation
    • Mayinger, P., Bankaitis, V.A. and Meyer, D.I. (1995) Sac1p mediates the adenosine-triphosphate transport into yeast endoplasmic-reticulum that is required for protein translocation. J. Cell Biol., 131, 1377-1386.
    • (1995) J. Cell Biol. , vol.131 , pp. 1377-1386
    • Mayinger, P.1    Bankaitis, V.A.2    Meyer, D.I.3
  • 31
    • 2642622186 scopus 로고    scopus 로고
    • A presynaptic inositol-5-phosphatase
    • McPherson, P.S. et al. (1996) A presynaptic inositol-5-phosphatase. Nature, 379, 353-357.
    • (1996) Nature , vol.379 , pp. 353-357
    • McPherson, P.S.1
  • 32
    • 0030828058 scopus 로고    scopus 로고
    • Inducible membranes in yeast: Relation to the unfolded-protein-response pathway
    • Menzel, R., Vogel, F., Kargel, E. and Schunck, W.H. (1997) Inducible membranes in yeast: relation to the unfolded-protein-response pathway. Yeast, 13, 1211-1229.
    • (1997) Yeast , vol.13 , pp. 1211-1229
    • Menzel, R.1    Vogel, F.2    Kargel, E.3    Schunck, W.H.4
  • 33
    • 0027182508 scopus 로고
    • Vectors for the inducible overexpression of glutathione S-transferase fusion proteins in yeast
    • Mitchell, D.A., Marshall, T.K. and Deschenes, R.J. (1993) Vectors for the inducible overexpression of glutathione S-transferase fusion proteins in yeast. Yeaast, 9, 715-722.
    • (1993) Yeaast , vol.9 , pp. 715-722
    • Mitchell, D.A.1    Marshall, T.K.2    Deschenes, R.J.3
  • 34
    • 0024395160 scopus 로고
    • S.cerevisiae encodes an essential protein homologous in sequence and function to mammalian BiP
    • Normington, K., Kohno, K., Kozutsumi, Y., Gething, M.J. and Sambrook, J. (1989) S.cerevisiae encodes an essential protein homologous in sequence and function to mammalian BiP. Cell, 57, 1223-1236.
    • (1989) Cell , vol.57 , pp. 1223-1236
    • Normington, K.1    Kohno, K.2    Kozutsumi, Y.3    Gething, M.J.4    Sambrook, J.5
  • 35
    • 0024549504 scopus 로고
    • Suppressors of yeast actin mutations
    • Novick, P. Osmond, B.C. and Botstein, D. (1989) Suppressors of yeast actin mutations. Genetics, 121, 659-674.
    • (1989) Genetics , vol.121 , pp. 659-674
    • Novick, P.1    Osmond, B.C.2    Botstein, D.3
  • 36
    • 0028997459 scopus 로고
    • Posttranslational protein transport in yeast reconstituted with a purified complex of Sec proteins and Kar2p
    • Panzner, S., Dreier, L., Hartmann, E., Kostka, S. and Rapoport, T.A. (1995) Posttranslational protein transport in yeast reconstituted with a purified complex of Sec proteins and Kar2p. Cell, 81, 561-570.
    • (1995) Cell , vol.81 , pp. 561-570
    • Panzner, S.1    Dreier, L.2    Hartmann, E.3    Kostka, S.4    Rapoport, T.A.5
  • 37
    • 0024338964 scopus 로고
    • KAR2, a karyogamy gene. Is the yeast homolog of the mammalian BiP/GRP78
    • Rose, M.D., Misra, L.M. and Vogel, J.P. (1989) KAR2, a karyogamy gene. is the yeast homolog of the mammalian BiP/GRP78. Cell, 57, 1211-1221.
    • (1989) Cell , vol.57 , pp. 1211-1221
    • Rose, M.D.1    Misra, L.M.2    Vogel, J.P.3
  • 38
    • 0023058247 scopus 로고
    • Secretion in yeast: Reconstitution of the translocation and glycosylation of α-factor and invertase in a homologous cell-free system
    • Rothblatt, J.A. and Meyer, D.I. (1986) Secretion in yeast: reconstitution of the translocation and glycosylation of α-factor and invertase in a homologous cell-free system. Cell, 44, 619-628.
    • (1986) Cell , vol.44 , pp. 619-628
    • Rothblatt, J.A.1    Meyer, D.I.2
  • 39
    • 0026589260 scopus 로고
    • Sec61p and BiP directly facilitate polypeptide translocation into the ER
    • Sanders, S.L., Whitfield, K.M., Vogel, J.P., Rose, M.D. and Schekman, R.W. (1992) Sec61p and BiP directly facilitate polypeptide translocation into the ER. Cell, 69, 353-365.
    • (1992) Cell , vol.69 , pp. 353-365
    • Sanders, S.L.1    Whitfield, K.M.2    Vogel, J.P.3    Rose, M.D.4    Schekman, R.W.5
  • 40
    • 0024410239 scopus 로고
    • Secretion in yeast: Preprotein binding to a membrane receptor and ATP-dependent translocation are sequential and separable events in vitro
    • Sanz, P. and Meyer, D.I. (1989) Secretion in yeast: preprotein binding to a membrane receptor and ATP-dependent translocation are sequential and separable events in vitro. J. Cell Biol. 108, 2101-2106.
    • (1989) J. Cell Biol. , vol.108 , pp. 2101-2106
    • Sanz, P.1    Meyer, D.I.2
  • 41
    • 0031008564 scopus 로고    scopus 로고
    • The Hsp70 homologue Lhs1p is involved in a novel function of the yeast endoplasmic reticulum, refolding and stabilization of heat-denatured protein aggregates
    • Saris, N., Holkeri, H., Craven, R.A., Stirling, C.J. and Makarow, M. (1997) The Hsp70 homologue Lhs1p is involved in a novel function of the yeast endoplasmic reticulum, refolding and stabilization of heat-denatured protein aggregates. J. Cell Biol. 137, 813-824.
    • (1997) J. Cell Biol. , vol.137 , pp. 813-824
    • Saris, N.1    Holkeri, H.2    Craven, R.A.3    Stirling, C.J.4    Makarow, M.5
  • 42
    • 0029979607 scopus 로고    scopus 로고
    • Common principles of protein translocation across membranes
    • Schatz, G. and Dobberstein, B. (1996) Common principles of protein translocation across membranes. Science, 271, 1519-1526.
    • (1996) Science , vol.271 , pp. 1519-1526
    • Schatz, G.1    Dobberstein, B.2
  • 43
    • 0032509939 scopus 로고    scopus 로고
    • Splicing: HACking into the unfolded-protein response
    • Shamu, C.E. (1998) Splicing: HACking into the unfolded-protein response. Curr. Biol., 8, R121-R123.
    • (1998) Curr. Biol. , vol.8
    • Shamu, C.E.1
  • 44
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski, R.S. and Hieter, P. (1989) A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics, 122, 19-27.
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 45
    • 0029042422 scopus 로고
    • BiP/ Kar2p serves as a molecular chaperone during carboxypeptidase Y folding in yeast
    • Simons, J.F. Ferro-Novick, S., Rose, M.D. and Helenius, A. (1995) BiP/ Kar2p serves as a molecular chaperone during carboxypeptidase Y folding in yeast. J. Cell Biol., 130, 41-49.
    • (1995) J. Cell Biol. , vol.130 , pp. 41-49
    • Simons, J.F.1    Ferro-Novick, S.2    Rose, M.D.3    Helenius, A.4
  • 46
    • 0030686464 scopus 로고    scopus 로고
    • Disruption of three phosphatidylinositol-polyphosphate 5-phosphatase genes from Saccharomyces cerevisiae results in pleiotropic abnormalities of vacuole morphology, cell shape and osmohomeostasis
    • Srinivasan, S., Seaman, M., Nemoto, Y., Daniell, L., Suchy, S.F., Emr, S., De Camilli, P. and Nussbaum, R. (1997) Disruption of three phosphatidylinositol-polyphosphate 5-phosphatase genes from Saccharomyces cerevisiae results in pleiotropic abnormalities of vacuole morphology, cell shape and osmohomeostasis. Eur. J. Cell Biol., 74, 350-360.
    • (1997) Eur. J. Cell Biol. , vol.74 , pp. 350-360
    • Srinivasan, S.1    Seaman, M.2    Nemoto, Y.3    Daniell, L.4    Suchy, S.F.5    Emr, S.6    De Camilli, P.7    Nussbaum, R.8
  • 47
    • 0031893414 scopus 로고    scopus 로고
    • Identification and characterization of an essential family of inositol polyphosphate 5-phosphatases (INP51, INP52 and INP53 gene products) in the yeast Saccharomyces cerevisiae
    • Stolz, L.E., Huynh, C.V., Thorner, J. and York, J.D. (1998a) Identification and characterization of an essential family of inositol polyphosphate 5-phosphatases (INP51, INP52 and INP53 gene products) in the yeast Saccharomyces cerevisiae. Genetics, 148, 1715-1729.
    • (1998) Genetics , vol.148 , pp. 1715-1729
    • Stolz, L.E.1    Huynh, C.V.2    Thorner, J.3    York, J.D.4
  • 48
    • 0032496156 scopus 로고    scopus 로고
    • INP51, a yeast inositol polyphosphate 5-phosphatase required for phosphatidylinositol 4,5-bisphosphate homeostasis and whose absence confers a cold-resistant phenotype
    • Stolz, L.E., Kuo, W.J., Longchamps, J., Sekhon, M.K. and York, J.D. (1998b) INP51, a yeast inositol polyphosphate 5-phosphatase required for phosphatidylinositol 4,5-bisphosphate homeostasis and whose absence confers a cold-resistant phenotype. J. Biol. Chem., 273, 11852-11861.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11852-11861
    • Stolz, L.E.1    Kuo, W.J.2    Longchamps, J.3    Sekhon, M.K.4    York, J.D.5
  • 49
    • 0028356669 scopus 로고
    • The genetic interaction of kar2 and wbp1 mutations. Distinct functions of binding protein BiP and N-linked glycosylation in the processing pathway of secreted proteins in Saccharomyces cerevisiae
    • Te Heesen, H.S. and Aebi, M. (1994) The genetic interaction of kar2 and wbp1 mutations. Distinct functions of binding protein BiP and N-linked glycosylation in the processing pathway of secreted proteins in Saccharomyces cerevisiae. Eur. J. Biochem., 222, 631-637.
    • (1994) Eur. J. Biochem. , vol.222 , pp. 631-637
    • Te Heesen, H.S.1    Aebi, M.2
  • 50
    • 0027269974 scopus 로고
    • Sac1p is an integral membrane protein that influences the cellular requirement for phospholipid transfer protein function and inositol in yeast
    • Whitters, E.A., Cleves, A.E., McGee, T.P., Skinner, H.B. and Bankaitis, V.A. (1993) Sac1p is an integral membrane protein that influences the cellular requirement for phospholipid transfer protein function and inositol in yeast. J. Cell Biol., 122, 79-94.
    • (1993) J. Cell Biol. , vol.122 , pp. 79-94
    • Whitters, E.A.1    Cleves, A.E.2    McGee, T.P.3    Skinner, H.B.4    Bankaitis, V.A.5
  • 51
    • 0030996072 scopus 로고    scopus 로고
    • Phospholipid transfer proteins revisited
    • Wirtz, K.W. (1997) Phospholipid transfer proteins revisited. Biochem. J., 324, 353-360.
    • (1997) Biochem. J. , vol.324 , pp. 353-360
    • Wirtz, K.W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.