메뉴 건너뛰기




Volumn 15, Issue 23, 1996, Pages 6575-6583

Yeast Gpi8p is essential for GPI anchor attachment onto proteins

Author keywords

Glycosylphosphatidylinositol; Membrane anchors; Saccharomyces cerevisiae; Transamidase

Indexed keywords

FUNGAL PROTEIN; GLYCOSYLPHOSPHATIDYLINOSITOL; MEMBRANE PROTEIN; PROTEINASE;

EID: 0029827249     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1002/j.1460-2075.1996.tb01048.x     Document Type: Article
Times cited : (158)

References (61)
  • 2
    • 0029379575 scopus 로고
    • A putative vacuolar processing protease is regulated by ethylene and also during fruit ripening in citrus fruit
    • Alonso, J.M. and Granell, A. (1995) A putative vacuolar processing protease is regulated by ethylene and also during fruit ripening in citrus fruit. Plant Physiol., 109, 541-547.
    • (1995) Plant Physiol. , vol.109 , pp. 541-547
    • Alonso, J.M.1    Granell, A.2
  • 3
    • 0018608516 scopus 로고
    • Primary structural requirements for N-glycosylation of peptides in rat liver
    • Bause, E. and Hettkamp, H. (1979) Primary structural requirements for N-glycosylation of peptides in rat liver. FEBS Lett., 108, 341-344.
    • (1979) FEBS Lett. , vol.108 , pp. 341-344
    • Bause, E.1    Hettkamp, H.2
  • 4
    • 0018595953 scopus 로고
    • Enzymatic N-Glycosylation and O-Glycosylation of synthetic peptide acceptors by dolichol-linked sugar derivatives in yeast
    • Bause, E. and Lehle, L. (1979) Enzymatic N-Glycosylation and O-Glycosylation of synthetic peptide acceptors by dolichol-linked sugar derivatives in yeast. Eur. J. Biochem., 101, 531-540.
    • (1979) Eur. J. Biochem. , vol.101 , pp. 531-540
    • Bause, E.1    Lehle, L.2
  • 5
    • 0028958785 scopus 로고
    • Purification, cDNA cloning and characterization of proteinase B, an asparagine-specific endopeptidase from germinating vetch (Vicia sativa L.) seeds
    • Becker, C., Shutov, A.D., Nong, V.H., Senyuk, V.I., Jung, R., Horstmann, C., Fischer, J., Nielsen, N.C. and Müntz, K. (1995) Purification, cDNA cloning and characterization of proteinase B, an asparagine-specific endopeptidase from germinating vetch (Vicia sativa L.) seeds. Eur. J. Biochem., 228, 456-462.
    • (1995) Eur. J. Biochem. , vol.228 , pp. 456-462
    • Becker, C.1    Shutov, A.D.2    Nong, V.H.3    Senyuk, V.I.4    Jung, R.5    Horstmann, C.6    Fischer, J.7    Nielsen, N.C.8    Müntz, K.9
  • 6
    • 0025974216 scopus 로고
    • High-efficiency transformation of yeast by electroporation
    • Becker, D.M. and Guarente, L. (1991) High-efficiency transformation of yeast by electroporation. Methods Enzymol., 194, 182-187.
    • (1991) Methods Enzymol. , vol.194 , pp. 182-187
    • Becker, D.M.1    Guarente, L.2
  • 7
    • 0029124071 scopus 로고
    • Identification of six complementation classes involved in the biosynthesis of glycosylphosphatidylinositol anchors in Saccharomyces cerevisiae
    • Benghezal, M., Lipke, P.N. and Conzelmann, A. (1995) Identification of six complementation classes involved in the biosynthesis of glycosylphosphatidylinositol anchors in Saccharomyces cerevisiae. J. Cell Biol., 130, 1333-1344.
    • (1995) J. Cell Biol. , vol.130 , pp. 1333-1344
    • Benghezal, M.1    Lipke, P.N.2    Conzelmann, A.3
  • 8
    • 0020024572 scopus 로고
    • Codon selection in yeast
    • Bennetzen, J.L. and Hall, B.D. (1982) Codon selection in yeast. J. Biol. Chem., 257, 3026-3031.
    • (1982) J. Biol. Chem. , vol.257 , pp. 3026-3031
    • Bennetzen, J.L.1    Hall, B.D.2
  • 9
    • 0023483123 scopus 로고
    • Signal for attachment of a phospholipid membrane anchor in decay accelerating factor
    • Caras, I.W., Weddell, G.N., Davitz, M.A., Nussenzweig, V. and Martin, D.W., Jr (1987) Signal for attachment of a phospholipid membrane anchor in decay accelerating factor. Science, 238, 1280-1283.
    • (1987) Science , vol.238 , pp. 1280-1283
    • Caras, I.W.1    Weddell, G.N.2    Davitz, M.A.3    Nussenzweig, V.4    Martin Jr., D.W.5
  • 10
    • 0022990811 scopus 로고
    • Anchoring of membrane proteins via phosphatidylinositol is deficient in two classes of Thy-1 negative mutant lymphoma cells
    • Conzelmann, A., Spiazzi, A., Hyman, R. and Bron, C. (1986) Anchoring of membrane proteins via phosphatidylinositol is deficient in two classes of Thy-1 negative mutant lymphoma cells. EMBO J., 5, 3291-3296.
    • (1986) EMBO J. , vol.5 , pp. 3291-3296
    • Conzelmann, A.1    Spiazzi, A.2    Hyman, R.3    Bron, C.4
  • 11
    • 0023846083 scopus 로고
    • No glycolipid anchors are added to Thy-1 glycoprotein in Thy-1-negative mutant thymoma cells of four different complementation classes
    • Conzelmann, A., Spiazzi, A., Bron, C. and Hyman, R. (1988) No glycolipid anchors are added to Thy-1 glycoprotein in Thy-1-negative mutant thymoma cells of four different complementation classes. Mol. Cell. Biol., 8, 674-678.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 674-678
    • Conzelmann, A.1    Spiazzi, A.2    Bron, C.3    Hyman, R.4
  • 12
    • 0026592312 scopus 로고
    • Two different types of lipid moieties are present in glycophosphoinositol-anchored membrane proteins of Saccharomyces cerevisiae
    • Conzelmann, A., Puoti, A., Lester, R.L. and Desponds, C. (1992) Two different types of lipid moieties are present in glycophosphoinositol-anchored membrane proteins of Saccharomyces cerevisiae. EMBO J., 11, 457-466.
    • (1992) EMBO J. , vol.11 , pp. 457-466
    • Conzelmann, A.1    Puoti, A.2    Lester, R.L.3    Desponds, C.4
  • 13
    • 0023656149 scopus 로고
    • Cloning and gene expression of Schistosoma mansoni protease
    • Davis, A.H., Nanduri, J. and Watson, D.C. (1987) Cloning and gene expression of Schistosoma mansoni protease. J. Biol. Chem., 262, 12851-12855.
    • (1987) J. Biol. Chem. , vol.262 , pp. 12851-12855
    • Davis, A.H.1    Nanduri, J.2    Watson, D.C.3
  • 15
    • 0027294030 scopus 로고
    • The structure and biosynthesis of glycosyl phosphatidylinositol protein anchors
    • Englund, P.T. (1993) The structure and biosynthesis of glycosyl phosphatidylinositol protein anchors. Annu. Rev. Biochem., 62, 121-138.
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 121-138
    • Englund, P.T.1
  • 16
    • 0028022701 scopus 로고
    • Sec72 contributes to the selective recognition of signal peptides by the secretory polypeptide translocation complex
    • Feldheim, D. and Schekman, R. (1994) Sec72 contributes to the selective recognition of signal peptides by the secretory polypeptide translocation complex. J. Cell Biol., 126, 935-943.
    • (1994) J. Cell Biol. , vol.126 , pp. 935-943
    • Feldheim, D.1    Schekman, R.2
  • 17
    • 0028029829 scopus 로고
    • Signal-mediated retrieval of a membrane protein from the Golgi to the ER in yeast
    • Gaynor, E.C., te Heesen, S., Graham, T.R., Aebi, M. and Emr, S.D. (1994) Signal-mediated retrieval of a membrane protein from the Golgi to the ER in yeast. J. Cell Biol., 127, 653-665.
    • (1994) J. Cell Biol. , vol.127 , pp. 653-665
    • Gaynor, E.C.1    Te Heesen, S.2    Graham, T.R.3    Aebi, M.4    Emr, S.D.5
  • 18
    • 0026780325 scopus 로고
    • Phosphatidylinositol glycan (PI-G) anchored membrane proteins. Amino acid requirements adjacent to the site of cleavage and PI-G attachment in the COOH-terminal signal peptide
    • Gerber, L.D., Kodukula, K. and Udenfriend, S. (1992) Phosphatidylinositol glycan (PI-G) anchored membrane proteins. Amino acid requirements adjacent to the site of cleavage and PI-G attachment in the COOH-terminal signal peptide. J. Biol. Chem., 267, 12168-12173.
    • (1992) J. Biol. Chem. , vol.267 , pp. 12168-12173
    • Gerber, L.D.1    Kodukula, K.2    Udenfriend, S.3
  • 19
    • 0024495898 scopus 로고
    • Cysteine proteases of positive strand RNA viruses and chymotrypsin-like serine proteases
    • Gorbalenya, A.E., Donchenko, A.P., Blinov, V.M. and Koonin, E.V. (1989) Cysteine proteases of positive strand RNA viruses and chymotrypsin-like serine proteases. FEBS Lett., 243, 103-114.
    • (1989) FEBS Lett. , vol.243 , pp. 103-114
    • Gorbalenya, A.E.1    Donchenko, A.P.2    Blinov, V.M.3    Koonin, E.V.4
  • 20
    • 0024276923 scopus 로고
    • A GTP-binding protein required for secretion rapidly associates with secretory vesicles and the plasma membrane in yeast
    • Goud, B., Salminen, A., Walworth, N.C. and Novick, P.J. (1988) A GTP-binding protein required for secretion rapidly associates with secretory vesicles and the plasma membrane in yeast. Cell, 53, 753-768.
    • (1988) Cell , vol.53 , pp. 753-768
    • Goud, B.1    Salminen, A.2    Walworth, N.C.3    Novick, P.J.4
  • 21
    • 0028940341 scopus 로고
    • Yeast Gaa1p is required for attachment of a completed GPI anchor onto proteins
    • Hamburger, D., Egerton, M. and Riezman, H. (1995) Yeast Gaa1p is required for attachment of a completed GPI anchor onto proteins. J. Cell Biol., 129, 629-639.
    • (1995) J. Cell Biol. , vol.129 , pp. 629-639
    • Hamburger, D.1    Egerton, M.2    Riezman, H.3
  • 22
    • 0025986480 scopus 로고
    • A unique vacuolar processing enzyme responsible for conversion of several proprotein precursors into the mature forms
    • Hara-Nishimura, I., Inoue, K. and Nishimura, M. (1991) A unique vacuolar processing enzyme responsible for conversion of several proprotein precursors into the mature forms. FEBS Lett., 294, 89-93.
    • (1991) FEBS Lett. , vol.294 , pp. 89-93
    • Hara-Nishimura, I.1    Inoue, K.2    Nishimura, M.3
  • 23
    • 0027688051 scopus 로고
    • Molecular charaterization of vacuolar processing enzyme related to a putative cysteine proteinase of Schistosoma mansoni
    • Hara-Nishimura, I., Takeuchi, Y. and Nishimura, M. (1993) Molecular charaterization of vacuolar processing enzyme related to a putative cysteine proteinase of Schistosoma mansoni. Plant Cell, 5, 1651-1659.
    • (1993) Plant Cell , vol.5 , pp. 1651-1659
    • Hara-Nishimura, I.1    Takeuchi, Y.2    Nishimura, M.3
  • 24
    • 0003448569 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Harlow, E. and Lane, D. (eds) (1988) Antibodies: A Laboratory Manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1988) Antibodies: A Laboratory Manual
    • Harlow, E.1    Lane, D.2
  • 25
    • 0024393375 scopus 로고
    • Introduction of a cysteine protease active site into trypsin
    • Higaki, J.N., Evnin, L.B. and Craik, C.S. (1989) Introduction of a cysteine protease active site into trypsin. Biochemistry, 28, 9256-9263.
    • (1989) Biochemistry , vol.28 , pp. 9256-9263
    • Higaki, J.N.1    Evnin, L.B.2    Craik, C.S.3
  • 27
    • 0022781503 scopus 로고
    • Yeast/E. coli shuttle vectors with multiple unique restriction sites
    • Hill, J.E., Myers, A.M., Koerner, T.J. and Tzagaloff, A. (1986) Yeast/E. coli shuttle vectors with multiple unique restriction sites. Yeast, 2, 163-168.
    • (1986) Yeast , vol.2 , pp. 163-168
    • Hill, J.E.1    Myers, A.M.2    Koerner, T.J.3    Tzagaloff, A.4
  • 28
    • 0029379549 scopus 로고
    • Homologues of vacuolar processing enzyme that are expressed in different organs in Arabidopsis thaliana
    • Kinoshita, T., Nishimura, M. and Hara-Nishimura, I. (1995) Homologues of vacuolar processing enzyme that are expressed in different organs in Arabidopsis thaliana. Plant Mol. Biol., 29, 81-89.
    • (1995) Plant Mol. Biol. , vol.29 , pp. 81-89
    • Kinoshita, T.1    Nishimura, M.2    Hara-Nishimura, I.3
  • 29
    • 0026663723 scopus 로고
    • Biosynthesis of phosphatidylinositol-glycan (PI-G)-anchored membrane proteins in cell-free systems: PI-G is an obligatory cosubstrate for COOH-terminal processing of nascent proteins
    • Kodukula, K., Amthauer, R., Cines, D., Yeh, E.T., Brink, L., Thomas L.J. and Udenfriend, S. (1992) Biosynthesis of phosphatidylinositol-glycan (PI-G)-anchored membrane proteins in cell-free systems: PI-G is an obligatory cosubstrate for COOH-terminal processing of nascent proteins. Proc. Natl Acad. Sci. USA, 89, 4982-4985.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 4982-4985
    • Kodukula, K.1    Amthauer, R.2    Cines, D.3    Yeh, E.T.4    Brink, L.5    Thomas, L.J.6    Udenfriend, S.7
  • 30
    • 0027498149 scopus 로고
    • Biosynthesis of glycosylphosphatidylinositol (GPI)-anchored membrane proteins in intact cells: Specific amino acid requirements adjacent to the site of cleavage and GPI attachment
    • Kodukula, K., Gerber, L.D., Amthauer, R., Brink, L. and Udenfriend, S. (1993) Biosynthesis of glycosylphosphatidylinositol (GPI)-anchored membrane proteins in intact cells: specific amino acid requirements adjacent to the site of cleavage and GPI attachment. J. Cell Biol., 120, 657-664.
    • (1993) J. Cell Biol. , vol.120 , pp. 657-664
    • Kodukula, K.1    Gerber, L.D.2    Amthauer, R.3    Brink, L.4    Udenfriend, S.5
  • 31
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 32
    • 0029079927 scopus 로고
    • Comparative expressed-sequence-tag analysis of differential gene expression profiles in PC-12 cells before and after nerve growth factor treatment
    • Lee, N.H. et al. (1995) Comparative expressed-sequence-tag analysis of differential gene expression profiles in PC-12 cells before and after nerve growth factor treatment. Proc. Natl Acad. Sci. USA, 92, 8303-8307.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 8303-8307
    • Lee, N.H.1
  • 33
    • 0028361106 scopus 로고
    • A conditionally lethal yeast mutant blocked at the first step in glycosyl phosphatidylinositol anchor synthesis
    • Leidich, S.D., Drapp, D.A. and Orlean, P. (1994) A conditionally lethal yeast mutant blocked at the first step in glycosyl phosphatidylinositol anchor synthesis. J. Biol. Chem., 269, 10193-10196.
    • (1994) J. Biol. Chem. , vol.269 , pp. 10193-10196
    • Leidich, S.D.1    Drapp, D.A.2    Orlean, P.3
  • 34
    • 0028998118 scopus 로고
    • Temperature-sensitive yeast GPI anchoring mutants gpi2 and gpi3 are defective in the synthesis of N-acctylglucosaminyl phosphatidylinositol
    • Leidich, S.D., Kostova, Z., Latek, R.R., Costello, L.C., Drapp, D.A., Gray, W., Fassler, J.S. and Orlean, P. (1995) Temperature-sensitive yeast GPI anchoring mutants gpi2 and gpi3 are defective in the synthesis of N-acctylglucosaminyl phosphatidylinositol. J. Biol. Chem., 270, 13029-13035.
    • (1995) J. Biol. Chem. , vol.270 , pp. 13029-13035
    • Leidich, S.D.1    Kostova, Z.2    Latek, R.R.3    Costello, L.C.4    Drapp, D.A.5    Gray, W.6    Fassler, J.S.7    Orlean, P.8
  • 35
    • 0029096233 scopus 로고
    • An active carbonyl formed during glycophosphatidylinositol addition to a protein is evidence of catalysis by transamidase
    • Maxwell, E.S., Ramalingam, S., Gerber, L.D., Brink, L. and Udenfriend, S. (1995) An active carbonyl formed during glycophosphatidylinositol addition to a protein is evidence of catalysis by transamidase. J. Biol. Chem., 270, 19576-19582.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19576-19582
    • Maxwell, E.S.1    Ramalingam, S.2    Gerber, L.D.3    Brink, L.4    Udenfriend, S.5
  • 36
    • 0027257177 scopus 로고
    • The structure, biosynthesis and function of glycosylated phosphatidylinositols in the parasitic protozoa and higher eukaryotes
    • McConville, M.J. and Ferguson, M.A. (1993) The structure, biosynthesis and function of glycosylated phosphatidylinositols in the parasitic protozoa and higher eukaryotes. Biochem. J., 294, 305-324.
    • (1993) Biochem. J. , vol.294 , pp. 305-324
    • McConville, M.J.1    Ferguson, M.A.2
  • 37
    • 0028170762 scopus 로고
    • cDNA sequences of Schistosoma japonicum coding for two cathepsin B-like proteins and Sj32
    • Merckelbach, A., Hasse, H., Dell, R., Eschlbeck, A. and Ruppel A. (1994) cDNA sequences of Schistosoma japonicum coding for two cathepsin B-like proteins and Sj32. Trop. Med. Parasitol., 45, 193-198.
    • (1994) Trop. Med. Parasitol. , vol.45 , pp. 193-198
    • Merckelbach, A.1    Hasse, H.2    Dell, R.3    Eschlbeck, A.4    Ruppel, A.5
  • 38
    • 0025073250 scopus 로고
    • Selectivity of the cleavage/attachment site of phosphatidylinositol-glycan anchored membrane proteins determined by site specific mutagenesis at Asp-484 of placental alkaline phosphatase
    • Micanovic, R., Gerber, L.D., Berger, J., Kodukula, K. and Udenfriend, S. (1990) Selectivity of the cleavage/attachment site of phosphatidylinositol-glycan anchored membrane proteins determined by site specific mutagenesis at Asp-484 of placental alkaline phosphatase. Proc. Natl Acad. Sci. USA, 87, 157-161.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 157-161
    • Micanovic, R.1    Gerber, L.D.2    Berger, J.3    Kodukula, K.4    Udenfriend, S.5
  • 39
    • 0028231033 scopus 로고
    • Glycoinositol phospholipid anchor-defective K562 mutants with biochemical lesions distinct from those in Thy-1-murine lymphoma mutants
    • Mohney, R.P., Knez, J.J., Ravi, L., Sevlever, D., Rosenberry, T.L., Hirose, S. and Medof, M.E. (1994) Glycoinositol phospholipid anchor-defective K562 mutants with biochemical lesions distinct from those in Thy-1-murine lymphoma mutants. J. Biol. Chem., 269, 6536-6542.
    • (1994) J. Biol. Chem. , vol.269 , pp. 6536-6542
    • Mohney, R.P.1    Knez, J.J.2    Ravi, L.3    Sevlever, D.4    Rosenberry, T.L.5    Hirose, S.6    Medof, M.E.7
  • 40
    • 0026348933 scopus 로고
    • Fusion of sequence elements from non-anchored proteins to generate a fully functional signal for glycophosphatidylinositol membrane anchor attachment
    • Moran, P. and Caras, I.W. (1991a) Fusion of sequence elements from non-anchored proteins to generate a fully functional signal for glycophosphatidylinositol membrane anchor attachment. J. Cell Biol., 115, 1595-1600.
    • (1991) J. Cell Biol. , vol.115 , pp. 1595-1600
    • Moran, P.1    Caras, I.W.2
  • 41
    • 0025932246 scopus 로고
    • A nonfunctional sequence converted to a signal for glycophosphatidylinositol membrane anchor attachment
    • Moran, P. and Caras, I.W. (1991b) A nonfunctional sequence converted to a signal for glycophosphatidylinositol membrane anchor attachment. J. Cell Biol., 115, 329-336.
    • (1991) J. Cell Biol. , vol.115 , pp. 329-336
    • Moran, P.1    Caras, I.W.2
  • 42
    • 0028327126 scopus 로고
    • Requirements for glycosylphosphatidylinositol attachment are similar but not identical in mammalian cells and parasitic protozoa
    • Moran, P. and Caras, I.W. (1994) Requirements for glycosylphosphatidylinositol attachment are similar but not identical in mammalian cells and parasitic protozoa. J. Cell Biol., 125, 333-343.
    • (1994) J. Cell Biol. , vol.125 , pp. 333-343
    • Moran, P.1    Caras, I.W.2
  • 43
    • 0026033050 scopus 로고
    • Glycophospholipid membrane anchor attachment. Molecular analysis of the cleavage/ attachment site
    • Moran, P., Raab, H., Kohr, W.J. and Caras, I.W. (1991) Glycophospholipid membrane anchor attachment. Molecular analysis of the cleavage/ attachment site. J. Biol. Chem., 266, 1250-1257.
    • (1991) J. Biol. Chem. , vol.266 , pp. 1250-1257
    • Moran, P.1    Raab, H.2    Kohr, W.J.3    Caras, I.W.4
  • 44
  • 45
    • 0027249370 scopus 로고
    • A high-order structure of plant storage proprotein allows its second conversion by an asparagine-specific cysteine protease, a novel proteolytic enzyme
    • Muramatsu, M. and Fukasawa, C. (1993) A high-order structure of plant storage proprotein allows its second conversion by an asparagine-specific cysteine protease, a novel proteolytic enzyme. Eur. J. Biochem., 215, 123-132.
    • (1993) Eur. J. Biochem. , vol.215 , pp. 123-132
    • Muramatsu, M.1    Fukasawa, C.2
  • 46
    • 0026057813 scopus 로고
    • Determinants for glycophospholipid anchoring of the Saccharomyces cerevisiae GAS1 protein to the plasma membrane
    • Nuoffer, C., Jeno, P., Conzelmann, A. and Riezman, H. (1991) Determinants for glycophospholipid anchoring of the Saccharomyces cerevisiae GAS1 protein to the plasma membrane. Mol. Cell. Biol., 11, 27-37.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 27-37
    • Nuoffer, C.1    Jeno, P.2    Conzelmann, A.3    Riezman, H.4
  • 47
    • 0027270310 scopus 로고
    • Analysis of the sequence requirements for glycosylphosphatidylinositol anchoring of Saccharomyces cerevisiae Gas1 protein
    • Nuoffer, C., Horvath, A. and Riezman, H. (1993) Analysis of the sequence requirements for glycosylphosphatidylinositol anchoring of Saccharomyces cerevisiae Gas1 protein. J. Biol. Chem., 268, 10558-10563.
    • (1993) J. Biol. Chem. , vol.268 , pp. 10558-10563
    • Nuoffer, C.1    Horvath, A.2    Riezman, H.3
  • 48
    • 0028902788 scopus 로고
    • Transmembrane helices predicted at 95% accuracy
    • Rost, B., Casadio, R., Fariselli, P. and Sander, C. (1995) Transmembrane helices predicted at 95% accuracy. Protein Sci., 4, 521-533.
    • (1995) Protein Sci. , vol.4 , pp. 521-533
    • Rost, B.1    Casadio, R.2    Fariselli, P.3    Sander, C.4
  • 50
    • 0029025250 scopus 로고
    • The yeast spt14 is homologous to the human PIG-A gene and is required for GPI anchor synthesis
    • Schönbächler, M., Horvath, A., Fassler, J. and Riezman, H. (1995) The yeast spt14 is homologous to the human PIG-A gene and is required for GPI anchor synthesis. EMBO J., 14, 1637-1645.
    • (1995) EMBO J. , vol.14 , pp. 1637-1645
    • Schönbächler, M.1    Horvath, A.2    Fassler, J.3    Riezman, H.4
  • 51
    • 0025099013 scopus 로고
    • Genetic and biochemical evaluation of eucaryotic membrane protein topology: Multiple transmembrane domains of Saccharomyces cerevisiae 3-hydroxy-3-methylglutaryl coenzyme A reductase
    • Sengstag, C., Stirling, C., Schekman, R. and Rine, J. (1990) Genetic and biochemical evaluation of eucaryotic membrane protein topology: multiple transmembrane domains of Saccharomyces cerevisiae 3-hydroxy-3-methylglutaryl coenzyme A reductase. Mol. Cell. Biol., 10, 672-680.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 672-680
    • Sengstag, C.1    Stirling, C.2    Schekman, R.3    Rine, J.4
  • 52
    • 0028446555 scopus 로고
    • Vacuolar processing enzyme of soybean that converts proproteins to the corresponding mature forms
    • Shimada, T., Hiraiwa, N., Nishimura, M. and Hara-Nishimura, I. (1994) Vacuolar processing enzyme of soybean that converts proproteins to the corresponding mature forms. Plant Cell Physiol., 35, 713-718.
    • (1994) Plant Cell Physiol. , vol.35 , pp. 713-718
    • Shimada, T.1    Hiraiwa, N.2    Nishimura, M.3    Hara-Nishimura, I.4
  • 53
    • 0028236034 scopus 로고
    • New phenotype of mutations deficient in glucosylation of the lipid-linked oligosaccharide: Cloning of the ALG8 locus
    • Stagljar, I., te Heesen, S. and Aebi, M. (1994) New phenotype of mutations deficient in glucosylation of the lipid-linked oligosaccharide: cloning of the ALG8 locus. Proc. Natl Acad. Sci. USA, 91, 5977-5981.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 5977-5981
    • Stagljar, I.1    Te Heesen, S.2    Aebi, M.3
  • 54
    • 0025963058 scopus 로고
    • Recovery of plasmids from yeast into Escherichia coli: Shuttle vectors
    • Strathern, J.N. and Higgins, D.R. (1991) Recovery of plasmids from yeast into Escherichia coli: shuttle vectors. Methods Enzymol., 194, 319-329.
    • (1991) Methods Enzymol. , vol.194 , pp. 319-329
    • Strathern, J.N.1    Higgins, D.R.2
  • 56
    • 0027990302 scopus 로고
    • Isolation and analysis of cDNA encoding a precursor of Canavalia ensiformis asparaginyl endopeptidase (Legumain)
    • Takeda, O., Miura, Y., Mitta, M., Matsushita, H., Kato, I., Abe, Y., Yokosawa, H. and Ishii, S. (1994) Isolation and analysis of cDNA encoding a precursor of Canavalia ensiformis asparaginyl endopeptidase (Legumain). J. Biochem., 116, 541-546.
    • (1994) J. Biochem. , vol.116 , pp. 541-546
    • Takeda, O.1    Miura, Y.2    Mitta, M.3    Matsushita, H.4    Kato, I.5    Abe, Y.6    Yokosawa, H.7    Ishii, S.8
  • 57
    • 0026063416 scopus 로고
    • An essential 45 kDa yeast transmembrane protein reacts with antinuclear pore antibodies: Purification of the protein, immunolocalization and cloning of the gene
    • te Heesen, S., Rauhut, R., Aebersold, R., Abelson, J. and Aebi, M. (1991) An essential 45 kDa yeast transmembrane protein reacts with antinuclear pore antibodies: purification of the protein, immunolocalization and cloning of the gene. Eur. J. Cell Biol., 56, 8-18.
    • (1991) Eur. J. Cell Biol. , vol.56 , pp. 8-18
    • Te Heesen, S.1    Rauhut, R.2    Aebersold, R.3    Abelson, J.4    Aebi, M.5
  • 58
    • 0023046815 scopus 로고
    • A new method for predicting signal sequence cleavage sites
    • von Heijne, G. (1986) A new method for predicting signal sequence cleavage sites. Nucleic Acids Res., 14, 4683-4690.
    • (1986) Nucleic Acids Res. , vol.14 , pp. 4683-4690
    • Von Heijne, G.1
  • 59
    • 0028915532 scopus 로고
    • Identification of SPT14/ CWH6 as the yeast homologue of hPIG-A, a gene involved in the biosynthesis of GPI anchors
    • Vossen, J.H., Ram, A.F.J. and Klis, F.M. (1995) Identification of SPT14/ CWH6 as the yeast homologue of hPIG-A, a gene involved in the biosynthesis of GPI anchors. Biochim. Biophys. Acta, 1243, 549-551.
    • (1995) Biochim. Biophys. Acta , vol.1243 , pp. 549-551
    • Vossen, J.H.1    Ram, A.F.J.2    Klis, F.M.3
  • 60
    • 0028676232 scopus 로고
    • New heterologous modules for classical or PCR-based gene disruptions in Saccharomyces cerevisae
    • Wach, A., Brachat, A., Pöhlmann, R. and Philippsen, P. (1994) New heterologous modules for classical or PCR-based gene disruptions in Saccharomyces cerevisae. Yeast, 10, 1793-1808.
    • (1994) Yeast , vol.10 , pp. 1793-1808
    • Wach, A.1    Brachat, A.2    Pöhlmann, R.3    Philippsen, P.4
  • 61
    • 84873787842 scopus 로고
    • A critical evaluation of the nitrogen assimilation tests commonly used in the classification of yeasts
    • Wickerham, L.J. (1946) A critical evaluation of the nitrogen assimilation tests commonly used in the classification of yeasts. J. Bacteriol., 52, 293-301.
    • (1946) J. Bacteriol. , vol.52 , pp. 293-301
    • Wickerham, L.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.