메뉴 건너뛰기




Volumn 142, Issue 5, 1998, Pages 1223-1233

Degradation of misfolded endoplasmic reticulum glycoproteins in saccharomyces cerevisiae is determined by a specific oligosaccharide structure

Author keywords

Endoplasmic reticulum; Glycosylation; Mannosidase; Protein degradation; Yeast

Indexed keywords

ALPHA 1,2 GLUCOSE LINKAGE; CARBOXYPEPTIDASE C; GLYCOPROTEIN; MANNOSIDASE; UNCLASSIFIED DRUG;

EID: 0032494135     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.142.5.1223     Document Type: Article
Times cited : (309)

References (66)
  • 1
    • 0029778262 scopus 로고    scopus 로고
    • Cloning and characterization of the ALG3 gene of Saccharornvces cerevisiae
    • Aebi, M., J. Gassenhuber, H. Domdey, and S. te Heesen. 1996. Cloning and characterization of the ALG3 gene of Saccharornvces cerevisiae. Glycobiology. 6:439-444.
    • (1996) Glycobiology , vol.6 , pp. 439-444
    • Aebi, M.1    Gassenhuber, J.2    Domdey, H.3    Te Heesen, S.4
  • 2
    • 0027327253 scopus 로고    scopus 로고
    • Effect of bromoconduritol on glucosidase II from rat liver
    • Alonso, J.M., A. Santa-Cecilia, and P. Calvo. Effect of bromoconduritol on glucosidase II from rat liver. Eur. J. Biochem. 215:37-42.
    • Eur. J. Biochem. , vol.215 , pp. 37-42
    • Alonso, J.M.1    Santa-Cecilia, A.2    Calvo, P.3
  • 3
    • 0029985369 scopus 로고    scopus 로고
    • Degradation of subunits of the Sec61p complex, an integral component of the ER membrane, by the ubiquitin-proteasome pathway
    • Biederer, T., C. Volkwein, and T. Sommer. 1996. Degradation of subunits of the Sec61p complex, an integral component of the ER membrane, by the ubiquitin-proteasome pathway. EMBO (Eur. Mol. Biol. Organ.) J. 15:2069-2076.
    • (1996) EMBO (Eur. Mol. Biol. Organ.) J. , vol.15 , pp. 2069-2076
    • Biederer, T.1    Volkwein, C.2    Sommer, T.3
  • 4
    • 0021099732 scopus 로고
    • Evidence for an α-mannosidase in endoplasmic reticulum of rat liver
    • Bischoff, J., and R. Kornfeld, 1983. Evidence for an α-mannosidase in endoplasmic reticulum of rat liver. J. Biol. Chem. 258:7907-7910.
    • (1983) J. Biol. Chem. , vol.258 , pp. 7907-7910
    • Bischoff, J.1    Kornfeld, R.2
  • 5
    • 0029852685 scopus 로고    scopus 로고
    • Reversal of fortune for nascent proteins
    • Bonifacino, J.S. 1996. Reversal of fortune for nascent proteins. Nature. 384: 405-106.
    • (1996) Nature , vol.384 , pp. 405-1106
    • Bonifacino, J.S.1
  • 6
    • 0031774710 scopus 로고    scopus 로고
    • The ALG10 locus of Saccharomyces cerevisiae encodes the α-1,2 glucosyltransferase of the endoplasmic reticulum: The terminal glucose of the lipid-linked oligosaccharide is required for efficient N-linked glycosylation
    • Burda, P., and M. Aebi. 1998. The ALG10 locus of Saccharomyces cerevisiae encodes the α-1,2 glucosyltransferase of the endoplasmic reticulum: the terminal glucose of the lipid-linked oligosaccharide is required for efficient N-linked glycosylation. Glycobiology. 8:455-462.
    • (1998) Glycobiology , vol.8 , pp. 455-462
    • Burda, P.1    Aebi, M.2
  • 7
    • 0029959440 scopus 로고    scopus 로고
    • Stepwise assembly of the lipid-linked oligosaccharide in the endoplasmic reticulum of Saccharomyces cerevisiae: Identification of the ALG9 gene encoding a putative mannosyltransferase
    • Burda, P., S. te Heesen, A. Brachat, A. Wach, A. Dusterhoft, and M. Aebi. 1996. Stepwise assembly of the lipid-linked oligosaccharide in the endoplasmic reticulum of Saccharomyces cerevisiae: identification of the ALG9 gene encoding a putative mannosyltransferase. Proc. Natl. Acad. Sci. USA. 93: 7160-7165.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 7160-7165
    • Burda, P.1    Te Heesen, S.2    Brachat, A.3    Wach, A.4    Dusterhoft, A.5    Aebi, M.6
  • 8
    • 0020491529 scopus 로고
    • Glycoprotein synthesis in yeast. Identification of Man8GlcNAc2 as an essential intermediate in oligosaccharide processing
    • Byrd, J.C., A.L. Tarentino, F. Maley, P.H. Aikinson, and R.B. Trimble. 1982. Glycoprotein synthesis in yeast. Identification of Man8GlcNAc2 as an essential intermediate in oligosaccharide processing. J. Biol. Chem. 257:14657-14666.
    • (1982) J. Biol. Chem. , vol.257 , pp. 14657-14666
    • Byrd, J.C.1    Tarentino, A.L.2    Maley, F.3    Aikinson, P.H.4    Trimble, R.B.5
  • 9
    • 0027203025 scopus 로고
    • Effect of cell attachment and growth on the synthesis and fate of dolichol-linked oligosaccharides in Chinese hamster ovary cells
    • Cacan, R., O. Labiau, A.M. Mir, and A. Verbert. 1993. Effect of cell attachment and growth on the synthesis and fate of dolichol-linked oligosaccharides in Chinese hamster ovary cells. Eur. J. Biochem. 215:873-881.
    • (1993) Eur. J. Biochem. , vol.215 , pp. 873-881
    • Cacan, R.1    Labiau, O.2    Mir, A.M.3    Verbert, A.4
  • 10
    • 0028172714 scopus 로고
    • Mammalian alpha-mannosidases-multiple forms but a common purpose?
    • Daniel, P.F., B. Winchester, and C.D. Warren. 1994. Mammalian alpha-mannosidases-multiple forms but a common purpose? Glycobiology. 4:551-566.
    • (1994) Glycobiology , vol.4 , pp. 551-566
    • Daniel, P.F.1    Winchester, B.2    Warren, C.D.3
  • 11
    • 0024094923 scopus 로고
    • Characterization of a component of the yeast secretion machinery: Identification of the SEC18 gene product
    • Eakle, K.A., M. Bernstein, and S.D. Emr. 1988. Characterization of a component of the yeast secretion machinery: identification of the SEC18 gene product. Mol. Cell. Biol. 8:4098-4109.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 4098-4109
    • Eakle, K.A.1    Bernstein, M.2    Emr, S.D.3
  • 12
    • 0342506459 scopus 로고    scopus 로고
    • Differential fate of glycoproteins carrying a monoglucosylated form of truncated N-glycan in a new CHO cell line. MadIA214, selected for a thermosensitive secretory defect
    • Ermonval, M., R. Cacan, K. Gorgas, I. Haas, A. Verbert, and G. Buttin. 1997. Differential fate of glycoproteins carrying a monoglucosylated form of truncated N-glycan in a new CHO cell line. MadIA214, selected for a thermosensitive secretory defect. J. Cell Sci. 110:323-336.
    • (1997) J. Cell Sci. , vol.110 , pp. 323-336
    • Ermonval, M.1    Cacan, R.2    Gorgas, K.3    Haas, I.4    Verbert, A.5    Buttin, G.6
  • 13
    • 0028150802 scopus 로고
    • Purification to homogeneity of UDP-glucose:glycoprotein glucosyltransferase from Schizosaccharomyces pombe and apparent absence of the enzyme from Saccharomyces cerevisiae
    • Fernandez, F.S., S.E. Trombetta, U. Hellman, and A.J. Parodi. 1994. Purification to homogeneity of UDP-glucose:glycoprotein glucosyltransferase from Schizosaccharomyces pombe and apparent absence of the enzyme from Saccharomyces cerevisiae. J. Biol. Chem. 269:30701-30706.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30701-30706
    • Fernandez, F.S.1    Trombetta, S.E.2    Hellman, U.3    Parodi, A.J.4
  • 14
    • 0027137885 scopus 로고
    • Analysis of two mutated vacuolar proteins reveals a degradation pathway in the endoplasmic reticulum or a related compartment of yeast
    • Finger, A., M. Knop, and D.H. Wolf. 1993. Analysis of two mutated vacuolar proteins reveals a degradation pathway in the endoplasmic reticulum or a related compartment of yeast. Eur. J. Biochem. 218:565-574.
    • (1993) Eur. J. Biochem. , vol.218 , pp. 565-574
    • Finger, A.1    Knop, M.2    Wolf, D.H.3
  • 15
    • 0026030418 scopus 로고
    • Analysis of polypeptide transit through yeast secretory pathway
    • Franzusoff, A., J. Rothblatt, and R. Schekman. 1991. Analysis of polypeptide transit through yeast secretory pathway. Methods Enzymol. 194:662-674.
    • (1991) Methods Enzymol. , vol.194 , pp. 662-674
    • Franzusoff, A.1    Rothblatt, J.2    Schekman, R.3
  • 16
    • 0026781418 scopus 로고
    • Topology of ER processing alpha-mannosidase of Saccharomyces cerevisiae
    • Grondin, B., and A. Herscovics. 1992. Topology of ER processing alpha-mannosidase of Saccharomyces cerevisiae. Glycobiology. 2:369-372.
    • (1992) Glycobiology , vol.2 , pp. 369-372
    • Grondin, B.1    Herscovics, A.2
  • 19
    • 0027402074 scopus 로고
    • Glycoprotein biosynthesis in yeast
    • Herscovics, A., and P. Orlean. 1993. Glycoprotein biosynthesis in yeast. FASEB J. 7:540-550.
    • (1993) FASEB J. , vol.7 , pp. 540-550
    • Herscovics, A.1    Orlean, P.2
  • 20
    • 0029838640 scopus 로고    scopus 로고
    • ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway
    • Hiller, M.M., A. Finger, M. Schweiger, and D.H. Wolf. 1996. ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway Science. 273:1725-1728.
    • (1996) Science , vol.273 , pp. 1725-1728
    • Hiller, M.M.1    Finger, A.2    Schweiger, M.3    Wolf, D.H.4
  • 22
    • 0018786795 scopus 로고
    • Synthesis and processing of protein-linked oligosaccharides in vivo
    • Hubbard, S.C., and P.W. Robbins. 1979. Synthesis and processing of protein-linked oligosaccharides in vivo. J. Biol. Chem. 254:4568-4576.
    • (1979) J. Biol. Chem. , vol.254 , pp. 4568-4576
    • Hubbard, S.C.1    Robbins, P.W.2
  • 23
    • 0020049833 scopus 로고
    • Temperature-sensitive yeast mutants deficient in asparagine-linked glycosylation
    • Huffaker, T.C., and P.W. Robbins. 1981. Temperature-sensitive yeast mutants deficient in asparagine-linked glycosylation. J. Biol. Chem. 257:3203-3210.
    • (1981) J. Biol. Chem. , vol.257 , pp. 3203-3210
    • Huffaker, T.C.1    Robbins, P.W.2
  • 24
    • 0021067823 scopus 로고
    • Yeast mutants deficient in protein glycosylation
    • Huffaker, T.C., and P.W. Robbins. 1983. Yeast mutants deficient in protein glycosylation. Proc. Natl. Acad. Sci. USA. 80:7466-7470.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 7466-7470
    • Huffaker, T.C.1    Robbins, P.W.2
  • 25
    • 0031884897 scopus 로고    scopus 로고
    • Genetic tailoring of N-linked oligosaccharides: The role of glucose residues in glycoprotein processing of Saccharomyces cerevisiae in vivo
    • Jakob, C.A., P. Burda, S. te Heesen, M. Aebi, and J. Roth. 1998. Genetic tailoring of N-linked oligosaccharides: the role of glucose residues in glycoprotein processing of Saccharomyces cerevisiae in vivo. Glycobiology. 8:155-164.
    • (1998) Glycobiology , vol.8 , pp. 155-164
    • Jakob, C.A.1    Burda, P.2    Te Heesen, S.3    Aebi, M.4    Roth, J.5
  • 26
    • 0029162583 scopus 로고
    • Selective protein degradation: A journey's end within the proteasome
    • Jentsch, S., and S. Schlenker. 1995. Selective protein degradation: a journey's end within the proteasome. Cell. 82:881-884.
    • (1995) Cell , vol.82 , pp. 881-884
    • Jentsch, S.1    Schlenker, S.2
  • 27
    • 0029817714 scopus 로고    scopus 로고
    • N-glycosylation affects endoplasmic reticulum degradation of a mutated derivative of carboxypeptidase Yscy in yeast
    • Knop, M., N. Hauser, and D.H. Wolf. 1996. N-glycosylation affects endoplasmic reticulum degradation of a mutated derivative of carboxypeptidase Yscy in yeast. Yeast. 12:1229-1238.
    • (1996) Yeast , vol.12 , pp. 1229-1238
    • Knop, M.1    Hauser, N.2    Wolf, D.H.3
  • 28
    • 0030949874 scopus 로고    scopus 로고
    • ER quality control: The cytoplasmic connection
    • Kopito, R.R. 1997. ER quality control: the cytoplasmic connection. Cell. 88: 427-430.
    • (1997) Cell , vol.88 , pp. 427-430
    • Kopito, R.R.1
  • 29
    • 0030814254 scopus 로고    scopus 로고
    • COPII and secretory cargo capture into transport vesicles
    • Kuehn, M.J., and R. Schekman. 1997. COPII and secretory cargo capture into transport vesicles. Curr. Opin. Cell Biol. 9:477-483.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 477-483
    • Kuehn, M.J.1    Schekman, R.2
  • 30
    • 0030898233 scopus 로고    scopus 로고
    • Intracrllular disposal of incompletely folded human alphal-antitrypsin involves release from calnexin and post-translational trimming of asparagine-linked oligosaccharides
    • Liu, Y., P. Choudhury, C.M. Cabrai, and R.N. Sifers. 1997. Intracrllular disposal of incompletely folded human alphal-antitrypsin involves release from calnexin and post-translational trimming of asparagine-linked oligosaccharides. J. Biol. Chem. 272:7946-7951.
    • (1997) J. Biol. Chem. , vol.272 , pp. 7946-7951
    • Liu, Y.1    Choudhury, P.2    Cabrai, C.M.3    Sifers, R.N.4
  • 32
    • 0030070704 scopus 로고    scopus 로고
    • Assembly of ER-associated protein degradation in vitro: Dependence on cytosol, calnexin, and ATP
    • McCracken, A.A., and J.L. Brodsky. 1996. Assembly of ER-associated protein degradation in vitro: dependence on cytosol, calnexin, and ATP. J. Cell Biol. 132:291-298.
    • (1996) J. Cell Biol. , vol.132 , pp. 291-298
    • McCracken, A.A.1    Brodsky, J.L.2
  • 33
    • 0028213490 scopus 로고
    • Glycosidases of the asparagine-linked oligosaccharidc processing pathway
    • Moremen, K.W., R.B. Trimble, and A. Herscovics. 1994. Glycosidases of the asparagine-linked oligosaccharidc processing pathway. Glycobiology. 4:113-125.
    • (1994) Glycobiology , vol.4 , pp. 113-125
    • Moremen, K.W.1    Trimble, R.B.2    Herscovics, A.3
  • 34
    • 0018930046 scopus 로고
    • Identification of 23 complementation groups required for post-translational events in the yeast secretory pathway
    • Novick, P., C. Field, and R. Schekman. 1980. Identification of 23 complementation groups required for post-translational events in the yeast secretory pathway. Cell. 21:205-215.
    • (1980) Cell , vol.21 , pp. 205-215
    • Novick, P.1    Field, C.2    Schekman, R.3
  • 35
    • 0000912342 scopus 로고    scopus 로고
    • Biogenesis of yeast wall and surface proteins
    • J.R. Pringle, J.R. Broach, and E.W. Jones, editors. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Orlean, P. 1997. Biogenesis of yeast wall and surface proteins. In Molecular and Cellular Biology of the Yeast Saccharomyces, Cell Cycle and Cell Biology. J.R. Pringle, J.R. Broach, and E.W. Jones, editors. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1997) Molecular and Cellular Biology of the Yeast Saccharomyces, Cell Cycle and Cell Biology
    • Orlean, P.1
  • 36
    • 0030789680 scopus 로고    scopus 로고
    • Sec61p mediates export of a misfolded secretory protein from the endoplasmic reticulum to the cytosol for degradation
    • Pilon, M., R. Schekman, and K. Römisch. 1997. Sec61p mediates export of a misfolded secretory protein from the endoplasmic reticulum to the cytosol for degradation. EMBO (Eur. Mol. Biol. Organ.) J. 16:4540-4548.
    • (1997) EMBO (Eur. Mol. Biol. Organ.) J. , vol.16 , pp. 4540-4548
    • Pilon, M.1    Schekman, R.2    Römisch, K.3
  • 37
    • 1842409617 scopus 로고    scopus 로고
    • Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation
    • Plemper, R.K., S. Böhmler, J. Bordallo, T. Sommer, and D.H. Wolf. 1997. Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation. Nature. 388:891-895.
    • (1997) Nature , vol.388 , pp. 891-895
    • Plemper, R.K.1    Böhmler, S.2    Bordallo, J.3    Sommer, T.4    Wolf, D.H.5
  • 38
    • 0027535261 scopus 로고
    • Disruption of the processing alpha-mannosidase gene does not prevent outer chain synthesis in Succharomyces cerevisiae
    • Puccia, R., B. Grondin, and A. Herscovics. 1993. Disruption of the processing alpha-mannosidase gene does not prevent outer chain synthesis in Succharomyces cerevisiae. Biochem. J. 290:21-26.
    • (1993) Biochem. J. , vol.290 , pp. 21-26
    • Puccia, R.1    Grondin, B.2    Herscovics, A.3
  • 39
    • 0029799792 scopus 로고    scopus 로고
    • Isolation of the ALG6 locus of Saccharomyces cerevisiae required for glucosylation in the N-linked glycosylation pathway
    • Reiss, G., S. te Heesen, J. Zimmerman, P.W. Robbins, and M. Aebi. 1996. Isolation of the ALG6 locus of Saccharomyces cerevisiae required for glucosylation in the N-linked glycosylation pathway. Glycobiology. 6:493-498.
    • (1996) Glycobiology , vol.6 , pp. 493-498
    • Reiss, G.1    Te Heesen, S.2    Zimmerman, J.3    Robbins, P.W.4    Aebi, M.5
  • 40
    • 0000810848 scopus 로고
    • Biosynthesis: Compartmentation of glycoprotein biosynthesis
    • J. Montreuil, H. Schachter, and J.F.G. Vliegenthart, editors. Elsevier, New York
    • Roth, J. 1995. Biosynthesis: compartmentation of glycoprotein biosynthesis. In Glycoproteins. J. Montreuil, H. Schachter, and J.F.G. Vliegenthart, editors. Elsevier, New York. 287-312.
    • (1995) Glycoproteins , pp. 287-312
    • Roth, J.1
  • 41
    • 0342637690 scopus 로고
    • A sensitive and rapid protein assay impervious to detergents
    • Sailer, A., and C. Weissmann. 1991. A sensitive and rapid protein assay impervious to detergents. Technique (Phila.). 3:37-38.
    • (1991) Technique (Phila.) , vol.3 , pp. 37-38
    • Sailer, A.1    Weissmann, C.2
  • 42
    • 0025814817 scopus 로고
    • Use of polymerase chain reaction for rapid detection of gene insertions in whole yeast cells
    • Sathe, G.M., S. O'Brien, M.M. McLaughlin, F. Watson, and G.P. Livi. 1991. Use of polymerase chain reaction for rapid detection of gene insertions in whole yeast cells. Nucleic Acids Res. 19:4775.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 4775
    • Sathe, G.M.1    O'Brien, S.2    McLaughlin, M.M.3    Watson, F.4    Livi, G.P.5
  • 44
    • 0019570379 scopus 로고
    • N-Glycosylation of yeast proteins. Characterization of the solubilized oligosaccharyl transferase
    • Sharma, C.B., L. Lehle, and W. Tanner. 1981. N-Glycosylation of yeast proteins. Characterization of the solubilized oligosaccharyl transferase. Eur. J. Biochem. 116:101-108.
    • (1981) Eur. J. Biochem. , vol.116 , pp. 101-108
    • Sharma, C.B.1    Lehle, L.2    Tanner, W.3
  • 45
    • 0029991763 scopus 로고    scopus 로고
    • Biochemistry, molecular biology, and genetics of the oligosaccharyltransferase
    • Silberstein, S., and R. Gilmore. 1996. Biochemistry, molecular biology, and genetics of the oligosaccharyltransferase. FASEB J. 10:849-858.
    • (1996) FASEB J. , vol.10 , pp. 849-858
    • Silberstein, S.1    Gilmore, R.2
  • 46
    • 0029042422 scopus 로고
    • BiP/Kar2p serves as a molecular chaperone during carboxypeptidase Y folding in yeast
    • Simons, J.F., S. Ferro-Novick, M.D. Rose, and A. Helenius. 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
  • 47
    • 0030700576 scopus 로고    scopus 로고
    • Endoplasmic reticulum degradation: Reverse protein flow of no return
    • Sommer, T., and D.H. Wolf. 1997. Endoplasmic reticulum degradation: reverse protein flow of no return. FASEB J. 11:1227-1233.
    • (1997) FASEB J. , vol.11 , pp. 1227-1233
    • Sommer, T.1    Wolf, D.H.2
  • 48
    • 0029126624 scopus 로고
    • The molecular basis for the recognition of the UDP-Glc:glycoprotein glucosyltransferase with the acceptor glycoprotein
    • Sousa, M.C., and A.J. Parodi. 1995. The molecular basis for the recognition of the UDP-Glc:glycoprotein glucosyltransferase with the acceptor glycoprotein. EMBO (Eur. Mol. Biol. Organ.) J. 14:4196-4203.
    • (1995) EMBO (Eur. Mol. Biol. Organ.) J. , vol.14 , pp. 4196-4203
    • Sousa, M.C.1    Parodi, A.J.2
  • 49
    • 15844386822 scopus 로고    scopus 로고
    • Definition of the lectin-like properties of the molecular chaperone, calreticulin, and demonstration of its copurification with endomannosidase from rat liver Golgi
    • Spiro, R.G., Q. Zhu, V. Bhoyroo, and H.D. Soling. 1996. Definition of the lectin-like properties of the molecular chaperone, calreticulin, and demonstration of its copurification with endomannosidase from rat liver Golgi. J. Biol. Chem. 271:11588-11594.
    • (1996) J. Biol. Chem. , vol.271 , pp. 11588-11594
    • Spiro, R.G.1    Zhu, Q.2    Bhoyroo, V.3    Soling, H.D.4
  • 50
    • 0028236034 scopus 로고
    • New phenotype of mutations deficient in the glycosylation of the lipid-linked oligosaccharide: The cloning of the ALG8 locus
    • Stagljar, I., S. te Heesen, and M. Aebi. 1994. New phenotype of mutations deficient in the glycosylation of the lipid-linked oligosaccharide: the 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
  • 51
    • 0027238561 scopus 로고
    • Pre-golgi degradation of yeast prepro-α-factor expressed in a mammalian cell
    • Su, K., T. Stoller, J. Rocco, J. Zemsky, and R. Green. 1993. Pre-golgi degradation of yeast prepro-α-factor expressed in a mammalian cell. J. Biol. Chem. 268:14.101-14309.
    • (1993) J. Biol. Chem. , vol.268 , pp. 14101-14309
    • Su, K.1    Stoller, T.2    Rocco, J.3    Zemsky, J.4    Green, R.5
  • 52
    • 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, S., and M. Aebi. 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. Ear. J. Biochem. 222:631-637.
    • (1994) Ear. J. Biochem. , vol.222 , pp. 631-637
    • Te Heesen, S.1    Aebi, M.2
  • 53
    • 0026607905 scopus 로고
    • The yeast WBP1 is essential for oligosaccharyltransferase activity in vivo and in vitro
    • te Heesen, S., B. Janetzky, L. Lehle, and M. Aebi. 1992. The yeast WBP1 is essential for oligosaccharyltransferase activity in vivo and in vitro. EMBO (Eur. Mol. Biol. Organ.) J. 11:2071-2075.
    • (1992) EMBO (Eur. Mol. Biol. Organ.) J. , vol.11 , pp. 2071-2075
    • Te Heesen, S.1    Janetzky, B.2    Lehle, L.3    Aebi, M.4
  • 54
    • 0027968807 scopus 로고
    • Isolation of the ALG8 locus encoding the UDP-glucose:dolichyl-phosphate glucosyltransferase from Saccharomyces cerevisitae
    • te Heesen, S., L. Lehle, A. Weissmann, and M. Aebi. 1994. Isolation of the ALG8 locus encoding the UDP-glucose:dolichyl-phosphate glucosyltransferase from Saccharomyces cerevisitae. Eur. J. Biochem. 224:71-79.
    • (1994) Eur. J. Biochem. , vol.224 , pp. 71-79
    • Te Heesen, S.1    Lehle, L.2    Weissmann, A.3    Aebi, M.4
  • 55
  • 56
    • 0026044927 scopus 로고
    • Structure of Saccharomyces cervisiae alg3,sec18 mutant oligosaccharides
    • Verostek, M.F., P.M. Atkinson, and R.B. Trimble. 1991. Structure of Saccharomyces cervisiae alg3,sec18 mutant oligosaccharides. J. Biol. Chem. 266: 5547-5551.
    • (1991) J. Biol. Chem. , vol.266 , pp. 5547-5551
    • Verostek, M.F.1    Atkinson, P.M.2    Trimble, R.B.3
  • 57
    • 0027174395 scopus 로고
    • Glycoprotein biosynthesis in the alg3 Saccharomyces cerevisine mutant. 1. Role of glucose in the initial glycosylalion of invertase in the endoplasmic reticulum
    • Verostek, M.F., P.M. Atkinson, and R.B. Trimble. 1993. Glycoprotein biosynthesis in the alg3 Saccharomyces cerevisine mutant. 1. Role of glucose in the initial glycosylalion of invertase in the endoplasmic reticulum. J. Biol. Chem. 268:12095-12103.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12095-12103
    • Verostek, M.F.1    Atkinson, P.M.2    Trimble, R.B.3
  • 58
    • 0028084472 scopus 로고
    • Release of oligomannoside-type glycans as a marker of the degradation of newly synthesized glycoproteins
    • Villers, C., R. Cacan, A.-M. Mir, O. Labiau, and A. Verbert. 1994. Release of oligomannoside-type glycans as a marker of the degradation of newly synthesized glycoproteins. Biochem. J. 298:135-142.
    • (1994) Biochem. J. , vol.298 , pp. 135-142
    • Villers, C.1    Cacan, R.2    Mir, A.-M.3    Labiau, O.4    Verbert, A.5
  • 59
    • 0028676232 scopus 로고
    • New heterologous modules for classical or PCR-based gene disruptions in Saccharomyces cerevisiae
    • Wach, A., A. Brachat, R. Pöhlmann, and P. Philippsen. 1994. New heterologous modules for classical or PCR-based gene disruptions in Saccharomyces cerevisiae. Yeast. 10:1793-1808.
    • (1994) Yeast , vol.10 , pp. 1793-1808
    • Wach, A.1    Brachat, A.2    Pöhlmann, R.3    Philippsen, P.4
  • 60
    • 0027331577 scopus 로고
    • Demonstration that a kifunensine-resistant α-mannosidase with a unique processing action on N-linked oligosaccharides occurs in rat liver cndoplasmic reticulum and various cultured cells
    • Weng, S., and R.G. Spiro. 1993. Demonstration that a kifunensine-resistant α-mannosidase with a unique processing action on N-linked oligosaccharides occurs in rat liver cndoplasmic reticulum and various cultured cells. J. Biol. Chem. 268:25656-25663.
    • (1993) J. Biol. Chem. , vol.268 , pp. 25656-25663
    • Weng, S.1    Spiro, R.G.2
  • 61
    • 0030445531 scopus 로고    scopus 로고
    • 2 isomers: Evidence that endomannosidase functions in vivo in the absence of a glucosidase blockade
    • 2 isomers: evidence that endomannosidase functions in vivo in the absence of a glucosidase blockade. Glycobiology. 6:861-868.
    • (1996) Glycobiology , vol.6 , pp. 861-868
    • Weng, S.1    Spiro, R.G.2
  • 62
    • 0025782243 scopus 로고
    • Yeast carboxypeptidase Y requires glycosylation for efficient intracellular transport, but not for vacuolar sorting, in vivo stability, or activity
    • Winther, J.R., T.H. Stevens, and M.C. Kielland-Brandt. 1991. Yeast carboxypeptidase Y requires glycosylation for efficient intracellular transport, but not for vacuolar sorting, in vivo stability, or activity. Eur. J. Biocliem. 197: 681-689.
    • (1991) Eur. J. Biocliem. , vol.197 , pp. 681-689
    • Winther, J.R.1    Stevens, T.H.2    Kielland-Brandt, M.C.3
  • 63
    • 0016836498 scopus 로고
    • Proteinase C (carboxypeptidase Y) mutant of yeast
    • Wolf, D.H., and G.R. Fink. 1975. Proteinase C (carboxypeptidase Y) mutant of yeast. J. Bacteriol. 123:1150-1156.
    • (1975) J. Bacteriol. , vol.123 , pp. 1150-1156
    • Wolf, D.H.1    Fink, G.R.2
  • 64
    • 0032536903 scopus 로고    scopus 로고
    • Novel aspects of degradation of T cell receptor subunits from the endoplasmic reticulum in T cells: Importance of oligosaccharide processing, ubiquitination, and proteasome-dependent removal from ER membranes
    • Yang, M., S. Oemura. J.S. Bonifacino, and A.M. Weissman. 1998. Novel aspects of degradation of T cell receptor subunits from the endoplasmic reticulum in T cells: importance of oligosaccharide processing, ubiquitination, and proteasome-dependent removal from ER membranes. J. Exp. Med. 187:835-846.
    • (1998) J. Exp. Med. , vol.187 , pp. 835-846
    • Yang, M.1    Oemura, S.2    Bonifacino, J.S.3    Weissman, A.M.4
  • 65
    • 0026343406 scopus 로고
    • Glycoprotein biosynthesis in yeast: Purification and characterisation of the endoplasmic reticulum Man9 processing α-mannosidase
    • Ziegler, F.D., and R.B. Trimble. 1991. Glycoprotein biosynthesis in yeast: purification and characterisation of the endoplasmic reticulum Man9 processing α-mannosidase. Glycobiology. 1:605-614.
    • (1991) Glycobiology , vol.1 , pp. 605-614
    • Ziegler, F.D.1    Trimble, R.B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.