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Volumn 348, Issue 1, 2000, Pages 1-13

Role of N-oligosaccharide endoplasmic reticulum processing reactions in glycoprotein folding and degradation

Author keywords

Calnexin calreticulin; Glucosyltransferase; Glycoprotein degradation; Quality control

Indexed keywords

CALNEXIN; CALRETICULIN; DOLICHOL PHOSPHATE; GLUCOSIDASE; GLUCOSYLTRANSFERASE; GLYCAN; GLYCOPROTEIN; OLIGOSACCHARIDE; PROTEASOME;

EID: 0034657712     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/0264-6021:3480001     Document Type: Review
Times cited : (289)

References (145)
  • 1
    • 0018799051 scopus 로고
    • The role of lipid intermediates in the glycosylation of proteins in the eucaryotic cell
    • 1 Parodi, A. J. and Leloir, L. F. (1979) The role of lipid intermediates in the glycosylation of proteins in the eucaryotic cell. Biochim. Biophys. Acta 559, 1-37
    • (1979) Biochim. Biophys. Acta , vol.559 , pp. 1-37
    • Parodi, A.J.1    Leloir, L.F.2
  • 2
    • 0019377631 scopus 로고
    • Synthesis and processing of asparagine-linked oligosaccharides
    • 2 Hubbard, S. C. and Ivatt, R. J. (1981) Synthesis and processing of asparagine-linked oligosaccharides. Annu. Rev. Biochem. 50, 555-583
    • (1981) Annu. Rev. Biochem. , vol.50 , pp. 555-583
    • Hubbard, S.C.1    Ivatt, R.J.2
  • 3
    • 0021891884 scopus 로고
    • Assemby of asparagine-linked oligosaccharides
    • 3 Kornfeld, R. and Kornfeld, S. (1985) Assemby of asparagine-linked oligosaccharides. Annu. Rev. Biochem. 54, 631-664
    • (1985) Annu. Rev. Biochem. , vol.54 , pp. 631-664
    • Kornfeld, R.1    Kornfeld, S.2
  • 4
    • 0040320246 scopus 로고
    • A mutation that prevents glucosylation of the lipid-linked oligosaccharide precursor leads to underglycosylation of secreted yeast invertase
    • 4 Ballou, L., Gopal, P., Krummel, B., Tammi, M. and Ballou, C. E. (1986) A mutation that prevents glucosylation of the lipid-linked oligosaccharide precursor leads to underglycosylation of secreted yeast invertase. Proc. Natl. Acad. Sci. U.S.A. 83, 3081-3085
    • (1986) Proc. Natl. Acad. Sci. U.S.A. , vol.83 , pp. 3081-3085
    • Ballou, L.1    Gopal, P.2    Krummel, B.3    Tammi, M.4    Ballou, C.E.5
  • 5
    • 0029910144 scopus 로고    scopus 로고
    • Endoplasmic reticulum glucosidase II is composed of a catalytic subunit, conserved from yeast to mammals, and a tightly bound noncatalytic HDEL-containing subunit
    • 5 Trombetta, E. S., Simons, J. F. and Helenius, A. (1996) Endoplasmic reticulum glucosidase II is composed of a catalytic subunit, conserved from yeast to mammals, and a tightly bound noncatalytic HDEL-containing subunit. J. Biol. Chem. 271, 27509-27516
    • (1996) J. Biol. Chem. , vol.271 , pp. 27509-27516
    • Trombetta, E.S.1    Simons, J.F.2    Helenius, A.3
  • 6
    • 0038187312 scopus 로고    scopus 로고
    • Genetic evidence for the heterodimeric structure of glucosidase II. The effect of disrupting the subunit-encoding genes on glycoprotein folding
    • 6 D'Alessio, C., Fernández, F., Trombetta, E. S. and Parodi, A. J. (1999) Genetic evidence for the heterodimeric structure of glucosidase II. The effect of disrupting the subunit-encoding genes on glycoprotein folding. J. Biol. Chem. 274, 25899-25905
    • (1999) J. Biol. Chem. , vol.274 , pp. 25899-25905
    • D'Alessio, C.1    Fernández, F.2    Trombetta, E.S.3    Parodi, A.J.4
  • 7
    • 0027331577 scopus 로고
    • Demonstration that a kifunensin-resistant α-mannosidase with a processing action on N-linked oligosaccharides occurs in rat liver endoplasmic reticulum and various cultured cells
    • 7 Weng, S. and Spiro, R. G. (1993) Demonstration that a kifunensin-resistant α-mannosidase with a processing action on N-linked oligosaccharides occurs in rat liver endoplasmic 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
  • 9
    • 0027318961 scopus 로고
    • Biological roles of oligosaccharides: All of the theories are correct
    • 9 Varki, A. (1993) Biological roles of oligosaccharides: all of the theories are correct. Glycobiology 3, 97-130
    • (1993) Glycobiology , vol.3 , pp. 97-130
    • Varki, A.1
  • 10
    • 0027282621 scopus 로고
    • N-glycosylation in trypanosomatid protozoa
    • 10 Parodi, A. J. (1993) N-glycosylation in trypanosomatid protozoa. Glycobiology 3, 193-199
    • (1993) Glycobiology , vol.3 , pp. 193-199
    • Parodi, A.J.1
  • 11
    • 0024297303 scopus 로고
    • Characterization of dolichol diphosphate oligosaccharide:Protein oligosaccharyltransferase and of glycoprotein processing glucosidases occurring in trypanosomatids
    • 11 Bosch, M., Trombetta, S., Engstrom, U. and Parodi, A. J. (1988) Characterization of dolichol diphosphate oligosaccharide:protein oligosaccharyltransferase and of glycoprotein processing glucosidases occurring in trypanosomatids. J. Biol. Chem. 263, 17360-17365
    • (1988) J. Biol. Chem. , vol.263 , pp. 17360-17365
    • Bosch, M.1    Trombetta, S.2    Engstrom, U.3    Parodi, A.J.4
  • 12
    • 0020587404 scopus 로고
    • Protein glycosylation in Trypanosoma cruzi. The mechanism of glycosylation and structure of protein-bound oligosaccharides
    • 12 Parodi, A. J., Lederkremer, G. Z. and Mendelzon, D. H. (1983) Protein glycosylation in Trypanosoma cruzi. The mechanism of glycosylation and structure of protein-bound oligosaccharides. J. Biol. Chem. 258, 5589-5595
    • (1983) J. Biol. Chem. , vol.258 , pp. 5589-5595
    • Parodi, A.J.1    Lederkremer, G.Z.2    Mendelzon, D.H.3
  • 13
    • 0023655783 scopus 로고
    • Synthesis of dolichol derivatives in trypanosomatids. Characterization of enzymatic patterns
    • 13 de la Canal, L. and Parodi, A. J. (1987) Synthesis of dolichol derivatives in trypanosomatids. Characterization of enzymatic patterns. J. Biol. Chem. 262, 11128-11133
    • (1987) J. Biol. Chem. , vol.262 , pp. 11128-11133
    • De La Canal, L.1    Parodi, A.J.2
  • 14
    • 0020957538 scopus 로고
    • 2 in calf thyroid slices: A possible recognition signal in the processing of glycoproteins
    • 2 in calf thyroid slices: a possible recognition signal in the processing of glycoproteins. J. Biol. Chem 258, 8260-8265
    • (1983) J. Biol. Chem , vol.258 , pp. 8260-8265
    • Parodi, A.J.1    Mendelzon, D.H.2    Lederkremer, G.Z.3
  • 16
    • 0023009114 scopus 로고
    • Processing of asparagine-linked saccharides in Mucor rouxii
    • 16 Lederkremer, G. Z. and Parodi, A. J. (1986) Processing of asparagine-linked saccharides in Mucor rouxii. Biochim. Biophys. Acta 884, 363-369
    • (1986) Biochim. Biophys. Acta , vol.884 , pp. 363-369
    • Lederkremer, G.Z.1    Parodi, A.J.2
  • 17
    • 0024468302 scopus 로고
    • Glucosylation of glycoproteins by mammalian, plant, fungal and trypanosomatid protozoa microsomal proteins
    • 17 Trombetta, S., Bosch, M. and Parodi, A. J. (1989) Glucosylation of glycoproteins by mammalian, plant, fungal and trypanosomatid protozoa microsomal proteins. Biochemistry 28, 8108-8116
    • (1989) Biochemistry , vol.28 , pp. 8108-8116
    • Trombetta, S.1    Bosch, M.2    Parodi, A.J.3
  • 18
    • 0026500202 scopus 로고
    • Recognition of the oligosaccharide and protein moieties of glycoproteins by the UDP-Glc:Glycoprotein glucosyltransferase
    • 18 Sousa, M., Ferrero-García, M. and Parodi, A. J. (1992) Recognition of the oligosaccharide and protein moieties of glycoproteins by the UDP-Glc:glycoprotein glucosyltransferase. Biochemistry 31, 97-105
    • (1992) Biochemistry , vol.31 , pp. 97-105
    • Sousa, M.1    Ferrero-García, M.2    Parodi, A.J.3
  • 19
    • 0024598083 scopus 로고
    • Selective retention of monoglucosylated high mannose oligosaccharides by a class of mutant vesicular stomatis virus G proteins
    • 19 Suh, P., Bergmann, J. E. and Gabel, C. A. (1989) Selective retention of monoglucosylated high mannose oligosaccharides by a class of mutant vesicular stomatis virus G proteins. J. Cell Biol. 108, 811-819
    • (1989) J. Cell Biol. , vol.108 , pp. 811-819
    • Suh, P.1    Bergmann, J.E.2    Gabel, C.A.3
  • 20
    • 0025905709 scopus 로고
    • A major proportion of N-glycoproteins are transiently glucosylated in the endoplasmic reticulum
    • 20 Gañán, S., Cazzulo, J. J. and Parodi, A. J. (1991) A major proportion of N-glycoproteins are transiently glucosylated in the endoplasmic reticulum. Biochemistry 30, 3098-3104
    • (1991) Biochemistry , vol.30 , pp. 3098-3104
    • Gañán, S.1    Cazzulo, J.J.2    Parodi, A.J.3
  • 21
    • 0026799435 scopus 로고
    • Purification to apparent homogeneity and partial characterization of rat liver UDP-Glc:Glycoprotein glucosyltransferase
    • 21 Trombetta, S. and Parodi, A. J. (1992) Purification to apparent homogeneity and partial characterization of rat liver UDP-Glc:glycoprotein glucosyltransferase. J. Biol. Chem. 267, 9236-9240
    • (1992) J. Biol. Chem. , vol.267 , pp. 9236-9240
    • Trombetta, S.1    Parodi, A.J.2
  • 22
    • 0028150802 scopus 로고
    • Purification to homogeneity of UDP-Glc:Glycoprotein glucosyltransferase from Schizosaccharomyces pombe and apparent absence of the enzyme from Saccharomyces cerevisiae
    • 22 Fernández, F., Trombetta, S.E., Hellman, U. and Parodi, A. J. (1994) Purification to homogeneity of UDP-Glc: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
    • Fernández, F.1    Trombetta, S.E.2    Hellman, U.3    Parodi, A.J.4
  • 23
    • 0028987945 scopus 로고
    • Drosophila UDP-Glc:Glycoprotein glucosyltransferase: Sequence and characterization of an enzyme that distinguishes between denatured and native proteins
    • 23 Parker, C. G., Fessler, L. I., Nelson, R. E. and Fessler, J. H. (1995) Drosophila UDP-Glc:glycoprotein glucosyltransferase: sequence and characterization of an enzyme that distinguishes between denatured and native proteins. EMBO J. 14, 1294-1303
    • (1995) EMBO J. , vol.14 , pp. 1294-1303
    • Parker, C.G.1    Fessler, L.I.2    Nelson, R.E.3    Fessler, J.H.4
  • 24
    • 0029126624 scopus 로고
    • The molecular basis for the recognition of misfolded glycoproteins by the UDP-Glc:Glycoprotein glucosyltransferase
    • 24 Sousa, M. and Parodi, A. J. (1995) The molecular basis for the recognition of misfolded glycoproteins by the UDP-Glc:glycoprotein glucosyltransferase. EMBO J. 15, 4196-4203
    • (1995) EMBO J. , vol.15 , pp. 4196-4203
    • Sousa, M.1    Parodi, A.J.2
  • 25
    • 0028921961 scopus 로고
    • X-ray structure of the soybean agglutinin cross-linked with a biantennary analog of the blood group I carbohydrate antigen
    • 25 Dessen, A., Gupta, D., Sabewsan, S., Brewer, C. F. and Sacchettini, J. C. (1995) X-ray structure of the soybean agglutinin cross-linked with a biantennary analog of the blood group I carbohydrate antigen. Biochemistry 34, 4933-4942
    • (1995) Biochemistry , vol.34 , pp. 4933-4942
    • Dessen, A.1    Gupta, D.2    Sabewsan, S.3    Brewer, C.F.4    Sacchettini, J.C.5
  • 26
    • 0021485787 scopus 로고
    • Optimizing hydrolysis of N-linked high mannose oligosaccharides by endo-β-N-acetylglucosaminidase H
    • 26 Trimble, R. B. and Maley, F. (1984) Optimizing hydrolysis of N-linked high mannose oligosaccharides by endo-β-N-acetylglucosaminidase H. Anal. Biochem. 141, 515-522
    • (1984) Anal. Biochem. , vol.141 , pp. 515-522
    • Trimble, R.B.1    Maley, F.2
  • 27
    • 0019332339 scopus 로고
    • Substrate specificities of rat liver microsomal glucosidases which process glycoproteins
    • 27 Grinna, L. S. and Robbins, P. W. (1980) Substrate specificities of rat liver microsomal glucosidases which process glycoproteins. J. Biol. Chem. 255, 2255-2258
    • (1980) J. Biol. Chem. , vol.255 , pp. 2255-2258
    • Grinna, L.S.1    Robbins, P.W.2
  • 28
    • 0034689022 scopus 로고    scopus 로고
    • Conformational requirements for glycoprotein reglucosylation in the endoplasmic reticulum
    • in the press
    • 27a Trombetta, E. S. and Helenius, A. (2000) Conformational requirements for glycoprotein reglucosylation in the endoplasmic reticulum. J. Cell Biol. 275, in the press
    • (2000) J. Cell Biol. , vol.275
    • Trombetta, E.S.1    Helenius, A.2
  • 29
    • 0032531734 scopus 로고    scopus 로고
    • A misfolded protein conformation is not a sufficient condition for in vivo glucosylation by the UDP-Glc:Glycoprotein glucosyltransferase
    • 28 Fernández, F., D'Alessio, C., Fanchiotti, S. and Parodi, A. J. (1998) A misfolded protein conformation is not a sufficient condition for in vivo glucosylation by the UDP-Glc:glycoprotein glucosyltransferase. EMBO J. 17, 5877-5886
    • (1998) EMBO J. , vol.17 , pp. 5877-5886
    • Fernández, F.1    D'Alessio, C.2    Fanchiotti, S.3    Parodi, A.J.4
  • 30
    • 0032918454 scopus 로고    scopus 로고
    • Trypanosoma cruzi calreticulin is a lectin that binds monoglucosylated oligosaccharides but not protein moieties of glycoproteins
    • 29 Labriola, C., Cazzulo, J. J. and Parodi, A. J. (1999) Trypanosoma cruzi calreticulin is a lectin that binds monoglucosylated oligosaccharides but not protein moieties of glycoproteins. Mol. Biol. Cell 10, 1381-1394
    • (1999) Mol. Biol. Cell , vol.10 , pp. 1381-1394
    • Labriola, C.1    Cazzulo, J.J.2    Parodi, A.J.3
  • 31
    • 0030020169 scopus 로고    scopus 로고
    • A new stress protein: Synthesis of Schizosaccharomyces pombe UDP-Glc:Glycoprotein glucosyltransferase mRNA is induced under stress conditions but the enzyme is not essential for cell viability
    • 30 Fernández, F., Jannatipour, M., Hellman, U., Rokeach, L. and Parodi, A. J. (1996) A new stress protein: synthesis of Schizosaccharomyces pombe UDP-Glc:glycoprotein glucosyltransferase mRNA is induced under stress conditions but the enzyme is not essential for cell viability. EMBO J. 15, 705-713
    • (1996) EMBO J. , vol.15 , pp. 705-713
    • Fernández, F.1    Jannatipour, M.2    Hellman, U.3    Rokeach, L.4    Parodi, A.J.5
  • 32
    • 0031128320 scopus 로고    scopus 로고
    • ER-associated and proteasome-mediated protein degradation: How two topologically restricted events came together
    • 31 Brodsky, J. L. and McCracken, A. A. (1997) ER-associated and proteasome-mediated protein degradation: how two topologically restricted events came together. Trends Cell Biol. 7, 151-156
    • (1997) Trends Cell Biol. , vol.7 , pp. 151-156
    • Brodsky, J.L.1    McCracken, A.A.2
  • 33
    • 0033168382 scopus 로고    scopus 로고
    • Retrograde protein translocation: ERADication of secretory proteins in health and disease
    • 32 Plemper, R. K. and Wolf, D. H. (1999) Retrograde protein translocation: ERADication of secretory proteins in health and disease. Trends Biochem. Sci. 24, 266-270
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 266-270
    • Plemper, R.K.1    Wolf, D.H.2
  • 34
    • 0024461745 scopus 로고
    • Protein oligomerization in the endoplasmic reticulum
    • 33 Hurtley, S. M. and Helenius, A. (1989) Protein oligomerization in the endoplasmic reticulum. Annu. Rev. Cell Biol. 5, 277-307
    • (1989) Annu. Rev. Cell Biol. , vol.5 , pp. 277-307
    • Hurtley, S.M.1    Helenius, A.2
  • 35
    • 0025070112 scopus 로고
    • ERp72, an abundant luminal endoplasmic reticulum protein, contains three copies of the active site sequences of protein disulfide isomerase
    • 34 Mazzarella, R. A., Srinivasan, M., Haugejorden, S. M. and Green, M. (1990) ERp72, an abundant luminal endoplasmic reticulum protein, contains three copies of the active site sequences of protein disulfide isomerase. J. Biol. Chem. 265, 1094-1101
    • (1990) J. Biol. Chem. , vol.265 , pp. 1094-1101
    • Mazzarella, R.A.1    Srinivasan, M.2    Haugejorden, S.M.3    Green, M.4
  • 36
    • 0026533996 scopus 로고
    • The gene for a novel protein, a member of the protein disulphide isomerase/form I phosphoinositide-specific phospholipase C family, is amplified in hydroxyurea-resistant cells
    • 35 Chaudhuri, M. M., Tonin, P. N., Lewis, W. H. and Srinivasan, P. R. (1992) The gene for a novel protein, a member of the protein disulphide isomerase/form I phosphoinositide-specific phospholipase C family, is amplified in hydroxyurea-resistant cells. Biochem. J. 281, 645-650
    • (1992) Biochem. J. , vol.281 , pp. 645-650
    • Chaudhuri, M.M.1    Tonin, P.N.2    Lewis, W.H.3    Srinivasan, P.R.4
  • 38
    • 0021076098 scopus 로고
    • Immunoglobulin heavy chain binding protein
    • 37 Haas, I. G. and Wabl, M. (1983) Immunoglobulin heavy chain binding protein. Nature (London) 306, 387-389
    • (1983) Nature (London) , vol.306 , pp. 387-389
    • Haas, I.G.1    Wabl, M.2
  • 39
    • 0023660117 scopus 로고
    • The glucose-regulated protein grp94 is related to heat shock protein hsp90
    • 38 Sorger, P. K. and Pelham, H. R. (1987) The glucose-regulated protein grp94 is related to heat shock protein hsp90. J. Mol. Biol. 194, 341-344
    • (1987) J. Mol. Biol. , vol.194 , pp. 341-344
    • Sorger, P.K.1    Pelham, H.R.2
  • 40
    • 0027136174 scopus 로고
    • The 170-kDa glucose-regulated stress protein is an endoplasmic reticulum protein that binds immunoglobulin
    • 39 Lin, H. Y., Masso-Welch, P., Di, Y. P., Cai, J. W., Shen, J. W. and Subjeck, J. R. (1993) The 170-kDa glucose-regulated stress protein is an endoplasmic reticulum protein that binds immunoglobulin. Mol. Biol. Cell 4, 1109-1119
    • (1993) Mol. Biol. Cell , vol.4 , pp. 1109-1119
    • Lin, H.Y.1    Masso-Welch, P.2    Di, Y.P.3    Cai, J.W.4    Shen, J.W.5    Subjeck, J.R.6
  • 42
    • 0029268063 scopus 로고
    • Calnexin: A molecular chaperone with a taste for carbohydrate
    • 41 Williams, D. B. (1995) Calnexin: a molecular chaperone with a taste for carbohydrate. Biochem. Cell Biol. 73, 123-132
    • (1995) Biochem. Cell Biol. , vol.73 , pp. 123-132
    • Williams, D.B.1
  • 45
    • 0021241353 scopus 로고
    • Role of glycosylation in the processing of newly translated insulin proreceptor in 3T3-L1 adipocytes
    • 44 Ronnett, G. V., Knutson, V. P., Kohanski, R. A., Simpson, T. L. and Lane, M. D. (1984) Role of glycosylation in the processing of newly translated insulin proreceptor in 3T3-L1 adipocytes. J. Biol. Chem. 259, 4566-4575
    • (1984) J. Biol. Chem. , vol.259 , pp. 4566-4575
    • Ronnett, G.V.1    Knutson, V.P.2    Kohanski, R.A.3    Simpson, T.L.4    Lane, M.D.5
  • 46
    • 0022979880 scopus 로고
    • Synthesis of epidermal growth factor receptor in human A431 cells. Glycosylation dependent acquisition of ligand binding activity occurs post-translationally in the endoplasmic reticulum
    • 45 Slieker, L. J., Martensen, T. M. and Lane, M. D. (1986) Synthesis of epidermal growth factor receptor in human A431 cells. Glycosylation dependent acquisition of ligand binding activity occurs post-translationally in the endoplasmic reticulum. J. Biol. Chem. 261, 15233-15241
    • (1986) J. Biol. Chem. , vol.261 , pp. 15233-15241
    • Slieker, L.J.1    Martensen, T.M.2    Lane, M.D.3
  • 47
    • 0023919087 scopus 로고
    • Glycosylation of CD4. Tunicamycin inhibits surface expression
    • 46 König, R., Ashwell, G. and Hannover, J. A. (1988) Glycosylation of CD4. Tunicamycin inhibits surface expression. J. Biol. Chem. 263, 9502-9507
    • (1988) J. Biol. Chem. , vol.263 , pp. 9502-9507
    • König, R.1    Ashwell, G.2    Hannover, J.A.3
  • 48
    • 0026014164 scopus 로고
    • A mutated transferrin receptor lacking asparagine-linked glycosylation sites shows reduced functionality and an association with binding immunoglobulin protein
    • 47 Williams, A. M. and Enns, C. A. (1991) A mutated transferrin receptor lacking asparagine-linked glycosylation sites shows reduced functionality and an association with binding immunoglobulin protein. J. Biol. Chem. 266, 17648-17654
    • (1991) J. Biol. Chem. , Issue.266 , pp. 17648-17654
    • Williams, A.M.1    Enns, C.A.2
  • 49
    • 0026563680 scopus 로고
    • Misfolding and aggregation of newly synthesized proteins in the endoplasmic reticulum
    • 48 Marquardt, T. and Helenius, A. (1992) Misfolding and aggregation of newly synthesized proteins in the endoplasmic reticulum. J. Cell Biol. 117, 505-513
    • (1992) J. Cell Biol. , vol.117 , pp. 505-513
    • Marquardt, T.1    Helenius, A.2
  • 50
    • 0018083350 scopus 로고
    • Effect of tunicamycin on IgM, IgA and IgG secretion by mouse plasmacytoma cells
    • 49 Hickman, J. and Kornfeld, S. (1978) Effect of tunicamycin on IgM, IgA and IgG secretion by mouse plasmacytoma cells. J. Immunol. 121, 990-996
    • (1978) J. Immunol. , vol.121 , pp. 990-996
    • Hickman, J.1    Kornfeld, S.2
  • 51
    • 0023723072 scopus 로고
    • Selective removal of a heavy-chain glycosylation site causes immunoglobulin A degradation and reduced secretion
    • 50 Taylor, A. K. and Wall, R. (1988) Selective removal of a heavy-chain glycosylation site causes immunoglobulin A degradation and reduced secretion. Mol. Cell. Biol. 8, 4197-4203
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 4197-4203
    • Taylor, A.K.1    Wall, R.2
  • 52
    • 0024270999 scopus 로고
    • Glycosylation at specific sites of erythropoietin is essential for biosynthesis, secretion, and biological function
    • 51 Dubé, S., Fisher, J. W. and Powell, J. S. (1988) Glycosylation at specific sites of erythropoietin is essential for biosynthesis, secretion, and biological function. J. Biol. Chem. 263, 17516-17521
    • (1988) J. Biol. Chem. , vol.263 , pp. 17516-17521
    • Dubé, S.1    Fisher, J.W.2    Powell, J.S.3
  • 53
    • 0025264381 scopus 로고
    • In vitro expression and site-specific mutagenesis of the cloned human lipoprotein lipase gene. Potential N-linked glycosylation site asparagine 43 is important for both enzyme activity and secretion
    • 52 Semenkovich, C. F., Luo, C. C., Nakanishi, M. K., Chen, S. H., Smith, L. C. and Chan, L. (1990) In vitro expression and site-specific mutagenesis of the cloned human lipoprotein lipase gene. Potential N-linked glycosylation site asparagine 43 is important for both enzyme activity and secretion. J. Biol. Chem. 265, 5429-5433
    • (1990) J. Biol. Chem. , vol.265 , pp. 5429-5433
    • Semenkovich, C.F.1    Luo, C.C.2    Nakanishi, M.K.3    Chen, S.H.4    Smith, L.C.5    Chan, L.6
  • 54
    • 0024242218 scopus 로고
    • Addition of carbohydrate side chains at novel sites on influenza virus hemagglutinin can modulate the folding, transport and activity of the molecule
    • 53 Gallagher, P. J., Henneberry, J., Wilson, I., Sambrook, J. and Gething, M. J. (1988) Addition of carbohydrate side chains at novel sites on influenza virus hemagglutinin can modulate the folding, transport and activity of the molecule. J. Cell Biol. 107, 2059-2073
    • (1988) J. Cell Biol. , vol.107 , pp. 2059-2073
    • Gallagher, P.J.1    Henneberry, J.2    Wilson, I.3    Sambrook, J.4    Gething, M.J.5
  • 55
    • 0025765996 scopus 로고
    • Removal of N-glycosylation sites of the yeast acid phosphatase severely affects protein folding
    • 54 Riederer, M. A. and Hinnen, A. (1991) Removal of N-glycosylation sites of the yeast acid phosphatase severely affects protein folding. J. Bacteriol. 173, 3539-3546
    • (1991) J. Bacteriol. , vol.173 , pp. 3539-3546
    • Riederer, M.A.1    Hinnen, A.2
  • 56
    • 0023906050 scopus 로고
    • Influence of new glycosylation sites on expression of the vesicular stomatitis virus G protein at the plasma membrane
    • 55 Machamer, C. E. and Rose, J. K. (1988) Influence of new glycosylation sites on expression of the vesicular stomatitis virus G protein at the plasma membrane. J. Biol. Chem. 263, 5948-5954
    • (1988) J. Biol. Chem. , vol.263 , pp. 5948-5954
    • Machamer, C.E.1    Rose, J.K.2
  • 57
    • 0023879525 scopus 로고
    • Vesicular stomatis virus G proteins with altered glycosylation sites display temperature-sensitive intracellular transport and are subject to aberrant intermolecular disulfide bonding
    • 56 Machamer, C. E. and Rose, J. K. (1988) Vesicular stomatis virus G proteins with altered glycosylation sites display temperature-sensitive intracellular transport and are subject to aberrant intermolecular disulfide bonding. J. Biol. Chem. 263, 5955-5960
    • (1988) J. Biol. Chem. , vol.263 , pp. 5955-5960
    • Machamer, C.E.1    Rose, J.K.2
  • 58
    • 0021264739 scopus 로고
    • Influence of the N-linked oligosaccharides on the biosynthesis, intracellular routing, and function of the human asialoglycoprotein receptor
    • 57 Breitfeld, P. P., Rup, D. and Schwartz, A. L. (1984) Influence of the N-linked oligosaccharides on the biosynthesis, intracellular routing, and function of the human asialoglycoprotein receptor. J. Biol. Chem. 259, 10414-10421
    • (1984) J. Biol. Chem. , vol.259 , pp. 10414-10421
    • Breitfeld, P.P.1    Rup, D.2    Schwartz, A.L.3
  • 59
    • 0022897160 scopus 로고
    • N-glycosylation in expression and function of β-adrenergic receptors
    • 58 George, S. T., Ruoho, A. E. and Malbon, C. C. (1986) N-glycosylation in expression and function of β-adrenergic receptors. J. Biol. Chem. 261, 16559-16564
    • (1986) J. Biol. Chem. , vol.261 , pp. 16559-16564
    • George, S.T.1    Ruoho, A.E.2    Malbon, C.C.3
  • 60
    • 0025642826 scopus 로고
    • 2 muscarinic acetycholine receptor. Analysis of the role of N-glycosylation in receptor expression and function
    • 2 muscarinic acetycholine receptor. Analysis of the role of N-glycosylation in receptor expression and function. J. Biol. Chem. 265, 20887-20892
    • (1990) J. Biol. Chem. , vol.265 , pp. 20887-20892
    • Van Koppen, C.J.1    Nathanson, N.M.2
  • 61
    • 0024379308 scopus 로고
    • A single amino acid substitution eliminates the stringent carbohydrate requirement for intracellular transport of a viral glycoprotein
    • 60 Pitta, A. M., Rose, J. K. and Machamer, C. E. (1989) A single amino acid substitution eliminates the stringent carbohydrate requirement for intracellular transport of a viral glycoprotein. J. Virol. 63, 906-913
    • (1989) J. Virol. , vol.63 , pp. 906-913
    • Pitta, A.M.1    Rose, J.K.2    Machamer, C.E.3
  • 62
    • 0022130861 scopus 로고
    • Glycosylation allows cell-surface expression of an anchored secretory protein
    • 61 Guan, J. L., Machamer, C. E. and Rose, J. K. (1985) Glycosylation allows cell-surface expression of an anchored secretory protein. Cell 42, 489-496
    • (1985) Cell , vol.42 , pp. 489-496
    • Guan, J.L.1    Machamer, C.E.2    Rose, J.K.3
  • 63
    • 0026022577 scopus 로고
    • Participation of a novel 88-kDa protein in the biogenesis of murine class I histocompatibility molecules
    • 62 Degen, E. and Williams, D. B. (1991) Participation of a novel 88-kDa protein in the biogenesis of murine class I histocompatibility molecules. J. Cell Biol. 112, 1099-1115
    • (1991) J. Cell Biol. , vol.112 , pp. 1099-1115
    • Degen, E.1    Williams, D.B.2
  • 64
    • 0026511275 scopus 로고
    • Endoplasmic reticulum resident protein of 90 kilodaltons associates with the T-and B-cell antigen receptors and major histocompatibility complex antigens during their assembly
    • 63 Hochstenbach, F., David, V., Watkins, S. and Brenner, M. B. (1992) Endoplasmic reticulum resident protein of 90 kilodaltons associates with the T-and B-cell antigen receptors and major histocompatibility complex antigens during their assembly. Proc. Natl. Acad. Sci. U.S.A. 89, 4734-4738
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 4734-4738
    • Hochstenbach, F.1    David, V.2    Watkins, S.3    Brenner, M.B.4
  • 65
    • 0027295871 scopus 로고
    • Association of folding intermediates of glycoproteins with calnexin during protein maturation
    • 64 Ou, W.-J., Cameron, P. H., Thomas, D. Y. and Bergeron, J. J. M. (1993) Association of folding intermediates of glycoproteins with calnexin during protein maturation. Nature (London) 364, 771-776
    • (1993) Nature (London) , vol.364 , pp. 771-776
    • Ou, W.-J.1    Cameron, P.H.2    Thomas, D.Y.3    Bergeron, J.J.M.4
  • 66
    • 0028103695 scopus 로고
    • Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control
    • 65 Hammond, C., Braakman, I. and Helenius, A. (1994) Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control. Proc. Natl. Acad. Sci. U.S.A. 91, 913-917
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , Issue.91 , pp. 913-917
    • Hammond, C.1    Braakman, I.2    Helenius, A.3
  • 67
    • 0029024748 scopus 로고
    • Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulum
    • 66 Hebert, D. N., Foellmer, B. and Helenius, A. (1995) Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulum. Cell 81, 425-433
    • (1995) Cell , vol.81 , pp. 425-433
    • Hebert, D.N.1    Foellmer, B.2    Helenius, A.3
  • 68
    • 0029160540 scopus 로고
    • Calreticulin is a lectin-like molecular chaperone for glycoproteins of the endoplasmic reticulum
    • 67 Peterson, J. R., Ora, A., Van Nguyen, P. and Helenius, A. (1995) Calreticulin is a lectin-like molecular chaperone for glycoproteins of the endoplasmic reticulum. Mol. Biol. Cell 6, 1173-1184
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1173-1184
    • Peterson, J.R.1    Ora, A.2    Van Nguyen, P.3    Helenius, A.4
  • 69
    • 0028964421 scopus 로고
    • Calreticulin functions as a molecular chaperone in the biosynthesis of myeloperoxidase
    • 68 Nauseef, W. M., McCormick, S. J. and Clark, R. A. (1995) Calreticulin functions as a molecular chaperone in the biosynthesis of myeloperoxidase. J. Biol. Chem. 270, 4741-4747
    • (1995) J. Biol. Chem. , vol.270 , pp. 4741-4747
    • Nauseef, W.M.1    McCormick, S.J.2    Clark, R.A.3
  • 70
    • 0030053103 scopus 로고    scopus 로고
    • Calreticulin interacts with newly synthesized human immunodeficiency virus Type 1 envelope glycoprotein, suggesting a chaperone function similar to that of calnexin
    • 69 Otteken, A. and Moss, B. (1996) Calreticulin interacts with newly synthesized human immunodeficiency virus Type 1 envelope glycoprotein, suggesting a chaperone function similar to that of calnexin. J. Biol. Chem. 271, 97-103
    • (1996) J. Biol. Chem. , vol.271 , pp. 97-103
    • Otteken, A.1    Moss, B.2
  • 71
    • 0029134004 scopus 로고
    • Chaperone function of calreticulin when expressed in the endoplasmic reticulum as the membrane-anchored and soluble forms
    • 70 Wada, I., Imai, S., Kai, M., Sakane, F. and Kanoh, H. (1995) Chaperone function of calreticulin when expressed in the endoplasmic reticulum as the membrane-anchored and soluble forms. J. Biol. Chem. 270, 20298-20304
    • (1995) J. Biol. Chem. , vol.270 , pp. 20298-20304
    • Wada, I.1    Imai, S.2    Kai, M.3    Sakane, F.4    Kanoh, H.5
  • 72
    • 0029925940 scopus 로고    scopus 로고
    • The molecular chaperone calnexin facilitates folding and assembly of class I histocompatibility molecules
    • 71 Vassilakos, A., Cohen-Doyle, M. F., Peterson, P. A., Jackson, M. R. and Williams, D. B. (1996) The molecular chaperone calnexin facilitates folding and assembly of class I histocompatibility molecules. EMBO J. 15, 1495-1506
    • (1996) EMBO J. , vol.15 , pp. 1495-1506
    • Vassilakos, A.1    Cohen-Doyle, M.F.2    Peterson, P.A.3    Jackson, M.R.4    Williams, D.B.5
  • 73
    • 0028906481 scopus 로고
    • Calnexin recognizes carbohydrate and protein determinants of class I major histocompatibility complex molecules
    • 72 Zhang, Q., Tector, M. and Salter, R. D. (1995) Calnexin recognizes carbohydrate and protein determinants of class I major histocompatibility complex molecules. J. Biol. Chem. 270, 3944-3948
    • (1995) J. Biol. Chem. , vol.270 , pp. 3944-3948
    • Zhang, Q.1    Tector, M.2    Salter, R.D.3
  • 74
    • 0028810104 scopus 로고
    • Unique expression of major histocompatibility complex class I proteins in the absence of glucose trimming and calnexin association
    • 73 Balow, J. P., Weissman, J. D. and Kearse, K. P. (1995) Unique expression of major histocompatibility complex class I proteins in the absence of glucose trimming and calnexin association. J. Biol. Chem. 270, 29025-29029
    • (1995) J. Biol. Chem. , vol.270 , pp. 29025-29029
    • Balow, J.P.1    Weissman, J.D.2    Kearse, K.P.3
  • 75
    • 0029993522 scopus 로고    scopus 로고
    • Calnexin associates exclusively with individual CD3δ and T cell antigen receptor (TCR) α proteins containing incompletely trimmed glycans that are not assembled into multisubunit TCR complexes
    • 74 Van Leeuwen, J. E. M. and Kearse, K. P. (1996) Calnexin associates exclusively with individual CD3δ and T cell antigen receptor (TCR) α proteins containing incompletely trimmed glycans that are not assembled into multisubunit TCR complexes. J. Biol. Chem. 271, 9660-9665
    • (1996) J. Biol. Chem. , vol.271 , pp. 9660-9665
    • Van Leeuwen, J.E.M.1    Kearse, K.P.2
  • 76
    • 0027993624 scopus 로고
    • Persistence of glucose residues on core oligosaccharides prevents association of TCRα and TCRβ proteins with calnexin and results specifically in accelerated degradation of nascent TCRα proteins within the endoplasmic reticulum
    • 75 Kearse, K. P., Williams, D. B. and Singer, A. (1994) Persistence of glucose residues on core oligosaccharides prevents association of TCRα and TCRβ proteins with calnexin and results specifically in accelerated degradation of nascent TCRα proteins within the endoplasmic reticulum. EMBO J. 13, 3678-3686
    • (1994) EMBO J. , vol.13 , pp. 3678-3686
    • Kearse, K.P.1    Williams, D.B.2    Singer, A.3
  • 77
    • 0030716254 scopus 로고    scopus 로고
    • Calnexin-dependent enhancement of nicotinic acetylcholine receptor assembly and surface expression
    • 76 Chang, W., Gelman, M. S. and Prives, J. M. (1997) Calnexin-dependent enhancement of nicotinic acetylcholine receptor assembly and surface expression. J. Biol. Chem. 272, 28925-28932
    • (1997) J. Biol. Chem. , vol.272 , pp. 28925-28932
    • Chang, W.1    Gelman, M.S.2    Prives, J.M.3
  • 78
    • 0032479290 scopus 로고    scopus 로고
    • Inhibition of glucose trimming with castanospermine reduces calnexin association and promotes proteasome degradation of the α-subunit of the nicotinic acetylcholine receptor
    • 77 Keller, S. H., Lindstrom, J. and Taylor, P. (1998) Inhibition of glucose trimming with castanospermine reduces calnexin association and promotes proteasome degradation of the α-subunit of the nicotinic acetylcholine receptor. J. Biol. Chem. 273, 17064-17072
    • (1998) J. Biol. Chem. , vol.273 , pp. 17064-17072
    • Keller, S.H.1    Lindstrom, J.2    Taylor, P.3
  • 79
    • 0032482220 scopus 로고    scopus 로고
    • Folding of insulin receptor monomers is facilitated by the molecular chaperones calnexin and calreticulin and impaired by rapid dimerization
    • 78 Bass, J., Chiu, G., Argon, Y. and Steiner, D. F. (1998) Folding of insulin receptor monomers is facilitated by the molecular chaperones calnexin and calreticulin and impaired by rapid dimerization. J. Cell Biol. 141, 637-646
    • (1998) J. Cell Biol. , vol.141 , pp. 637-646
    • Bass, J.1    Chiu, G.2    Argon, Y.3    Steiner, D.F.4
  • 80
    • 0032478644 scopus 로고    scopus 로고
    • Differential interaction of coagulation factor VIII and factor V with protein chaperones calnexin and calreticulin
    • 79 Pipe, S. W., Morris, J. A., Shah, J. and Kaufman, R. J. (1998) Differential interaction of coagulation factor VIII and factor V with protein chaperones calnexin and calreticulin. J. Biol. Chem. 273, 8537-8544
    • (1998) J. Biol. Chem. , vol.273 , pp. 8537-8544
    • Pipe, S.W.1    Morris, J.A.2    Shah, J.3    Kaufman, R.J.4
  • 82
    • 0028883409 scopus 로고
    • Calnexin fails to associate with substrate proteins in glucosidase-deficient cell lines
    • 81 Ora, A. and Helenius, A. (1995) Calnexin fails to associate with substrate proteins in glucosidase-deficient cell lines. J. Biol. Chem. 270, 26060-26062
    • (1995) J. Biol. Chem. , vol.270 , pp. 26060-26062
    • Ora, A.1    Helenius, A.2
  • 83
    • 0033548479 scopus 로고    scopus 로고
    • Trimming and readdition of glucose to N-linked oligosaccharides determines calnexin association of a substrate glycoprotein in living cells
    • 82 Cannon, K. and Helenius, A. (1999) Trimming and readdition of glucose to N-linked oligosaccharides determines calnexin association of a substrate glycoprotein in living cells. J. Biol. Chem. 274, 7537-7544
    • (1999) J. Biol. Chem. , vol.274 , pp. 7537-7544
    • Cannon, K.1    Helenius, A.2
  • 84
    • 0030815129 scopus 로고    scopus 로고
    • Promotion of transferrin folding by cyclic interactions with calnexin and calreticulin
    • 83 Wada, I., Kai, M., Imai, S., Sakane, F. and Kanoh, H. (1997) Promotion of transferrin folding by cyclic interactions with calnexin and calreticulin. EMBO J 16, 5420-5432
    • (1997) EMBO J , vol.16 , pp. 5420-5432
    • Wada, I.1    Kai, M.2    Imai, S.3    Sakane, F.4    Kanoh, H.5
  • 85
    • 0029085605 scopus 로고
    • Retention of glucose residues added by the UDP-Glc:Glycoprotein glucosyltransferase delays exit of glycoproteins from the endoplasmic reticulum
    • 84 Labriola, C., Cazzulo, J. J. and Parodi, A. J. (1995) Retention of glucose residues added by the UDP-Glc:glycoprotein glucosyltransferase delays exit of glycoproteins from the endoplasmic reticulum. J. Cell Biol. 130, 771-779
    • (1995) J. Cell Biol. , vol.130 , pp. 771-779
    • Labriola, C.1    Cazzulo, J.J.2    Parodi, A.J.3
  • 87
    • 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
    • 86 Spiro, R. G., Zhu, Q., Bhoyroo, V. and Söling, H.-D. (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    Söling, H.-D.4
  • 88
    • 0032502282 scopus 로고    scopus 로고
    • Oligosaccharide binding characteristics of the molecular chaperones calnexin and calreticulin
    • 87 Vassilakos, A., Michalak, M., Lehrman, M. A. and Williams, D. B. (1998) Oligosaccharide binding characteristics of the molecular chaperones calnexin and calreticulin. Biochemistry 37, 3480-3490
    • (1998) Biochemistry , vol.37 , pp. 3480-3490
    • Vassilakos, A.1    Michalak, M.2    Lehrman, M.A.3    Williams, D.B.4
  • 89
    • 0030449989 scopus 로고    scopus 로고
    • N-linked oligosaccharides are necessary and sufficient for association of glycosylated forms of bovine RNase with calnexin and calreticulin
    • 88 Rodan, A. R., Simons, J. F., Trombetta, E. S. and Helenius, A. (1996) N-linked oligosaccharides are necessary and sufficient for association of glycosylated forms of bovine RNase with calnexin and calreticulin. EMBO J. 15, 6921-6930
    • (1996) EMBO J. , vol.15 , pp. 6921-6930
    • Rodan, A.R.1    Simons, J.F.2    Trombetta, E.S.3    Helenius, A.4
  • 90
    • 0030933129 scopus 로고    scopus 로고
    • Conformation independent binding of monoglucosylated ribonuclease B to calnexin
    • 89 Zapun, A., Petrescu, S., Rudd, P. M., Dwek, R. A., Thomas, D. Y. and Bergeron, J. J. (1997) Conformation independent binding of monoglucosylated ribonuclease B to calnexin. Cell 88, 29-38
    • (1997) Cell , vol.88 , pp. 29-38
    • Zapun, A.1    Petrescu, S.2    Rudd, P.M.3    Dwek, R.A.4    Thomas, D.Y.5    Bergeron, J.J.6
  • 91
    • 0031963654 scopus 로고    scopus 로고
    • Distinct patterns of folding and interactions with calnexin and calreticulin in human class I MHC proteins with altered N-glycosylation
    • 90 Zhang, Q. and Salter, R. D. (1998) Distinct patterns of folding and interactions with calnexin and calreticulin in human class I MHC proteins with altered N-glycosylation. J. Immunol. 160, 831-837
    • (1998) J. Immunol. , vol.160 , pp. 831-837
    • Zhang, Q.1    Salter, R.D.2
  • 92
    • 15844379984 scopus 로고    scopus 로고
    • Glycan-dependent and -independent association of vesicular stomatitis virus G protein with calnexin
    • 91 Cannon, K. S., Hebert, D. N. and Helenius, A. (1996) Glycan-dependent and -independent association of vesicular stomatitis virus G protein with calnexin. J. Biol. Chem 271, 14280-14284
    • (1996) J. Biol. Chem , vol.271 , pp. 14280-14284
    • Cannon, K.S.1    Hebert, D.N.2    Helenius, A.3
  • 93
    • 0029794718 scopus 로고    scopus 로고
    • The related molecular chaperones calnexin and calreticulin differentially associate with nascent T cell antigen receptor proteins within the endoplasmic reticulum
    • 92 Van Leeuwen, J. E. M. and Kearse, K. P. (1996) The related molecular chaperones calnexin and calreticulin differentially associate with nascent T cell antigen receptor proteins within the endoplasmic reticulum. J. Biol. Chem. 271, 25345-25349
    • (1996) J. Biol. Chem. , vol.271 , pp. 25345-25349
    • Van Leeuwen, J.E.M.1    Kearse, K.P.2
  • 94
    • 0034724690 scopus 로고    scopus 로고
    • Functional relationship between calreticulin, calnexin, and the ER luminal domain of calnexin
    • in the press
    • 92a Damilczyk, U. G., Cohen-Doyle, M. F. and Williams, D. B. (2000) Functional relationship between calreticulin, calnexin, and the ER luminal domain of calnexin. J. Biol. Chem. 275, in the press
    • (2000) J. Biol. Chem. , vol.275
    • Damilczyk, U.G.1    Cohen-Doyle, M.F.2    Williams, D.B.3
  • 95
    • 0030667061 scopus 로고    scopus 로고
    • The number and location of glycans on influenza hemagglutinin determine folding and association with calnexin and calreticulin
    • 93 Hebert, D. N., Zhang, J. X., Chen, W., Foellmer, B. and Helenius, A. (1997) The number and location of glycans on influenza hemagglutinin determine folding and association with calnexin and calreticulin. J. Cell Biol. 139, 613-623
    • (1997) J. Cell Biol. , vol.139 , pp. 613-623
    • Hebert, D.N.1    Zhang, J.X.2    Chen, W.3    Foellmer, B.4    Helenius, A.5
  • 96
    • 0030217926 scopus 로고    scopus 로고
    • Roles for calreticulin and a novel glycoprotein, tapasin, in the interaction of MHC class I molecules with TAP
    • 94 Sadasivan, B., Lehner, P. J., Ortmann, B., Spies, T. and Cresswell, P. (1996) Roles for calreticulin and a novel glycoprotein, tapasin, in the interaction of MHC class I molecules with TAP. Immunity 5, 103-114
    • (1996) Immunity , vol.5 , pp. 103-114
    • Sadasivan, B.1    Lehner, P.J.2    Ortmann, B.3    Spies, T.4    Cresswell, P.5
  • 97
    • 0032101943 scopus 로고    scopus 로고
    • Calreticulin and calnexin interact with different protein and glycan determinants during the assembly of MHC class I
    • 95 Harris, M. R., Yu, Y. Y. L., Kindle, C. S., Hansen, T. H. and Solheim, J. C. (1998) Calreticulin and calnexin interact with different protein and glycan determinants during the assembly of MHC class I. J. Immunol. 160, 5404-5409
    • (1998) J. Immunol. , vol.160 , pp. 5404-5409
    • Harris, M.R.1    Yu, Y.Y.L.2    Kindle, C.S.3    Hansen, T.H.4    Solheim, J.C.5
  • 98
    • 0030467255 scopus 로고    scopus 로고
    • Deglucosylation of N-linked glycans is an important step in the dissociation of calreticulin-class I-TAP complexes
    • 96 Van Leeuwen, J. E. M. and Kearse, K. P. (1996) Deglucosylation of N-linked glycans is an important step in the dissociation of calreticulin-class I-TAP complexes. Proc. Natl. Acad. Sci. U.S.A. 93, 13997-14001
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 13997-14001
    • Van Leeuwen, J.E.M.1    Kearse, K.P.2
  • 99
    • 0032482319 scopus 로고    scopus 로고
    • Evidence for successive peptide binding and quality control stages during MHC class I assembly
    • 97 Lewis, J. W. and Elliott, T. (1998) Evidence for successive peptide binding and quality control stages during MHC class I assembly. Curr. Biol. 8, 717-720
    • (1998) Curr. Biol. , vol.8 , pp. 717-720
    • Lewis, J.W.1    Elliott, T.2
  • 100
    • 0032128150 scopus 로고    scopus 로고
    • Assembly, sorting and exit of oligomeric proteins from the endoplasmic reticulum
    • 98 Reddy, P. S. and Corley, R. B. (1998) Assembly, sorting and exit of oligomeric proteins from the endoplasmic reticulum. BioEssays 20, 546-554
    • (1998) BioEssays , vol.20 , pp. 546-554
    • Reddy, P.S.1    Corley, R.B.2
  • 101
    • 0030881717 scopus 로고    scopus 로고
    • Quality control in the secretory pathway: The role of calreticulin, calnexin and BiP in the retention of glycoproteins with C-terminal truncations
    • 99 Zhang, J.-X., Braakman, I., Matlack, K. E. S. and Helenius, A. (1997) Quality control in the secretory pathway: the role of calreticulin, calnexin and BiP in the retention of glycoproteins with C-terminal truncations. Mol. Biol. Cell 8, 1943-1954
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1943-1954
    • Zhang, J.-X.1    Braakman, I.2    Matlack, K.E.S.3    Helenius, A.4
  • 102
    • 0029934119 scopus 로고    scopus 로고
    • Calnexin and calreticulin promote folding, delay oligomerizatlon and suppress degradation of influenza hemagglutinin in microsomes
    • 100 Hebert, D. N., Foellmer, B. and Helenius, A. (1996) Calnexin and calreticulin promote folding, delay oligomerizatlon and suppress degradation of influenza hemagglutinin in microsomes. EMBO J. 15, 2961-2968
    • (1996) EMBO J. , vol.15 , pp. 2961-2968
    • Hebert, D.N.1    Foellmer, B.2    Helenius, A.3
  • 103
    • 0028339518 scopus 로고
    • Quality control in the secretory pathway: Retention of a misfolded viral membrane glycoprotein involves cycling between the ER, intermediate compartment, and Golgi apparatus
    • 101 Hammond, C. and Helenius, A. (1994) Quality control in the secretory pathway: retention of a misfolded viral membrane glycoprotein involves cycling between the ER, intermediate compartment, and Golgi apparatus. J. Cell Biol. 126, 41-52
    • (1994) J. Cell Biol. , vol.126 , pp. 41-52
    • Hammond, C.1    Helenius, A.2
  • 104
    • 0031035644 scopus 로고    scopus 로고
    • Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins
    • 102 Oliver, J. D., Van der Wal, F., Bulleid, N. J. and High, S. (1997) Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins. Science 275, 86-88
    • (1997) Science , vol.275 , pp. 86-88
    • Oliver, J.D.1    Van Der Wal, F.2    Bulleid, N.J.3    High, S.4
  • 105
    • 0030960372 scopus 로고    scopus 로고
    • The thiol-dependent reductase ERp57 interacts specifically with N-glycosylated integral membrane proteins
    • 103 Elliott, J. G., Oliver, J. D. and High, S. (1997) The thiol-dependent reductase ERp57 interacts specifically with N-glycosylated integral membrane proteins. J. Biol. Chem. 272, 13849-13855
    • (1997) J. Biol. Chem. , vol.272 , pp. 13849-13855
    • Elliott, J.G.1    Oliver, J.D.2    High, S.3
  • 106
    • 0032807338 scopus 로고    scopus 로고
    • ERp57 functions as a subunit of specific complexes formed with the ER lectins calreticulin and calnexin Mol
    • 104 Oliver, J. D., Llewelyn Roderick, H., Llewelyn, D. H. and High, S. (1999) ERp57 functions as a subunit of specific complexes formed with the ER lectins calreticulin and calnexin Mol. Biol. Cell 10, 2573-2582
    • (1999) Biol. Cell , vol.10 , pp. 2573-2582
    • Oliver, J.D.1    Llewelyn Roderick, H.2    Llewelyn, D.H.3    High, S.4
  • 107
    • 0032513212 scopus 로고    scopus 로고
    • Enhanced catalysis of ribonuclease B folding by the interaction of calnexin or calreticulin with ERp57
    • 105 Zapun, A., Darby, N. J., Tessier, D. C., Michalak, M., Bergeron, J. J. M. and Thomas, D. Y. (1998) Enhanced catalysis of ribonuclease B folding by the interaction of calnexin or calreticulin with ERp57. J. Biol. Chem. 273, 6009-6012
    • (1998) J. Biol. Chem. , vol.273 , pp. 6009-6012
    • Zapun, A.1    Darby, N.J.2    Tessier, D.C.3    Michalak, M.4    Bergeron, J.J.M.5    Thomas, D.Y.6
  • 108
    • 0028888054 scopus 로고
    • Molecular requirements for the interaction of class II major histocompalibility complex and invariant chain with calnexin
    • 106 Arunachalam, B. and Cresswell, P. (1995) Molecular requirements for the interaction of class II major histocompalibility complex and invariant chain with calnexin. J. Biol. Chem. 270, 2784-2790
    • (1995) J. Biol. Chem. , vol.270 , pp. 2784-2790
    • Arunachalam, B.1    Cresswell, P.2
  • 110
    • 0033197741 scopus 로고    scopus 로고
    • Calnexin discriminates between protein conformational states and functions as a molecular chaperone in vitro
    • 108 Ihara, Y., Cohen-Doyle, M. F., Saito, Y. and Williams, D. B. (1999) Calnexin discriminates between protein conformational states and functions as a molecular chaperone in vitro. Mol. Cell 4, 331-341
    • (1999) Mol. Cell , vol.4 , pp. 331-341
    • Ihara, Y.1    Cohen-Doyle, M.F.2    Saito, Y.3    Williams, D.B.4
  • 111
    • 0033485263 scopus 로고    scopus 로고
    • Calreticulin functions in vitro as a molecular chaperone for both glycosylated and non-glycosylated proteins
    • 109 Saito, Y., Ihara, Y., Leach, M. R., Cohen-Doyle, M. F. and Williams, D. B. (1999) Calreticulin functions in vitro as a molecular chaperone for both glycosylated and non-glycosylated proteins. EMBO J. 18, 6718-6729
    • (1999) EMBO J. , vol.18 , pp. 6718-6729
    • Saito, Y.1    Ihara, Y.2    Leach, M.R.3    Cohen-Doyle, M.F.4    Williams, D.B.5
  • 112
    • 0029073719 scopus 로고
    • Aglycosylated and phosphatidylinositol-anchored MHC class I molecules are associated with calnexin. Evidence implicating the class 1-connecting peptide segment in calnexin association
    • 110 Carreño, B. M., Schreiber, K. L., McKean, D. J., Stroynowski, Y. and Hansen, T. H. (1995) Aglycosylated and phosphatidylinositol-anchored MHC class I molecules are associated with calnexin. Evidence implicating the class 1-connecting peptide segment in calnexin association. J. Immunol 154, 5173-5180
    • (1995) J. Immunol , vol.154 , pp. 5173-5180
    • Carreño, B.M.1    Schreiber, K.L.2    McKean, D.J.3    Stroynowski, Y.4    Hansen, T.H.5
  • 113
    • 0018786653 scopus 로고
    • The nonglycosylated glycoprotein of vesicular stomatitis virus is temperature sensitive and undergoes intracellular aggregation at elevated temperatures
    • 111 Gibson, R., Schlesinger, S. and Kornfeld, S. (1979) The nonglycosylated glycoprotein of vesicular stomatitis virus is temperature sensitive and undergoes intracellular aggregation at elevated temperatures. J. Biol. Chem. 254, 3600-3605
    • (1979) J. Biol. Chem. , vol.254 , pp. 3600-3605
    • Gibson, R.1    Schlesinger, S.2    Kornfeld, S.3
  • 114
    • 0024400060 scopus 로고
    • Interactions of misfolded influenza virus hemagglutinin with binding protein (BiP)
    • 112 Hurtley, S. M., Bole, D. G., Hoover-Litty, H., Helenius, A. and Copeland, C. S. (1989) Interactions of misfolded influenza virus hemagglutinin with binding protein (BiP). J. Cell Biol. 108, 2117-2126
    • (1989) J. Cell Biol. , vol.108 , pp. 2117-2126
    • Hurtley, S.M.1    Bole, D.G.2    Hoover-Litty, H.3    Helenius, A.4    Copeland, C.S.5
  • 115
    • 0032476580 scopus 로고    scopus 로고
    • The UDP-Glc:Glycoprotein glucosyltransferase is essential for Schizosaccharomyces pombe viability under conditions of extreme endoplasmic reticulum stress
    • 113 Fanchiotti, S., Fernández, F., D'Alessio, C. and Parodi, A. J. (1998) The UDP-Glc:glycoprotein glucosyltransferase is essential for Schizosaccharomyces pombe viability under conditions of extreme endoplasmic reticulum stress. J. Cell Biol. 143, 625-635
    • (1998) J. Cell Biol. , vol.143 , pp. 625-635
    • Fanchiotti, S.1    Fernández, F.2    D'Alessio, C.3    Parodi, A.J.4
  • 116
    • 0026317971 scopus 로고
    • A novel glycosylation phenotype expressed by Lec23, a Chinese hamster ovary mutant deficient in α-glucosidase I
    • 114 Ray, M. K., Young, J., Sundaram, S. and Stanley, P. (1991) A novel glycosylation phenotype expressed by Lec23, a Chinese hamster ovary mutant deficient in α-glucosidase I. J. Biol. Chem. 266, 22818-22825
    • (1991) J. Biol. Chem. , vol.266 , pp. 22818-22825
    • Ray, M.K.1    Young, J.2    Sundaram, S.3    Stanley, P.4
  • 117
    • 0020385681 scopus 로고
    • A lectin-resistant mouse lymphoma cell line is deficient in glucosidase II, a glycoprotein processing enzyme
    • 115 Reitman, M. L., Trowbridge, L. S. and Kornfeld, S. (1982) A lectin-resistant mouse lymphoma cell line is deficient in glucosidase II, a glycoprotein processing enzyme. J. Biol. Chem. 257, 10357-10363
    • (1982) J. Biol. Chem. , vol.257 , pp. 10357-10363
    • Reitman, M.L.1    Trowbridge, L.S.2    Kornfeld, S.3
  • 118
    • 0029001576 scopus 로고
    • A novel signal transduction pathway from the endoplasmic reticulum to the nucleus is mediated by transcription factor NF-kappa B
    • 116 Pahl, H. L. and Baeuerle, P. A. (1995) A novel signal transduction pathway from the endoplasmic reticulum to the nucleus is mediated by transcription factor NF-kappa B. EMBO J. 14, 2580-2588
    • (1995) EMBO J. , vol.14 , pp. 2580-2588
    • Pahl, H.L.1    Baeuerle, P.A.2
  • 119
    • 0031884897 scopus 로고    scopus 로고
    • Genetic tailoring of N-linked oligosaccharides: The role of glucose residues in glycoprotein processing in Saccharomyces cerevisiae in vivo
    • 117 Jakob, C. A., Burda, P., te Heesen, S., Aebi, M. and Roth, J. (1998) Genetic tailoring of N-linked oligosaccharides: the role of glucose residues in glycoprotein processing in 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
  • 120
    • 0032518912 scopus 로고    scopus 로고
    • Cell wall 1,6-β-glucan synthesis in Saccharomyces cerevisiae depends on ER glucosidases I and II, and the molecular chaperone BiP/Kar2p
    • 118 Simons, J. F., Ebersold, M. and Helenius, A. (1998) Cell wall 1,6-β-glucan synthesis in Saccharomyces cerevisiae depends on ER glucosidases I and II, and the molecular chaperone BiP/Kar2p. EMBO J. 17, 396-405
    • (1998) EMBO J. , vol.17 , pp. 396-405
    • Simons, J.F.1    Ebersold, M.2    Helenius, A.3
  • 121
    • 0028881645 scopus 로고
    • Saccharomyces cerevisiae CNE1 encodes an endoplasmic reticulum (ER) membrane protein with sequence similarity to calnexin and calreticulin and functions as a constituent of the ER quality control apparatus
    • 119 Parlati, F., Domínguez, M., Bergeron, J. J. M. and Thomas, D. Y. (1995) Saccharomyces cerevisiae CNE1 encodes an endoplasmic reticulum (ER) membrane protein with sequence similarity to calnexin and calreticulin and functions as a constituent of the ER quality control apparatus. J. Biol. Chem. 270, 244-253
    • (1995) J. Biol. Chem. , vol.270 , pp. 244-253
    • Parlati, F.1    Domínguez, M.2    Bergeron, J.J.M.3    Thomas, D.Y.4
  • 123
    • 0023639057 scopus 로고
    • Interference with HIV-induced syncytium formation and viral infectivity by inhibitors of trimming glucosidases
    • 121 Gruters, R. A., Neefjes, J. J., Tersmette, M., Tulp, A., Huisman, H. G., Miedema, F. and Ploegh, H. L. (1987) Interference with HIV-induced syncytium formation and viral infectivity by inhibitors of trimming glucosidases. Nature (London) 330, 74-77
    • (1987) Nature (London) , vol.330 , pp. 74-77
    • Gruters, R.A.1    Neefjes, J.J.2    Tersmette, M.3    Tulp, A.4    Huisman, H.G.5    Miedema, F.6    Ploegh, H.L.7
  • 124
    • 0029819131 scopus 로고    scopus 로고
    • N-butyldeoxynojirimycin-mediated inhibition of human Immunodeficiency virus entry correlates with changes in antibody recognition of the V1-V2 region of gp120
    • 122 Fischer, P. B., Karlsson, G. B., Butters, T. D., Dwek, R. A. and Platt, F. M. (1996) N-butyldeoxynojirimycin-mediated inhibition of human Immunodeficiency virus entry correlates with changes in antibody recognition of the V1-V2 region of gp120. J. Virol. 70, 7143-7152
    • (1996) J. Virol. , vol.70 , pp. 7143-7152
    • Fischer, P.B.1    Karlsson, G.B.2    Butters, T.D.3    Dwek, R.A.4    Platt, F.M.5
  • 125
    • 0031058830 scopus 로고    scopus 로고
    • Hepatitis B virus (HBV) envelope glycoproteins vary drastically in their sensitivity to glycan processing: Evidence that alteration of a single N-linked glycosylation site can regulate HBV secretion
    • 123 Mehta, A., Lu, X., Block, T. M., Blumberg, B. S. and Dwek, R. A. (1997) Hepatitis B virus (HBV) envelope glycoproteins vary drastically in their sensitivity to glycan processing: evidence that alteration of a single N-linked glycosylation site can regulate HBV secretion. Proc. Natl. Acad. Sci. U.S.A. 94, 1822-1827
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 1822-1827
    • Mehta, A.1    Lu, X.2    Block, T.M.3    Blumberg, B.S.4    Dwek, R.A.5
  • 126
    • 0030898710 scopus 로고    scopus 로고
    • Proteasome inhibition leads to a heat-shock response, induction of endoplasmic reticulum chaperones and thermotolerance
    • 124 Busch, K. T., Goldberg, A. L. and Nigam, S. K. (1997) Proteasome inhibition leads to a heat-shock response, induction of endoplasmic reticulum chaperones and thermotolerance. J. Biol. Chem. 272, 9086-9092
    • (1997) J. Biol. Chem. , vol.272 , pp. 9086-9092
    • Busch, K.T.1    Goldberg, A.L.2    Nigam, S.K.3
  • 127
    • 0032555648 scopus 로고    scopus 로고
    • Peptides glycosylated in the endoplasmic reticulum of yeast are subsequently deglycosylated by a soluble peptide:N-glycanase activity
    • 125 Suzuki, T., Park, H., Kitajima, K. and Lennarz, W. J. (1998) Peptides glycosylated in the endoplasmic reticulum of yeast are subsequently deglycosylated by a soluble peptide:N-glycanase activity. J. Biol. Chem. 273, 21526-21530
    • (1998) J. Biol. Chem. , vol.273 , pp. 21526-21530
    • Suzuki, T.1    Park, H.2    Kitajima, K.3    Lennarz, W.J.4
  • 128
    • 0029915568 scopus 로고    scopus 로고
    • The human cytomegalovirus US11 gene product dislocates MHC class 1 heavy chains from the endoplasmic reticulum to the cytosol
    • 126 Wiertz, E. J. H. J., Jones, T. R., Sun, L., Bogyo, M., Geuze, H. J. and Ploegh, H. L. (1996) The human cytomegalovirus US11 gene product dislocates MHC class 1 heavy chains from the endoplasmic reticulum to the cytosol. Cell 84, 769-779
    • (1996) Cell , vol.84 , pp. 769-779
    • Wiertz, E.J.H.J.1    Jones, T.R.2    Sun, L.3    Bogyo, M.4    Geuze, H.J.5    Ploegh, H.L.6
  • 129
    • 0032491397 scopus 로고    scopus 로고
    • The mechanism underlying cystic fibrosis transmembrane conductance regulator transport from the endoplasmic reticulum to the proteasome includes Sec61b and a cytosolic, deglycosylated intermediary
    • 127 Bebök, Z., Mazzochi, C., King, S. A., Hong, J. S. and Sorscher, E. J. (1998) The mechanism underlying cystic fibrosis transmembrane conductance regulator transport from the endoplasmic reticulum to the proteasome includes Sec61b and a cytosolic, deglycosylated intermediary. J. Biol. Chem. 273, 29873-29878
    • (1998) J. Biol. Chem. , vol.273 , pp. 29873-29878
    • Bebök, Z.1    Mazzochi, C.2    King, S.A.3    Hong, J.S.4    Sorscher, E.J.5
  • 130
    • 0031030663 scopus 로고    scopus 로고
    • Transfer of free polymannose-type oligosaccharides from the cytosol to lysosomes in cultured human hepatocellular carcinoma HEPG2 cells
    • 128 Saint-Pol, A., Bauvy, C., Codogno, P. and Moore, S.E. H. (1997) Transfer of free polymannose-type oligosaccharides from the cytosol to lysosomes in cultured human hepatocellular carcinoma HEPG2 cells. J. Cell Biol. 136, 45-59
    • (1997) J. Cell Biol. , vol.136 , pp. 45-59
    • Saint-Pol, A.1    Bauvy, C.2    Codogno, P.3    Moore, S.E.H.4
  • 131
    • 0029829005 scopus 로고    scopus 로고
    • A pathway for targeting soluble misfolded proteins to the yeast vacuole
    • 129 Hong, E., Davidson, A. R. and Kaiser, C. A. (1996) A pathway for targeting soluble misfolded proteins to the yeast vacuole. J. Cell Biol. 135, 623-633
    • (1996) J. Cell Biol. , vol.135 , pp. 623-633
    • Hong, E.1    Davidson, A.R.2    Kaiser, C.A.3
  • 132
    • 0038785977 scopus 로고    scopus 로고
    • Ligand recognition and domain structure of Vps10p, a vacuolar protein sorting receptor in Saccharomyces cerevisiae
    • 130 Jörgensen, M. U., Emr, S.D. and Winther, J. R. (1999) Ligand recognition and domain structure of Vps10p, a vacuolar protein sorting receptor in Saccharomyces cerevisiae. Eur. J. Biochem. 260, 461-469
    • (1999) Eur. J. Biochem. , vol.260 , pp. 461-469
    • Jörgensen, M.U.1    Emr, S.D.2    Winther, J.R.3
  • 133
    • 0030948755 scopus 로고    scopus 로고
    • Inhibition of N-glycan processing in B16 melanoma cells results in inactivation of tyrosinase but does not prevent its transport to the melanosome
    • 131 Petrescu, S. M., Petrescu, A. J., Titu, H. N., Dwek, R. A. and Platt, F. M. (1997) Inhibition of N-glycan processing in B16 melanoma cells results in inactivation of tyrosinase but does not prevent its transport to the melanosome. J. Biol. Chem. 272, 15796-15803
    • (1997) J. Biol. Chem. , vol.272 , pp. 15796-15803
    • Petrescu, S.M.1    Petrescu, A.J.2    Titu, H.N.3    Dwek, R.A.4    Platt, F.M.5
  • 135
    • 0032494135 scopus 로고    scopus 로고
    • Degradation of misfolded endoplasmic reticulum glycoproteins in Saccharomyces cerevisiae is determined by a specific oligosaccharide structure
    • 133 Jakob, C. A., Burda, P., Roth, J. and Aebi, M. (1998) Degradation of misfolded endoplasmic reticulum glycoproteins in Saccharomyces cerevisiae is determined by a specific oligosaccharide structure. J. Cell Biol. 142, 1223-1233
    • (1998) J. Cell Biol. , vol.142 , pp. 1223-1233
    • Jakob, C.A.1    Burda, P.2    Roth, J.3    Aebi, M.4
  • 136
    • 0028359625 scopus 로고
    • Glycoprotein synthesis in yeast. Early events in N-oligosaccharide processing in Schizosaccharomyces pombe
    • 134 Ziegler, F. D., Gemmill, T. R. and Trimble, R. B. (1994) Glycoprotein synthesis in yeast. Early events in N-oligosaccharide processing in Schizosaccharomyces pombe. J. Biol. Chem. 269, 12527-12535
    • (1994) J. Biol. Chem. , vol.269 , pp. 12527-12535
    • Ziegler, F.D.1    Gemmill, T.R.2    Trimble, R.B.3
  • 137
    • 0032536903 scopus 로고    scopus 로고
    • Novel aspects of degradation of T cell receptor subunits from the endoplasmic reticulum (ER) in T cells: Importance of oligosaccharide processing, ubiquitination, and proteasome-dependent removal from ER membranes
    • 135 Yang, M., Omura, S., Bonifacino, J. S. and Weissman, A. M. (1998) Novel aspects of degradation of T cell receptor subunits from the endoplasmic reticulum (ER) 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    Omura, S.2    Bonifacino, J.S.3    Weissman, A.M.4
  • 138
    • 0033605219 scopus 로고    scopus 로고
    • Oligosaccharide modification in the early secretory pathway directs the selection of a misfolded glycoprotein for degradation by the proteasome
    • 136 Liu, Y., Choudhury, P., Cabral, C. M. and Sifers, R. N. (1999) Oligosaccharide modification in the early secretory pathway directs the selection of a misfolded glycoprotein for degradation by the proteasome. J. Biol. Chem. 274, 5861-5867
    • (1999) J. Biol. Chem. , vol.274 , pp. 5861-5867
    • Liu, Y.1    Choudhury, P.2    Cabral, C.M.3    Sifers, R.N.4
  • 139
    • 0027238561 scopus 로고
    • Pre-Golgi degradation of yeast prepro-α-factor expressed in a mammalian cell. Influence of cell type-specific oligosaccharide processing on intracellular fate
    • 137 Su, K., Stoller, T., Rocco, J., Zemsky, J. and Green, R. (1993) Pre-Golgi degradation of yeast prepro-α-factor expressed in a mammalian cell. Influence of cell type-specific oligosaccharide processing on intracellular fate. J. Biol. Chem. 268, 14301-14309
    • (1993) J. Biol. Chem. , vol.268 , pp. 14301-14309
    • Su, K.1    Stoller, T.2    Rocco, J.3    Zemsky, J.4    Green, R.5
  • 141
    • 0345253853 scopus 로고    scopus 로고
    • Degradation of a short-lived glycoprotein from the lumen of the endoplasmic reticulum: The role of N-linked glycans and the unfolded protein response
    • 139 de Virgilio, M., Kitzmüller, C., Schwaiger, E., Klein, M., Kreibich, G. and Ivessa, N. E. (1999) Degradation of a short-lived glycoprotein from the lumen of the endoplasmic reticulum: the role of N-linked glycans and the unfolded protein response. Mol. Biol. Cell 10, 4059-4073
    • (1999) Mol. Biol. Cell , vol.10 , pp. 4059-4073
    • De Virgilio, M.1    Kitzmüller, C.2    Schwaiger, E.3    Klein, M.4    Kreibich, G.5    Ivessa, N.E.6
  • 142
    • 0027401887 scopus 로고
    • Inhibition of glucose trimming by castanospermine results in rapid degradation of unassembled major histocompatibility complex class I molecules
    • 140 Moore, S.E. and Spiro, R. G. (1993) Inhibition of glucose trimming by castanospermine results in rapid degradation of unassembled major histocompatibility complex class I molecules. J. Biol. Chem. 268, 3809-3812
    • (1993) J. Biol. Chem. , vol.268 , pp. 3809-3812
    • Moore, S.E.1    Spiro, R.G.2
  • 143
  • 144
    • 0032538638 scopus 로고    scopus 로고
    • Proteasome-mediated degradation of apolipoprotein B targets both nascent peptides cotranslationally before translocation and full-length apolipoprotein B after translocation into the endoplasmic reticulum
    • 142 Liao, W., Yeung, S.-C. J. and Chan, L. (1998) Proteasome-mediated degradation of apolipoprotein B targets both nascent peptides cotranslationally before translocation and full-length apolipoprotein B after translocation into the endoplasmic reticulum. J. Biol. Chem. 273, 27225-27230
    • (1998) J. Biol. Chem. , vol.273 , pp. 27225-27230
    • Liao, W.1    Yeung, S.-C.J.2    Chan, L.3
  • 145
    • 0030070704 scopus 로고    scopus 로고
    • Assembly of ER-associated protein degradation in vitro: Dependence on cytosol, calnexin, and ATP
    • 143 McCracken, A. A. and Brodsky, J. L. (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


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