메뉴 건너뛰기




Volumn 31, Issue 5, 1998, Pages 601-614

The quality control of glycoprotein folding in the endoplasmic reticulum, a trip from trypanosomes to mammals

Author keywords

Endoplasmic reticulum; Folding; Glucosylation; Glycoproteins; N glycosylation

Indexed keywords

MAMMALIA; PROTOZOA; TRYPANOSOMATIDAE;

EID: 0032065335     PISSN: 0100879X     EISSN: 1414431X     Source Type: Journal    
DOI: 10.1590/S0100-879X1998000500002     Document Type: Article
Times cited : (15)

References (67)
  • 3
    • 0019377631 scopus 로고
    • Synthesis and processing of asparagine-linked oligosaccharides
    • Hubbard SC & Ivatt RJ (1981). Synthesis and processing of asparagine-linked oligosaccharides. Annual Review of Biochemistry, 50: 555-583.
    • (1981) Annual Review of Biochemistry , vol.50 , pp. 555-583
    • Hubbard, S.C.1    Ivatt, R.J.2
  • 4
    • 0026716017 scopus 로고
    • Oligosaccharyltransferase activity is associated with a protein complex composed of ribophorins I and II and a 48 kDa protein
    • Kelleher DJ, Kreibich G & Gilmore R (1992). Oligosaccharyltransferase activity is associated with a protein complex composed of ribophorins I and II and a 48 kDa protein. Cell, 69: 55-65.
    • (1992) Cell , vol.69 , pp. 55-65
    • Kelleher, D.J.1    Kreibich, G.2    Gilmore, R.3
  • 5
    • 0017741488 scopus 로고
    • Comparative rates of transfer of lipidlinked oligosaccharides to endogenous glycoprotein acceptors in vitro
    • Turco S, Stetson B & Robboins PW (1977). Comparative rates of transfer of lipidlinked oligosaccharides to endogenous glycoprotein acceptors in vitro. Proceedings of the National Academy of Sciences, USA, 74: 4411-4414.
    • (1977) Proceedings of the National Academy of Sciences, USA , vol.74 , pp. 4411-4414
    • Turco, S.1    Stetson, B.2    Robboins, P.W.3
  • 6
    • 0040320246 scopus 로고
    • A mutation that prevents glucosylation of the lipid-linked oligosaccharide precursor leads to under-glycosylation of secreted yeast invertase
    • Ballou L, Gopal P, Krummel B, Tammi M & Ballou CE (1986). A mutation that prevents glucosylation of the lipid-linked oligosaccharide precursor leads to under-glycosylation of secreted yeast invertase. Proceedings of the National Academy of Sciences, USA, 83: 3081-3085.
    • (1986) Proceedings of the National Academy of Sciences, USA , vol.83 , pp. 3081-3085
    • Ballou, L.1    Gopal, P.2    Krummel, B.3    Tammi, M.4    Ballou, C.E.5
  • 7
    • 0021150615 scopus 로고
    • Purification by affinity chromatography of glucosidase I, an endoplasmic reticulum hydrolase involved in the processing of asparagine-linked oligosaccharides
    • Hettkamp H, Legler G & Bause E (1984). Purification by affinity chromatography of glucosidase I, an endoplasmic reticulum hydrolase involved in the processing of asparagine-linked oligosaccharides. European Journal of Biochemistry. 142: 85-90.
    • (1984) European Journal of Biochemistry , vol.142 , pp. 85-90
    • Hettkamp, H.1    Legler, G.2    Bause, E.3
  • 8
    • 0021245984 scopus 로고
    • Isolation of a homogeneous glucosidase II from pig kidney microsomes
    • Brada D & Dubach UC (1984). Isolation of a homogeneous glucosidase II from pig kidney microsomes. European Journal of Biochemistry, 141: 149-156.
    • (1984) European Journal of Biochemistry , vol.141 , pp. 149-156
    • Brada, D.1    Dubach, U.C.2
  • 9
    • 0022976402 scopus 로고
    • The use of 1-deoxymannojirimycin to evaluate the role of various oc-mannosidases in oligosaccharide processing in intact cells
    • Bischoff J, Liscum L & Kornfeld R (1986). The use of 1-deoxymannojirimycin to evaluate the role of various oc-mannosidases in oligosaccharide processing in intact cells. Journal of Biological Chemistry, 261: 4766-4774.
    • (1986) Journal of Biological Chemistry , vol.261 , pp. 4766-4774
    • Bischoff, J.1    Liscum, L.2    Kornfeld, R.3
  • 10
    • 0027331577 scopus 로고
    • Demonstration that a kifunensin-resistant α-mannosidase with a unique processing action on N-linked oligosaccharides occurs in rat liver endoplasmic reticulum and various cultured cells
    • Weng S & Spiro RG (1993). Demonstration that a kifunensin-resistant α-mannosidase with a unique processing action on N-linked oligosaccharides occurs in rat liver endoplasmic reticulum and various cultured cells. Journal of Biological Chemistry, 268: 25656-25663.
    • (1993) Journal of Biological Chemistry , vol.268 , pp. 25656-25663
    • Weng, S.1    Spiro, R.G.2
  • 11
    • 0023754150 scopus 로고
    • Glycoprotein biosynthesis in Saccharomyces cerevisiae. Purification of the α-mannosidase which removes one specific mannose residue from MangGlcNAc
    • Jelinek-Kelly S & Herscovics A (1988). Glycoprotein biosynthesis in Saccharomyces cerevisiae. Purification of the α-mannosidase which removes one specific mannose residue from MangGlcNAc. Journal of Biological Chemistry, 263: 14757-14763.
    • (1988) Journal of Biological Chemistry , vol.263 , pp. 14757-14763
    • Jelinek-Kelly, S.1    Herscovics, A.2
  • 12
    • 0002827648 scopus 로고
    • The diversity of the kinetoplastid flagellates
    • Lumsden WHR & Evans DA (Editors), Academic Press, New York
    • Vickerham K (1976). The diversity of the kinetoplastid flagellates. In: Lumsden WHR & Evans DA (Editors), Biology of Kinetoplastida. Academic Press, New York.
    • (1976) Biology of Kinetoplastida
    • Vickerham, K.1
  • 13
    • 0027282621 scopus 로고
    • N-glycosylation in trypanosomatid protozoa
    • Parodi AJ (1993). N-glycosylation in trypanosomatid protozoa. Glycobiology, 3: 193-199.
    • (1993) Glycobiology , vol.3 , pp. 193-199
    • Parodi, A.J.1
  • 14
    • 0027227797 scopus 로고
    • Biosynthesis of proteinlinked oligosaccharides intrypanosomatid flagellates
    • Parodi AJ (1993). Biosynthesis of proteinlinked oligosaccharides intrypanosomatid flagellates. Parasitology Today, 9: 373-377.
    • (1993) Parasitology Today , vol.9 , pp. 373-377
    • Parodi, A.J.1
  • 15
    • 0023655783 scopus 로고
    • Synthesis of dolichol derivatives in trypanosomatids, Characterization of enzymatic patterns
    • de la Canal L & Parodi AJ (1987). Synthesis of dolichol derivatives in trypanosomatids, Characterization of enzymatic patterns. Journal of Biological Chemistry, 262: 11128-11133.
    • (1987) Journal of Biological Chemistry , vol.262 , pp. 11128-11133
    • De La Canal, L.1    Parodi, A.J.2
  • 16
    • 0019918697 scopus 로고
    • Protein glycosylation in Trypanosoma cruzi, II. Partial characterization of protein-bound oligosaccharides labeled in vivo
    • Parodi AJ & Cazzulo JJ (1982). Protein glycosylation in Trypanosoma cruzi, II. Partial characterization of protein-bound oligosaccharides labeled in vivo. Journal of Biological Chemistry, 257: 7641-7645.
    • (1982) Journal of Biological Chemistry , vol.257 , pp. 7641-7645
    • Parodi, A.J.1    Cazzulo, J.J.2
  • 17
    • 0020587404 scopus 로고
    • Protein glycosylation in Trypanosoma cruzi. The mechanism of glycosylation and structure of protein-bound oligosaccharides
    • Parodi AJ, Lederkremer GZ & Mendelzon DH (1983). Protein glycosylation in Trypanosoma cruzi. The mechanism of glycosylation and structure of protein-bound oligosaccharides. Journal of Biological Chemistry, 258: 5589-5595.
    • (1983) Journal of Biological Chemistry , vol.258 , pp. 5589-5595
    • Parodi, A.J.1    Lederkremer, G.Z.2    Mendelzon, D.H.3
  • 19
    • 0022970907 scopus 로고
    • N-linked, high mannose-type oligosaccharides in the protozoa Crithidia fasciculata and Crithidia harmosa contain in galactofuranose residues
    • Mendelzon DH & Parodi AJ (1986). N-linked, high mannose-type oligosaccharides in the protozoa Crithidia fasciculata and Crithidia harmosa contain in galactofuranose residues. Journal of Biological Chemistry, 261: 2129-2133.
    • (1986) Journal of Biological Chemistry , vol.261 , pp. 2129-2133
    • Mendelzon, D.H.1    Parodi, A.J.2
  • 21
    • 0024297303 scopus 로고
    • Characterization of dolichol diphosphate oligosaccharide:protein oligosaccharyltransferase and of glycoprotein processing glucosidases occurring in trypanosomatids
    • Bosch M, Trombetta S, Engstrom U & Parodi AJ (1988). Characterization of dolichol diphosphate oligosaccharide:protein oligosaccharyltransferase and of glycoprotein processing glucosidases occurring in trypanosomatids. Journal of Biological Chemistry, 263: 17360-17365.
    • (1988) Journal of Biological Chemistry , vol.263 , pp. 17360-17365
    • Bosch, M.1    Trombetta, S.2    Engstrom, U.3    Parodi, A.J.4
  • 24
    • 0023009114 scopus 로고
    • Processing of asparagine-linked saccharides in Mucor rouxii
    • Lederkremer GZ & Parodi AJ (1986). Processing of asparagine-linked saccharides in Mucor rouxii. Biochimica et Biophysica Acta, 884: 363-369.
    • (1986) Biochimica et Biophysica Acta , vol.884 , pp. 363-369
    • Lederkremer, G.Z.1    Parodi, A.J.2
  • 25
    • 0018265515 scopus 로고
    • The synthesis of complex-type oligosaccharides. II. Characterization of the processing intermediates in the synthesis of the complex units of the vesicular stomatitis virus G protein
    • Kornfeld S, Li E & Tabas I (1978). The synthesis of complex-type oligosaccharides. II. Characterization of the processing intermediates in the synthesis of the complex units of the vesicular stomatitis virus G protein. Journal of Biological Chemistry, 253: 7771-7778.
    • (1978) Journal of Biological Chemistry , vol.253 , pp. 7771-7778
    • Kornfeld, S.1    Li, E.2    Tabas, I.3
  • 27
    • 0024468302 scopus 로고
    • Glucosylation of glycoproteins by mam-malian, plant, fungal and trypanosomatid protozoa microsomal proteins
    • Trombetta S, Bosch M & Parodi AJ (1989) Glucosylation of glycoproteins by mam-malian, 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
  • 28
    • 0026101730 scopus 로고
    • The UDP-Glc:glycoprotein glucosyltransferase is a soluble protein of the endoplasmic reticulum
    • Trombetta S, Gan̄án S & Parodi AJ (1991). The UDP-Glc:glycoprotein glucosyltransferase is a soluble protein of the endoplasmic reticulum. Glycobiology, 1: 155-161.
    • (1991) Glycobiology , vol.1 , pp. 155-161
    • Trombetta, S.1    Ganán, S.2    Parodi, A.J.3
  • 29
    • 0026500202 scopus 로고
    • Recognition of the oligosaccharide and protein moieties of glycoproteins by the UDP-Glc:glycoprotein glucosyl-transferase
    • Sousa M, Ferrero-Garcia MA & Parodi AJ (1992). Recognition of the oligosaccharide and protein moieties of glycoproteins by the UDP-Glc:glycoprotein glucosyl-transferase Biochemistry, 31: 97-105.
    • (1992) Biochemistry , vol.31 , pp. 97-105
    • Sousa, M.1    Ferrero-Garcia, M.A.2    Parodi, A.J.3
  • 30
    • 0026799435 scopus 로고
    • Purification to apparent homogeneity and partial characterization of rat liver UDP-Glc:glycoprotein glucosyltransferase
    • Trombetta S & Parodi AJ (1992). Purification to apparent homogeneity and partial characterization of rat liver UDP-Glc:glycoprotein glucosyltransferase. Journal of Biological Chemistry, 267: 9236-9240.
    • (1992) Journal of Biological Chemistry , vol.267 , pp. 9236-9240
    • Trombetta, S.1    Parodi, A.J.2
  • 31
    • 0028150802 scopus 로고
    • Purification to homogeneity of UDP-Glc:glycoprotein glucosyl-transferase from Schizosaccharomyces pombe and apparent absence of the enzyme from Saccharomyces cerevisiae
    • Fernȧndez F, Trombetta S, Hellman U & Parodi AJ (1994). Purification to homogeneity of UDP-Glc:glycoprotein glucosyl-transferase from Schizosaccharomyces pombe and apparent absence of the enzyme from Saccharomyces cerevisiae. Journal of Biological Chemistry, 269: 30701-30706.
    • (1994) Journal of Biological Chemistry , vol.269 , pp. 30701-30706
    • Fernandez, F.1    Trombetta, S.2    Hellman, U.3    Parodi, A.J.4
  • 32
    • 0022854037 scopus 로고
    • Topography of glycosylation reactions in the rough endoplasmic reticulum membrane
    • Pėrez M & Hirschberg C (1986). Topography of glycosylation reactions in the rough endoplasmic reticulum membrane. Journal of Biological Chemistry, 261: 6822-6830.
    • (1986) Journal of Biological Chemistry , vol.261 , pp. 6822-6830
    • Perez, M.1    Hirschberg, C.2
  • 33
    • 0025905709 scopus 로고
    • A major proportion of N-glycoproteins are transiently glucosylated in the endoplasmic reticulum
    • Gan̄án S, Cazzulo JJ & Parodi AJ (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
    • Ganán, S.1    Cazzulo, J.J.2    Parodi, A.J.3
  • 35
    • 0029085605 scopus 로고
    • Retention of glucose residues added by the UDP-Glc:glycoprotein glucosyltransferase delays exit of glycoproteins from the endoplasmic reticulum
    • Labriola C, Cazzulo JJ & Parodi AJ (1995). Retention of glucose residues added by the UDP-Glc:glycoprotein glucosyltransferase delays exit of glycoproteins from the endoplasmic reticulum. Journal of Cell Biology, 130: 771-779.
    • (1995) Journal of Cell Biology , vol.130 , pp. 771-779
    • Labriola, C.1    Cazzulo, J.J.2    Parodi, A.J.3
  • 36
    • 0029126624 scopus 로고
    • The molecular basis for the recognition of misfolded glycoproteins by the UDP-Glc:glycoprotein glucosyltransferase
    • Sousa M & Parodi AJ (1995). The molecular basis for the recognition of misfolded glycoproteins by the UDP-Glc:glycoprotein glucosyltransferase. EMBO Journal, 14: 4196-4203.
    • (1995) EMBO Journal , vol.14 , pp. 4196-4203
    • Sousa, M.1    Parodi, A.J.2
  • 37
    • 0021485787 scopus 로고
    • Optimizing hydrolysis of N-linked high mannose oligosaccharides by endo-ß-N-acetylglucosaminidase H
    • Trimble RB & Maley F (1984). Optimizing hydrolysis of N-linked high mannose oligosaccharides by endo-ß-N-acetylglucosaminidase H. Analytical Biochemistry, 141: 515-522.
    • (1984) Analytical Biochemistry , vol.141 , pp. 515-522
    • Trimble, R.B.1    Maley, F.2
  • 38
    • 0028096754 scopus 로고
    • Mapping staphylococcal nuclease conformation using an EDTA-Fe derivative attached to genetically engineered cysteine residues
    • Ermacora MR, Ledman DW, Hellinga HW, Hsu GW & Fox RO (1994). Mapping staphylococcal nuclease conformation using an EDTA-Fe derivative attached to genetically engineered cysteine residues. Biochemistry, 33: 13625-13641.
    • (1994) Biochemistry , vol.33 , pp. 13625-13641
    • Ermacora, M.R.1    Ledman, D.W.2    Hellinga, H.W.3    Hsu, G.W.4    Fox, R.O.5
  • 39
    • 0024963569 scopus 로고
    • Residual structure in large fragments of staphylococcal nuclease: Effects of amino acid substitutions
    • Shortle DA & Meeker A (1989). Residual structure in large fragments of staphylococcal nuclease: effects of amino acid substitutions. Biochemistry, 28: 936-944.
    • (1989) Biochemistry , vol.28 , pp. 936-944
    • Shortle, D.A.1    Meeker, A.2
  • 41
    • 0028987945 scopus 로고
    • DrosophilaUDP-Glc:glycoprotein glucosyltransferase: Sequence and characterization of an enzyme that distinguishes between denatured and native proteins
    • Parker CG, Fessier LI, Nelson RE & Fessier JH (1995). DrosophilaUDP-Glc:glycoprotein glucosyltransferase: sequence and characterization of an enzyme that distinguishes between denatured and native proteins. EMBO Journal, 14: 1294-1303.
    • (1995) EMBO Journal , vol.14 , pp. 1294-1303
    • Parker, C.G.1    Fessier, L.I.2    Nelson, R.E.3    Fessier, J.H.4
  • 42
    • 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
    • Fernández F, Jannatipour M, Hellman U, Rokeach L & Parodi AJ (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 Journal, 15: 705-713.
    • (1996) EMBO Journal , vol.15 , pp. 705-713
    • Fernández, F.1    Jannatipour, M.2    Hellman, U.3    Rokeach, L.4    Parodi, A.J.5
  • 43
    • 0027184721 scopus 로고
    • Molecular chaperone functions of heat-shock proteins
    • Hendrick JP & Hartl FU (1993). Molecular chaperone functions of heat-shock proteins. Annual Review of Biochemistry, 62: 349-384.
    • (1993) Annual Review of Biochemistry , vol.62 , pp. 349-384
    • Hendrick, J.P.1    Hartl, F.U.2
  • 44
    • 0025339572 scopus 로고
    • The yeast KRE5 gene encodes a probable endoplasmic reticulum protein required for (1-6)-ß-D-glucan synthesis and normal cell growth
    • Meaden P, Hill K, Wagner J, Slipetz D, Sommer SS & Bussey H (1990). The yeast KRE5 gene encodes a probable endoplasmic reticulum protein required for (1-6)-ß-D-glucan synthesis and normal cell growth. Molecular and Cellular Biology, 10: 3013-3019.
    • (1990) Molecular and Cellular Biology , vol.10 , pp. 3013-3019
    • Meaden, P.1    Hill, K.2    Wagner, J.3    Slipetz, D.4    Sommer, S.S.5    Bussey, H.6
  • 45
    • 0028198111 scopus 로고
    • How N-linked oligosaccharides affect glycoprotein folding in the endoplasmic reticulum
    • Helenius A (1994). How N-linked oligosaccharides affect glycoprotein folding in the endoplasmic reticulum. Molecular Biology of the Cell. 5: 253-265
    • (1994) Molecular Biology of the Cell , vol.5 , pp. 253-265
    • Helenius, A.1
  • 46
    • 0023879525 scopus 로고
    • Vesicular stomatitis virus G proteins with altered glycosylation sites display temperature-sensitive intracellular transport and are subject to aberrant intermolecular disulfide bonding
    • Machamer CE & Rose JK (1988). Vesicular stomatitis virus G proteins with altered glycosylation sites display temperature-sensitive intracellular transport and are subject to aberrant intermolecular disulfide bonding. Journal of Biological Chemistry, 263: 5955-5960.
    • (1988) Journal of Biological Chemistry , vol.263 , pp. 5955-5960
    • Machamer, C.E.1    Rose, J.K.2
  • 47
    • 0027238117 scopus 로고
    • Role of conserved glycosylation sites in maturation and transport of influenza A virus hemagglutinin
    • Roberts PC, Garten W & Klenk HD (1993). Role of conserved glycosylation sites in maturation and transport of influenza A virus hemagglutinin. Journal of Virology, 67: 3048-3060.
    • (1993) Journal of Virology , vol.67 , pp. 3048-3060
    • Roberts, P.C.1    Garten, W.2    Klenk, H.D.3
  • 48
    • 0018083350 scopus 로고
    • Effect of tunicamycin on IgM, IgA and IgG secretion by mouse plasmacytoma cells
    • Hickman J & Kornfeld S (1978). Effect of tunicamycin on IgM, IgA and IgG secretion by mouse plasmacytoma cells. Journal of Immunology, 121: 990-996.
    • (1978) Journal of Immunology , vol.121 , pp. 990-996
    • Hickman, J.1    Kornfeld, S.2
  • 50
    • 0017944868 scopus 로고
    • Role of carbohydrates in protein secretion and turnover: Effect of tunicamycin on the major cell surface glycoprotein of chick embryo fibroblasts
    • Olden K, Pratt RM & Yamada KM (1978). Role of carbohydrates in protein secretion and turnover: effect of tunicamycin on the major cell surface glycoprotein of chick embryo fibroblasts. Cell, 13: 461-473.
    • (1978) Cell , vol.13 , pp. 461-473
    • Olden, K.1    Pratt, R.M.2    Yamada, K.M.3
  • 51
    • 0020701014 scopus 로고
    • Analysis of the oligosaccharides on the HLA-DR and DC-1 B cell antigens
    • Shackelford DA & Strominger JL (1983). Analysis of the oligosaccharides on the HLA-DR and DC-1 B cell antigens. Journal of Immunology, 130: 274-282.
    • (1983) Journal of Immunology , vol.130 , pp. 274-282
    • Shackelford, D.A.1    Strominger, J.L.2
  • 52
    • 0021930520 scopus 로고
    • Differential glycosylation requirements for the cell surface expression of class I molecules
    • Landolfi N, Rich R & Cook RG (1985). Differential glycosylation requirements for the cell surface expression of class I molecules. Journal of Immunology, 134: 423-430.
    • (1985) Journal of Immunology , vol.134 , pp. 423-430
    • Landolfi, N.1    Rich, R.2    Cook, R.G.3
  • 53
    • 0024379308 scopus 로고
    • A single amino acid substitution eliminates the stringent carbohydrate re-quirement for intracellular transport of a viral glycoprotein
    • Pitta AM, Rose JK & Machamer CE (1989). A single amino acid substitution eliminates the stringent carbohydrate re-quirement for intracellular transport of a viral glycoprotein. Journal of Virology, 63: 906-913.
    • (1989) Journal of Virology , vol.63 , pp. 906-913
    • Pitta, A.M.1    Rose, J.K.2    Machamer, C.E.3
  • 54
    • 0027217557 scopus 로고
    • A region of the C-terminal portion of the human transferrin receptor contains an aspar-agine-linked glycosylation site critical for receptor structure and function
    • Williams AM & Enns CA (1993). A region of the C-terminal portion of the human transferrin receptor contains an aspar-agine-linked glycosylation site critical for receptor structure and function. Journal of Biological Chemistry, 268: 12780-12786.
    • (1993) Journal of Biological Chemistry , vol.268 , pp. 12780-12786
    • Williams, A.M.1    Enns, C.A.2
  • 55
    • 0027288659 scopus 로고
    • The role of glycosylation and phosphory-lation in the expression of active human ß-glucuronidase
    • Shipley JM, Grubb JH & Sly WS (1993). The role of glycosylation and phosphory-lation in the expression of active human ß-glucuronidase. Journal of Biological Chemistry, 268: 12193-12198.
    • (1993) Journal of Biological Chemistry , vol.268 , pp. 12193-12198
    • Shipley, J.M.1    Grubb, J.H.2    Sly, W.S.3
  • 56
    • 0023906050 scopus 로고
    • Influ-ence of new glycosylation sites on ex-pression of the vesicular stomatitis virus G protein at the plasma membrane
    • Machamer CE & Rose JK (1988). Influ-ence of new glycosylation sites on ex-pression of the vesicular stomatitis virus G protein at the plasma membrane. Journal of Biological Chemistry, 263: 5948-5954.
    • (1988) Journal of Biological Chemistry , vol.263 , pp. 5948-5954
    • Machamer, C.E.1    Rose, J.K.2
  • 57
    • 0022236656 scopus 로고
    • A single N-linked oligosaccharide at either of the two normal sites is sufficient for transport of vesicular stomatitis virus G protein to the cell surface
    • Machamer CE, Florkiewicz RZ & Rose JK (1985). A single N-linked oligosaccharide at either of the two normal sites is sufficient for transport of vesicular stomatitis virus G protein to the cell surface. Molecular and Cellular Biology, 5: 3074-3083.
    • (1985) Molecular and Cellular Biology , vol.5 , pp. 3074-3083
    • Machamer, C.E.1    Florkiewicz, R.Z.2    Rose, J.K.3
  • 58
    • 0026022577 scopus 로고
    • Participation of a novel 88-kDa protein in the biogenesis of murine class I histocompatibility molecules
    • Degen E & Williams DB (1991). Participation of a novel 88-kDa protein in the biogenesis of murine class I histocompatibility molecules. Journal of Cell Biology, 112: 1099-1115.
    • (1991) Journal of Cell Biology , vol.112 , pp. 1099-1115
    • Degen, E.1    Williams, D.B.2
  • 59
    • 0027156495 scopus 로고
    • Interaction with newly synthesized and retained proteins in the endoplasmic reticulum suggests a chaperone function for human integral membrane protein 190 (calnexin)
    • David V, Hochstenbach F, Rajagopalan S & Brenner MB (1993). Interaction with newly synthesized and retained proteins in the endoplasmic reticulum suggests a chaperone function for human integral membrane protein 190 (calnexin). Journal of Biological Chemistry, 268: 9585-9592.
    • (1993) Journal of Biological Chemistry , vol.268 , pp. 9585-9592
    • David, V.1    Hochstenbach, F.2    Rajagopalan, S.3    Brenner, M.B.4
  • 61
    • 0027295871 scopus 로고
    • Association of folding intermediates of glycoproteins with calnexin during protein maturation
    • Ou WJ, Cameron PH, Thomas DY & Bergeron JJM (1993). Association of folding intermediates of glycoproteins with calnexin during protein maturation. Nature, 364: 771-776.
    • (1993) Nature , vol.364 , pp. 771-776
    • Ou, W.J.1    Cameron, P.H.2    Thomas, D.Y.3    Bergeron, J.J.M.4
  • 62
    • 0028103695 scopus 로고
    • Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control
    • Hammond C, Braakman I & Helenius A (1994). Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control. Proceedings of the National A-cademy of Sciences, USA, 91: 913-917.
    • (1994) Proceedings of the National A-cademy of Sciences, USA , vol.91 , pp. 913-917
    • Hammond, C.1    Braakman, I.2    Helenius, A.3
  • 63
    • 0030449989 scopus 로고    scopus 로고
    • N-linked oligosaccharides are necessary and sufficient for association of glycosylated forms of bovine RNase with calnexin and calreticulin
    • Rodan AR, Simons JF, Trombetta ES & Helenius A (1996). N-linked oligosaccharides are necessary and sufficient for association of glycosylated forms of bovine RNase with calnexin and calreticulin. EMBO Journal, 15: 6921-6930.
    • (1996) EMBO Journal , vol.15 , pp. 6921-6930
    • Rodan, A.R.1    Simons, J.F.2    Trombetta, E.S.3    Helenius, A.4
  • 67
    • 0029934119 scopus 로고    scopus 로고
    • Calnexin and calreticulin promote folding, delay oligomerization and suppress degradation of influenza hemagglutinin in microsomes
    • Hebert DN, Foellmer B & Helenius A (1996). Calnexin and calreticulin promote folding, delay oligomerization and suppress degradation of influenza hemagglutinin in microsomes. EMBO Journal. 15: 2961-2968.
    • (1996) EMBO Journal , vol.15 , pp. 2961-2968
    • Hebert, D.N.1    Foellmer, B.2    Helenius, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.