메뉴 건너뛰기




Volumn 8, Issue 10, 1997, Pages 1943-1954

Quality control in the secretory pathway: The role of calreticulin, calnexin and BiP in the retention of glycoproteins with C-terminal truncations

Author keywords

[No Author keywords available]

Indexed keywords

CALNEXIN; CALRETICULIN; CELL PROTEIN; GLYCOPROTEIN; HEAT SHOCK PROTEIN 70; VIRUS HEMAGGLUTININ;

EID: 0030881717     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.8.10.1943     Document Type: Article
Times cited : (172)

References (59)
  • 2
    • 0026604334 scopus 로고
    • Manipulating disulfide bond formation and protein folding in the endoplasmic reticulum
    • Braakman, I., Helenius, J., and Helenius, A. (1992). Manipulating disulfide bond formation and protein folding in the endoplasmic reticulum. EMBO J., 11, 1717-1722.
    • (1992) EMBO J. , vol.11 , pp. 1717-1722
    • Braakman, I.1    Helenius, J.2    Helenius, A.3
  • 3
    • 0025816663 scopus 로고
    • Folding of influenza hemagglutinin in the endoplasmic reticulum
    • Braakman, I., Hoover-Litty, H., Wagner, K.R., and Helenius, A. (1991). Folding of influenza hemagglutinin in the endoplasmic reticulum. J. Cell Biol. 114, 401-411.
    • (1991) J. Cell Biol. , vol.114 , pp. 401-411
    • Braakman, I.1    Hoover-Litty, H.2    Wagner, K.R.3    Helenius, A.4
  • 4
    • 0028023726 scopus 로고
    • Structure of influenza haemagglutinin at the pH of membrane fusion
    • Bullough, P.A., Hughson, F.M., Skehel, J.J., and Wiley, D.C. (1994). Structure of influenza haemagglutinin at the pH of membrane fusion. Nature 371, 37-43.
    • (1994) Nature , vol.371 , pp. 37-43
    • Bullough, P.A.1    Hughson, F.M.2    Skehel, J.J.3    Wiley, D.C.4
  • 5
    • 0027253445 scopus 로고
    • A spring-loaded mechanism for the conformational change of influenza hemagglutinin
    • Carr, C.M., and Kim, P.S. (1993). A spring-loaded mechanism for the conformational change of influenza hemagglutinin. Cell 73, 823-832.
    • (1993) Cell , vol.73 , pp. 823-832
    • Carr, C.M.1    Kim, P.S.2
  • 6
    • 0029558245 scopus 로고
    • A soluble domain of the membrane-anchoring chain of influenza virus hemagglutinin (HA2) folds in Escherichia coli into the low-pH-induced conformation
    • Chen, J., Wharton, S.A., Weissenhorn, W., Calder, L.J., Hughson, F.M., Skehel, J.J., and Wiley, D.C. (1995a). A soluble domain of the membrane-anchoring chain of influenza virus hemagglutinin (HA2) folds in Escherichia coli into the low-pH-induced conformation. Proc. Natl. Acad. Sci. USA 92, 12205-12209.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 12205-12209
    • Chen, J.1    Wharton, S.A.2    Weissenhorn, W.3    Calder, L.J.4    Hughson, F.M.5    Skehel, J.J.6    Wiley, D.C.7
  • 7
    • 0029049090 scopus 로고
    • Cotranslational folding and calnexin binding of influenza hemagglutinin in the endoplasmic reticulum
    • Chen, W., Helenius, J., Braakman, I., and Helenius, A. (1995b). Cotranslational folding and calnexin binding of influenza hemagglutinin in the endoplasmic reticulum. Proc. Natl. Acad. Sci. USA 92, 6229-6233.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 6229-6233
    • Chen, W.1    Helenius, J.2    Braakman, I.3    Helenius, A.4
  • 8
    • 0025242929 scopus 로고
    • Defective intracellular transport and processing of CFTR is the molecular basis of most cystic fibrosis
    • Cheng, S.H., Gregory, R.J., Marshall, J., Palu, S., Souza, D.W., White, G.A., O'Riordian, C.R., and Smith, A.E. (1990). Defective intracellular transport and processing of CFTR is the molecular basis of most cystic fibrosis. Cell 63, 827-834.
    • (1990) Cell , vol.63 , pp. 827-834
    • Cheng, S.H.1    Gregory, R.J.2    Marshall, J.3    Palu, S.4    Souza, D.W.5    White, G.A.6    O'Riordian, C.R.7    Smith, A.E.8
  • 9
    • 0023006195 scopus 로고
    • Assembly of influenza hemagglutinin trimers and its role in intracellular transport
    • Copeland, C.S., Doms, R.W., Bolzau, E.M., Webster, R.G., and Helenius, A. (1986). Assembly of influenza hemagglutinin trimers and its role in intracellular transport. J. Cell Biol. 103, 1179-1191.
    • (1986) J. Cell Biol. , vol.103 , pp. 1179-1191
    • Copeland, C.S.1    Doms, R.W.2    Bolzau, E.M.3    Webster, R.G.4    Helenius, A.5
  • 10
    • 0020955303 scopus 로고
    • Analyses of antigenicity of influenza hemagglutinin at the pH optimum for virus-mediated membrane fusion
    • Daniels, R.S., Douglas, A.R., Skehel, J.J., and Wiley, D.C. (1983). Analyses of antigenicity of influenza hemagglutinin at the pH optimum for virus-mediated membrane fusion. J. Gen. Virol. 64, 1657-1662.
    • (1983) J. Gen. Virol. , vol.64 , pp. 1657-1662
    • Daniels, R.S.1    Douglas, A.R.2    Skehel, J.J.3    Wiley, D.C.4
  • 12
    • 0021879568 scopus 로고
    • An efficient method for introducing macromolecules into living cells
    • Doxsey, S.J., Sambrook, J., Helenius, A., and White, J. (1985). An efficient method for introducing macromolecules into living cells. J. Cell Biol. 101, 19-27.
    • (1985) J. Cell Biol. , vol.101 , pp. 19-27
    • Doxsey, S.J.1    Sambrook, J.2    Helenius, A.3    White, J.4
  • 13
    • 0027440769 scopus 로고
    • Quality control of ER synthesized proteins: An exposed thiol group as a three-way switch mediating assembly, retention and degradation
    • Fra, A.M., Fagioli, C., Finazzi, D., Sitia, R., and Alberini, C.M. (1993). Quality control of ER synthesized proteins: an exposed thiol group as a three-way switch mediating assembly, retention and degradation. EMBO J. 12, 4755-4761.
    • (1993) EMBO J. , vol.12 , pp. 4755-4761
    • Fra, A.M.1    Fagioli, C.2    Finazzi, D.3    Sitia, R.4    Alberini, C.M.5
  • 14
    • 0022552149 scopus 로고
    • Expression of wild-type and mutant forms of Influenza hemagglutinin: The role of folding in intracellular transport
    • Gething, M.-J., K. McCammon, and Sambrook, J. (1986). Expression of wild-type and mutant forms of Influenza hemagglutinin: the role of folding in intracellular transport. Cell 46, 939-950.
    • (1986) Cell , vol.46 , pp. 939-950
    • Gething, M.-J.1    McCammon, K.2    Sambrook, J.3
  • 15
    • 0020381457 scopus 로고
    • Construction of influenza haemagglutinin genes that code for intracellular and secreted forms of the protein
    • Gething, M.-J., and Sambrook, J. (1982). Construction of influenza haemagglutinin genes that code for intracellular and secreted forms of the protein. Nature 300, 598-603.
    • (1982) Nature , vol.300 , pp. 598-603
    • Gething, M.-J.1    Sambrook, J.2
  • 16
    • 0026584271 scopus 로고
    • Protein folding in the cell
    • Gething, M.-J., and Sambrook, J. (1992). Protein folding in the cell. Nature 355, 33-45.
    • (1992) Nature , vol.355 , pp. 33-45
    • Gething, M.-J.1    Sambrook, J.2
  • 17
    • 0029984570 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport
    • Gorlich, D., and Mattaj, I.W. (1996). Nucleocytoplasmic transport. Science 271, 1513-1518.
    • (1996) Science , vol.271 , pp. 1513-1518
    • Gorlich, D.1    Mattaj, I.W.2
  • 18
    • 0020626189 scopus 로고
    • Preparation of influenza subviral particles lacking the HA1 subunit of hemagglutinin: Unmasking of cross-reactive determinants
    • Graves, P.N., Schulman, L., Young, J.F., and Palese, P. (1983). Preparation of influenza subviral particles lacking the HA1 subunit of hemagglutinin: unmasking of cross-reactive determinants. Virology 126, 106-119.
    • (1983) Virology , vol.126 , pp. 106-119
    • Graves, P.N.1    Schulman, L.2    Young, J.F.3    Palese, P.4
  • 19
    • 0023839303 scopus 로고
    • The mannose 6-phosphate receptor and the biogenesis of lysosomes
    • Griffiths, G., Hoflack, B., Simons, K., Mellman, I., and Kornfeld, S. (1988). The mannose 6-phosphate receptor and the biogenesis of lysosomes. Cell 52, 329-341.
    • (1988) Cell , vol.52 , pp. 329-341
    • Griffiths, G.1    Hoflack, B.2    Simons, K.3    Mellman, I.4    Kornfeld, S.5
  • 20
    • 0028168233 scopus 로고
    • The efficiency of cystein-mediated intracellular retention determines the differential fate of secretory IgA and IgM in B and plasma cells
    • Guenzi, S., Fra, A., Sparvoli, A., Rocco, M., and Sitia, R. (1994). The efficiency of cystein-mediated intracellular retention determines the differential fate of secretory IgA and IgM in B and plasma cells. Eur. J. Immunol. 24, 2477-2482.
    • (1994) Eur. J. Immunol. , vol.24 , pp. 2477-2482
    • Guenzi, S.1    Fra, A.2    Sparvoli, A.3    Rocco, M.4    Sitia, R.5
  • 21
    • 0028103695 scopus 로고
    • Role of N-linked oligosaccharides, glucose trimming and calnexin during glycoprotein folding in the endoplasmic reticulum
    • Hammond, C., Braakman, I., and Helenius, A. (1994). Role of N-linked oligosaccharides, glucose trimming and calnexin during glycoprotein folding in the endoplasmic reticulum. Proc. Natl. Acad. Sci. USA 91, 913-917.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 913-917
    • Hammond, C.1    Braakman, I.2    Helenius, A.3
  • 22
    • 0027141852 scopus 로고
    • A chaperone with a sweet tooth
    • Hammond, C., and Helenius, A. (1993). A chaperone with a sweet tooth. Curr. Biol. 3, 884-885.
    • (1993) Curr. Biol. , vol.3 , pp. 884-885
    • Hammond, C.1    Helenius, A.2
  • 23
    • 0028076031 scopus 로고
    • Folding of VSV G protein: Sequential interaction with BiP and calnexin
    • Hammond, C., and Helenius, A. (1994a). Folding of VSV G protein: sequential interaction with BiP and calnexin. Science 266, 456-458.
    • (1994) Science , vol.266 , pp. 456-458
    • Hammond, C.1    Helenius, A.2
  • 24
    • 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
    • Hammond, C., and Helenius, A. (1994b). 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
  • 25
    • 0029094253 scopus 로고
    • Quality control in the secretory pathway
    • Hammond, C., and Helenius, A. (1995). Quality control in the secretory pathway. Curr. Opin. Cell Biol. 7, 523-529.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 523-529
    • Hammond, C.1    Helenius, A.2
  • 26
    • 0029024748 scopus 로고
    • Glucose trimming and reglucosylation determines glycoprotein association with calnexin
    • Hebert, D.N., Foellmer, B., and Helenius, A. (1995). Glucose trimming and reglucosylation determines glycoprotein association with calnexin. Cell 81, 425-433.
    • (1995) Cell , vol.81 , pp. 425-433
    • Hebert, D.N.1    Foellmer, B.2    Helenius, A.3
  • 27
    • 0029934119 scopus 로고    scopus 로고
    • Calnexin and calreticulin promote folding, delay oligomerization and suppress degradation of influenza hemagglutinin in microsomes
    • Hebert, D.N., Foellmer, B., and Helenius, A. (1996). Calnexin and calreticulin promote folding, delay oligomerization 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
  • 29
    • 0024400060 scopus 로고
    • Interactions of misfolded Influenza hemagglutinin with binding protein (BiP)
    • Hurtley, S.M., Bole, D.G., Hoover-Litty, H., Helenius, A., and Copeland, C.S. (1989). Interactions of misfolded Influenza 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
  • 30
    • 0024461745 scopus 로고
    • Protein oligomerization in the endoplasmic reticulum
    • 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
  • 31
    • 0024751077 scopus 로고
    • Architectural editing: Determining the fate of newly synthesized membrane proteins
    • Klausner, R.D. 1989. Architectural editing: determining the fate of newly synthesized membrane proteins. New Biol. 1, 3-8.
    • (1989) New Biol. , vol.1 , pp. 3-8
    • Klausner, R.D.1
  • 32
    • 0023838784 scopus 로고
    • Transport of secretory and membrane glycoproteins from the rough endoplasmic reticulum to Golgi
    • Lodish, H.F. 1988. Transport of secretory and membrane glycoproteins from the rough endoplasmic reticulum to Golgi. J. Biol. Chem. 263, 2107-2110.
    • (1988) J. Biol. Chem. , vol.263 , pp. 2107-2110
    • Lodish, H.F.1
  • 33
    • 0000603264 scopus 로고
    • Puromycin inhibition of protein synthesis: Incorporation of puromycin into peptide chains
    • Nathans, D. (1964). Puromycin inhibition of protein synthesis: incorporation of puromycin into peptide chains. Proc. Natl. Acad. Sci. USA 51, 585-592.
    • (1964) Proc. Natl. Acad. Sci. USA , vol.51 , pp. 585-592
    • Nathans, D.1
  • 34
    • 0024314706 scopus 로고
    • Short cytoplasmic sequences serve as retention signals for transmembrane proteins in the endoplasmic reticulum
    • Nilsson, T., Jackson, M., and Peterson, P.A. (1989). Short cytoplasmic sequences serve as retention signals for transmembrane proteins in the endoplasmic reticulum. Cell 58, 707-718.
    • (1989) Cell , vol.58 , pp. 707-718
    • Nilsson, T.1    Jackson, M.2    Peterson, P.A.3
  • 35
    • 0027295871 scopus 로고
    • Association of folding intermediates of glycoproteins with calnexin during protein maturation
    • 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 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
  • 36
    • 0024427039 scopus 로고
    • Control of protein exit from the endoplasmic reticulum
    • Pelham, H.R.B. (1989). Control of protein exit from the endoplasmic reticulum. Annu. Rev. Cell Biol. 5, 1-23.
    • (1989) Annu. Rev. Cell Biol. , vol.5 , pp. 1-23
    • Pelham, H.R.B.1
  • 37
    • 0029160540 scopus 로고
    • Transient, lectin-like association of calreticulin with folding intermediates of cellular viral glycoproteins
    • Peterson, J.R., Ora, A., Nguyen Van' P., and Helenius, A. (1995). Transient, lectin-like association of calreticulin with folding intermediates of cellular viral glycoproteins. Mol. Biol. Cell 6, 1173-1184.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1173-1184
    • Peterson, J.R.1    Ora, A.2    Nguyen Van', P.3    Helenius, A.4
  • 38
    • 0023077578 scopus 로고
    • Biosynthetic protein transport and sorting by endoplasmic reticulum and the Golgi
    • Pfeffer, S.R., and Rothman, J.E. (1987). Biosynthetic protein transport and sorting by endoplasmic reticulum and the Golgi. Annu. Rev. Biochem. 56, 829-852.
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 829-852
    • Pfeffer, S.R.1    Rothman, J.E.2
  • 39
    • 0028147528 scopus 로고
    • Retention of unassembled components of integral membrane proteins by calnexin
    • Rajagopalan, S., Xu, Y., and Brenner, M.B. (1994). Retention of unassembled components of integral membrane proteins by calnexin. Science 263, 387-390.
    • (1994) Science , vol.263 , pp. 387-390
    • Rajagopalan, S.1    Xu, Y.2    Brenner, M.B.3
  • 40
    • 0013936848 scopus 로고
    • Vectorial discharge of peptides released by puromycin from attached ribosomes
    • Redman, C.M., and Sabatini, D.D. (1966). Vectorial discharge of peptides released by puromycin from attached ribosomes. Proc. Natl. Acad. Sci. USA 56, 608-615.
    • (1966) Proc. Natl. Acad. Sci. USA , vol.56 , pp. 608-615
    • Redman, C.M.1    Sabatini, D.D.2
  • 41
    • 0017429069 scopus 로고
    • Areas, volumes, packing and protein structure
    • Richards, F.M. 1977. Areas, volumes, packing and protein structure. Annu. Rev. Biophys. Bioeng. 6, 151-176.
    • (1977) Annu. Rev. Biophys. Bioeng. , vol.6 , pp. 151-176
    • Richards, F.M.1
  • 42
    • 0030449989 scopus 로고    scopus 로고
    • N-linked oligosaccharides are necessary and sufficient for association of RNase B with calnexin and calreticulin
    • Rodan, A.R., Simons, J.F., Trombetta, E.S., and Helenius, A. (1996). N-linked oligosaccharides are necessary and sufficient for association of RNase B 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
  • 43
    • 0024149621 scopus 로고
    • Regulation of protein export from the endoplasmic reticulum
    • Rose, J.K., and Doms, R.W. (1988). Regulation of protein export from the endoplasmic reticulum. Annu. Rev. Cell Biol. 4, 257-288.
    • (1988) Annu. Rev. Cell Biol. , vol.4 , pp. 257-288
    • Rose, J.K.1    Doms, R.W.2
  • 44
    • 0029979607 scopus 로고    scopus 로고
    • Common principles of protein translocation across membranes
    • Schatz, G., and Dobberstein, B. (1996). Common principles of protein translocation across membranes. Science 271, 1519-1526.
    • (1996) Science , vol.271 , pp. 1519-1526
    • Schatz, G.1    Dobberstein, B.2
  • 45
    • 0026774570 scopus 로고
    • Molecular biology and genetics of alpha-1-antitrypsin deficiency
    • Sifers, R.N., Finegold, M.J., and Woo, S.L.C. (1992). Molecular biology and genetics of alpha-1-antitrypsin deficiency. Semin. Liver Dis. 12, 301-310.
    • (1992) Semin. Liver Dis. , vol.12 , pp. 301-310
    • Sifers, R.N.1    Finegold, M.J.2    Woo, S.L.C.3
  • 46
    • 0025037651 scopus 로고
    • Intracellular transport of soluble and membrane-bound glycoproteins: Folding, assembly and secretion of anchor-free influenza hemagglutinin
    • Singh, I., Doms, R.W., Wagner, K.R., and Helenius, A. (1990). Intracellular transport of soluble and membrane-bound glycoproteins: folding, assembly and secretion of anchor-free influenza hemagglutinin. EMBO J. 9, 631-639.
    • (1990) EMBO J. , vol.9 , pp. 631-639
    • Singh, I.1    Doms, R.W.2    Wagner, K.R.3    Helenius, A.4
  • 47
    • 0025230696 scopus 로고
    • Developmental regulation of IgM secretion: The role of the carboxy-terminal cysteine
    • Sitia, R., Neuberger, M., Alberini, C., Bet, P., Fra, A., Valetti, C., Williams, G., and Milstein, C. (1990). Developmental regulation of IgM secretion: the role of the carboxy-terminal cysteine. Cell 60, 781-790.
    • (1990) Cell , vol.60 , pp. 781-790
    • Sitia, R.1    Neuberger, M.2    Alberini, C.3    Bet, P.4    Fra, A.5    Valetti, C.6    Williams, G.7    Milstein, C.8
  • 48
    • 0019420560 scopus 로고
    • Very low density lipoprotein synthesis and secretion. Extrusion of apoprotein B nascent chains through the membrane of the endoplasmic reticulum without protein synthesis
    • Siuta-Mangano, P., and Lane, M.D. (1981). Very low density lipoprotein synthesis and secretion. Extrusion of apoprotein B nascent chains through the membrane of the endoplasmic reticulum without protein synthesis. J. Biol. Chem. 256, 2094-2097.
    • (1981) J. Biol. Chem. , vol.256 , pp. 2094-2097
    • Siuta-Mangano, P.1    Lane, M.D.2
  • 49
    • 0026500202 scopus 로고
    • Recognition of the oligosaccharide and protein moities of glycoproteins by the UDP-Glc:glycoprotein glucosyltransferase
    • Sousa, M.C., Ferrero-Garcia M.A., and Parodi, A.J. (1992). Recognition of the oligosaccharide and protein moities of glycoproteins by the UDP-Glc:glycoprotein glucosyltransferase. Biochemistry 31, 97-105.
    • (1992) Biochemistry , vol.31 , pp. 97-105
    • Sousa, M.C.1    Ferrero-Garcia, M.A.2    Parodi, A.J.3
  • 50
    • 0027174340 scopus 로고
    • Membrane glycoprotein folding, oligomerization and intracellular transport: Effects of dithiothreitol in living cells
    • Tatu, U., Braakman, I., and Helenius, A. (1993). Membrane glycoprotein folding, oligomerization and intracellular transport: effects of dithiothreitol in living cells. EMBO J. 12, 2151-2157.
    • (1993) EMBO J. , vol.12 , pp. 2151-2157
    • Tatu, U.1    Braakman, I.2    Helenius, A.3
  • 51
    • 0028906029 scopus 로고
    • Folding and oligomerization of influenza hemagglutinin in the ER and the intermediate compartment
    • Tatu, U., Hammond, C., and Helenius, A. (1995). Folding and oligomerization of influenza hemagglutinin in the ER and the intermediate compartment. EMBO J. 14, 1340-1348.
    • (1995) EMBO J. , vol.14 , pp. 1340-1348
    • Tatu, U.1    Hammond, C.2    Helenius, A.3
  • 52
    • 0024400243 scopus 로고
    • Condensation-sorting events in the rough endoplasmic reticulum of exocrine pancreatic cells
    • Tooze, J., Kern, H.F., Fuller, S.D., and Howell, K.E. (1989). Condensation-sorting events in the rough endoplasmic reticulum of exocrine pancreatic cells. J. Cell Biol. 109, 35-50.
    • (1989) J. Cell Biol. , vol.109 , pp. 35-50
    • Tooze, J.1    Kern, H.F.2    Fuller, S.D.3    Howell, K.E.4
  • 53
    • 0026799435 scopus 로고
    • Purification to apparent homogeneity and partial characterization of rat liver UDP-glucose: Glycoprotein glucosyltransferase
    • Trombetta, S.E., and Parodi, A.J. (1992). Purification to apparent homogeneity and partial characterization of rat liver UDP-glucose: glycoprotein glucosyltransferase. J. Biol. Chem. 267, 9236-9240.
    • (1992) J. Biol. Chem. , vol.267 , pp. 9236-9240
    • Trombetta, S.E.1    Parodi, A.J.2
  • 54
    • 0021764898 scopus 로고
    • Translation is a non-uniform process. Effect of tRNA availability on the rate of elongation of nascent polypeptide chains
    • Varenne, S., Buc, J., Lloubes, R., and Lazdunski, C. (1984). Translation is a non-uniform process. Effect of tRNA availability on the rate of elongation of nascent polypeptide chains. J. Mol. Biol. 180, 549-576.
    • (1984) J. Mol. Biol. , vol.180 , pp. 549-576
    • Varenne, S.1    Buc, J.2    Lloubes, R.3    Lazdunski, C.4
  • 55
    • 0029925940 scopus 로고    scopus 로고
    • The molecular chaperone calnexin facilitates folding and assembly of class I histocompatibility molecules
    • Vassilakos, A., M.F. Cohen-Doyle, 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
  • 57
    • 0023082135 scopus 로고
    • The structure and function of the hemagglutinin membrane glycoprotein of influenza virus
    • Wiley, D.C., and Skehel, J.J. (1987). The structure and function of the hemagglutinin membrane glycoprotein of influenza virus. Annu. Rev. Biochem. 56, 365-395.
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 365-395
    • Wiley, D.C.1    Skehel, J.J.2
  • 58
    • 0024117032 scopus 로고
    • Ribosome pausing and stacking during translation of a eukariotic mRNA
    • Wolin, S.L., and Walter, P. (1988). Ribosome pausing and stacking during translation of a eukariotic mRNA. EMBO J. 7, 3559-3569.
    • (1988) EMBO J. , vol.7 , pp. 3559-3569
    • Wolin, S.L.1    Walter, P.2
  • 59
    • 0030933129 scopus 로고    scopus 로고
    • Conformation independent binding of monoglucosylated ribonuclease B to calnexin
    • Zapun, A., Petrescu, S.M., Rudd, P.M., Dwek, R.A., Thomas, D.Y., and Bergeron, J.J.M. (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.M.2    Rudd, P.M.3    Dwek, R.A.4    Thomas, D.Y.5    Bergeron, J.J.M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.