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Volumn 72, Issue 5, 1998, Pages 3851-3858

Involvement of endoplasmic reticulum chaperones in the folding of hepatitis C virus glycoproteins

Author keywords

[No Author keywords available]

Indexed keywords

CALNEXIN; CALRETICULIN; CHAPERONE; TUNICAMYCIN; VIRUS GLYCOPROTEIN;

EID: 0031957011     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/jvi.72.5.3851-3858.1998     Document Type: Article
Times cited : (162)

References (66)
  • 2
    • 15844379984 scopus 로고    scopus 로고
    • Glycan-dependent and -independent association of vesicular stomatitis virus G protein with calnexin
    • Cannon, K. S., D. N. Hebert, and A. Helenius. 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
  • 3
    • 0018700703 scopus 로고
    • Fluorographic detection of radioactivity in polyacrylamide gels with the water-soluble fluor, sodium salicylate
    • Chamberlain, J. P. 1979. Fluorographic detection of radioactivity in polyacrylamide gels with the water-soluble fluor, sodium salicylate. Anal. Biochem. 98:132-135.
    • (1979) Anal. Biochem. , vol.98 , pp. 132-135
    • Chamberlain, J.P.1
  • 4
    • 0024509701 scopus 로고
    • Isolation of a cDNA clone derived from a blood-borne non-A, non-B viral hepatitis genome
    • Choo, Q.-L., G. Kuo, A. J. Weiner, L. R. Overby, D. W. Bradley, and M. Houghton. 1989. Isolation of a cDNA clone derived from a blood-borne non-A, non-B viral hepatitis genome. Science 244:359-362.
    • (1989) Science , vol.244 , pp. 359-362
    • Choo, Q.-L.1    Kuo, G.2    Weiner, A.J.3    Overby, L.R.4    Bradley, D.W.5    Houghton, M.6
  • 5
    • 0031911782 scopus 로고    scopus 로고
    • A retention signal necessary and sufficient for endoplasmic reticulum localization maps to the transmembrane domain of hepatitis C virus glycoprotein E2
    • Cocquerel, L., J.-C. Meunier, A. Pillez, C. Wychowski, and J. Dubuisson. 1998. A retention signal necessary and sufficient for endoplasmic reticulum localization maps to the transmembrane domain of hepatitis C virus glycoprotein E2. J. Virol. 72:2183-2191.
    • (1998) J. Virol. , vol.72 , pp. 2183-2191
    • Cocquerel, L.1    Meunier, J.-C.2    Pillez, A.3    Wychowski, C.4    Dubuisson, J.5
  • 7
    • 0023708177 scopus 로고
    • Reduction of endogenous GRP78 levels improves secretion of a heterologous protein in CHO cells
    • Dorner, A. J., M. G. Krane, and R. J. Kaufman. 1988. Reduction of endogenous GRP78 levels improves secretion of a heterologous protein in CHO cells. Mol. Cell. Biol. 8:4063-4070.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 4063-4070
    • Dorner, A.J.1    Krane, M.G.2    Kaufman, R.J.3
  • 8
    • 0026511824 scopus 로고
    • Overexpression of GRP78 mitigates stress induction of glucose regulated protein and blocks secretion of selective proteins in Chinese hamster ovary cells
    • Dorner, A. J., L. C. Wasley, and R. J. Kaufman. 1992. Overexpression of GRP78 mitigates stress induction of glucose regulated protein and blocks secretion of selective proteins in Chinese hamster ovary cells. EMBO J. 11:1563-1572.
    • (1992) EMBO J. , vol.11 , pp. 1563-1572
    • Dorner, A.J.1    Wasley, L.C.2    Kaufman, R.J.3
  • 9
    • 0020045092 scopus 로고
    • Complementation and genetic linkage between vaccinia virus temperature-sensitive mutants
    • Drillien, R., D. Spehner, and A. Kirn. 1982. Complementation and genetic linkage between vaccinia virus temperature-sensitive mutants. Virology 119: 372-381.
    • (1982) Virology , vol.119 , pp. 372-381
    • Drillien, R.1    Spehner, D.2    Kirn, A.3
  • 10
    • 0028021952 scopus 로고
    • Formation and intracellular localization of hepatitis C virus envelope glycoprotein complexes expressed by recombinant vaccinia and Sindbis viruses
    • Dubuisson, J., H. H. Hsu, R. C. Cheung, H. B. Greenberg, D. G. Russell, and C. M. Rice. 1994. Formation and intracellular localization of hepatitis C virus envelope glycoprotein complexes expressed by recombinant vaccinia and Sindbis viruses. J. Virol. 68:6147-6160.
    • (1994) J. Virol. , vol.68 , pp. 6147-6160
    • Dubuisson, J.1    Hsu, H.H.2    Cheung, R.C.3    Greenberg, H.B.4    Russell, D.G.5    Rice, C.M.6
  • 12
    • 0030030042 scopus 로고    scopus 로고
    • Hepatitis C virus glycoprotein folding: Disulfide bond formation and association with calnexin
    • Dubuisson, J., and C. M. Rice. 1996. Hepatitis C virus glycoprotein folding: disulfide bond formation and association with calnexin. J. Virol. 70:778-786.
    • (1996) J. Virol. , vol.70 , pp. 778-786
    • Dubuisson, J.1    Rice, C.M.2
  • 13
    • 0026029621 scopus 로고
    • Folding, interaction with GRP78-BiP, assembly, and transport of the human immunodeficiency virus type 1 envelope protein
    • Earl, P. L., B. Moss, and R. W. Doms. 1991. Folding, interaction with GRP78-BiP, assembly, and transport of the human immunodeficiency virus type 1 envelope protein. J. Virol. 65:2047-2055.
    • (1991) J. Virol. , vol.65 , pp. 2047-2055
    • Earl, P.L.1    Moss, B.2    Doms, R.W.3
  • 14
    • 0024819297 scopus 로고
    • Molecular cloning of the high affinity calcium-binding protein (calreticulin) of skeletal muscle sarcoplasmic reticulum
    • Fliegei, L., B. Kimberly, D. H. MacLennan, R. A. F. Reithmeier, and M. Michalak. 1989. Molecular cloning of the high affinity calcium-binding protein (calreticulin) of skeletal muscle sarcoplasmic reticulum. J. Biol. Chem. 264:21522-21528.
    • (1989) J. Biol. Chem. , vol.264 , pp. 21522-21528
    • Fliegei, L.1    Kimberly, B.2    MacLennan, D.H.3    Reithmeier, R.A.F.4    Michalak, M.5
  • 15
    • 0029897920 scopus 로고    scopus 로고
    • Processing of the E1 glycoprotein of hepatitis C virus expressed in mammalian cells
    • Fournillier-Jacob, A., A. Cahour, N. Escriou, M. Girard, and C. Wychowski. 1996. Processing of the E1 glycoprotein of hepatitis C virus expressed in mammalian cells. J. Gen. Virol. 77:1055-1064.
    • (1996) J. Gen. Virol. , vol.77 , pp. 1055-1064
    • Fournillier-Jacob, A.1    Cahour, A.2    Escriou, N.3    Girard, M.4    Wychowski, C.5
  • 16
    • 0000357440 scopus 로고
    • Classification and nomenclature of viruses. Fifth report of the International Committee on Taxonomy of Viruses
    • Francki, R. I. B., C. M. Fauquet, D. L. Knudson, and F. Brown. 1991. Classification and nomenclature of viruses. Fifth report of the International Committee on Taxonomy of Viruses. Arch. Virol. 2 (Suppl):223.
    • (1991) Arch. Virol. , vol.2 , Issue.SUPPL. , pp. 223
    • Francki, R.I.B.1    Fauquet, C.M.2    Knudson, D.L.3    Brown, F.4
  • 17
    • 0000233999 scopus 로고
    • Eukaryotic transient-expression system based on recombinant vaccinia virus that synthesizes bacteriophage T7 RNA polymerase
    • Fuerst, T. R., E. G. Niles, F. W. Studier, and B. Moss. 1986. Eukaryotic transient-expression system based on recombinant vaccinia virus that synthesizes bacteriophage T7 RNA polymerase. Proc. Natl. Acad. Sci. USA 83:8122-8126.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 8122-8126
    • Fuerst, T.R.1    Niles, E.G.2    Studier, F.W.3    Moss, B.4
  • 18
    • 0031000682 scopus 로고    scopus 로고
    • Folding of rabies virus glycoprotein: Epitope acquisition and interaction with endoplasmic reticulum chaperones
    • Gaudin, Y. 1997. Folding of rabies virus glycoprotein: epitope acquisition and interaction with endoplasmic reticulum chaperones. J. Virol. 71:3742-3750.
    • (1997) J. Virol. , vol.71 , pp. 3742-3750
    • Gaudin, Y.1
  • 19
    • 0026584271 scopus 로고
    • Protein folding in the cell
    • Gething, M.-J., and J. Sambrook. 1992. Protein folding in the cell. Nature 355:33-45.
    • (1992) Nature , vol.355 , pp. 33-45
    • Gething, M.-J.1    Sambrook, J.2
  • 20
    • 0027476809 scopus 로고
    • Expression and identification of hepatitis C virus polyprotein cleavage products
    • Grakoui, A., C. Wychowski, C. Lin, S. M. Feinstone, and C. M. Rice. 1993. Expression and identification of hepatitis C virus polyprotein cleavage products. J. Virol. 67:1385-1395.
    • (1993) J. Virol. , vol.67 , pp. 1385-1395
    • Grakoui, A.1    Wychowski, C.2    Lin, C.3    Feinstone, S.M.4    Rice, C.M.5
  • 22
    • 0028103695 scopus 로고
    • Role of N-linked oligosaccharides, glucose trimming and calnexin during glycoprotein folding in the endoplasmic reticulum
    • Hammond, C., I. Braakman, and A. Helenius. 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
  • 23
    • 0029094253 scopus 로고
    • Quality control in the secretory pathway
    • Hammond, C., and A. Helenius. 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
  • 24
    • 0028117314 scopus 로고
    • Molecular chaperones in protein folding: The art of avoiding sticky situations
    • Hartl, F.-U., R. Hlodan, and T. Langer. 1994. Molecular chaperones in protein folding: the art of avoiding sticky situations. Trends Biochem. Sci. 19:20-25.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 20-25
    • Hartl, F.-U.1    Hlodan, R.2    Langer, T.3
  • 25
    • 0029934119 scopus 로고    scopus 로고
    • Calnexin and calreticulin promote folding, delay oligomerization and suppress degradation of influenza hemagglutinin in microsomes
    • Hebert, D. N., B. Foellmer, and A. Helenius. 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
  • 26
    • 0029024748 scopus 로고
    • Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulum
    • Hebert, D. N., B. Foellmer, and A. Helenius. 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
  • 27
    • 0024400060 scopus 로고
    • Interaction of misfolded influenza virus hemagglutinin with binding protein (BiP)
    • Hurtley, S. M., D. G. Bole, H. Hoover-Litty, A. Helenius, and C. S. Copeland. 1989. Interaction 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
  • 28
    • 0028284571 scopus 로고
    • Assisting spontaneity: The role of Hsp90 and small Hsps as molecular chaperones
    • Jakob, U., and J. Buchner. 1994. Assisting spontaneity: the role of Hsp90 and small Hsps as molecular chaperones. Trends Biochem. Sci. 19:205-211.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 205-211
    • Jakob, U.1    Buchner, J.2
  • 30
    • 0028801931 scopus 로고
    • Calnexin and BiP act as sequential molecular chaperones during thyroglobulin folding in the endoplasmic reticulum
    • Kim, P. S., and P. Arvan. 1995. Calnexin and BiP act as sequential molecular chaperones during thyroglobulin folding in the endoplasmic reticulum. J. Cell Biol. 128:29-38.
    • (1995) J. Cell Biol. , vol.128 , pp. 29-38
    • Kim, P.S.1    Arvan, P.2
  • 31
    • 0021891884 scopus 로고
    • Assembly of asparagine-linked oligosaccharides
    • Kornfeld, R., and S. Kornfeld. 1985. Assembly 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
  • 32
    • 0024845992 scopus 로고
    • Identification of immunoglobulin heavy chain binding protein as glucose-related protein 78 on the basis of amino acid sequence, immunological cross-reactivity, and functional activity
    • Kozutsumi, Y., K. Normington, E. Press, C. Slaughter, J. Sambrook, and M.-J. Gething. 1989. Identification of immunoglobulin heavy chain binding protein as glucose-related protein 78 on the basis of amino acid sequence, immunological cross-reactivity, and functional activity. J. Cell Sci. Suppl. 11:115-137.
    • (1989) J. Cell Sci. Suppl. , vol.11 , pp. 115-137
    • Kozutsumi, Y.1    Normington, K.2    Press, E.3    Slaughter, C.4    Sambrook, J.5    Gething, M.-J.6
  • 33
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 34
    • 0027420380 scopus 로고
    • Analysis of hepatitis C virus capsid, E1, and E2/NS1 proteins expressed in insect cells
    • Lanford, R. E., L. Notvall, D. Chavez, R. White, G. Frenzel, C. Simonsen, and J. Kim. 1993. Analysis of hepatitis C virus capsid, E1, and E2/NS1 proteins expressed in insect cells. Virology 197:225-235.
    • (1993) Virology , vol.197 , pp. 225-235
    • Lanford, R.E.1    Notvall, L.2    Chavez, D.3    White, R.4    Frenzel, G.5    Simonsen, C.6    Kim, J.7
  • 35
    • 0028127183 scopus 로고
    • Prolonged association of temperature-sensitive mutants of human P-grycoprotein with calnexin during biogenesis
    • Loo, T. W., and D. M. Clarke. 1994. Prolonged association of temperature-sensitive mutants of human P-grycoprotein with calnexin during biogenesis. J. Biol. Chem. 269:28683-28689.
    • (1994) J. Biol. Chem. , vol.269 , pp. 28683-28689
    • Loo, T.W.1    Clarke, D.M.2
  • 36
    • 0025210448 scopus 로고
    • Heavy chain binding protein recognizes incompletely disulfide-bonded forms of vesicular stomatitis virus G proteins
    • Machamer, C. E., R. W. Doms, D. G. Bole, A. Helenius, and J. K. Rose. 1990. Heavy chain binding protein recognizes incompletely disulfide-bonded forms of vesicular stomatitis virus G proteins. J. Biol. Chem. 265:6879-6883.
    • (1990) J. Biol. Chem. , vol.265 , pp. 6879-6883
    • Machamer, C.E.1    Doms, R.W.2    Bole, D.G.3    Helenius, A.4    Rose, J.K.5
  • 37
    • 0027250528 scopus 로고
    • Post-translational folding of influenza hemagglutinin in isolated endoplasmic reticulum-derived microsomes
    • Marquardt, M., D. Hebert, and A. Helenius. 1993. Post-translational folding of influenza hemagglutinin in isolated endoplasmic reticulum-derived microsomes. J. Biol. Chem. 268:19618-19625.
    • (1993) J. Biol. Chem. , vol.268 , pp. 19618-19625
    • Marquardt, M.1    Hebert, D.2    Helenius, A.3
  • 38
    • 0028805715 scopus 로고
    • Identification and site-directed mutagenesis of the primary (2A/2B) cleavage site of the hepatitis A virus polyprotein: Functional impact on infectivity of HAV RNA transcripts
    • Martin, A., N. Escriou, S. F. Chao, S. M. Lemon, M. Girard, and C. Wychowski. 1995. Identification and site-directed mutagenesis of the primary (2A/2B) cleavage site of the hepatitis A virus polyprotein: functional impact on infectivity of HAV RNA transcripts. Virology 213:213-222.
    • (1995) Virology , vol.213 , pp. 213-222
    • Martin, A.1    Escriou, N.2    Chao, S.F.3    Lemon, S.M.4    Girard, M.5    Wychowski, C.6
  • 39
    • 0000407708 scopus 로고
    • The molecular biology of hepatitis C virus
    • Matsuura, Y., and T. Miyamura. 1993. The molecular biology of hepatitis C virus. Semin. Virol. 4:297-304.
    • (1993) Semin. Virol. , vol.4 , pp. 297-304
    • Matsuura, Y.1    Miyamura, T.2
  • 40
    • 0026808864 scopus 로고
    • The endoplasmic reticulum stress protein GRP94, in addition to BiP, associates with assembled immunoglobulin chains
    • Melnick, J., S. Aviel, and Y. Argon. 1992. The endoplasmic reticulum stress protein GRP94, in addition to BiP, associates with assembled immunoglobulin chains. J. Biol. Chem. 267:21303-21306.
    • (1992) J. Biol. Chem. , vol.267 , pp. 21303-21306
    • Melnick, J.1    Aviel, S.2    Argon, Y.3
  • 41
    • 0028170231 scopus 로고
    • Sequential interaction of the chaperones BiP and GRP94 with immunoglobulin chains in the endoplasmic reticulum
    • Melnick, J., J. L. Dul, and Y. Argon. 1994. Sequential interaction of the chaperones BiP and GRP94 with immunoglobulin chains in the endoplasmic reticulum. Nature 370:373-375.
    • (1994) Nature , vol.370 , pp. 373-375
    • Melnick, J.1    Dul, J.L.2    Argon, Y.3
  • 43
    • 0000557448 scopus 로고    scopus 로고
    • Poxviridae: The viruses and their replication
    • B. N. Fields, D. M. Knipe, and P. M. Howley (ed.), Lippincott-Raven, Philadelphia, Pa.
    • Moss, B. 1996. Poxviridae: the viruses and their replication, p. 2637-2671. In B. N. Fields, D. M. Knipe, and P. M. Howley (ed.), Fields virology, 3rd ed. Lippincott-Raven, Philadelphia, Pa.
    • (1996) Fields Virology, 3rd Ed. , pp. 2637-2671
    • Moss, B.1
  • 45
    • 0023052239 scopus 로고
    • An hsp-70 like protein in the ER: Identity with the 78 Kd glucose-regulated protein and immunoglobulin heavy chain binding protein
    • Munro, S., and H. R. B. Pelham. 1986. An hsp-70 like protein in the ER: identity with the 78 Kd glucose-regulated protein and immunoglobulin heavy chain binding protein. Cell 44:291-300.
    • (1986) Cell , vol.44 , pp. 291-300
    • Munro, S.1    Pelham, H.R.B.2
  • 46
    • 0023052239 scopus 로고
    • An HSP-like protein in the ER: Identity with the 78 Kd glucose regulated protein and immunoglobulin heavy chain binding protein
    • Munro, S., and H. R. B. Pelham. 1986. An HSP-like protein in the ER: identity with the 78 Kd glucose regulated protein and immunoglobulin heavy chain binding protein. Cell 46:291-300.
    • (1986) Cell , vol.46 , pp. 291-300
    • Munro, S.1    Pelham, H.R.B.2
  • 47
    • 0028964421 scopus 로고
    • Calreticulin functions as a molecular chaperone in the biosynthesis of myeloperoxidase
    • Nauseef, W. M., S. J. McCormick, and R. A. Clark. 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
  • 48
    • 0025784485 scopus 로고
    • A mutation in the ectodomain of herpes simplex virus 1 glycoprotein B causes defective processing and retention in the endoplasmic reticulum
    • Navarro, D., I. Qadri, and L. Pereira. 1991. A mutation in the ectodomain of herpes simplex virus 1 glycoprotein B causes defective processing and retention in the endoplasmic reticulum. Virology 184:253-264.
    • (1991) Virology , vol.184 , pp. 253-264
    • Navarro, D.1    Qadri, I.2    Pereira, L.3
  • 49
    • 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
    • Otteken, A., and B. Moss. 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
  • 50
    • 0027295871 scopus 로고
    • Association of folding intermediates of glycoproteins with calnexin during protein maturation
    • Ou, W.-J., P. H. Cameron, D. Y. Thomas, and J. J. M. Bergeron. 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
  • 51
    • 0029160540 scopus 로고
    • Transient, lectin-like association of calreticulin with folding intermediates of cellular and viral glycoprotein
    • Peterson, J. R., A. Ora, P. Nguyen Van, and A. Helenius. 1995. Transient, lectin-like association of calreticulin with folding intermediates of cellular and viral glycoprotein. Mol. Biol. 6:1173-1184.
    • (1995) Mol. Biol. , vol.6 , pp. 1173-1184
    • Peterson, J.R.1    Ora, A.2    Van Nguyen, P.3    Helenius, A.4
  • 52
    • 0028147528 scopus 로고
    • Retention of unassembled components of integral membrane proteins by calnexin
    • Rajagopalan, S., Y. Xu, and M. B. Brenner. 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
  • 54
    • 0001424128 scopus 로고    scopus 로고
    • Flaviviridae: Viruses and their replication
    • B. N. Fields, D. M. Knipe, and P. M. Howley (ed.), Lippincott-Raven, Philadelphia, Pa.
    • Rice, C. M. 1996. Flaviviridae: viruses and their replication, p. 931-959. In B. N. Fields, D. M. Knipe, and P. M. Howley (ed.), Fields virology, 3rd ed. Lippincott-Raven, Philadelphia, Pa.
    • (1996) Fields Virology, 3rd Ed. , pp. 931-959
    • Rice, C.M.1
  • 55
    • 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, A. R., J. F. Simons, E. S. Trombetta, and A. Helenius. 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
  • 56
    • 0028486023 scopus 로고
    • A single purification procedure for the major resident proteins of the ER lumen: Endoplasmin, BiP, calreticulin and protein disulfide isomerase
    • Rowling, P., S. H. McLaugblin, G. S. Pollock, and R. B. Freedman. 1994. A single purification procedure for the major resident proteins of the ER lumen: endoplasmin, BiP, calreticulin and protein disulfide isomerase. Protein Expression Purif. 5:331-336.
    • (1994) Protein Expression Purif. , vol.5 , pp. 331-336
    • Rowling, P.1    McLaugblin, S.H.2    Pollock, G.S.3    Freedman, R.B.4
  • 58
    • 0026742999 scopus 로고
    • HLA-DR associates with specific stress proteins and is retained in the endoplasmic reticulum in invariant chain negative cells
    • Schaiff, W. T., K. A. Hruska, D. W. McCourt, M. Green, and B. D. Schwartz. 1992. HLA-DR associates with specific stress proteins and is retained in the endoplasmic reticulum in invariant chain negative cells. J. Exp. Med. 176: 657-666.
    • (1992) J. Exp. Med. , vol.176 , pp. 657-666
    • Schaiff, W.T.1    Hruska, K.A.2    McCourt, D.W.3    Green, M.4    Schwartz, B.D.5
  • 59
    • 0029126624 scopus 로고
    • The molecular basis for the recognition of misfolded glycoproteins by the UDP-Glc:glycoprotein glucosyltransferase
    • Sousa, M., and A. J. Parodi. 1995. The molecular basis for the recognition of misfolded glycoproteins by the UDP-Glc:glycoprotein glucosyltransferase. EMBO J. 14:4196-4203.
    • (1995) EMBO J. , vol.14 , pp. 4196-4203
    • Sousa, M.1    Parodi, A.J.2
  • 60
    • 0026500202 scopus 로고
    • Recognition of the oligosaccharide and protein moieties of glycoproteins by the UDP-Glc: Glycoprotein glucosyltranferase
    • Sousa, M. C., M. A. Ferrero-Garcia, and A. J. Parodi. 1992. Recognition of the oligosaccharide and protein moieties of glycoproteins by the UDP-Glc: glycoprotein glucosyltranferase. Biochemistry 31:97-105.
    • (1992) Biochemistry , vol.31 , pp. 97-105
    • Sousa, M.C.1    Ferrero-Garcia, M.A.2    Parodi, A.J.3
  • 62
    • 0029993522 scopus 로고    scopus 로고
    • Calnexin associates exclusively with individual CD3d and T cell antigen receptor (TCR) a protein containing incompletely trimmed glycans that are not assembled into multisubunit TCR complexes
    • Van Leeuwen, J. E. M., and K. P. Kears. 1996. Calnexin associates exclusively with individual CD3d and T cell antigen receptor (TCR) a protein 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    Kears, K.P.2
  • 63
    • 0029134004 scopus 로고
    • Chaperone function of calreticulin when expressed in the endoplasmic reticulum as the membrane-anchored and soluble forms
    • Wada, I., S. Imai, M. Kai, F. Sakane, and H. Kanoh. 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
  • 64
    • 0028932360 scopus 로고
    • The molecular chaperone calnexin binds Glc1Man9GlcNAc2 oligosaccharide as an initial step in recognizing unfolded glycoproteins
    • Ware, F. E., A. Vassilakos, P. A. Peterson, M. R. Jackson, M. A. Lehrman, and D. B. Williams. 1995. The molecular chaperone calnexin binds Glc1Man9GlcNAc2 oligosaccharide as an initial step in recognizing unfolded glycoproteins. J. Biol. Chem. 270:4697-4704.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4697-4704
    • Ware, F.E.1    Vassilakos, A.2    Peterson, P.A.3    Jackson, M.R.4    Lehrman, M.A.5    Williams, D.B.6
  • 65
    • 0029872240 scopus 로고    scopus 로고
    • Calnexin acts as a molecular chaperone during the folding of glycoprotein B of human cytomegalovirus
    • Yamashita, Y., K. Shimokata, S. Mizuno, T. Daikoku, T. Tsurumi, and Y. Nishiyama. 1996. Calnexin acts as a molecular chaperone during the folding of glycoprotein B of human cytomegalovirus. J. Virol. 70:2237-2246.
    • (1996) J. Virol. , vol.70 , pp. 2237-2246
    • Yamashita, Y.1    Shimokata, K.2    Mizuno, S.3    Daikoku, T.4    Tsurumi, T.5    Nishiyama, Y.6
  • 66
    • 0030933129 scopus 로고    scopus 로고
    • Conformation-independent binding of monoglucosylated ribonuclease B to calnexin
    • Zapun, A., S. M. Petrescu, P. M. Rudd, R. A. Dwek, D. Y. Thomas, and J. J. M. Bergeron. 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.