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Volumn 61, Issue 5, 2004, Pages 547-556

Assembly of MHC class I peptide complexes from the perspective of disulfide bond formation

Author keywords

Disulfide bond formation; Disulfide isomerization; ER quality control; ERp57; MHC class I; Peptide loading complex; Tapasin

Indexed keywords

ERP57 PROTEIN; LIGAND; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; MEMBRANE PROTEIN; POLYPEPTIDE; PROTEIN DISULFIDE ISOMERASE; TAPASIN; THIOREDOXIN; UNCLASSIFIED DRUG;

EID: 1642334894     PISSN: 1420682X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00018-003-3271-9     Document Type: Review
Times cited : (31)

References (77)
  • 1
    • 0030937833 scopus 로고    scopus 로고
    • Capture and processing of exogenous antigens for presentation on MHC molecules
    • Watts C. (1997) Capture and processing of exogenous antigens for presentation on MHC molecules. Annu. Rev. Immunol. 15: 821-850
    • (1997) Annu. Rev. Immunol. , vol.15 , pp. 821-850
    • Watts, C.1
  • 2
    • 0031895637 scopus 로고    scopus 로고
    • Mechanisms of MHC class I-restricted antigen processing
    • Pamer E. and Cresswell P. (1998) Mechanisms of MHC class I-restricted antigen processing. Annu. Rev. Immunol. 16: 323-258
    • (1998) Annu. Rev. Immunol. , vol.16 , pp. 323-1258
    • Pamer, E.1    Cresswell, P.2
  • 3
  • 4
    • 0034813655 scopus 로고    scopus 로고
    • Comparative genomics of the MHC: Glimpses into the evolution of the adaptive immune system
    • Flajnik M. F. and Kasahara M. (2001) Comparative genomics of the MHC: glimpses into the evolution of the adaptive immune system. Immunity 15: 351-362
    • (2001) Immunity , vol.15 , pp. 351-362
    • Flajnik, M.F.1    Kasahara, M.2
  • 5
    • 0028922319 scopus 로고
    • Chemistry of peptides associated with MHC class I and class II molecules
    • Rammensee H. G. (1995) Chemistry of peptides associated with MHC class I and class II molecules. Curr. Opin. Immunol. 7: 85-96
    • (1995) Curr. Opin. Immunol. , vol.7 , pp. 85-96
    • Rammensee, H.G.1
  • 7
    • 0034173387 scopus 로고    scopus 로고
    • Intracellular surveillance: Controlling the assembly of MHC class I-peptide complexes
    • Cresswell P. (2000) Intracellular surveillance: controlling the assembly of MHC class I-peptide complexes. Traffic 1: 301-305
    • (2000) Traffic , vol.1 , pp. 301-305
    • Cresswell, P.1
  • 8
    • 0034601092 scopus 로고    scopus 로고
    • Affinity, specificity, diversity: A challenge for the ABC transporter TAP in cellular immunity
    • Schmitt L. and Tampe R. (2000) Affinity, specificity, diversity: a challenge for the ABC transporter TAP in cellular immunity. Chembiochem. 1: 16-35
    • (2000) Chembiochem. , vol.1 , pp. 16-35
    • Schmitt, L.1    Tampe, R.2
  • 9
    • 0036776746 scopus 로고    scopus 로고
    • Tapasin-the keystone of the loading complex optimizing peptide binding by MHC class I molecules in the endoplasmic reticulum
    • Momburg F. and Tan P. (2002) Tapasin-the keystone of the loading complex optimizing peptide binding by MHC class I molecules in the endoplasmic reticulum. Mol. Immunol. 39: 217-233
    • (2002) Mol. Immunol. , vol.39 , pp. 217-233
    • Momburg, F.1    Tan, P.2
  • 10
    • 0036230677 scopus 로고    scopus 로고
    • Optimization of the MHC class I peptide cargo is dependent on tapasin
    • Williams A. P., Peh C. A., Purcell A. W., McCluskey J. and Elliott T. (2002) Optimization of the MHC class I peptide cargo is dependent on tapasin. Immunity 16: 509-520
    • (2002) Immunity , vol.16 , pp. 509-520
    • Williams, A.P.1    Peh, C.A.2    Purcell, A.W.3    McCluskey, J.4    Elliott, T.5
  • 11
    • 0037083299 scopus 로고    scopus 로고
    • Recruitment of MHC class I molecules by tapasin into the transporter associated with antigen processing-associated complex is essential for optimal peptide loading
    • Tan P., Kropshofer H., Mandelboim O., Bulbuc N., Hammerling G. J. and Momburg F. (2002) Recruitment of MHC class I molecules by tapasin into the transporter associated with antigen processing-associated complex is essential for optimal peptide loading. J. Immunol. 168: 1950-1960
    • (2002) J. Immunol. , vol.168 , pp. 1950-1960
    • Tan, P.1    Kropshofer, H.2    Mandelboim, O.3    Bulbuc, N.4    Hammerling, G.J.5    Momburg, F.6
  • 12
    • 0030217926 scopus 로고    scopus 로고
    • Roles for calreticulin and a novel glycoprotein, tapasin, in the interaction of MHC class I molecules with TAP
    • 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
  • 13
    • 0035937505 scopus 로고    scopus 로고
    • Intracellular functions of N-linked glycans
    • Helenius A. and Aebi M. (2001) Intracellular functions of N-linked glycans. Science 291: 2364-2369
    • (2001) Science , vol.291 , pp. 2364-2369
    • Helenius, A.1    Aebi, M.2
  • 14
    • 0032482384 scopus 로고    scopus 로고
    • The thiol oxidoreductase ERp57 is a component of the MHC class I peptide-loading complex
    • Hughes E. A. and Cresswell P. (1998) The thiol oxidoreductase ERp57 is a component of the MHC class I peptide-loading complex. Curr. Biol. 8: 709-712
    • (1998) Curr. Biol. , vol.8 , pp. 709-712
    • Hughes, E.A.1    Cresswell, P.2
  • 15
    • 0032522392 scopus 로고    scopus 로고
    • ER-60, a chaperone with thiol-dependent reductase activity involved in MHC class I assembly
    • Lindquist J. A., Jensen O. N., Mann M. and Hammerling G. J. (1998) ER-60, a chaperone with thiol-dependent reductase activity involved in MHC class I assembly. EMBO J. 17: 2186-2195
    • (1998) EMBO J. , vol.17 , pp. 2186-2195
    • Lindquist, J.A.1    Jensen, O.N.2    Mann, M.3    Hammerling, G.J.4
  • 16
    • 0032482385 scopus 로고    scopus 로고
    • A role for the thiol-dependent reductase ERp57 in the assembly of MHC class I molecules
    • Morrice N. A. and Powis S. J. (1998) A role for the thiol-dependent reductase ERp57 in the assembly of MHC class I molecules. Curr. Biol. 8: 713-716
    • (1998) Curr. Biol. , vol.8 , pp. 713-716
    • Morrice, N.A.1    Powis, S.J.2
  • 17
    • 0032807338 scopus 로고    scopus 로고
    • ERp57 functions as a subunit of specific complexes formed with the ER lectins calreticulin and calnexin
    • Oliver J. D., Roderick H. L., Llewellyn 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) Mol. Biol. Cell , vol.10 , pp. 2573-2582
    • Oliver, J.D.1    Roderick, H.L.2    Llewellyn, D.H.3    High, S.4
  • 18
    • 2442761708 scopus 로고    scopus 로고
    • The protein disulphide-isomerase family: Unravelling a string of folds
    • Ferrari D. M. and Soling H. D. (1999) The protein disulphide-isomerase family: unravelling a string of folds. Biochem. J. 339 (Pt 1): 1-10
    • (1999) Biochem. J. , vol.339 , Issue.1 PART , pp. 1-10
    • Ferrari, D.M.1    Soling, H.D.2
  • 19
    • 0037336295 scopus 로고    scopus 로고
    • Quality control in the endoplasmic reticulum
    • Ellgaard L. and Helenius A. (2003) Quality control in the endoplasmic reticulum. Nat. Rev. Mol. Cell. Biol. 4: 181-191
    • (2003) Nat. Rev. Mol. Cell. Biol. , vol.4 , pp. 181-191
    • Ellgaard, L.1    Helenius, A.2
  • 20
    • 0032773506 scopus 로고    scopus 로고
    • The immunoglobulin fold family: Sequence analysis and 3D structure comparisons
    • Halaby D. M., Poupon A. and Mornon J. (1999) The immunoglobulin fold family: sequence analysis and 3D structure comparisons. Protein Eng. 12: 563-571
    • (1999) Protein Eng. , vol.12 , pp. 563-571
    • Halaby, D.M.1    Poupon, A.2    Mornon, J.3
  • 21
    • 0032815051 scopus 로고    scopus 로고
    • Conservation of cys-cys trp structural triads and their geometry in the protein domains of immunoglobulin superfamily members
    • Ioerger T. R., Du C. and Linthicum D. S. (1999) Conservation of cys-cys trp structural triads and their geometry in the protein domains of immunoglobulin superfamily members. Mol. Immunol. 36: 373-386
    • (1999) Mol. Immunol. , vol.36 , pp. 373-386
    • Ioerger, T.R.1    Du, C.2    Linthicum, D.S.3
  • 23
    • 0026728457 scopus 로고
    • Emerging principles for the recognition of peptide antigens by MHC class I molecules
    • Matsumura M., Fremont D. H., Peterson P. A. and Wilson I. A. (1992) Emerging principles for the recognition of peptide antigens by MHC class I molecules. Science 257: 927-934
    • (1992) Science , vol.257 , pp. 927-934
    • Matsumura, M.1    Fremont, D.H.2    Peterson, P.A.3    Wilson, I.A.4
  • 24
    • 0029046720 scopus 로고
    • Characterization of class I MHC folding intermediates and their disparate interactions with peptide and beta 2-microglobulin
    • Smith J. D., Solheim J. C., Carreno B. M. and Hansen T. H. (1995) Characterization of class I MHC folding intermediates and their disparate interactions with peptide and beta 2-microglobulin. Mol. Immunol. 32: 531-540
    • (1995) Mol. Immunol. , vol.32 , pp. 531-540
    • Smith, J.D.1    Solheim, J.C.2    Carreno, B.M.3    Hansen, T.H.4
  • 25
    • 0034771715 scopus 로고    scopus 로고
    • Efficient assembly of recombinant major histocompatibility complex class I molecules with preformed disulfide bonds
    • Ostergaard Pedersen L., Nissen M. H., Hansen N. J., Nielsen L. L., Lauenmoller S. L., Blicher T. et al. (2001) Efficient assembly of recombinant major histocompatibility complex class I molecules with preformed disulfide bonds. Eur. J. Immunol. 31: 2986-2996
    • (2001) Eur. J. Immunol. , vol.31 , pp. 2986-2996
    • Ostergaard Pedersen, L.1    Nissen, M.H.2    Hansen, N.J.3    Nielsen, L.L.4    Lauenmoller, S.L.5    Blicher, T.6
  • 26
    • 0037013950 scopus 로고    scopus 로고
    • The oxidoreductase ERp57 efficiently reduces partially folded in preference to fully folded MHC class I molecules
    • Antoniou A. N., Ford S., Alphey M., Osborne A., Elliott T. and Powis S. J. (2002) The oxidoreductase ERp57 efficiently reduces partially folded in preference to fully folded MHC class I molecules. EMBO J. 21: 2655-2663
    • (2002) EMBO J. , vol.21 , pp. 2655-2663
    • Antoniou, A.N.1    Ford, S.2    Alphey, M.3    Osborne, A.4    Elliott, T.5    Powis, S.J.6
  • 27
    • 0025231788 scopus 로고
    • Failure of cell surface expression of a class I major histocompatibility antigen caused by somatic point mutation
    • Zeff R. A., Nakagawa M., Mashimo H., Gopas J. and Nathenson S. G. (1990) Failure of cell surface expression of a class I major histocompatibility antigen caused by somatic point mutation. Transplantation 49: 803-808
    • (1990) Transplantation , vol.49 , pp. 803-808
    • Zeff, R.A.1    Nakagawa, M.2    Mashimo, H.3    Gopas, J.4    Nathenson, S.G.5
  • 28
    • 0035338645 scopus 로고    scopus 로고
    • Association of ERp57 with mouse MHC class I molecules is tapasin dependent and mimics that of calreticulin and not calnexin
    • Harris M. R., Lybarger L., Yu Y. Y., Myers N. B. and Hansen T. H. (2001) Association of ERp57 with mouse MHC class I molecules is tapasin dependent and mimics that of calreticulin and not calnexin. J. Immunol. 166: 6686-6692
    • (2001) J. Immunol. , vol.166 , pp. 6686-6692
    • Harris, M.R.1    Lybarger, L.2    Yu, Y.Y.3    Myers, N.B.4    Hansen, T.H.5
  • 29
    • 0031091739 scopus 로고    scopus 로고
    • Prominence of beta 2-microglobulin, class I heavy chain conformation and tapasin in the interactions of class I heavy chain with calreticulin and the transporter associated with antigen processing
    • Solheim J. C., Harris M. R., Kindle C. S. and Hansen T. H. (1997) Prominence of beta 2-microglobulin, class I heavy chain conformation and tapasin in the interactions of class I heavy chain with calreticulin and the transporter associated with antigen processing. J. Immunol. 158: 2236-2241
    • (1997) J. Immunol. , vol.158 , pp. 2236-2241
    • Solheim, J.C.1    Harris, M.R.2    Kindle, C.S.3    Hansen, T.H.4
  • 30
    • 0021751894 scopus 로고
    • Role of a disulfide bridge in the immune function of major histocompatibility class I antigen as studied by in vitro mutagenesis
    • Shiroishi T., Evans G. A., Appella E. and Ozato K. (1984) Role of a disulfide bridge in the immune function of major histocompatibility class I antigen as studied by in vitro mutagenesis. Proc. Natl. Acad. Sci. USA 81: 7544-7548
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 7544-7548
    • Shiroishi, T.1    Evans, G.A.2    Appella, E.3    Ozato, K.4
  • 31
    • 0028177703 scopus 로고
    • Mutation of the alpha 2 domain disulfide bridge of the class I molecule HLA-A*0201. Effect on maturation and peptide presentation
    • Warburton R. J., Matsui M., Rowland-Jones S. L., Gammon M. C., Katzenstein G. E., Wei T. et al. (1994) Mutation of the alpha 2 domain disulfide bridge of the class I molecule HLA-A*0201. Effect on maturation and peptide presentation. Hum. Immunol. 39:261-271
    • (1994) Hum. Immunol. , vol.39 , pp. 261-271
    • Warburton, R.J.1    Matsui, M.2    Rowland-Jones, S.L.3    Gammon, M.C.4    Katzenstein, G.E.5    Wei, T.6
  • 32
    • 0026718034 scopus 로고
    • Reptilian class I major histocompatibility complex genes reveal conserved elements in class I structure
    • Grossberger D. and Parham P. (1992) Reptilian class I major histocompatibility complex genes reveal conserved elements in class I structure. Immunogenetics 36: 166-174
    • (1992) Immunogenetics , vol.36 , pp. 166-174
    • Grossberger, D.1    Parham, P.2
  • 33
    • 0031424262 scopus 로고    scopus 로고
    • The most primitive vertebrates with jaws possess highly polymorphic MHC class I genes comparable to those of humans
    • Okamura K., Ototake M., Nakanishi T., Kurosawa Y. and Hashimoto K. (1997) The most primitive vertebrates with jaws possess highly polymorphic MHC class I genes comparable to those of humans. Immunity 7: 777-790
    • (1997) Immunity , vol.7 , pp. 777-790
    • Okamura, K.1    Ototake, M.2    Nakanishi, T.3    Kurosawa, Y.4    Hashimoto, K.5
  • 34
    • 0026085454 scopus 로고
    • Evolution of the major histocompatibility complex: Molecular cloning of major histocompatibility complex class I from the amphibian Xenopus
    • Flajnik M. F., Canel C., Kramer J. and Kasahara M. (1991) Evolution of the major histocompatibility complex: molecular cloning of major histocompatibility complex class I from the amphibian Xenopus. Proc. Natl. Acad. Sci. USA 88: 537-541
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 537-541
    • Flajnik, M.F.1    Canel, C.2    Kramer, J.3    Kasahara, M.4
  • 36
    • 0023181056 scopus 로고
    • Tissue-specific expression and structure of a divergent member of a class I MHC gene family
    • Ehrlich R., Lifshitz R., Pescovitz M. D., Rudikoff S. and Singer D. S. (1987) Tissue-specific expression and structure of a divergent member of a class I MHC gene family. J. Immunol. 139: 593-602
    • (1987) J. Immunol. , vol.139 , pp. 593-602
    • Ehrlich, R.1    Lifshitz, R.2    Pescovitz, M.D.3    Rudikoff, S.4    Singer, D.S.5
  • 37
    • 0026697413 scopus 로고
    • Interferon-inducible gene expression in chimpanzee liver infected with hepatitis C virus
    • Kato T., Esumi M., Yamashita S., Abe K. and Shikata T. (1992) Interferon-inducible gene expression in chimpanzee liver infected with hepatitis C virus. Virology 190: 856-860
    • (1992) Virology , vol.190 , pp. 856-860
    • Kato, T.1    Esumi, M.2    Yamashita, S.3    Abe, K.4    Shikata, T.5
  • 38
    • 0031051784 scopus 로고    scopus 로고
    • MHC class I and class II structures
    • Jones E. Y. (1997) MHC class I and class II structures. Curr. Opin. Immunol. 9: 75-79
    • (1997) Curr. Opin. Immunol. , vol.9 , pp. 75-79
    • Jones, E.Y.1
  • 40
    • 0027362677 scopus 로고
    • Disulfide bonds and the stability of globular proteins
    • Betz S. F. (1993) Disulfide bonds and the stability of globular proteins. Protein Sci. 2: 1551-1558
    • (1993) Protein Sci. , vol.2 , pp. 1551-1558
    • Betz, S.F.1
  • 41
    • 0023956149 scopus 로고
    • Disulphide bonds and protein stability
    • Creighton T. E. (1988) Disulphide bonds and protein stability. Bioessays 8: 57-63
    • (1988) Bioessays , vol.8 , pp. 57-63
    • Creighton, T.E.1
  • 42
    • 0037044749 scopus 로고    scopus 로고
    • The cystine knot promotes folding and not thermodynamic stability in vascular endothelial growth factor
    • Muller Y. A., Heiring C., Misselwitz R., Welfle K. and Welfle H. (2002) The cystine knot promotes folding and not thermodynamic stability in vascular endothelial growth factor. J. Biol. Chem. 277: 43410-43416
    • (2002) J. Biol. Chem. , vol.277 , pp. 43410-43416
    • Muller, Y.A.1    Heiring, C.2    Misselwitz, R.3    Welfle, K.4    Welfle, H.5
  • 43
    • 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
  • 44
    • 0026698060 scopus 로고
    • Oxidized redox state of glutathione in the endoplasmic reticulum
    • Hwang C., Sinskey A. J. and Lodish H. F. (1992) Oxidized redox state of glutathione in the endoplasmic reticulum. Science 257: 1496-1502
    • (1992) Science , vol.257 , pp. 1496-1502
    • Hwang, C.1    Sinskey, A.J.2    Lodish, H.F.3
  • 45
    • 0031609760 scopus 로고    scopus 로고
    • The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum
    • Frand A. R. and Kaiser C. A. (1998) The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum. Mol. Cell. 1: 161-170
    • (1998) Mol. Cell. , vol.1 , pp. 161-170
    • Frand, A.R.1    Kaiser, C.A.2
  • 46
    • 0033163758 scopus 로고    scopus 로고
    • Competition between glutathione and protein thiols for disulphide-bond formation
    • Cuozzo J. W. and Kaiser C. A. (1999) Competition between glutathione and protein thiols for disulphide-bond formation. Nat. Cell Biol. 1: 130-135
    • (1999) Nat. Cell Biol. , vol.1 , pp. 130-135
    • Cuozzo, J.W.1    Kaiser, C.A.2
  • 47
    • 0033213605 scopus 로고    scopus 로고
    • Erolp oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulum
    • Frand A. R. and Kaiser C. A. (1999) Erolp oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulum. Mol. Cell. 4: 469-477
    • (1999) Mol. Cell. , vol.4 , pp. 469-477
    • Frand, A.R.1    Kaiser, C.A.2
  • 48
    • 0034711439 scopus 로고    scopus 로고
    • Biochemical basis of oxidative protein folding in the endoplasmic reticulum
    • Tu B. P., Ho-Schleyer S. C., Travers K. J. and Weissman J. S. (2000) Biochemical basis of oxidative protein folding in the endoplasmic reticulum. Science 290: 1571-1574
    • (2000) Science , vol.290 , pp. 1571-1574
    • Tu, B.P.1    Ho-Schleyer, S.C.2    Travers, K.J.3    Weissman, J.S.4
  • 49
    • 0036862532 scopus 로고    scopus 로고
    • The FAD- and O(2)-dependent reaction cycle of Erol-mediated oxidative protein folding in the endoplasmic reticulum
    • Tu B. P. and Weissman J. S. (2002) The FAD-and O(2)-dependent reaction cycle of Erol-mediated oxidative protein folding in the endoplasmic reticulum. Mol. Cell. 10: 983-994
    • (2002) Mol. Cell. , vol.10 , pp. 983-994
    • Tu, B.P.1    Weissman, J.S.2
  • 50
    • 0036224573 scopus 로고    scopus 로고
    • Oxidative protein folding in bacteria
    • Collet J. F. and Bardwell J. C. (2002) Oxidative protein folding in bacteria. Mol. Microbiol. 44: 1-8
    • (2002) Mol. Microbiol. , vol.44 , pp. 1-8
    • Collet, J.F.1    Bardwell, J.C.2
  • 51
    • 0032513212 scopus 로고    scopus 로고
    • Enhanced catalysis of ribonuclease B folding by the interaction of calnexin or calreticulin with ERp57
    • Zapun A., Darby N. J., Tessier D. C., Michalak M., Bergeron J. J. 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.5    Thomas, D.Y.6
  • 52
    • 0031035644 scopus 로고    scopus 로고
    • Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins
    • Oliver J. D., van der Wal F. J., 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.J.2    Bulleid, N.J.3    High, S.4
  • 53
    • 0031614141 scopus 로고    scopus 로고
    • The role of the lectin calnexin in conformation independent binding to N-linked glycoproteins and quality control
    • Bergeron J. J., Zapun A., Ou W. J., Hemming R., Parlati F., Cameron P. H. et al. (1998) The role of the lectin calnexin in conformation independent binding to N-linked glycoproteins and quality control. Adv. Exp. Med. Biol. 435: 105-116
    • (1998) Adv. Exp. Med. Biol. , vol.435 , pp. 105-116
    • Bergeron, J.J.1    Zapun, A.2    Ou, W.J.3    Hemming, R.4    Parlati, F.5    Cameron, P.H.6
  • 54
    • 0034799402 scopus 로고    scopus 로고
    • The Structure of calnexin, an ER chaperone involved in quality control of protein folding
    • Schrag J. D., Bergeron J. J., Li Y., Borisova S., Hahn M., Thomas D. Y. et al. (2001) The Structure of calnexin, an ER chaperone involved in quality control of protein folding. Mol. Cell. 8: 633-644
    • (2001) Mol. Cell. , vol.8 , pp. 633-644
    • Schrag, J.D.1    Bergeron, J.J.2    Li, Y.3    Borisova, S.4    Hahn, M.5    Thomas, D.Y.6
  • 56
    • 0037119465 scopus 로고    scopus 로고
    • Localization of the lectin, ERp57 binding, and polypeptide binding sites of calnexin and calreticulin
    • Leach M. R., Cohen-Doyle M. F., Thomas D. Y. and Williams D. B. (2002) Localization of the lectin, ERp57 binding, and polypeptide binding sites of calnexin and calreticulin. J. Biol. Chem. 277: 29686-29697
    • (2002) J. Biol. Chem. , vol.277 , pp. 29686-29697
    • Leach, M.R.1    Cohen-Doyle, M.F.2    Thomas, D.Y.3    Williams, D.B.4
  • 57
    • 0034031279 scopus 로고    scopus 로고
    • Recognition of local glycoprotein misfolding by the ER folding sensor UDP-glucose:glycoprotein glucosyltransferase
    • Ritter C. and Helenius A. (2000) Recognition of local glycoprotein misfolding by the ER folding sensor UDP-glucose:glycoprotein glucosyltransferase. Nat. Struct. Biol. 7: 278-280
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 278-280
    • Ritter, C.1    Helenius, A.2
  • 58
    • 0036371484 scopus 로고    scopus 로고
    • Thiol oxidation and reduction in major histocompatibility complex class I-restricted antigen processing and presentation
    • Dick T. P. and Cresswell P. (2002) Thiol oxidation and reduction in major histocompatibility complex class I-restricted antigen processing and presentation. Methods Enzymol. 348: 49-54
    • (2002) Methods Enzymol. , vol.348 , pp. 49-54
    • Dick, T.P.1    Cresswell, P.2
  • 59
    • 0033523910 scopus 로고    scopus 로고
    • Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells
    • Molinari M. and Helenius A. (1999) Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells. Nature 402: 90-93
    • (1999) Nature , vol.402 , pp. 90-93
    • Molinari, M.1    Helenius, A.2
  • 60
    • 0035890070 scopus 로고    scopus 로고
    • Manipulation of oxidative protein folding and PDI redox state in mammalian cells
    • Mezghrani A., Fassio A., Benham A., Simmen T., Braakman I. and Sitia R. (2001) Manipulation of oxidative protein folding and PDI redox state in mammalian cells. EMBO J. 20: 6288-6296
    • (2001) EMBO J. , vol.20 , pp. 6288-6296
    • Mezghrani, A.1    Fassio, A.2    Benham, A.3    Simmen, T.4    Braakman, I.5    Sitia, R.6
  • 61
    • 0030765974 scopus 로고    scopus 로고
    • Beta 2-microglobulin and calnexin can independently promote folding and disulfide bond formation in class I histocompatibility proteins
    • Tector M., Zhang Q. and Salter R. D. (1997) Beta 2-microglobulin and calnexin can independently promote folding and disulfide bond formation in class I histocompatibility proteins. Mol. Immunol. 34:401-408
    • (1997) Mol. Immunol. , vol.34 , pp. 401-408
    • Tector, M.1    Zhang, Q.2    Salter, R.D.3
  • 62
    • 0023653141 scopus 로고
    • In vivo cross-linking of protein disulfide isomerase to immunoglobulins
    • Roth R. A. and Pierce S. B. (1987) In vivo cross-linking of protein disulfide isomerase to immunoglobulins. Biochemistry 26: 4179-4182
    • (1987) Biochemistry , vol.26 , pp. 4179-4182
    • Roth, R.A.1    Pierce, S.B.2
  • 63
    • 0026758276 scopus 로고
    • Independent and synergistic effects of disulfide bond formation, beta 2-microglobulin and peptides on class I MHC folding and assembly in an in vitro translation system
    • Ribaudo R. K. and Margulies D. H. (1992) Independent and synergistic effects of disulfide bond formation, beta 2-microglobulin and peptides on class I MHC folding and assembly in an in vitro translation system. J. Immunol. 149: 2935-2944
    • (1992) J. Immunol. , vol.149 , pp. 2935-2944
    • Ribaudo, R.K.1    Margulies, D.H.2
  • 64
    • 0028037904 scopus 로고
    • Ab initio association with beta 2-microglobulin during biosynthesis of the H-2Ld class I major histocompatibility complex heavy chain promotes proper disulfide bond formation and stable peptide binding
    • Wang H., Capps G. G., Robinson B. E. and Zuniga M. C. (1994) Ab initio association with beta 2-microglobulin during biosynthesis of the H-2Ld class I major histocompatibility complex heavy chain promotes proper disulfide bond formation and stable peptide binding. J. Biol. Chem. 269: 22276-22281
    • (1994) J. Biol. Chem. , vol.269 , pp. 22276-22281
    • Wang, H.1    Capps, G.G.2    Robinson, B.E.3    Zuniga, M.C.4
  • 65
    • 0032076171 scopus 로고    scopus 로고
    • HLA-B27-restricted antigen presentation in the absence of tapasin reveals polymorphism in mechanisms of HLA class I peptide loading
    • Peh C. A., Burrows S. R., Barnden M., Khanna R., Cresswell P., Moss D. J. et al. (1998) HLA-B27-restricted antigen presentation in the absence of tapasin reveals polymorphism in mechanisms of HLA class I peptide loading. Immunity 8: 531-542
    • (1998) Immunity , vol.8 , pp. 531-542
    • Peh, C.A.1    Burrows, S.R.2    Barnden, M.3    Khanna, R.4    Cresswell, P.5    Moss, D.J.6
  • 66
    • 0026022577 scopus 로고
    • Participation of a novel 88-kD protein in the biogenesis of murine class I histocompatibility molecules
    • Degen E. and Williams D. B. (1991) Participation of a novel 88-kD 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
  • 67
    • 0034686044 scopus 로고    scopus 로고
    • The role of ERp57 in disulfide bond formation during the assembly of major histocompatibility complex class I in a synchronized semipermeabilized cell translation system
    • Farmery M. R., Allen S., Allen A. J. and Bulleid N. J. (2000) The role of ERp57 in disulfide bond formation during the assembly of major histocompatibility complex class I in a synchronized semipermeabilized cell translation system. J. Biol. Chem. 275: 14933-14938
    • (2000) J. Biol. Chem. , vol.275 , pp. 14933-14938
    • Farmery, M.R.1    Allen, S.2    Allen, A.J.3    Bulleid, N.J.4
  • 68
    • 0036166431 scopus 로고    scopus 로고
    • Disulfide bond isomerization and the assembly of MHC class I-peptide complexes
    • Dick T. P., Bangia N., Peaper D. R. and Cresswell P. (2002) Disulfide bond isomerization and the assembly of MHC class I-peptide complexes. Immunity 16: 87-98
    • (2002) Immunity , vol.16 , pp. 87-98
    • Dick, T.P.1    Bangia, N.2    Peaper, D.R.3    Cresswell, P.4
  • 69
    • 0035378323 scopus 로고    scopus 로고
    • ER60/ERp57 forms disulfide-bonded intermediates with MHC class I heavy chain
    • Lindquist J. A., Hammerling G. J. and Trowsdale J. (2001) ER60/ERp57 forms disulfide-bonded intermediates with MHC class I heavy chain. FASEB J. 15: 1448-1450
    • (2001) FASEB J. , vol.15 , pp. 1448-1450
    • Lindquist, J.A.1    Hammerling, G.J.2    Trowsdale, J.3
  • 70
    • 2242469355 scopus 로고    scopus 로고
    • Identification of specific glycoforms of major histocompatibility complex class I heavy chains suggests that class I peptide loading is an adaptation of the quality control pathway involving calreticulin and ERp57
    • Radcliffe C. M., Diedrich G., Harvey D. J., Dwek R. A., Cresswell P. and Rudd P. M. (2002) Identification of specific glycoforms of major histocompatibility complex class I heavy chains suggests that class I peptide loading is an adaptation of the quality control pathway involving calreticulin and ERp57. J. Biol. Chem 277: 46415-46423
    • (2002) J. Biol. Chem , vol.277 , pp. 46415-46423
    • Radcliffe, C.M.1    Diedrich, G.2    Harvey, D.J.3    Dwek, R.A.4    Cresswell, P.5    Rudd, P.M.6
  • 72
    • 0026695747 scopus 로고
    • Ligand-dependent secretion of rat retinol-binding protein expressed in HeLa cells
    • Melhus H., Laurent B., Rask L. and Peterson P. A. (1992) Ligand-dependent secretion of rat retinol-binding protein expressed in HeLa cells. J. Biol. Chem. 267: 12036-12041
    • (1992) J. Biol. Chem. , vol.267 , pp. 12036-12041
    • Melhus, H.1    Laurent, B.2    Rask, L.3    Peterson, P.A.4
  • 73
    • 0026720053 scopus 로고
    • Regulation of plasma retinol binding protein secretion in human HepG2 cells
    • Tosetti F., Ferrari N., Pfeffer U., Brigati C. and Vidali G. (1992) Regulation of plasma retinol binding protein secretion in human HepG2 cells. Exp. Cell Res. 200: 467-472
    • (1992) Exp. Cell Res. , vol.200 , pp. 467-472
    • Tosetti, F.1    Ferrari, N.2    Pfeffer, U.3    Brigati, C.4    Vidali, G.5
  • 74
    • 0030022473 scopus 로고    scopus 로고
    • Retinol binding protein and transthyretin are secreted as a complex formed in the endoplasmic reticulum in HepG2 human hepatocarcinoma cells
    • Bellovino D., Morimoto T., Tosetti F. and Gaetani S. (1996) Retinol binding protein and transthyretin are secreted as a complex formed in the endoplasmic reticulum in HepG2 human hepatocarcinoma cells. Exp. Cell Res. 222: 77-83
    • (1996) Exp. Cell Res. , vol.222 , pp. 77-83
    • Bellovino, D.1    Morimoto, T.2    Tosetti, F.3    Gaetani, S.4
  • 75
    • 0037245727 scopus 로고    scopus 로고
    • N-linked glycans direct the cotranslational folding pathway of influenza hemagglutinin
    • Daniels R., Kurowski B., Johnson A. E. and Hebert D. N. (2003) N-linked glycans direct the cotranslational folding pathway of influenza hemagglutinin. Mol. Cell. 11: 79-90
    • (2003) Mol. Cell. , vol.11 , pp. 79-90
    • Daniels, R.1    Kurowski, B.2    Johnson, A.E.3    Hebert, D.N.4


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