메뉴 건너뛰기




Volumn 24, Issue , 2008, Pages 343-368

Regulation of MHC class I assembly and peptide binding

Author keywords

Antigen processing; ERp57; Glycoprotein folding; Tapasin

Indexed keywords

CALNEXIN; CALRETICULIN; CHAPERONE; GLYCOPROTEIN; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; OXIDOREDUCTASE; PROTEIN DISULFIDE ISOMERASE; PROTEIN P57; TAPASIN;

EID: 55849088319     PISSN: 10810706     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.cellbio.24.110707.175347     Document Type: Review
Times cited : (167)

References (161)
  • 1
    • 4544336851 scopus 로고    scopus 로고
    • The ABCs of immunology: Structure and function of TAP, the transporter associated with antigen processing
    • Abele R, Tampe R. 2004. The ABCs of immunology: structure and function of TAP, the transporter associated with antigen processing. Physiology 19:216-24
    • (2004) Physiology , vol.19 , pp. 216-224
    • Abele, R.1    Tampe, R.2
  • 2
    • 0037013950 scopus 로고    scopus 로고
    • The oxidoreductase ERp57 efficiently reduces partially folded in preference to fully folded MHC class I molecules
    • Antoniou AN, Ford S, Alphey M, Osborne A, Elliott T, Powis SJ. 2002. The oxidoreductase ERp57 efficiently reduces partially folded in preference to fully folded MHC class I molecules. EMBO J. 21:2655-63
    • (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
  • 3
    • 0041761701 scopus 로고    scopus 로고
    • Characterization of the ERp57-Tapasin complex by rapid cellular acidification and thiol modification
    • Antoniou AN, Powis SJ. 2003. Characterization of the ERp57-Tapasin complex by rapid cellular acidification and thiol modification. Antioxid. Redox Signal. 5:375-79
    • (2003) Antioxid. Redox Signal , vol.5 , pp. 375-379
    • Antoniou, A.N.1    Powis, S.J.2
  • 5
    • 34247572423 scopus 로고    scopus 로고
    • ERp57 interacts with conserved cysteine residues in the MHC class I peptide-binding groove
    • Antoniou AN, Santos SG, Campbell EC, Lynch S, Arosa FA, Powis SJ. 2007. ERp57 interacts with conserved cysteine residues in the MHC class I peptide-binding groove. FEBS Lett. 581:1988-92
    • (2007) FEBS Lett , vol.581 , pp. 1988-1992
    • Antoniou, A.N.1    Santos, S.G.2    Campbell, E.C.3    Lynch, S.4    Arosa, F.A.5    Powis, S.J.6
  • 6
    • 0032754473 scopus 로고    scopus 로고
    • On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database
    • Apweiler R, Hermjakob H, Sharon N. 1999. On the frequency of protein glycosylation, as deduced from analysis of the SWISS-PROT database. Biochim. Biophys. Acta 1473:4-8
    • (1999) Biochim. Biophys. Acta , vol.1473 , pp. 4-8
    • Apweiler, R.1    Hermjakob, H.2    Sharon, N.3
  • 7
    • 0033060098 scopus 로고    scopus 로고
    • The N-terminal region of tapasin is required to stabilize the MHC class I loading complex
    • Bangia N, Lehner PJ, Hughes EA, Surman M, Cresswell P. 1999. The N-terminal region of tapasin is required to stabilize the MHC class I loading complex. Eur. J. Immunol. 29:1858-70
    • (1999) Eur. J. Immunol , vol.29 , pp. 1858-1870
    • Bangia, N.1    Lehner, P.J.2    Hughes, E.A.3    Surman, M.4    Cresswell, P.5
  • 8
    • 0035723840 scopus 로고    scopus 로고
    • The quantity of naturally processed peptides stably bound by HLA-A*0201 is significantly reduced in the absence of tapasin
    • Barber LD, Howarth M, Bowness P, Elliott T. 2001. The quantity of naturally processed peptides stably bound by HLA-A*0201 is significantly reduced in the absence of tapasin. Tissue Antigens 58:363-68
    • (2001) Tissue Antigens , vol.58 , pp. 363-368
    • Barber, L.D.1    Howarth, M.2    Bowness, P.3    Elliott, T.4
  • 9
    • 0034235461 scopus 로고    scopus 로고
    • Tapasin-mediated retention and optimization of peptide ligands during the assembly of class I molecules
    • Barnden MJ, Purcell AW, Gorman JJ, McCluskey J. 2000. Tapasin-mediated retention and optimization of peptide ligands during the assembly of class I molecules. J. Immunol. 165:322-30
    • (2000) J. Immunol , vol.165 , pp. 322-330
    • Barnden, M.J.1    Purcell, A.W.2    Gorman, J.J.3    McCluskey, J.4
  • 10
    • 0034282738 scopus 로고    scopus 로고
    • The CXXCXXC motif determines the folding, structure and stability of human Ero1-Lα
    • Benham AM, Cabibbo A, Fassio A, Bulleid N, Sitia R, Braakman I. 2000. The CXXCXXC motif determines the folding, structure and stability of human Ero1-Lα. EMBO J. 19:4493-502
    • (2000) EMBO J , vol.19 , pp. 4493-4502
    • Benham, A.M.1    Cabibbo, A.2    Fassio, A.3    Bulleid, N.4    Sitia, R.5    Braakman, I.6
  • 11
    • 0034681340 scopus 로고    scopus 로고
    • ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum
    • Cabibbo A, Pagani M, Fabbri M, Rocchi M, Farmery MR, et al. 2000. ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum. J. Biol. Chem. 275:4827-33
    • (2000) J. Biol. Chem , vol.275 , pp. 4827-4833
    • Cabibbo, A.1    Pagani, M.2    Fabbri, M.3    Rocchi, M.4    Farmery, M.R.5
  • 12
    • 0037422614 scopus 로고    scopus 로고
    • UDP-Glc:glycoprotein glucosyltransferase recognizes structured and solvent accessible hydrophobic patches in molten globule-like folding intermediates
    • Caramelo JJ, Castro OA, Alonso LG, De Prat-Gay G, Parodi AJ. 2003. UDP-Glc:glycoprotein glucosyltransferase recognizes structured and solvent accessible hydrophobic patches in molten globule-like folding intermediates. Proc. Natl. Acad. Sci. USA 100:86-91
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 86-91
    • Caramelo, J.J.1    Castro, O.A.2    Alonso, L.G.3    De Prat-Gay, G.4    Parodi, A.J.5
  • 13
    • 0035873704 scopus 로고    scopus 로고
    • 26S proteasomes and immunoproteasomes produce mainly N-extended versions of an antigenic peptide
    • Cascio P, Hilton C, Kisselev AF, Rock KL, Goldberg AL. 2001. 26S proteasomes and immunoproteasomes produce mainly N-extended versions of an antigenic peptide. EMBO J. 20:2357-66
    • (2001) EMBO J , vol.20 , pp. 2357-2366
    • Cascio, P.1    Hilton, C.2    Kisselev, A.F.3    Rock, K.L.4    Goldberg, A.L.5
  • 14
    • 38349107628 scopus 로고    scopus 로고
    • Formation of a major histocompatibility complex class I tapasin disulfide indicates a change in spatial organization of the peptide-loading complex during assembly
    • Chambers JE, Jessop CE, Bulleid NJ. 2008. Formation of a major histocompatibility complex class I tapasin disulfide indicates a change in spatial organization of the peptide-loading complex during assembly. J. Biol. Chem. 283:1862-69
    • (2008) J. Biol. Chem , vol.283 , pp. 1862-1869
    • Chambers, J.E.1    Jessop, C.E.2    Bulleid, N.J.3
  • 15
    • 28044456942 scopus 로고    scopus 로고
    • The ER aminopeptidase, ERAP1, trims precursors to lengths of MHC class I peptides by a "molecular ruler" mechanism
    • Chang SC, Momburg F, Bhutani N, Goldberg AL. 2005. The ER aminopeptidase, ERAP1, trims precursors to lengths of MHC class I peptides by a "molecular ruler" mechanism. Proc. Natl. Acad. Sci. USA 102:17107-12
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 17107-17112
    • Chang, S.C.1    Momburg, F.2    Bhutani, N.3    Goldberg, A.L.4
  • 16
    • 33947606283 scopus 로고    scopus 로고
    • Analysis of interactions in a tapasin/class I complex provides a mechanism for peptide selection
    • Chen M, Bouvier M. 2007. Analysis of interactions in a tapasin/class I complex provides a mechanism for peptide selection. EMBO J. 26:1681-90
    • (2007) EMBO J , vol.26 , pp. 1681-1690
    • Chen, M.1    Bouvier, M.2
  • 17
    • 2242427111 scopus 로고    scopus 로고
    • A characterization of the lumenal region of human tapasin reveals the presence of two structural domains
    • Chen M, Stafford WF, Diedrich G, Khan A, Bouvier M. 2002. A characterization of the lumenal region of human tapasin reveals the presence of two structural domains. Biochemistry 41:14539-45
    • (2002) Biochemistry , vol.41 , pp. 14539-14545
    • Chen, M.1    Stafford, W.F.2    Diedrich, G.3    Khan, A.4    Bouvier, M.5
  • 18
    • 0037245727 scopus 로고    scopus 로고
    • N-linked glycans direct the cotranslational folding pathway of influenza hemagglutinin
    • Daniels R, Kurowski B, Johnson AE, Hebert DN. 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
  • 19
    • 0029590754 scopus 로고
    • Characterization of the active site cysteine residues of the thioredoxin-like domains of protein disulfide isomerase
    • Darby NJ, Creighton TE. 1995. Characterization of the active site cysteine residues of the thioredoxin-like domains of protein disulfide isomerase. Biochemistry 34:16770-80
    • (1995) Biochemistry , vol.34 , pp. 16770-16780
    • Darby, N.J.1    Creighton, T.E.2
  • 20
    • 0029058494 scopus 로고
    • Refolding of bovine pancreatic trypsin inhibitor via non-native disulphide intermediates
    • Darby NJ, Morin PE, Talbo G, Creighton TE. 1995. Refolding of bovine pancreatic trypsin inhibitor via non-native disulphide intermediates. J. Mol. Biol. 249:463-77
    • (1995) J. Mol. Biol , vol.249 , pp. 463-477
    • Darby, N.J.1    Morin, P.E.2    Talbo, G.3    Creighton, T.E.4
  • 21
    • 1642334894 scopus 로고    scopus 로고
    • Assembly of MHC class I peptide complexes from the perspective of disulfide bond formation
    • Dick TB. 2004. Assembly of MHC class I peptide complexes from the perspective of disulfide bond formation. Cell. Mol. Life Sci. 61:547-56
    • (2004) Cell. Mol. Life Sci , vol.61 , pp. 547-556
    • Dick, T.B.1
  • 22
    • 0036166431 scopus 로고    scopus 로고
    • Disulfide bond isomerization and the assembly of MHC class I-peptide complexes
    • Dick TP, Bangia N, Peaper DR, 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
  • 23
    • 0036371484 scopus 로고    scopus 로고
    • Thiol oxidation and reduction in major histocompatibility complex class I-restricted antigen processing and presentation
    • Dick TP, 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
  • 24
    • 0035253721 scopus 로고    scopus 로고
    • A role for calnexin in the assembly of the MHC class I loading complex in the endoplasmic reticulum
    • Diedrich G, Bangia N, Pan M, Cresswell P. 2001. A role for calnexin in the assembly of the MHC class I loading complex in the endoplasmic reticulum. J. Immunol. 166:1703-9
    • (2001) J. Immunol , vol.166 , pp. 1703-1709
    • Diedrich, G.1    Bangia, N.2    Pan, M.3    Cresswell, P.4
  • 25
    • 0025971498 scopus 로고
    • Lack of HLA class I antigen expression by cultured melanoma cells FO-1 due to a defect in B2m gene expression
    • D'Urso CM, Wang ZG, Cao Y, Tatake R, Zeff RA, Ferrone S. 1991. Lack of HLA class I antigen expression by cultured melanoma cells FO-1 due to a defect in B2m gene expression. J. Clin. Investig. 87:284-92
    • (1991) J. Clin. Investig , vol.87 , pp. 284-292
    • D'Urso, C.M.1    Wang, Z.G.2    Cao, Y.3    Tatake, R.4    Zeff, R.A.5    Ferrone, S.6
  • 26
    • 0036387164 scopus 로고    scopus 로고
    • NMR structures of 36 and 73-residue fragments of the calreticulin P-domain
    • Ellgaard L, Bettendorff P, Braun D, Herrmann T, Fiorito F, et al. 2002. NMR structures of 36 and 73-residue fragments of the calreticulin P-domain. J. Mol. Biol. 322:773-84
    • (2002) J. Mol. Biol , vol.322 , pp. 773-784
    • Ellgaard, L.1    Bettendorff, P.2    Braun, D.3    Herrmann, T.4    Fiorito, F.5
  • 27
    • 2442629457 scopus 로고    scopus 로고
    • Calnexin, calreticulin, and ERp57: Teammates in glycoprotein folding
    • Ellgaard L, Frickel EM. 2003. Calnexin, calreticulin, and ERp57: teammates in glycoprotein folding. Cell. Biochem. Biophys. 39:223-47
    • (2003) Cell. Biochem. Biophys , vol.39 , pp. 223-247
    • Ellgaard, L.1    Frickel, E.M.2
  • 28
    • 0035846853 scopus 로고    scopus 로고
    • Three-dimensional structure topology of the calreticulin P-domain based on NMR assignment
    • Ellgaard L, Riek R, Braun D, Herrmann T, Helenius A, Wuthrich K. 2001a. Three-dimensional structure topology of the calreticulin P-domain based on NMR assignment. FEBS Lett. 488:69-73
    • (2001) FEBS Lett , vol.488 , pp. 69-73
    • Ellgaard, L.1    Riek, R.2    Braun, D.3    Herrmann, T.4    Helenius, A.5    Wuthrich, K.6
  • 30
    • 0024819297 scopus 로고
    • Molecular cloning of the high affinity calcium-binding protein (calreticulin) of skeletal muscle sarcoplasmic reticulum
    • Fliegel L, Burns K, MacLennan DH, Reithmeier RA, Michalak M. 1989. Molecular cloning of the high affinity calcium-binding protein (calreticulin) of skeletal muscle sarcoplasmic reticulum. J. Biol. Chem. 264:21522-28
    • (1989) J. Biol. Chem , vol.264 , pp. 21522-21528
    • Fliegel, L.1    Burns, K.2    MacLennan, D.H.3    Reithmeier, R.A.4    Michalak, M.5
  • 31
    • 33745265260 scopus 로고    scopus 로고
    • Protein disulfide isomerase-like proteins play opposing roles during retrotranslocation
    • Forster ML, Sivick K, Park YN, Arvan P, Lencer WI, Tsai B. 2006. Protein disulfide isomerase-like proteins play opposing roles during retrotranslocation. J. Cell. Biol. 173:853-59
    • (2006) J. Cell. Biol , vol.173 , pp. 853-859
    • Forster, M.L.1    Sivick, K.2    Park, Y.N.3    Arvan, P.4    Lencer, W.I.5    Tsai, B.6
  • 32
    • 0031609760 scopus 로고    scopus 로고
    • The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum
    • Frand AR, Kaiser CA. 1998. The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum. Mol. Cell 1:161-70
    • (1998) Mol. Cell , vol.1 , pp. 161-170
    • Frand, A.R.1    Kaiser, C.A.2
  • 33
    • 0033213605 scopus 로고    scopus 로고
    • Ero1p oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulum
    • Frand AR, Kaiser CA. 1999. Ero1p oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulum. Mol. Cell 4:469-77
    • (1999) Mol. Cell , vol.4 , pp. 469-477
    • Frand, A.R.1    Kaiser, C.A.2
  • 37
    • 0036169941 scopus 로고    scopus 로고
    • Assembly and antigen-presenting function of MHC class I molecules in cells lacking the ER chaperone calreticulin
    • Gao B, Adhikari R, Howarth M, Nakamura K, Gold MC, et al. 2002. Assembly and antigen-presenting function of MHC class I molecules in cells lacking the ER chaperone calreticulin. Immunity 16:99-109
    • (2002) Immunity , vol.16 , pp. 99-109
    • Gao, B.1    Adhikari, R.2    Howarth, M.3    Nakamura, K.4    Gold, M.C.5
  • 38
    • 0034279712 scopus 로고    scopus 로고
    • Impaired immune responses and altered peptide repertoire in tapasin-deficient mice
    • Garbi N, Tan P, Diehl AD, Chambers BJ, Ljunggren HG, et al. 2000. Impaired immune responses and altered peptide repertoire in tapasin-deficient mice. Nat. Immunol. 1:234-38
    • (2000) Nat. Immunol , vol.1 , pp. 234-238
    • Garbi, N.1    Tan, P.2    Diehl, A.D.3    Chambers, B.J.4    Ljunggren, H.G.5
  • 39
    • 29244474572 scopus 로고    scopus 로고
    • Impaired assembly of the major histocompatibility complex class I peptide-loading complex in mice deficient in the oxidoreductase ERp57
    • Garbi N, Tanaka S, Momburg F, Hammerling GJ. 2006. Impaired assembly of the major histocompatibility complex class I peptide-loading complex in mice deficient in the oxidoreductase ERp57. Nat. Immunol. 7:93-102
    • (2006) Nat. Immunol , vol.7 , pp. 93-102
    • Garbi, N.1    Tanaka, S.2    Momburg, F.3    Hammerling, G.J.4
  • 40
    • 0037261366 scopus 로고    scopus 로고
    • A major role for tapasin as a stabilizer of the TAP peptide transporter and consequences for MHC class I expression
    • Garbi N, Tiwari N, Momburg F, Hammerling GJ. 2003. A major role for tapasin as a stabilizer of the TAP peptide transporter and consequences for MHC class I expression. Eur. J. Immunol. 33:264-73
    • (2003) Eur. J. Immunol , vol.33 , pp. 264-273
    • Garbi, N.1    Tiwari, N.2    Momburg, F.3    Hammerling, G.J.4
  • 41
    • 0033681184 scopus 로고    scopus 로고
    • Impaired assembly yet normal trafficking of MHC class I molecules in Tapasin mutant mice
    • Grandea AG 3rd, Golovina TN, Hamilton SE, Sriram V, Spies T, et al. 2000. Impaired assembly yet normal trafficking of MHC class I molecules in Tapasin mutant mice. Immunity 13:213-22
    • (2000) Immunity , vol.13 , pp. 213-222
    • Grandea 3rd, A.G.1    Golovina, T.N.2    Hamilton, S.E.3    Sriram, V.4    Spies, T.5
  • 42
    • 0027988164 scopus 로고
    • Novel allele-specific, post-translational reduction in HLA class I expression in a mutant human B cell line
    • Greenwood R, Shimizu Y, Sekhon GS, DeMars R. 1994. Novel allele-specific, post-translational reduction in HLA class I expression in a mutant human B cell line. J. Immunol. 153:5525-36
    • (1994) J. Immunol , vol.153 , pp. 5525-5536
    • Greenwood, R.1    Shimizu, Y.2    Sekhon, G.S.3    DeMars, R.4
  • 43
    • 29244461714 scopus 로고    scopus 로고
    • The aminopeptidase ERAAP shapes the peptide repertoire displayed by major histocompatibility complex class I molecules
    • Hammer GE, Gonzalez F, Champsaur M, Cado D, Shastri N. 2006. The aminopeptidase ERAAP shapes the peptide repertoire displayed by major histocompatibility complex class I molecules. Nat. Immunol. 7:103-12
    • (2006) Nat. Immunol , vol.7 , pp. 103-112
    • Hammer, G.E.1    Gonzalez, F.2    Champsaur, M.3    Cado, D.4    Shastri, N.5
  • 44
    • 33846988640 scopus 로고    scopus 로고
    • In the absence of aminopeptidase ERAAP, MHC class I molecules present many unstable and highly immunogenic peptides
    • Hammer GE, Gonzalez F, James E, Nolla H, Shastri N. 2007. In the absence of aminopeptidase ERAAP, MHC class I molecules present many unstable and highly immunogenic peptides. Nat. Immunol. 8:101-8
    • (2007) Nat. Immunol , vol.8 , pp. 101-108
    • Hammer, G.E.1    Gonzalez, F.2    James, E.3    Nolla, H.4    Shastri, N.5
  • 45
    • 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. Proc. Natl. Acad. Sci. USA 91:913-17
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 913-917
    • Hammond, C.1    Braakman, I.2    Helenius, A.3
  • 46
    • 0028076031 scopus 로고
    • Folding of VSV G protein: Sequential interaction with BiP and calnexin
    • Hammond C, Helenius A. 1994. Folding of VSV G protein: sequential interaction with BiP and calnexin. Science 266:456-58
    • (1994) Science , vol.266 , pp. 456-458
    • Hammond, C.1    Helenius, A.2
  • 47
    • 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 MR, Lybarger L, Yu YY, Myers NB, Hansen TH. 2001. Association of ERp57 with mouse MHC class I molecules is tapasin dependent and mimics that of calreticulin and not calnexin. J. Immunol. 166:6686-92
    • (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
  • 48
    • 0029024748 scopus 로고
    • Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulum
    • Hebert DN, Foellmer B, Helenius A. 1995. Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulum. Cell 81:425-33
    • (1995) Cell , vol.81 , pp. 425-433
    • Hebert, D.N.1    Foellmer, B.2    Helenius, A.3
  • 49
    • 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 J. 15:2961-68
    • (1996) EMBO J , vol.15 , pp. 2961-2968
    • Hebert, D.N.1    Foellmer, B.2    Helenius, A.3
  • 50
    • 3943059566 scopus 로고    scopus 로고
    • Roles of N-linked glycans in the endoplasmic reticulum
    • Helenius A, Aebi M. 2004. Roles of N-linked glycans in the endoplasmic reticulum. Annu. Rev. Biochem. 73:1019-49
    • (2004) Annu. Rev. Biochem , vol.73 , pp. 1019-1049
    • Helenius, A.1    Aebi, M.2
  • 51
    • 4143051423 scopus 로고    scopus 로고
    • Tapasin enhances MHC class I peptide presentation according to peptide half-life
    • Howarth M, Williams A, Tolstrup AB, Elliott T. 2004. Tapasin enhances MHC class I peptide presentation according to peptide half-life. Proc. Natl. Acad. Sci. USA 101:11737-42
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 11737-11742
    • Howarth, M.1    Williams, A.2    Tolstrup, A.B.3    Elliott, T.4
  • 52
    • 0032482384 scopus 로고    scopus 로고
    • The thiol oxidoreductase ERp57 is a component of the MHC class I peptide-loading complex
    • Hughes EA, Cresswell P. 1998. The thiol oxidoreductase ERp57 is a component of the MHC class I peptide-loading complex. Curr. Biol. 8:709-12
    • (1998) Curr. Biol , vol.8 , pp. 709-712
    • Hughes, E.A.1    Cresswell, P.2
  • 53
    • 0029965803 scopus 로고    scopus 로고
    • The protease inhibitor, N-acetyl-L-leucyl-L-leucyl-leucyl-L-norleucinal, decreases the pool of major histocompatibility complex class I-binding peptides and inhibits peptide trimming in the endoplasmic reticulum
    • Hughes EA, Ortmann B, Surman M, Cresswell P. 1996. The protease inhibitor, N-acetyl-L-leucyl-L-leucyl-leucyl-L-norleucinal, decreases the pool of major histocompatibility complex class I-binding peptides and inhibits peptide trimming in the endoplasmic reticulum. J. Exp. Med. 183:1569-78
    • (1996) J. Exp. Med , vol.183 , pp. 1569-1578
    • Hughes, E.A.1    Ortmann, B.2    Surman, M.3    Cresswell, P.4
  • 54
    • 0026698060 scopus 로고
    • Oxidized redox state of glutathione in the endoplasmic reticulum
    • Hwang C, Sinskey AJ, Lodish HF. 1992. Oxidized redox state of glutathione in the endoplasmic reticulum. Science 257:1496-502
    • (1992) Science , vol.257 , pp. 1496-1502
    • Hwang, C.1    Sinskey, A.J.2    Lodish, H.F.3
  • 55
    • 0028181429 scopus 로고
    • Regulation of MHC class I transport by the molecular chaperone, calnexin (p88, IP90)
    • Jackson MR, Cohen-Doyle MF, Peterson PA, Williams DB. 1994. Regulation of MHC class I transport by the molecular chaperone, calnexin (p88, IP90). Science 263:384-87
    • (1994) Science , vol.263 , pp. 384-387
    • Jackson, M.R.1    Cohen-Doyle, M.F.2    Peterson, P.A.3    Williams, D.B.4
  • 56
    • 11244319355 scopus 로고    scopus 로고
    • Glutathione directly reduces an oxidoreductase in the endoplasmic reticulum of mammalian cells
    • Jessop CE, Bulleid NJ. 2004. Glutathione directly reduces an oxidoreductase in the endoplasmic reticulum of mammalian cells. J. Biol. Chem. 279:55341-47
    • (2004) J. Biol. Chem , vol.279 , pp. 55341-55347
    • Jessop, C.E.1    Bulleid, N.J.2
  • 57
  • 58
    • 33846233912 scopus 로고    scopus 로고
    • ERAAP synergizes with MHC class I molecules to make the final cut in the antigenic peptide precursors in the endoplasmic reticulum
    • Kanaseki T, Blanchard N, Hammer GE, Gonzalez F, Shastri N. 2006. ERAAP synergizes with MHC class I molecules to make the final cut in the antigenic peptide precursors in the endoplasmic reticulum. Immunity 25:795-806
    • (2006) Immunity , vol.25 , pp. 795-806
    • Kanaseki, T.1    Blanchard, N.2    Hammer, G.E.3    Gonzalez, F.4    Shastri, N.5
  • 59
    • 0037160108 scopus 로고    scopus 로고
    • Calnexin, calreticulin, and ERp57 cooperate in disulfide bond formation in human CD1d heavy chain
    • Kang SJ, Cresswell P. 2002. Calnexin, calreticulin, and ERp57 cooperate in disulfide bond formation in human CD1d heavy chain. J. Biol. Chem. 277:44838-44
    • (2002) J. Biol. Chem , vol.277 , pp. 44838-44844
    • Kang, S.J.1    Cresswell, P.2
  • 60
    • 0032479290 scopus 로고    scopus 로고
    • Inhibition of glucose trimming with castanospermine reduces calnexin association and promotes proteasome degradation of the α-subunit of the nicotinic acetylcholine receptor
    • Keller SH, Lindstrom J, Taylor P. 1998. Inhibition of glucose trimming with castanospermine reduces calnexin association and promotes proteasome degradation of the α-subunit of the nicotinic acetylcholine receptor. J. Biol. Chem. 273:17064-72
    • (1998) J. Biol. Chem , vol.273 , pp. 17064-17072
    • Keller, S.H.1    Lindstrom, J.2    Taylor, P.3
  • 61
    • 34547092165 scopus 로고    scopus 로고
    • Redox regulation of peptide receptivity of major histocompatibility complex class I molecules by ERp57 and tapasin
    • Kienast A, Preuss M, Winkler M, Dick TP. 2007. Redox regulation of peptide receptivity of major histocompatibility complex class I molecules by ERp57 and tapasin. Nat. Immunol. 8:864-72
    • (2007) Nat. Immunol , vol.8 , pp. 864-872
    • Kienast, A.1    Preuss, M.2    Winkler, M.3    Dick, T.P.4
  • 62
    • 0032481380 scopus 로고    scopus 로고
    • The b′ domain provides the principal peptide-binding site of protein disulfide isomerase but all domains contribute to binding of misfolded proteins
    • Klappa P, Ruddock LW, Darby NJ, Freedman RB. 1998. The b′ domain provides the principal peptide-binding site of protein disulfide isomerase but all domains contribute to binding of misfolded proteins. EMBO J. 17:927-35
    • (1998) EMBO J , vol.17 , pp. 927-935
    • Klappa, P.1    Ruddock, L.W.2    Darby, N.J.3    Freedman, R.B.4
  • 63
    • 3142587059 scopus 로고    scopus 로고
    • Protein folding and quality control in the endoplasmic reticulum
    • Kleizen B, Braakman I. 2004. Protein folding and quality control in the endoplasmic reticulum. Curr. Opin. Cell Biol. 16:343-49
    • (2004) Curr. Opin. Cell Biol , vol.16 , pp. 343-349
    • Kleizen, B.1    Braakman, I.2
  • 64
    • 1642290656 scopus 로고    scopus 로고
    • Functional dissection of the transmembrane domains of the transporter associated with antigen processing (TAP)
    • Koch J, Guntrum R, Heintke S, Kyritsis C, Tampe R. 2004. Functional dissection of the transmembrane domains of the transporter associated with antigen processing (TAP). J. Biol. Chem. 279:10142-47
    • (2004) J. Biol. Chem , vol.279 , pp. 10142-10147
    • Koch, J.1    Guntrum, R.2    Heintke, S.3    Kyritsis, C.4    Tampe, R.5
  • 65
    • 33746822999 scopus 로고    scopus 로고
    • Crystal structure of the bb′ domains of the protein disulfide isomerase ERp57
    • Kozlov G, Maattanen P, Schrag JD, Pollock S, Cygler M, et al. 2006. Crystal structure of the bb′ domains of the protein disulfide isomerase ERp57. Structure 14:1331-39
    • (2006) Structure , vol.14 , pp. 1331-1339
    • Kozlov, G.1    Maattanen, P.2    Schrag, J.D.3    Pollock, S.4    Cygler, M.5
  • 66
    • 33644868738 scopus 로고    scopus 로고
    • Domain architecture of protein-disulfide isomerase facilitates its dual role as an oxidase and an isomerase in Ero1p-mediated disulfide formation
    • Kulp MS, Frickel EM, Ellgaard L, Weissman JS. 2006. Domain architecture of protein-disulfide isomerase facilitates its dual role as an oxidase and an isomerase in Ero1p-mediated disulfide formation. J. Biol. Chem. 281:876-84
    • (2006) J. Biol. Chem , vol.281 , pp. 876-884
    • Kulp, M.S.1    Frickel, E.M.2    Ellgaard, L.3    Weissman, J.S.4
  • 67
    • 0028885790 scopus 로고
    • The essential function of protein-disulfide isomerase is to unscramble non-native disulfide bonds
    • Laboissiere MC, Sturley SL, Raines RT. 1995. The essential function of protein-disulfide isomerase is to unscramble non-native disulfide bonds. J. Biol. Chem. 270:28006-9
    • (1995) J. Biol. Chem , vol.270 , pp. 28006-28009
    • Laboissiere, M.C.1    Sturley, S.L.2    Raines, R.T.3
  • 68
    • 0029085605 scopus 로고
    • Retention of glucose units added by the UDP-GLC:glycoprotein glucosyltransferase delays exit of glycoproteins from the reticulum
    • Labriola C, Cazzulo JJ, Parodi AJ. 1995. Retention of glucose units added by the UDP-GLC:glycoprotein glucosyltransferase delays exit of glycoproteins from the reticulum. J. Cell Biol. 130:771-79
    • (1995) J. Cell Biol , vol.130 , pp. 771-779
    • Labriola, C.1    Cazzulo, J.J.2    Parodi, A.J.3
  • 69
    • 33750320380 scopus 로고    scopus 로고
    • Bap31 enhances the endoplasmic reticulum export and quality control of human class I MHC molecules
    • Ladasky JJ, Boyle S, Seth M, Li H, Pentcheva T, et al. 2006. Bap31 enhances the endoplasmic reticulum export and quality control of human class I MHC molecules. J. Immunol. 177:6172-81
    • (2006) J. Immunol , vol.177 , pp. 6172-6181
    • Ladasky, J.J.1    Boyle, S.2    Seth, M.3    Li, H.4    Pentcheva, T.5
  • 70
    • 0037119465 scopus 로고    scopus 로고
    • Localization of the lectin, ERp57 binding, and polypeptide binding sites of calnexin and calreticulin
    • Leach MR, Cohen-Doyle MF, Thomas DY, Williams DB. 2002. Localization of the lectin, ERp57 binding, and polypeptide binding sites of calnexin and calreticulin. J. Biol. Chem. 277:29686-97
    • (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
  • 71
    • 1542305433 scopus 로고    scopus 로고
    • Lectin-deficient calnexin is capable of binding class I histocompatibility molecules in vivo and preventing their degradation
    • Leach MR, Williams DB. 2004. Lectin-deficient calnexin is capable of binding class I histocompatibility molecules in vivo and preventing their degradation. J. Biol. Chem. 279:9072-79
    • (2004) J. Biol. Chem , vol.279 , pp. 9072-9079
    • Leach, M.R.1    Williams, D.B.2
  • 72
    • 0032005348 scopus 로고    scopus 로고
    • Soluble tapasin restores MHC class 1 expression and function in the tapasin-negative cell line .220
    • Lehner PJ, Surman MJ, Cresswell P. 1998. Soluble tapasin restores MHC class 1 expression and function in the tapasin-negative cell line .220. Immunity 8:221-31
    • (1998) Immunity , vol.8 , pp. 221-231
    • Lehner, P.J.1    Surman, M.J.2    Cresswell, P.3
  • 73
    • 26844477450 scopus 로고    scopus 로고
    • Critical role for the tapasin-docking site of TAP2 in the functional integrity of the MHC class I-peptide-loading complex
    • Leonhardt RM, Keusekotten K, Bekpen C, Knittler MR. 2005. Critical role for the tapasin-docking site of TAP2 in the functional integrity of the MHC class I-peptide-loading complex. J. Immunol. 175:5104-14
    • (2005) J. Immunol , vol.175 , pp. 5104-5114
    • Leonhardt, R.M.1    Keusekotten, K.2    Bekpen, C.3    Knittler, M.R.4
  • 74
    • 0032482319 scopus 로고    scopus 로고
    • Evidence for successive peptide binding and quality control stages during MHC class I assembly
    • Lewis JW, Elliott T. 1998. Evidence for successive peptide binding and quality control stages during MHC class I assembly. Curr. Biol. 8:717-20
    • (1998) Curr. Biol , vol.8 , pp. 717-720
    • Lewis, J.W.1    Elliott, T.2
  • 75
    • 33646546083 scopus 로고    scopus 로고
    • Annular arrangement and collaborative actions of four domains of protein-disulfide isomerase: A small angle X-ray scattering study in solution
    • Li SJ, Hong XG, Shi YY, Li H, Wang CC. 2006. Annular arrangement and collaborative actions of four domains of protein-disulfide isomerase: a small angle X-ray scattering study in solution. J. Biol. Chem. 281:6581-88
    • (2006) J. Biol. Chem , vol.281 , pp. 6581-6588
    • Li, S.J.1    Hong, X.G.2    Shi, Y.Y.3    Li, H.4    Wang, C.C.5
  • 76
    • 0035378323 scopus 로고    scopus 로고
    • ER60/ERp57 forms disulfide-bonded intermediates with MHC class I heavy chain
    • Lindquist JA, Hammerling GJ, Trowsdale J. 2001. ER60/ERp57 forms disulfide-bonded intermediates with MHC class I heavy chain. FASEB J. 15:1448-50
    • (2001) FASEB J , vol.15 , pp. 1448-1450
    • Lindquist, J.A.1    Hammerling, G.J.2    Trowsdale, J.3
  • 77
    • 0032522392 scopus 로고    scopus 로고
    • ER-60, a chaperone with thiol-dependent reductase activity involved in MHC class I assembly
    • Lindquist JA, Jensen ON, Mann M, Hammerling GJ. 1998. ER-60, a chaperone with thiol-dependent reductase activity involved in MHC class I assembly. EMBO J. 17:2186-95
    • (1998) EMBO J , vol.17 , pp. 2186-2195
    • Lindquist, J.A.1    Jensen, O.N.2    Mann, M.3    Hammerling, G.J.4
  • 78
    • 4444318357 scopus 로고    scopus 로고
    • ER chaperone functions during normal and stress conditions
    • Ma Y, Hendershot LM. 2004. ER chaperone functions during normal and stress conditions. J. Chem. Neuroanat. 28:51-65
    • (2004) J. Chem. Neuroanat , vol.28 , pp. 51-65
    • Ma, Y.1    Hendershot, L.M.2
  • 79
    • 0033180470 scopus 로고    scopus 로고
    • Lateral diffusion of GFP-tagged H2Ld molecules and of GFP-TAP1 reports on the assembly and retention of these molecules in the endoplasmic reticulum
    • Marguet D, Spiliotis ET, Pentcheva T, Lebowitz M, Schneck J, Edidin M. 1999. Lateral diffusion of GFP-tagged H2Ld molecules and of GFP-TAP1 reports on the assembly and retention of these molecules in the endoplasmic reticulum. Immunity 11:231-40
    • (1999) Immunity , vol.11 , pp. 231-240
    • Marguet, D.1    Spiliotis, E.T.2    Pentcheva, T.3    Lebowitz, M.4    Schneck, J.5    Edidin, M.6
  • 80
    • 0036911213 scopus 로고    scopus 로고
    • A subset: Of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins
    • Meunier L, Usherwood YK, Chung KT, Hendershot LM. 2002. A subset: of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins. Mol. Biol. Cell 13:4456-69
    • (2002) Mol. Biol. Cell , vol.13 , pp. 4456-4469
    • Meunier, L.1    Usherwood, Y.K.2    Chung, K.T.3    Hendershot, L.M.4
  • 81
    • 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, Sitia R. 2001. Manipulation of oxidative protein folding and PDI redox state in mammalian cells. EMBO J. 20:6288-96
    • (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
  • 82
    • 0037470410 scopus 로고    scopus 로고
    • Role of EDEM in the release of misfolded glycoproteins from the calnexin cycle
    • Molinari M, Calanca V, Galli C, Lucca P, Paganetti P. 2003. Role of EDEM in the release of misfolded glycoproteins from the calnexin cycle. Science 299:1397-400
    • (2003) Science , vol.299 , pp. 1397-1400
    • Molinari, M.1    Calanca, V.2    Galli, C.3    Lucca, P.4    Paganetti, P.5
  • 83
    • 1342334746 scopus 로고    scopus 로고
    • Contrasting functions of calreticulin and calnexin in glycoprotein folding and ER quality control
    • Molinari M, Eriksson KK, Calanca V, Galli C, Cresswell P, et al. 2004. Contrasting functions of calreticulin and calnexin in glycoprotein folding and ER quality control. Mol. Cell 13:125-35
    • (2004) Mol. Cell , vol.13 , pp. 125-135
    • Molinari, M.1    Eriksson, K.K.2    Calanca, V.3    Galli, C.4    Cresswell, P.5
  • 84
    • 0033523910 scopus 로고    scopus 로고
    • Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells
    • Molinari M, 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
  • 85
    • 0034646876 scopus 로고    scopus 로고
    • Chaperone selection during glycoprotein translocation into the reticulum
    • Molinari M, Helenius A. 2000. Chaperone selection during glycoprotein translocation into the reticulum. Science 288:331-33
    • (2000) Science , vol.288 , pp. 331-333
    • Molinari, M.1    Helenius, A.2
  • 87
    • 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, Tan P. 2002. Tapasin - the keystone of the loading complex optimizing peptide binding by MHC class I molecules in the endoplasmic reticulum. Mol. Immunol. 39:217-33
    • (2002) Mol. Immunol , vol.39 , pp. 217-233
    • Momburg, F.1    Tan, P.2
  • 88
    • 0032482385 scopus 로고    scopus 로고
    • A role for the thiol-dependent reductase ERp57 in the assembly of MHC class I molecules
    • Morrice NA, Powis SJ. 1998. A role for the thiol-dependent reductase ERp57 in the assembly of MHC class I molecules. Curr. Biol. 8:713-16
    • (1998) Curr. Biol , vol.8 , pp. 713-716
    • Morrice, N.A.1    Powis, S.J.2
  • 89
    • 0028917887 scopus 로고
    • Species-specific differences in chaperone interaction of human and mouse major histocompatibility complex class I molecules
    • Nossner E, Parham P. 1995. Species-specific differences in chaperone interaction of human and mouse major histocompatibility complex class I molecules. J. Exp. Med. 181:327-37
    • (1995) J. Exp. Med , vol.181 , pp. 327-337
    • Nossner, E.1    Parham, P.2
  • 90
    • 0037470515 scopus 로고    scopus 로고
    • EDEM as an acceptor of terminally misfolded glycoproteins released from calnexin
    • Oda Y, Hosokawa N, Wada I, Nagata K. 2003. EDEM as an acceptor of terminally misfolded glycoproteins released from calnexin. Science 299:1394-97
    • (2003) Science , vol.299 , pp. 1394-1397
    • Oda, Y.1    Hosokawa, N.2    Wada, I.3    Nagata, K.4
  • 91
    • 0032807338 scopus 로고    scopus 로고
    • ERp57 functions as a subunit of specific complexes formed with the ER lectins calreticulin and calnexin
    • Oliver JD, Roderick HL, Llewellyn DH, High S. 1999. ERp57 functions as a subunit of specific complexes formed with the ER lectins calreticulin and calnexin. Mol. Biol. Cell 10:2573-82
    • (1999) Mol. Biol. Cell , vol.10 , pp. 2573-2582
    • Oliver, J.D.1    Roderick, H.L.2    Llewellyn, D.H.3    High, S.4
  • 92
    • 0031035644 scopus 로고    scopus 로고
    • Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins
    • Oliver JD, van der Wal FJ, Bulleid NJ, 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
  • 93
    • 0030865333 scopus 로고    scopus 로고
    • A critical role for tapasin in the assembly and function of multimeric MHC class I-TAP complexes
    • Ortmann B, Copeman J, Lehner PJ, Sadasivan B, Herberg JA, et al. 1997. A critical role for tapasin in the assembly and function of multimeric MHC class I-TAP complexes. Science 277:1306-9
    • (1997) Science , vol.277 , pp. 1306-1309
    • Ortmann, B.1    Copeman, J.2    Lehner, P.J.3    Sadasivan, B.4    Herberg, J.A.5
  • 94
    • 0034604675 scopus 로고    scopus 로고
    • Endoplasmic reticulum oxidoreductin 1-Lβ (ERO1-Lβ), a human gene induced in the course of the unfolded protein response
    • Pagani M, Fabbri M, Benedetti C, Fassio A, Pilati S, et al. 2000. Endoplasmic reticulum oxidoreductin 1-Lβ (ERO1-Lβ), a human gene induced in the course of the unfolded protein response. J. Biol. Chem. 275:23685-92
    • (2000) J. Biol. Chem , vol.275 , pp. 23685-23692
    • Pagani, M.1    Fabbri, M.2    Benedetti, C.3    Fassio, A.4    Pilati, S.5
  • 95
    • 2942596020 scopus 로고    scopus 로고
    • Bap29/31 influences the intracellular traffic of MHC class I molecules
    • Paquet ME, Cohen-Doyle M, Shore GC, Williams DB. 2004. Bap29/31 influences the intracellular traffic of MHC class I molecules. J. Immunol. 172:7548-55
    • (2004) J. Immunol , vol.172 , pp. 7548-7555
    • Paquet, M.E.1    Cohen-Doyle, M.2    Shore, G.C.3    Williams, D.B.4
  • 96
    • 0037438347 scopus 로고    scopus 로고
    • A single polymorphic residue within the peptide-binding cleft of MHC class I molecules determines spectrum of tapasin dependence
    • Park B, Lee S, Kim E, Ahn K. 2003. A single polymorphic residue within the peptide-binding cleft of MHC class I molecules determines spectrum of tapasin dependence. J. Immunol. 170:961-68
    • (2003) J. Immunol , vol.170 , pp. 961-968
    • Park, B.1    Lee, S.2    Kim, E.3    Ahn, K.4
  • 97
    • 33750002010 scopus 로고    scopus 로고
    • Redox regulation facilitates optimal peptide selection by MHC class I during antigen processing
    • Park B, Lee S, Kim E, Cho K, Riddell SR, et al. 2006. Redox regulation facilitates optimal peptide selection by MHC class I during antigen processing. Cell 127:369-82
    • (2006) Cell , vol.127 , pp. 369-382
    • Park, B.1    Lee, S.2    Kim, E.3    Cho, K.4    Riddell, S.R.5
  • 98
    • 0030152620 scopus 로고    scopus 로고
    • A point mutation in HLA-A*0201 results in failure to bind the TAP complex and to present virus-derived peptides to CTL
    • Peace-Brewer AL, Tussey LG, Matsui M, Li G, Quinn DG, Frelinger JA. 1996. A point mutation in HLA-A*0201 results in failure to bind the TAP complex and to present virus-derived peptides to CTL. Immunity 4:505-14
    • (1996) Immunity , vol.4 , pp. 505-514
    • Peace-Brewer, A.L.1    Tussey, L.G.2    Matsui, M.3    Li, G.4    Quinn, D.G.5    Frelinger, J.A.6
  • 99
    • 27144497781 scopus 로고    scopus 로고
    • Tapasin and ERp57 form a stable disulfide-linked dimer within the MHC class I peptide-loading complex
    • Peaper DR, Wearsch PA, Cresswell P. 2005. Tapasin and ERp57 form a stable disulfide-linked dimer within the MHC class I peptide-loading complex. EMBO J. 24:3613-23
    • (2005) EMBO J , vol.24 , pp. 3613-3623
    • Peaper, D.R.1    Wearsch, P.A.2    Cresswell, P.3
  • 100
    • 0032076171 scopus 로고    scopus 로고
    • Peh CA, Burrows SR, Barnden M, Khanna R, Cresswell P, et al. 1998. HLA-B27-restricted antigen presentation in the absence of tapasin reveals polymorphism in mechanisms of HLA class I peptide loading. Immunity 8:531-42
    • Peh CA, Burrows SR, Barnden M, Khanna R, Cresswell P, et al. 1998. HLA-B27-restricted antigen presentation in the absence of tapasin reveals polymorphism in mechanisms of HLA class I peptide loading. Immunity 8:531-42
  • 101
    • 11844249995 scopus 로고    scopus 로고
    • A charged amino acid residue in the transmembrane/cytoplasmic region of tapasin influences MHC class I assembly and maturation
    • Petersen JL, Hickman-Miller HD, McIlhaney MM, Vargas SE, Purcell AW, et al. 2005. A charged amino acid residue in the transmembrane/cytoplasmic region of tapasin influences MHC class I assembly and maturation. J. Immunol. 174:962-69
    • (2005) J. Immunol , vol.174 , pp. 962-969
    • Petersen, J.L.1    Hickman-Miller, H.D.2    McIlhaney, M.M.3    Vargas, S.E.4    Purcell, A.W.5
  • 102
    • 12144288546 scopus 로고    scopus 로고
    • Molecular characterization of the principal substrate binding site of the ubiquitous folding catalyst protein disulfide isomerase
    • Pirneskoski A, Klappa P, Lobell M, Williamson RA, Byrne L, et al. 2004. Molecular characterization of the principal substrate binding site of the ubiquitous folding catalyst protein disulfide isomerase. J. Biol. Chem. 279:10374-81
    • (2004) J. Biol. Chem , vol.279 , pp. 10374-10381
    • Pirneskoski, A.1    Klappa, P.2    Lobell, M.3    Williamson, R.A.4    Byrne, L.5
  • 103
    • 0031610364 scopus 로고    scopus 로고
    • Ero1p: A novel and ubiquitous protein with an essential role in oxidative protein folding in the endoplasmic reticulum
    • Pollard MG, Travers KJ, Weissman JS. 1998. Ero1p: a novel and ubiquitous protein with an essential role in oxidative protein folding in the endoplasmic reticulum. Mol. Cell 1:171-82
    • (1998) Mol. Cell , vol.1 , pp. 171-182
    • Pollard, M.G.1    Travers, K.J.2    Weissman, J.S.3
  • 104
    • 12144291328 scopus 로고    scopus 로고
    • Specific interaction of ERp57 and calnexin determined by NMR spectroscopy and an ER two-hybrid system
    • Pollock S, Kozlov G, Pelletier MF, Trempe JF, Jansen G, et al. 2004. Specific interaction of ERp57 and calnexin determined by NMR spectroscopy and an ER two-hybrid system. EMBO J. 23:1020-29
    • (2004) EMBO J , vol.23 , pp. 1020-1029
    • Pollock, S.1    Kozlov, G.2    Pelletier, M.F.3    Trempe, J.F.4    Jansen, G.5
  • 105
    • 0035863732 scopus 로고    scopus 로고
    • Quantitative and qualitative influences of tapasin on the class I peptide repertoire
    • Purcell AW, Gorman JJ, Garcia-Peydro M, Paradela A, Burrows SR, et al. 2001. Quantitative and qualitative influences of tapasin on the class I peptide repertoire. J. Immunol. 166:1016-27
    • (2001) J. Immunol , vol.166 , pp. 1016-1027
    • Purcell, A.W.1    Gorman, J.J.2    Garcia-Peydro, M.3    Paradela, A.4    Burrows, S.R.5
  • 106
    • 33845327829 scopus 로고    scopus 로고
    • Direct peptide-regulatable interactions between MHC class I molecules and tapasin
    • Rizvi SM, Raghavan M. 2006. Direct peptide-regulatable interactions between MHC class I molecules and tapasin. Proc. Natl. Acad. Sci. USA 103:18220-25
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 18220-18225
    • Rizvi, S.M.1    Raghavan, M.2
  • 107
    • 38449098111 scopus 로고    scopus 로고
    • Molecular architecture of the TAP-associated MHC class I peptide-loading complex
    • Rufer E, Leonhardt RM, Knittler MR. 2007. Molecular architecture of the TAP-associated MHC class I peptide-loading complex. J. Immunol. 179:5717-27
    • (2007) J. Immunol , vol.179 , pp. 5717-5727
    • Rufer, E.1    Leonhardt, R.M.2    Knittler, M.R.3
  • 108
    • 2442607723 scopus 로고    scopus 로고
    • The primary substrate binding site in the b′ domain of ERp57 is adapted for endoplasmic reticulum lectin association
    • Russell SJ, Ruddock LW, Salo KE, Oliver JD, Roebuck QP, et al. 2004. The primary substrate binding site in the b′ domain of ERp57 is adapted for endoplasmic reticulum lectin association. J. Biol. Chem. 279:18861-69
    • (2004) J. Biol. Chem , vol.279 , pp. 18861-18869
    • Russell, S.J.1    Ruddock, L.W.2    Salo, K.E.3    Oliver, J.D.4    Roebuck, Q.P.5
  • 109
    • 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 PJ, Ortmann B, Spies T, Cresswell P. 1996. Roles for calreticulin and a novel glycoprotein, tapasin, in the interaction of MHC class I molecules with TAP. Immunity 5:103-14
    • (1996) Immunity , vol.5 , pp. 103-114
    • Sadasivan, B.1    Lehner, P.J.2    Ortmann, B.3    Spies, T.4    Cresswell, P.5
  • 111
    • 0022718930 scopus 로고
    • Impaired assembly and transport of HLA-A and -B antigens in a mutant TxB cell hybrid
    • Salter RD, Cresswell P. 1986. Impaired assembly and transport of HLA-A and -B antigens in a mutant TxB cell hybrid. EMBO J. 5:943-49
    • (1986) EMBO J , vol.5 , pp. 943-949
    • Salter, R.D.1    Cresswell, P.2
  • 112
    • 34547092183 scopus 로고    scopus 로고
    • Major histocompatibility complex class I-ERp57-tapasin interactions within the peptide-loading complex
    • Santos SG, Campbell EC, Lynch S, Wong V, Antoniou AN, Powis SJ. 2007. Major histocompatibility complex class I-ERp57-tapasin interactions within the peptide-loading complex. J. Biol. Chem. 282:17587-93
    • (2007) J. Biol. Chem , vol.282 , pp. 17587-17593
    • Santos, S.G.1    Campbell, E.C.2    Lynch, S.3    Wong, V.4    Antoniou, A.N.5    Powis, S.J.6
  • 113
    • 0036902105 scopus 로고    scopus 로고
    • An IFN-γ-induced aminopeptidase in the ER, ERAP1, trims precursors to MHC class I-presented peptides
    • Saric T, Chang SC, Hattori A, York IA, Markant S, et al. 2002. An IFN-γ-induced aminopeptidase in the ER, ERAP1, trims precursors to MHC class I-presented peptides. Nat. Immunol. 3:1169-76
    • (2002) Nat. Immunol , vol.3 , pp. 1169-1176
    • Saric, T.1    Chang, S.C.2    Hattori, A.3    York, I.A.4    Markant, S.5
  • 114
    • 0034799402 scopus 로고    scopus 로고
    • 2 001. The structure of calnexin, an ER chaperone involved in quality control of protein folding
    • Schrag JD, Bergeron JJ, Li Y, Borisova S, Hahn M, et al. 2 001. The structure of calnexin, an ER chaperone involved in quality control of protein folding. Mol. Cell 8:633-44
    • Mol. Cell , vol.8 , pp. 633-644
    • Schrag, J.D.1    Bergeron, J.J.2    Li, Y.3    Borisova, S.4    Hahn, M.5
  • 115
    • 0037015624 scopus 로고    scopus 로고
    • ERAAP customizes peptides for MHC class I molecules in the endoplasmic reticulum
    • Serwold T, Gonzalez F, Kim J, Jacob R, Shastri N. 2002. ERAAP customizes peptides for MHC class I molecules in the endoplasmic reticulum. Nature 419:480-83
    • (2002) Nature , vol.419 , pp. 480-483
    • Serwold, T.1    Gonzalez, F.2    Kim, J.3    Jacob, R.4    Shastri, N.5
  • 116
    • 20444362062 scopus 로고    scopus 로고
    • Qualitative and quantitative differences in peptides bound to HLA-B27 in the presence of mouse versus human tapasin define a role for tapasin as a size-dependent peptide editor
    • Sesma L, Galocha B, Vazquez M, Purcell AW, Marcilla M, et al. 2005. Qualitative and quantitative differences in peptides bound to HLA-B27 in the presence of mouse versus human tapasin define a role for tapasin as a size-dependent peptide editor. J. Immunol. 174:7833-44
    • (2005) J. Immunol , vol.174 , pp. 7833-7844
    • Sesma, L.1    Galocha, B.2    Vazquez, M.3    Purcell, A.W.4    Marcilla, M.5
  • 117
    • 0036842559 scopus 로고    scopus 로고
    • Formation and transfer of disulphide bonds in living cells
    • Sevier CS, Kaiser CA. 2002. Formation and transfer of disulphide bonds in living cells. Nat. Rev. Mol. Cell Biol. 3:836-47
    • (2002) Nat. Rev. Mol. Cell Biol , vol.3 , pp. 836-847
    • Sevier, C.S.1    Kaiser, C.A.2
  • 118
    • 1842690851 scopus 로고    scopus 로고
    • Identification and characterization of structural domains of human ERp57: Association with calreticulin requires several domains
    • Silvennoinen L, Myllyharju J, Ruoppolo M, Orru S, Caterino M, et al. 2004. Identification and characterization of structural domains of human ERp57: Association with calreticulin requires several domains. J. Biol. Chem. 279:13607-15
    • (2004) J. Biol. Chem , vol.279 , pp. 13607-13615
    • Silvennoinen, L.1    Myllyharju, J.2    Ruoppolo, M.3    Orru, S.4    Caterino, M.5
  • 119
    • 33646594461 scopus 로고    scopus 로고
    • Consequences of ERp57 deletion on oxidative folding of obligate and facultative clients of the calnexin cycle
    • Solda T, Garbi N, Hammerling GJ, Molinari M. 2006. Consequences of ERp57 deletion on oxidative folding of obligate and facultative clients of the calnexin cycle. J. Biol. Chem. 281:6219-26
    • (2006) J. Biol. Chem , vol.281 , pp. 6219-6226
    • Solda, T.1    Garbi, N.2    Hammerling, G.J.3    Molinari, M.4
  • 120
    • 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 JC, Harris MR, Kindle CS, Hansen TH. 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. 158:2236-41
    • (1997) J. Immunol , vol.158 , pp. 2236-2241
    • Solheim, J.C.1    Harris, M.R.2    Kindle, C.S.3    Hansen, T.H.4
  • 121
    • 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 J. 14:4196-203
    • (1995) EMBO J , vol.14 , pp. 4196-4203
    • Sousa, M.1    Parodi, A.J.2
  • 122
    • 0026500826 scopus 로고
    • Presentation of viral antigen by MHC class I molecules is dependent on a putative peptide transporter heterodimer
    • Spies T, Cerundolo V, Colonna M, Cresswell P, Townsend A, DeMars R. 1992. Presentation of viral antigen by MHC class I molecules is dependent on a putative peptide transporter heterodimer. Nature 355:644-46
    • (1992) Nature , vol.355 , pp. 644-646
    • Spies, T.1    Cerundolo, V.2    Colonna, M.3    Cresswell, P.4    Townsend, A.5    DeMars, R.6
  • 123
    • 0025845432 scopus 로고
    • Restored expression of major histocompatibility class I molecules by gene transfer of a putative peptide transporter
    • Spies T, DeMars R. 1991. Restored expression of major histocompatibility class I molecules by gene transfer of a putative peptide transporter. Nature 351:323-24
    • (1991) Nature , vol.351 , pp. 323-324
    • Spies, T.1    DeMars, R.2
  • 124
    • 0034517368 scopus 로고    scopus 로고
    • Selective export of MHC class I molecules from the ER after their dissociation from TAP
    • Spiliotis ET, Manley H, Osorio M, Zuniga MC, Edidin M. 2000. Selective export of MHC class I molecules from the ER after their dissociation from TAP. Immunity 13:841-51
    • (2000) Immunity , vol.13 , pp. 841-851
    • Spiliotis, E.T.1    Manley, H.2    Osorio, M.3    Zuniga, M.C.4    Edidin, M.5
  • 125
    • 26244445001 scopus 로고    scopus 로고
    • Interferon-γ, the functional plasticity of the ubiquitin-proteasome system, and MHC class I antigen processing
    • Strehl B, Seifert U, Kruger E, Heink S, Kuckelkorn U, Kloetzel PM. 2005. Interferon-γ, the functional plasticity of the ubiquitin-proteasome system, and MHC class I antigen processing. Immunol. Rev. 207:19-30
    • (2005) Immunol. Rev , vol.207 , pp. 19-30
    • Strehl, B.1    Seifert, U.2    Kruger, E.3    Heink, S.4    Kuckelkorn, U.5    Kloetzel, P.M.6
  • 126
    • 0033083288 scopus 로고    scopus 로고
    • Interaction of murine MHC class I molecules with tapasin and TAP enhances peptide loading and involves the heavy chain α3 domain
    • Suh WK, Derby MA, Cohen-Doyle MF, Schoenhals GJ, Fruh K, et al. 1999. Interaction of murine MHC class I molecules with tapasin and TAP enhances peptide loading and involves the heavy chain α3 domain. J. Immunol. 162:1530-40
    • (1999) J. Immunol , vol.162 , pp. 1530-1540
    • Suh, W.K.1    Derby, M.A.2    Cohen-Doyle, M.F.3    Schoenhals, G.J.4    Fruh, K.5
  • 127
    • 0029813510 scopus 로고    scopus 로고
    • MHC class I molecules form ternary complexes with calnexin and TAP and undergo peptide-regulated interaction with TAP via their extracellular domains
    • Suh WK, Mitchell EK, Yang Y, Peterson PA, Waneck GL, Williams DB. 1996. MHC class I molecules form ternary complexes with calnexin and TAP and undergo peptide-regulated interaction with TAP via their extracellular domains. J. Exp. Med. 184:337-48
    • (1996) J. Exp. Med , vol.184 , pp. 337-348
    • Suh, W.K.1    Mitchell, E.K.2    Yang, Y.3    Peterson, P.A.4    Waneck, G.L.5    Williams, D.B.6
  • 128
    • 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 GJ, 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. 168:1950-60
    • (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
  • 129
    • 33747766822 scopus 로고    scopus 로고
    • HLA-B44 polymorphisms at position 116 of the heavy chain influence TAP complex binding via an effect on peptide occupancy
    • Thammavongsa V, Raghuraman G, Filzen TM, Collins KL, Raghavan M. 2006. HLA-B44 polymorphisms at position 116 of the heavy chain influence TAP complex binding via an effect on peptide occupancy. J. Immunol. 177:3150-61
    • (2006) J. Immunol , vol.177 , pp. 3150-3161
    • Thammavongsa, V.1    Raghuraman, G.2    Filzen, T.M.3    Collins, K.L.4    Raghavan, M.5
  • 130
    • 30344444015 scopus 로고    scopus 로고
    • The crystal structure of yeast protein disulfide isomerase suggests cooperativity between its active sites
    • Tian G, Xiang S, Noiva R, Lennarz WJ, Schindelin H. 2006. The crystal structure of yeast protein disulfide isomerase suggests cooperativity between its active sites. Cell 124:61-73
    • (2006) Cell , vol.124 , pp. 61-73
    • Tian, G.1    Xiang, S.2    Noiva, R.3    Lennarz, W.J.4    Schindelin, H.5
  • 131
    • 0028205240 scopus 로고
    • Human, mouse, and rat calnexin cDNA cloning: Identification of potential calcium binding motifs and gene localization to human chromosome 5
    • Tjoelker LW, Seyfried CE, Eddy RL Jr, Byers MG, Shows TB, et al. 1994. Human, mouse, and rat calnexin cDNA cloning: identification of potential calcium binding motifs and gene localization to human chromosome 5. Biochemistry 33:3229-36
    • (1994) Biochemistry , vol.33 , pp. 3229-3236
    • Tjoelker, L.W.1    Seyfried, C.E.2    Eddy Jr, R.L.3    Byers, M.G.4    Shows, T.B.5
  • 135
    • 0031041169 scopus 로고    scopus 로고
    • Reglucosylation of N-linked glycans is critical for calnexin assembly with T cell receptor (TCR) α proteins but not TCRβ proteins
    • Van Leeuwen JE, Kearse KP. 1997. Reglucosylation of N-linked glycans is critical for calnexin assembly with T cell receptor (TCR) α proteins but not TCRβ proteins. J. Biol. Chem. 272:4179-86
    • (1997) J. Biol. Chem , vol.272 , pp. 4179-4186
    • Van Leeuwen, J.E.1    Kearse, K.P.2
  • 136
    • 0029925940 scopus 로고    scopus 로고
    • The molecular chaperone calnexin facilitates folding and assembly of class I histocompatibility molecules
    • Vassilakos A, Cohen-Doyle MF, Peterson PA, Jackson MR, Williams DB. 1996. The molecular chaperone calnexin facilitates folding and assembly of class I histocompatibility molecules. EMBO J. 15:1495-506
    • (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
  • 137
    • 0030898705 scopus 로고    scopus 로고
    • Scanning and escape during protein-disulfide isomerase-assisted folding
    • Walker KW, Gilbert HF. 1997. Scanning and escape during protein-disulfide isomerase-assisted folding. J. Biol. Chem. 272:8845-48
    • (1997) J. Biol. Chem , vol.272 , pp. 8845-8848
    • Walker, K.W.1    Gilbert, H.F.2
  • 138
    • 0030061006 scopus 로고    scopus 로고
    • Catalysis of oxidative protein folding by mutants of protein disulfide isomerase with a single active-site cysteine
    • Walker KW, Lyles MM, Gilbert HF. 1996. Catalysis of oxidative protein folding by mutants of protein disulfide isomerase with a single active-site cysteine. Biochemistry 35:1972-80
    • (1996) Biochemistry , vol.35 , pp. 1972-1980
    • Walker, K.W.1    Lyles, M.M.2    Gilbert, H.F.3
  • 139
    • 23044516246 scopus 로고    scopus 로고
    • The cotranslational maturation of the type I membrane glycoprotein tyrosinase: The heat shock protein 70 system hands off to the lectin-based chaperone system
    • Wang N, Daniels R, Hebert DN. 2005. The cotranslational maturation of the type I membrane glycoprotein tyrosinase: The heat shock protein 70 system hands off to the lectin-based chaperone system. Mol. Biol. Cell 16:3740-52
    • (2005) Mol. Biol. Cell , vol.16 , pp. 3740-3752
    • Wang, N.1    Daniels, R.2    Hebert, D.N.3
  • 140
    • 0028177703 scopus 로고
    • Mutation of the α2 domain disulfide bridge of the class I molecule HLA-A*0201. Effect on maturation and peptide presentation
    • Warburton RJ, Matsui M, Rowland-Jones SL, Gammon MC, Katzenstein GE, et al. 1994. Mutation of the α2 domain disulfide bridge of the class I molecule HLA-A*0201. Effect on maturation and peptide presentation. Hum. Immunol. 39:261-71
    • (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
  • 141
    • 0028932360 scopus 로고
    • The molecular chaperone calnexin binds Glc1Man9GlcNAc2 oligosaccharide as an initial step in recognizing unfolded glycoproteins
    • Ware FE, Vassilakos A, Peterson PA, Jackson MR, Lehrman MA, Williams DB. 1995. The molecular chaperone calnexin binds Glc1Man9GlcNAc2 oligosaccharide as an initial step in recognizing unfolded glycoproteins. J. Biol. Chem. 270:4697-704
    • (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
  • 142
    • 34547121970 scopus 로고    scopus 로고
    • Selective loading of high-affinity peptides onto major histocompatibility complex class I molecules by the tapasin-ERp57 heterodimer
    • Wearsch PA, Cresswell P. 2007. Selective loading of high-affinity peptides onto major histocompatibility complex class I molecules by the tapasin-ERp57 heterodimer. Nat. Immunol. 8:873-81
    • (2007) Nat. Immunol , vol.8 , pp. 873-881
    • Wearsch, P.A.1    Cresswell, P.2
  • 143
    • 2942620134 scopus 로고    scopus 로고
    • Major histocompatibility complex class I molecules expressed with monoglucosylated N-linked glycans bind calreticulin independently of their assembly status
    • Wearsch PA, Jakob CA, Vallin A, Dwek RA, Rudd PM, Cresswell P. 2004. Major histocompatibility complex class I molecules expressed with monoglucosylated N-linked glycans bind calreticulin independently of their assembly status. J. Biol. Chem. 279:25112-21
    • (2004) J. Biol. Chem , vol.279 , pp. 25112-25121
    • Wearsch, P.A.1    Jakob, C.A.2    Vallin, A.3    Dwek, R.A.4    Rudd, P.M.5    Cresswell, P.6
  • 144
    • 0026576422 scopus 로고
    • HLA-A2 molecules in an antigen-processing mutant cell contain signal sequence-derived peptides
    • Wei ML, Cresswell P. 1992. HLA-A2 molecules in an antigen-processing mutant cell contain signal sequence-derived peptides. Nature 356:443-46
    • (1992) Nature , vol.356 , pp. 443-446
    • Wei, M.L.1    Cresswell, P.2
  • 145
    • 0027270735 scopus 로고
    • Efficient catalysis of disulphide bond rearrangements by protein disulphide isomerase
    • Weissman JS, Kim PS. 1993. Efficient catalysis of disulphide bond rearrangements by protein disulphide isomerase. Nature 365:185-88
    • (1993) Nature , vol.365 , pp. 185-188
    • Weissman, J.S.1    Kim, P.S.2
  • 147
    • 0024502952 scopus 로고
    • Role of beta 2-microglobulin in the intracellular transport and surface expression of murine class I histocompatibility molecules
    • Williams DB, Barber BH, Flavell RA, Allen H. 1989. Role of beta 2-microglobulin in the intracellular transport and surface expression of murine class I histocompatibility molecules. J. Immunol. 142:2796-806
    • (1989) J. Immunol , vol.142 , pp. 2796-2806
    • Williams, D.B.1    Barber, B.H.2    Flavell, R.A.3    Allen, H.4
  • 148
    • 5044224594 scopus 로고    scopus 로고
    • Tapasin and other chaperones: Models of the MHC class I loading complex
    • Wright CA, Kozik P, Zacharias M, Springer S. 2004. Tapasin and other chaperones: models of the MHC class I loading complex. Biol. Chem. 385:763-78
    • (2004) Biol. Chem , vol.385 , pp. 763-778
    • Wright, C.A.1    Kozik, P.2    Zacharias, M.3    Springer, S.4
  • 149
    • 33645089946 scopus 로고    scopus 로고
    • In vivo role of ER-associated peptidase activity in tailoring peptides for presentation by MHC class Ia and class Ib molecules
    • Yan J, Parekh W, Mendez-Fernandez Y, Olivares-Villagomez D, Dragovic S, et al. 2006. In vivo role of ER-associated peptidase activity in tailoring peptides for presentation by MHC class Ia and class Ib molecules. J. Exp. Med. 203:647-59
    • (2006) J. Exp. Med , vol.203 , pp. 647-659
    • Yan, J.1    Parekh, W.2    Mendez-Fernandez, Y.3    Olivares-Villagomez, D.4    Dragovic, S.5
  • 150
    • 33745833084 scopus 로고    scopus 로고
    • The DRiP hypothesis decennial: Support, controversy, refinement and extension
    • Yewdell JW, Nicchitta CV. 2006. The DRiP hypothesis decennial: support, controversy, refinement and extension. Trends Immunol. 27:368-73
    • (2006) Trends Immunol , vol.27 , pp. 368-373
    • Yewdell, J.W.1    Nicchitta, C.V.2
  • 151
    • 33745125912 scopus 로고    scopus 로고
    • Endoplasmic reticulum aminopeptidase 1 (ERAP1) trims MHC class I-presented peptides in vivo and plays an important role in immunodominance
    • York IA, Brehm MA, Zendzian S, Towne CF, Rock KL. 2006. Endoplasmic reticulum aminopeptidase 1 (ERAP1) trims MHC class I-presented peptides in vivo and plays an important role in immunodominance. Proc. Natl. Acad. Sci. USA 103:9202-7
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 9202-9207
    • York, I.A.1    Brehm, M.A.2    Zendzian, S.3    Towne, C.F.4    Rock, K.L.5
  • 152
    • 0036884090 scopus 로고    scopus 로고
    • The ER aminopeptidase ERAP1 enhances or limits antigen presentation by trimming epitopes to 8-9 residues
    • York IA, Chang SC, Saric T, Keys JA, Favreau JM, et al. 2002. The ER aminopeptidase ERAP1 enhances or limits antigen presentation by trimming epitopes to 8-9 residues. Nat. Immunol. 3:1177-84
    • (2002) Nat. Immunol , vol.3 , pp. 1177-1184
    • York, I.A.1    Chang, S.C.2    Saric, T.3    Keys, J.A.4    Favreau, J.M.5
  • 153
    • 0032513212 scopus 로고    scopus 로고
    • Enhanced catalysis of ribonuclease B folding by the interaction of calnexin or calreticulin with ERp57
    • Zapun A, Darby NJ, Tessier DC, Michalak M, Bergeron JJ, Thomas DY. 1998. Enhanced catalysis of ribonuclease B folding by the interaction of calnexin or calreticulin with ERp57. J. Biol. Chem. 273:6009-12
    • (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
  • 154
    • 10744222173 scopus 로고    scopus 로고
    • Tapasin is a facilitator, not an editor, of class I MHC peptide binding
    • Zarling AL, Luckey CJ, Marto JA, White FM, Brame CJ, et al. 2003. Tapasin is a facilitator, not an editor, of class I MHC peptide binding. J. Immunol. 171:5287-95
    • (2003) J. Immunol , vol.171 , pp. 5287-5295
    • Zarling, A.L.1    Luckey, C.J.2    Marto, J.A.3    White, F.M.4    Brame, C.J.5
  • 155
    • 2942753075 scopus 로고    scopus 로고
    • Natural HLA class I polymorphism controls the pathway of antigen presentation and susceptibility to viral evasion
    • Zernich D, Purcell AW, Macdonald WA, Kjer-Nielsen L, Ely LK, et al. 2004. Natural HLA class I polymorphism controls the pathway of antigen presentation and susceptibility to viral evasion. J.. Exp. Med. 200:13-24
    • (2004) J.. Exp. Med , vol.200 , pp. 13-24
    • Zernich, D.1    Purcell, A.W.2    Macdonald, W.A.3    Kjer-Nielsen, L.4    Ely, L.K.5
  • 156
    • 33744961082 scopus 로고    scopus 로고
    • Functions of ERp57 in the folding and assembly of major histocompatibility complex class I molecules
    • Zhang Y, Baig E, Williams DB. 2006. Functions of ERp57 in the folding and assembly of major histocompatibility complex class I molecules. J. Biol. Chem. 281:14622-31
    • (2006) J. Biol. Chem , vol.281 , pp. 14622-14631
    • Zhang, Y.1    Baig, E.2    Williams, D.B.3
  • 158
    • 26244442247 scopus 로고    scopus 로고
    • Antigen processing and presentation
    • Reviews on all aspects of MHC biology
    • Reviews on all aspects of MHC biology: Cresswell P. 2005. Antigen processing and presentation. Immunol. Rev. 207:5-7
    • (2005) Immunol. Rev , vol.207 , pp. 5-7
    • Cresswell, P.1
  • 159
    • 3242804567 scopus 로고    scopus 로고
    • Cross presentation: Ackerman AL, Cresswell P. 2004. Cellular mechanisms governing cross-presentation of exogenous antigens. Nat. Immunol. 5:678-84
    • Cross presentation: Ackerman AL, Cresswell P. 2004. Cellular mechanisms governing cross-presentation of exogenous antigens. Nat. Immunol. 5:678-84
  • 160
    • 3242743087 scopus 로고    scopus 로고
    • The exogenous pathway for antigen presentation on major histocompatibility complex class II and CD1 molecules
    • MHC class II antigen processing and presentation
    • MHC class II antigen processing and presentation: Watts C. 2004. The exogenous pathway for antigen presentation on major histocompatibility complex class II and CD1 molecules. Nat. Immunol. 5:685-92
    • (2004) Nat. Immunol , vol.5 , pp. 685-692
    • Watts, C.1
  • 161
    • 36448952375 scopus 로고    scopus 로고
    • CD1d antigen presentation: Barrai DC, Brenner MB. 2007. CD1 antigen presentation: how it works. Nat. Rev. Immunol. 7:929-41
    • CD1d antigen presentation: Barrai DC, Brenner MB. 2007. CD1 antigen presentation: how it works. Nat. Rev. Immunol. 7:929-41


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.