메뉴 건너뛰기




Volumn 15, Issue 3, 2011, Pages 621-633

Redox-regulated peptide transfer from the transporter associated with antigen processing to major histocompatibility complex class i molecules by protein disulfide isomerase

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; HLA A2 ANTIGEN; LIGAND; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; PROTEASOME; PROTEIN DISULFIDE ISOMERASE;

EID: 79959971578     PISSN: 15230864     EISSN: 15577716     Source Type: Journal    
DOI: 10.1089/ars.2010.3756     Document Type: Article
Times cited : (17)

References (61)
  • 3
    • 0037290769 scopus 로고    scopus 로고
    • ISO: A critical evaluation of the role of peptides in heat shock/chaperone protein-mediated tumor rejection
    • DOI 10.1016/S0952791502000067
    • Baker-LePain JC, Reed RC, and Nicchitta CV. ISO: a critical evaluation of the role of peptides in heat shock/chaperone protein-mediated tumor rejection. Curr Opin Immunol 15; 89-94: 2003. (Pubitemid 35454198)
    • (2003) Current Opinion in Immunology , vol.15 , Issue.1 , pp. 89-94
    • Baker-LePain, J.C.1    Reed, R.C.2    Nicchitta, C.V.3
  • 4
    • 0036237529 scopus 로고    scopus 로고
    • Transfer of GRP94(Gp96)-Associated peptides onto endosomal MHC class I molecules
    • DOI 10.1034/j.1600-0854.2002.30505.x
    • Berwin B, Rosser MF, Brinker KG, and Nicchitta CV. Transfer of GRP94(Gp96)-associated peptides onto en-dosomal MHC class I molecules. Traffic 3: 358-366, 2002. (Pubitemid 34461045)
    • (2002) Traffic , vol.3 , Issue.5 , pp. 358-366
    • Berwin, B.1    Rosser, M.F.N.2    Brinker, G.3    Nicchitta, C.V.4
  • 5
    • 0034252620 scopus 로고    scopus 로고
    • CD91: A receptor for heat shock protein gp96
    • Binder RJ, Han DK, and Srivastava PK. CD91: a receptor for heat shock protein gp96. Nat Immunol 1: 151-155, 2000.
    • (2000) Nat Immunol , vol.1 , pp. 151-155
    • Binder, R.J.1    Han, D.K.2    Srivastava, P.K.3
  • 6
    • 0029680321 scopus 로고    scopus 로고
    • World distribution of HLA alleles and implica-tions for disease
    • discussion 253-258
    • Bodmer J. World distribution of HLA alleles and implica-tions for disease. Ciba Found Symp 197: 233-253; discussion 253-258, 1996.
    • (1996) Ciba Found Symp , vol.197 , pp. 233-253
    • Bodmer, J.1
  • 7
    • 0031906738 scopus 로고    scopus 로고
    • b-binding ovalbumin-derived peptides associated with the stress proteins HSP70 and GP96
    • DOI 10.1002/(SICI)1521-4141(199803)28:03<1016::AID-IMMU1016>3.0. CO;2-G
    • Breloer M, Marti T, Fleischer B, and von Bonin A. Isolation of processed, H-2Kb-binding ovalbumin-derived peptides associated with the stress proteins HSP70 and gp96. Eur J Immunol 28: 1016-1021, 1998. (Pubitemid 28116215)
    • (1998) European Journal of Immunology , vol.28 , Issue.3 , pp. 1016-1021
    • Breloer, M.1    Marti, T.2    Fleischer, B.3    Von Bonin, A.4
  • 8
    • 70350124054 scopus 로고    scopus 로고
    • Mapping of the ligand-binding site on the b' domain of human PDI: Interaction with peptide ligands and the x-linker region
    • Byrne LJ, Sidhu A, Wallis AK, Ruddock LW, Freedman RB, Howard MJ, and Williamson RA. Mapping of the ligand-binding site on the b' domain of human PDI: interaction with peptide ligands and the x-linker region. Biochem J 423: 209-217, 2009.
    • (2009) Biochem J , vol.423 , pp. 209-217
    • Byrne, L.J.1    Sidhu, A.2    Wallis, A.K.3    Ruddock, L.W.4    Freedman, R.B.5    Howard, M.J.6    Williamson, R.A.7
  • 9
    • 24044532894 scopus 로고    scopus 로고
    • Testing the role of gp96 as peptide chaperone in antigen processing
    • DOI 10.1074/jbc.M501233200
    • Demine R and Walden P. Testing the role of gp96 as peptide chaperone in antigen processing. J Biol Chem 280: 17573-17578, 2005. (Pubitemid 41388990)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.18 , pp. 17573-17578
    • Demine, R.1    Walden, P.2
  • 10
    • 2942627444 scopus 로고    scopus 로고
    • Coupling in silico and in vitro analysis of peptide-MHC binding: A bioinformatic approach enabling prediction of superbinding peptides and anchorless epitopes
    • Doytchinova IA, Walshe VA, Jones NA, Gloster SE, Borrow P, and Flower DR. Coupling in silico and in vitro analysis of peptide-MHC binding: a bioinformatic approach enabling prediction of superbinding peptides and anchorless epi-topes. J Immunol 172: 7495-7502, 2004. (Pubitemid 38747612)
    • (2004) Journal of Immunology , vol.172 , Issue.12 , pp. 7495-7502
    • Doytchinova, I.A.1    Walshe, V.A.2    Jones, N.A.3    Gloster, S.E.4    Borrow, P.5    Flower, D.R.6
  • 11
    • 26244451375 scopus 로고    scopus 로고
    • The optimization of peptide cargo bound to MHC class I molecules by the peptide-loading complex
    • DOI 10.1111/j.0105-2896.2005.00311.x
    • Elliott T and Williams A. The optimization of peptide cargo bound to MHC class I molecules by the peptide-loading complex. Immunol Rev 207: 89-99, 2005. (Pubitemid 41415010)
    • (2005) Immunological Reviews , vol.207 , pp. 89-99
    • Elliott, T.1    Williams, A.2
  • 13
    • 2442761708 scopus 로고    scopus 로고
    • The protein disulphide-isomerase family: Unravelling a string of folds
    • DOI 10.1042/0264-6021:3390001
    • Ferrari DM and Soling HD. The protein disulphide-isomer-ase family: unravelling a string of folds. Biochem J 339 (Pt 1): 1-10, 1999. (Pubitemid 29179283)
    • (1999) Biochemical Journal , vol.339 , Issue.1 , pp. 1-10
    • Ferrari, D.M.1    Soling, H.-D.2
  • 15
    • 0036810021 scopus 로고    scopus 로고
    • Redox-regulated molecular chaper-ones
    • Graf PC and Jakob U. Redox-regulated molecular chaper-ones. Cell Mol Life Sci 59: 1624-1631, 2002.
    • (2002) Cell Mol Life Sci , vol.59 , pp. 1624-1631
    • Graf, P.C.1    Jakob, U.2
  • 16
    • 0026698060 scopus 로고
    • Oxidized redox state of glutathione in the endoplasmic reticulum
    • Hwang C, Sinskey AJ, and Lodish HF. Oxidized redox state of glutathione in the endoplasmic reticulum. Science 257: 1496-1502, 1992.
    • (1992) Science , vol.257 , pp. 1496-1502
    • Hwang, C.1    Sinskey, A.J.2    Lodish, H.F.3
  • 18
    • 0031127294 scopus 로고    scopus 로고
    • The folding catalyst protein disulfide isomerase is constructed of active and inactive thioredoxin modules
    • Kemmink J, Darby NJ, Dijkstra K, Nilges M, and Creighton TE. The folding catalyst protein disulfide isomerase is con-structed of active and inactive thioredoxin modules. Curr Biol 7: 239-245, 1997. (Pubitemid 27176849)
    • (1997) Current Biology , vol.7 , Issue.4 , pp. 239-245
    • Kemmink, J.1    Darby, N.J.2    Dijkstrat, K.3    Nilges, M.4    Creighton, T.E.5
  • 19
    • 34547092165 scopus 로고    scopus 로고
    • Redox regulation of peptide receptivity of major histocompatibility complex class I molecules by ERp57 and tapasin
    • DOI 10.1038/ni1483, PII NI1483
    • Kienast A, Preuss M, Winkler M, and Dick TP. Redox reg-ulation of peptide receptivity of major histocompatibility complex class I molecules by ERp57 and tapasin. Nat Im-munol 8: 864-872, 2007. (Pubitemid 47099038)
    • (2007) Nature Immunology , vol.8 , Issue.8 , pp. 864-872
    • Kienast, A.1    Preuss, M.2    Winkler, M.3    Dick, T.P.4
  • 21
    • 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
    • DOI 10.1093/emboj/17.4.927
    • Klappa P, Ruddock LW, Darby NJ, and Freedman RB. The b' domain provides the principal peptide-binding site of pro-tein disulfide isomerase but all domains contribute to binding of misfolded proteins. EMBO J 17: 927-935, 1998. (Pubitemid 28077647)
    • (1998) EMBO Journal , vol.17 , Issue.4 , pp. 927-935
    • Klappa, P.1    Ruddock, L.W.2    Darby, N.J.3    Freedman, R.B.4
  • 22
    • 0033725154 scopus 로고    scopus 로고
    • Export of antigenic peptides from the endoplasmic reticulum intersects with retrograde protein translocation through the Sec61p channel
    • Koopmann JO, Albring J, Huter E, Bulbuc N, Spee P, Neefjes J, Hammerling GJ, and Momburg F. Export of antigenic peptides from the endoplasmic reticulum intersects with retrograde protein translocation through the Sec61p channel. Immunity 13: 117-127, 2000.
    • (2000) Immunity , vol.13 , pp. 117-127
    • Koopmann, J.O.1    Albring, J.2    Huter, E.3    Bulbuc, N.4    Spee, P.5    Neefjes, J.6    Hammerling, G.J.7    Momburg, F.8
  • 23
    • 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, and Weissman JS. 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: 876-884, 2006.
    • (2006) J Biol Chem , vol.281 , pp. 876-884
    • Kulp, M.S.1    Frickel, E.M.2    Ellgaard, L.3    Weissman, J.S.4
  • 24
    • 0141750441 scopus 로고    scopus 로고
    • The Group II chaperonin TRiC protects proteolytic intermediates from degradation in the MHC class I antigen processing pathway
    • DOI 10.1016/j.molcel.2003.08.009
    • Kunisawa J and Shastri N. The group II chaperonin TRiC pro-tects proteolytic intermediates from degradation in the MHC class I antigen processing pathway. Mol Cell 12: 565-576,2003. (Pubitemid 37222480)
    • (2003) Molecular Cell , vol.12 , Issue.3 , pp. 565-576
    • Kunisawa, J.1    Shastri, N.2
  • 26
    • 0030801405 scopus 로고    scopus 로고
    • Protein disulfide isomerase is the dominant acceptor for peptides translocated into the endoplasmic reticulum
    • DOI 10.1002/eji.1830270714
    • Lammert E, Stevanovic S, Brunner J, Rammensee HG, and Schild H. Protein disulfide isomerase is the dominant ac-ceptor for peptides translocated into the endoplasmic retic-ulum. Eur J Immunol 27: 1685-1690, 1997. (Pubitemid 27302850)
    • (1997) European Journal of Immunology , vol.27 , Issue.7 , pp. 1685-1690
    • Lammert, E.1    Stevanovic, S.2    Brunner, J.3    Rammensee, H.-G.4    Schild, H.5
  • 27
    • 0037341047 scopus 로고    scopus 로고
    • The calculus of immunity: Quantitating antigen processing
    • DOI 10.1016/S1074-7613(03)00061-X
    • Lehner PJ. The calculus of immunity: quantitating antigen processing. Immunity 18: 315-317, 2003. (Pubitemid 36351512)
    • (2003) Immunity , vol.18 , Issue.3 , pp. 315-317
    • Lehner, P.J.1
  • 28
    • 0031978551 scopus 로고    scopus 로고
    • Generation and TAP-mediated transport of peptides for major histocompatibility complex class I molecules
    • Momburg F and Hammerling GJ. Generation and TAP-mediated transport of peptides for major histocompatibility complex class I molecules. Adv Immunol 68: 191-256, 1998. (Pubitemid 28188794)
    • (1998) Advances in Immunology , vol.68 , pp. 191-256
    • Momburg, F.1    Hammerling, G.J.2
  • 29
    • 0033566953 scopus 로고    scopus 로고
    • Intracellular rate-limiting steps in MHC class I antigen processing
    • Montoya M and Del Val M. Intracellular rate-limiting steps in MHC class I antigen processing. J Immunol 163: 1914-1922, 1999. (Pubitemid 29382192)
    • (1999) Journal of Immunology , vol.163 , Issue.4 , pp. 1914-1922
    • Montoya, M.1    Del Val, M.2
  • 31
    • 0033152788 scopus 로고    scopus 로고
    • Calreticulin displays in vivo peptide-binding activity and can elicit CTL responses against bound peptides
    • Nair S, Wearsch PA, Mitchell DA, Wassenberg JJ, Gilboa E, and Nicchitta CV. Calreticulin displays in vivo peptide-binding activity and can elicit CTL responses against bound peptides. J Immunol 162: 6426-6432, 1999. (Pubitemid 29309363)
    • (1999) Journal of Immunology , vol.162 , Issue.11 , pp. 6426-6432
    • Nair, S.1    Wearsch, P.A.2    Mitchell, D.A.3    Wassenberg, J.J.4    Gilboa, E.5    Nicchitta, C.V.6
  • 33
    • 77955895736 scopus 로고    scopus 로고
    • ABC proteins in antigen transloca-tion and viral inhibition
    • Parcej D and Tampe R. ABC proteins in antigen transloca-tion and viral inhibition. Nat Chem Biol 6: 572-580, 2010.
    • (2010) Nat Chem Biol , vol.6 , pp. 572-580
    • Parcej, D.1    Tampe, R.2
  • 34
    • 0019806243 scopus 로고
    • Partial purification and some properties of BB7.2. A cytotoxic monoclonal antibody with specificity for HLA-A2 and a variant of HLA-A28
    • DOI 10.1016/0198-8859(81)90065-3
    • Parham P and Brodsky FM. Partial purification and some properties of BB7.2. A cytotoxic monoclonal antibody with specificity for HLA-A2 and a variant of HLA-A28. Hum Immunol 3: 277-299, 1981. (Pubitemid 12144723)
    • (1981) Human Immunology , vol.3 , Issue.4 , pp. 277-299
    • Parham, P.1    Brodsky, F.M.2
  • 35
    • 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, and Ahn K. A single polymorphic residue within the peptide-binding cleft of MHC class I molecules determines spectrum of tapasin dependence. J Immunol 170: 961-968, 2003. (Pubitemid 36070550)
    • (2003) Journal of Immunology , vol.170 , Issue.2 , pp. 961-968
    • Park, B.1    Lee, S.2    Kim, E.3    Ahn, K.4
  • 36
    • 33750002010 scopus 로고    scopus 로고
    • Redox regulation facilitates optimal peptide selection by MHC class I during antigen processing
    • DOI 10.1016/j.cell.2006.08.041, PII S0092867406012190
    • Park B, Lee S, Kim E, Cho K, Riddell SR, Cho S, and Ahn K. Redox regulation facilitates optimal peptide selection by MHC class I during antigen processing. Cell 127: 369-382, 2006. (Pubitemid 44572373)
    • (2006) Cell , vol.127 , Issue.2 , pp. 369-382
    • Park, B.1    Lee, S.2    Kim, E.3    Cho, K.4    Riddell, S.R.5    Cho, S.6    Ahn, K.7
  • 37
    • 0030665808 scopus 로고    scopus 로고
    • Green fluorescent protein as a signal for protein-protein interactions
    • Park SH and Raines RT. Green fluorescent protein as a signal for protein-protein interactions. Protein Sci 6:2344-2349,1997. (Pubitemid 27490744)
    • (1997) Protein Science , vol.6 , Issue.11 , pp. 2344-2349
    • Park, S.-H.1    Raines, R.T.2
  • 38
    • 55849088319 scopus 로고    scopus 로고
    • Regulation of MHC class i as-sembly and peptide binding
    • Peaper DR and Cresswell P. Regulation of MHC class I as-sembly and peptide binding. Annu Rev Cell Dev Biol 24: 343-368, 2008.
    • (2008) Annu Rev Cell Dev Biol , vol.24 , pp. 343-368
    • Peaper, D.R.1    Cresswell, P.2
  • 42
    • 0034795208 scopus 로고    scopus 로고
    • Endoplasmic reticulum chaperone gp96 is required for innate immunity but not cell viability
    • DOI 10.1038/ncb1001-891
    • Randow F and Seed B. Endoplasmic reticulum chaperone gp96 is required for innate immunity but not cell viability. Nat Cell Biol 3: 891-896, 2001. (Pubitemid 32952253)
    • (2001) Nature Cell Biology , vol.3 , Issue.10 , pp. 891-896
    • Randow, F.1    Seed, B.2
  • 43
    • 0037242017 scopus 로고    scopus 로고
    • Peptide diffusion, protection, and degradation in nuclear and cytoplasmic compartments before antigen presentation by MHC class I
    • DOI 10.1016/S1074-7613(02)00511-3
    • Reits E, Griekspoor A, Neijssen J, Groothuis T, Jalink K, van Veelen P, Janssen H, Calafat J, Drijfhout JW, and Neefjes J. Peptide diffusion, protection, and degradation in nuclear and cytoplasmic compartments before antigen presentation by MHC class I. Immunity 18: 97-108, 2003. (Pubitemid 36120691)
    • (2003) Immunity , vol.18 , Issue.1 , pp. 97-108
    • Reits, E.1    Griekspoor, A.2    Neijssen, J.3    Groothuis, T.4    Jalink, K.5    Van Veelen, P.6    Janssen, H.7    Calafat, J.8    Drijfhout, J.W.9    Neefjes, J.10
  • 44
    • 77949536081 scopus 로고    scopus 로고
    • Mechanisms of function of ta-pasin, a critical major histocompatibility complex class i assembly factor
    • Rizvi SM and Raghavan M. Mechanisms of function of ta-pasin, a critical major histocompatibility complex class I assembly factor. Traffic 11: 332-347, 2010.
    • (2010) Traffic , vol.11 , pp. 332-347
    • Rizvi, S.M.1    Raghavan, M.2
  • 45
    • 0027943180 scopus 로고
    • Trimming of TAP-translocated peptides in the endoplasmic reticulum and in the cytosol during recycling
    • DOI 10.1084/jem.180.5.1591
    • Roelse J, Gromme M, Momburg F, Hammerling G, and Neefjes J. Trimming of TAP-translocated peptides in the endoplasmic reticulum and in the cytosol during recycling. J Exp Med 180: 1591-1597, 1994. (Pubitemid 24328551)
    • (1994) Journal of Experimental Medicine , vol.180 , Issue.5 , pp. 1591-1597
    • Roelse, J.1    Gromme, M.2    Momburg, F.3    Hammerling, G.4    Neefjes, J.5
  • 46
    • 0030217926 scopus 로고    scopus 로고
    • Roles for calreticulin and a novel glycoprotein, tapasin, in the interaction of MHC class I molecules with TAP
    • DOI 10.1016/S1074-7613(00)80487-2
    • Sadasivan B, Lehner PJ, Ortmann B, Spies T, and Cresswell P. Roles for calreticulin and a novel glycoprotein, tapasin, in the interaction of MHC class I molecules with TAP. Im-munity 5: 103-114, 1996. (Pubitemid 26301087)
    • (1996) Immunity , vol.5 , Issue.2 , pp. 103-114
    • Sadasivan, B.1    Lehner, P.J.2    Ortmann, B.3    Spies, T.4    Cresswell, P.5
  • 47
    • 0036902105 scopus 로고    scopus 로고
    • An IFN-γ-induced aminopeptidase in the ER, ERAP I, trims precursors to MHC class I-presented peptides
    • DOI 10.1038/ni859
    • Saric T, Chang SC, Hattori A, York IA, Markant S, Rock KL, Tsujimoto M, and Goldberg AL. An IFN-gamma-induced aminopeptidase in the ER, ERAP1, trims precursors to MHC class I-presented peptides. Nat Immunol 3: 1169-1176, 2002. (Pubitemid 35476828)
    • (2002) Nature Immunology , vol.3 , Issue.12 , pp. 1169-1176
    • Saric, T.1    Chang, S.-C.2    Hattori, A.3    York, I.A.4    Markant, S.5    Rock, K.L.6    Tsujimoto, M.7    Goldberg, A.L.8
  • 48
    • 0037470064 scopus 로고    scopus 로고
    • Reduction-reoxidation cycles contribute to catalysis of disulfide isomerization by protein-disulfide isomerase
    • DOI 10.1074/jbc.M211036200
    • Schwaller M, Wilkinson B, and Gilbert HF. Reduction-reoxidation cycles contribute to catalysis of disulfide isom-erization by protein-disulfide isomerase. J Biol Chem 278: 7154-7159, 2003. (Pubitemid 36800714)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.9 , pp. 7154-7159
    • Schwaller, M.1    Wilkinson, B.2    Gilbert, H.F.3
  • 49
    • 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, and Shastri N. ERAAP customizes peptides for MHC class I molecules in the endoplasmic reticulum. Nature 419: 480-483, 2002.
    • (2002) Nature , vol.419 , pp. 480-483
    • Serwold, T.1    Gonzalez, F.2    Kim, J.3    Jacob, R.4    Shastri, N.5
  • 51
  • 52
    • 0030805217 scopus 로고    scopus 로고
    • TAP-translocated peptides specifically bind proteins in the endoplasmic reticulum, including gp96, protein disulfide isomerase and calreticulin
    • DOI 10.1002/eji.1830270944
    • Spee P and Neefjes J. TAP-translocated peptides specifically bind proteins in the endoplasmic reticulum, including gp96, protein disulfide isomerase and calreticulin. Eur J Immunol 27: 2441-2449, 1997. (Pubitemid 27404332)
    • (1997) European Journal of Immunology , vol.27 , Issue.9 , pp. 2441-2449
    • Spee, P.1    Neefjes, J.2
  • 53
    • 0033543175 scopus 로고    scopus 로고
    • Identification ofnovel peptide binding proteins in the endoplasmic reticulum: ERp72, cal-nexin, and grp170
    • Spee P, Subjeck J, and Neefjes J. Identification ofnovel peptide binding proteins in the endoplasmic reticulum: ERp72, cal-nexin, and grp170. Biochemistry 38: 10559-10566,1999.
    • (1999) Biochemistry , vol.38 , pp. 10559-10566
    • Spee, P.1    Subjeck, J.2    Neefjes, J.3
  • 54
    • 0021112868 scopus 로고
    • Correlation of sequence hy-drophobicities measures similarity in three-dimensional protein structure
    • Sweet RM and Eisenberg D. Correlation of sequence hy-drophobicities measures similarity in three-dimensional protein structure. J Mol Biol 171: 479-488, 1983.
    • (1983) J Mol Biol , vol.171 , pp. 479-488
    • Sweet, R.M.1    Eisenberg, D.2
  • 55
    • 0037191074 scopus 로고    scopus 로고
    • Unfolded cholera toxin is trans-ferred to the ER membrane and released from protein disulfide isomerase upon oxidation by Ero1
    • Tsai B and Rapoport TA. Unfolded cholera toxin is trans-ferred to the ER membrane and released from protein disulfide isomerase upon oxidation by Ero1. J Cell Biol 159: 207-216, 2002.
    • (2002) J Cell Biol , vol.159 , pp. 207-216
    • Tsai, B.1    Rapoport, T.A.2
  • 56
    • 0035937408 scopus 로고    scopus 로고
    • Protein disulfide isomerase acts as a redox-dependent chaperone to unfold cholera toxin
    • DOI 10.1016/S0092-8674(01)00289-6
    • Tsai B, Rodighiero C, Lencer WI, and Rapoport TA. Protein disulfide isomerase acts as a redox-dependent chaperone to unfold cholera toxin. Cell 104: 937-948, 2001. (Pubitemid 32289285)
    • (2001) Cell , vol.104 , Issue.6 , pp. 937-948
    • Tsai, B.1    Rodighiero, C.2    Lencer, W.I.3    Rapoport, T.A.4
  • 59
    • 34547121970 scopus 로고    scopus 로고
    • Selective loading of high-affinity peptides onto major histocompatibility complex class I molecules by the tapasin-ERp57 heterodimer
    • DOI 10.1038/ni1485, PII NI1485
    • Wearsch PA and Cresswell P. Selective loading of high-af-finity peptides onto major histocompatibility complex class I molecules by the tapasin-ERp57 heterodimer. Nat Immunol 8: 873-881, 2007. (Pubitemid 47099039)
    • (2007) Nature Immunology , vol.8 , Issue.8 , pp. 873-881
    • Wearsch, P.A.1    Cresswell, P.2
  • 60
    • 0036230677 scopus 로고    scopus 로고
    • Optimization of the MHC class I peptide cargo is dependent on tapasin
    • DOI 10.1016/S1074-7613(02)00304-7
    • Williams AP, Peh CA, Purcell AW, McCluskey J, and Elliott T. Optimization of the MHC class I peptide cargo is de-pendent on tapasin. Immunity 16: 509-520, 2002. (Pubitemid 34442576)
    • (2002) Immunity , vol.16 , Issue.4 , pp. 509-520
    • Williams, A.P.1    Peh, C.A.2    Purcell, A.W.3    McCluskey, J.4    Elliott, T.5
  • 61
    • 0036884090 scopus 로고    scopus 로고
    • The Er aminopeptidase ERAP I enhances or limits antigen presentation by trimming epitopes to 8-9 residues
    • DOI 10.1038/ni860
    • York IA, Chang SC, Saric T, Keys JA, Favreau JM, Goldberg AL, and Rock KL. The ER aminopeptidase ERAP1 enhances or limits antigen presentation by trimming epitopes to 8-9 residues. Nat Immunol 3: 1177-1184, 2002. (Pubitemid 35469702)
    • (2002) Nature Immunology , vol.3 , Issue.12 , pp. 1177-1184
    • York, I.A.1    Chang, S.-C.2    Saric, T.3    Keys, J.A.4    Favreau, J.M.5    Goldberg, A.L.6    Rock, K.L.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.