메뉴 건너뛰기




Volumn 62, Issue 9, 2005, Pages 1025-1037

Modeling the MHC class I pathway by combining predictions of proteasomal cleavage, TAP transport and MHC class I binding

Author keywords

Antigen processing; Epitope prediction; MHC; Proteasome; TAP

Indexed keywords

LYSINE; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; PEPTIDE HYDROLASE; TRANSPORTER ASSOCIATED WITH ANTIGEN PROCESSING 1; TRIPEPTIDYL PEPTIDASE II; UNCLASSIFIED DRUG;

EID: 20844434026     PISSN: 1420682X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00018-005-4528-2     Document Type: Article
Times cited : (299)

References (49)
  • 1
    • 0025855156 scopus 로고
    • Allele-specific motifs revealed by sequencing of self-peptides eluted from MHC molecules
    • Falk K., Rotzschke O., Stevanovic S., Jung G. and Rammensee H. G. (1991) Allele-specific motifs revealed by sequencing of self-peptides eluted from MHC molecules. Nature 351: 290-296
    • (1991) Nature , vol.351 , pp. 290-296
    • Falk, K.1    Rotzschke, O.2    Stevanovic, S.3    Jung, G.4    Rammensee, H.G.5
  • 2
    • 0030016595 scopus 로고    scopus 로고
    • Structure and functions of the 20S and 26S proteasomes
    • Coux O., Tanaka K. and Goldberg A. L. (1996) Structure and functions of the 20S and 26S proteasomes. Annu. Rev. Biochem. 65: 801-847
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 801-847
    • Coux, O.1    Tanaka, K.2    Goldberg, A.L.3
  • 3
    • 0035290730 scopus 로고    scopus 로고
    • Antigen processing by the proteasome
    • Kloetzel P. M. (2001) Antigen processing by the proteasome. Nat. Rev. Mol. Cell Biol. 2: 179-187
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 179-187
    • Kloetzel, P.M.1
  • 4
    • 0036017391 scopus 로고    scopus 로고
    • Protein degradation and the generation of MHC class I-presented peptides
    • Rock K. L., York I. A., Saric T. and Goldberg A. L. (2002) Protein degradation and the generation of MHC class I-presented peptides. Adv. Immunol. 80: 1-70
    • (2002) Adv. Immunol. , vol.80 , pp. 1-70
    • Rock, K.L.1    York, I.A.2    Saric, T.3    Goldberg, A.L.4
  • 5
  • 6
    • 0028970626 scopus 로고
    • The interferon-gamma-inducible 11 S regulator (PA28) and the LMP2/LMP7 subunits govern the peptide production by the 20 S proteasome in vitro
    • Groettrup M., Ruppert T., Kuehn L., Seeger M., Standera S., Koszinowski U. et al. (1995) The interferon-gamma-inducible 11 S regulator (PA28) and the LMP2/LMP7 subunits govern the peptide production by the 20 S proteasome in vitro. J. Biol. Chem. 270: 23808-23815
    • (1995) J. Biol. Chem. , vol.270 , pp. 23808-23815
    • Groettrup, M.1    Ruppert, T.2    Kuehn, L.3    Seeger, M.4    Standera, S.5    Koszinowski, U.6
  • 7
    • 0030924830 scopus 로고    scopus 로고
    • Bovine spleen multicatalytic proteinase complex (proteasome): Replacement of X, Y, and Z subunits by LMP7, LMP2, and MECL1 and changes in properties and specificity
    • Eleuteri A. M., Kohanski R. A., Cardozo C. and Orlowski M. (1997) Bovine spleen multicatalytic proteinase complex (proteasome): replacement of X, Y, and Z subunits by LMP7, LMP2, and MECL1 and changes in properties and specificity. J. Biol. Chem. 272: 11824-11831
    • (1997) J. Biol. Chem. , vol.272 , pp. 11824-11831
    • Eleuteri, A.M.1    Kohanski, R.A.2    Cardozo, C.3    Orlowski, M.4
  • 8
    • 0028097823 scopus 로고
    • Interferon gamma stimulation modulates the proteolytic activity and cleavage site preference of 20S mouse proteasomes
    • Boes B., Hengel H., Ruppert T., Multhaup G., Koszinowski U. H. and Kloetzel P. M. (1994) Interferon gamma stimulation modulates the proteolytic activity and cleavage site preference of 20S mouse proteasomes. J. Exp. Med. 179: 901-909
    • (1994) J. Exp. Med. , vol.179 , pp. 901-909
    • Boes, B.1    Hengel, H.2    Ruppert, T.3    Multhaup, G.4    Koszinowski, U.H.5    Kloetzel, P.M.6
  • 9
    • 0027214605 scopus 로고
    • Gamma-interferon and expression of MHC genes regulate peptide hydrolysis by proteasomes
    • Gaczynska M., Rock K. L. and Goldberg A. L. (1993) Gamma-interferon and expression of MHC genes regulate peptide hydrolysis by proteasomes. Nature 365: 264-267
    • (1993) Nature , vol.365 , pp. 264-267
    • Gaczynska, M.1    Rock, K.L.2    Goldberg, A.L.3
  • 10
    • 0032479162 scopus 로고    scopus 로고
    • Altered properties of the branched chain amino acid-preferring activity contribute to increased cleavages after branched chain residues by the 'immunoproteasome'
    • Cardozo C. and Kohanski R. A. (1998) Altered properties of the branched chain amino acid-preferring activity contribute to increased cleavages after branched chain residues by the 'immunoproteasome'. J. Biol. Chem. 273: 16764-16770
    • (1998) J. Biol. Chem. , vol.273 , pp. 16764-16770
    • Cardozo, C.1    Kohanski, R.A.2
  • 11
    • 0034614889 scopus 로고    scopus 로고
    • Efficient generation of a hepatitis B virus cytotoxic T lymphocyte epitope requires the structural features of immunoproteasomes
    • Sijts A. J., Ruppert T., Rehermann B., Schmidt M., Koszinowski U. and Kloetzel P. M. (2000) Efficient generation of a hepatitis B virus cytotoxic T lymphocyte epitope requires the structural features of immunoproteasomes. J. Exp. Med. 191: 503-514
    • (2000) J. Exp. Med. , vol.191 , pp. 503-514
    • Sijts, A.J.1    Ruppert, T.2    Rehermann, B.3    Schmidt, M.4    Koszinowski, U.5    Kloetzel, P.M.6
  • 12
    • 0034662001 scopus 로고    scopus 로고
    • Overexpression of the proteasome subunits LMP2, LMP7, and MECL-1, but not PA28 alpha/beta, enhances the presentation of an immunodominant lymphocytic choriomeningitis virus T cell epitope
    • Schwarz K., Broek M. van den, Kostka S., Kraft R., Soza A., Schmidtke G. et al. (2000) Overexpression of the proteasome subunits LMP2, LMP7, and MECL-1, but not PA28 alpha/beta, enhances the presentation of an immunodominant lymphocytic choriomeningitis virus T cell epitope. J.Immunol. 165: 768-778
    • (2000) J.Immunol. , vol.165 , pp. 768-778
    • Schwarz, K.1    Van Den Broek, M.2    Kostka, S.3    Kraft, R.4    Soza, A.5    Schmidtke, G.6
  • 13
    • 0033980648 scopus 로고    scopus 로고
    • Processing of some antigens by the standard proteasome but not by the immunoproteasome results in poor presentation by dendritic cells
    • Morel S., Levy F., Burlet-Schiltz O., Brasseur F., Probst-Kepper M., Peitrequin A. L. et al. (2000) Processing of some antigens by the standard proteasome but not by the immunoproteasome results in poor presentation by dendritic cells. Immunity 12: 107-117
    • (2000) Immunity , vol.12 , pp. 107-117
    • Morel, S.1    Levy, F.2    Burlet-Schiltz, O.3    Brasseur, F.4    Probst-Kepper, M.5    Peitrequin, A.L.6
  • 14
    • 0034193031 scopus 로고    scopus 로고
    • MHC class I antigen processing of an adenovirus CTL epitope is linked to the levels of immunoproteasomes in infected cells
    • Sijts A. J., Standera S., Toes R. E., Ruppert T., Beekman N. J., Veelen P. A. van et al. (2000) MHC class I antigen processing of an adenovirus CTL epitope is linked to the levels of immunoproteasomes in infected cells. J.Immunol. 164: 4500-4506
    • (2000) J.Immunol. , vol.164 , pp. 4500-4506
    • Sijts, A.J.1    Standera, S.2    Toes, R.E.3    Ruppert, T.4    Beekman, N.J.5    Van Veelen, P.A.6
  • 15
    • 0034698738 scopus 로고    scopus 로고
    • Differential influence on cytotoxic T lymphocyte epitope presentation by controlled expression of either proteasome immunosubunits or PA28
    • Hall T. van, Sijts A., Camps M., Offringa R., Melief C., Kloetzel P. M. et al. (2000) Differential influence on cytotoxic T lymphocyte epitope presentation by controlled expression of either proteasome immunosubunits or PA28. J. Exp. Med. 192: 483-494
    • (2000) J. Exp. Med. , vol.192 , pp. 483-494
    • Van Hall, T.1    Sijts, A.2    Camps, M.3    Offringa, R.4    Melief, C.5    Kloetzel, P.M.6
  • 16
    • 1842785206 scopus 로고    scopus 로고
    • A major role for TPPII in trimming proteasomal degradation products for MHC class I antigen presentation
    • Reits E., Neijssen J., Herberts C., Benckhuijsen W., Janssen L., Drijfhout J. W. et al. (2004) A major role for TPPII in trimming proteasomal degradation products for MHC class I antigen presentation. Immunity 20: 495-506
    • (2004) Immunity , vol.20 , pp. 495-506
    • Reits, E.1    Neijssen, J.2    Herberts, C.3    Benckhuijsen, W.4    Janssen, L.5    Drijfhout, J.W.6
  • 17
    • 0032563221 scopus 로고    scopus 로고
    • Interferon-gamma can stimulate post-proteasomal trimming of the N terminus of an antigenic peptide by inducing leucine aminopeptidase
    • Beninga J., Rock K. L. and Goldberg A. E. (1998) Interferon-gamma can stimulate post-proteasomal trimming of the N terminus of an antigenic peptide by inducing leucine aminopeptidase. J. Biol. Chem. 273: 18734-18742
    • (1998) J. Biol. Chem. , vol.273 , pp. 18734-18742
    • Beninga, J.1    Rock, K.L.2    Goldberg, A.E.3
  • 18
    • 0037108488 scopus 로고    scopus 로고
    • The final N-terminal trimming of a subaminoterminal proline-containing HLA class I-restricted antigenic peptide in the cytosol is mediated by two peptidases
    • Levy F., Burri E., Morel S., Peitrequin A. L., Levy N., Bachi A. et al. (2002) The final N-terminal trimming of a subaminoterminal proline-containing HLA class I-restricted antigenic peptide in the cytosol is mediated by two peptidases. J. Immunol. 169: 4161-4171
    • (2002) J. Immunol. , vol.169 , pp. 4161-4171
    • Levy, F.1    Burri, E.2    Morel, S.3    Peitrequin, A.L.4    Levy, N.5    Bachi, A.6
  • 20
    • 0033230777 scopus 로고    scopus 로고
    • Human transporters associated with antigen processing (TAPs) select epitope precursor peptides for processing in the endoplasmic reticulum and presentation to T cells
    • Lauvau G., Kakimi K., Niedermann G., Ostankovitch M., Yotnda P., Firat H. et al. (1999) Human transporters associated with antigen processing (TAPs) select epitope precursor peptides for processing in the endoplasmic reticulum and presentation to T cells. J. Exp. Med. 190: 1227-1239
    • (1999) J. Exp. Med. , vol.190 , pp. 1227-1239
    • Lauvau, G.1    Kakimi, K.2    Niedermann, G.3    Ostankovitch, M.4    Yotnda, P.5    Firat, H.6
  • 21
    • 0036902105 scopus 로고    scopus 로고
    • An IFN-gamma-induced aminopeptidase in the ER, ERAP1, trims precursors to MHC class I-presented peptides
    • Saric T., Chang S. C., Hattori A., York I. A., Markant S., Rock K. L. et al. (2002) An IFN-gamma-induced aminopeptidase in the ER, ERAP1, trims precursors to MHC class I-presented peptides. Nat. Immunol. 3: 1169-1176
    • (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    Rock, K.L.6
  • 22
    • 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. (2002) ERAAP customizes peptides for MHC class I molecules in the endoplasmic reticulum. Nature 419: 480-483
    • (2002) Nature , vol.419 , pp. 480-483
    • Serwold, T.1    Gonzalez, F.2    Kim, J.3    Jacob, R.4    Shastri, N.5
  • 24
    • 0041589474 scopus 로고    scopus 로고
    • Identifying MHC class I epitopes by predicting the TAP transport efficiency of epitope precursors
    • Peters B., Bulik S., Tampe R., Endert P. M. van and Holzhutter H. G. (2003) Identifying MHC class I epitopes by predicting the TAP transport efficiency of epitope precursors. J. Immunol. 171: 1741-1749
    • (2003) J. Immunol. , vol.171 , pp. 1741-1749
    • Peters, B.1    Bulik, S.2    Tampe, R.3    Van Endert, P.M.4    Holzhutter, H.G.5
  • 26
    • 1842684993 scopus 로고    scopus 로고
    • Proteasomes get by with lots of help from their friends
    • Yewdell J. W. and Princiotta M. F. (2004) Proteasomes get by with lots of help from their friends. Immunity 20: 362-363
    • (2004) Immunity , vol.20 , pp. 362-363
    • Yewdell, J.W.1    Princiotta, M.F.2
  • 27
    • 1642495749 scopus 로고    scopus 로고
    • Quantitative analysis of prion-protein degradation by constitutive and immuno-20S proteasomes indicates differences correlated with disease susceptibility
    • Tenzer S., Stoltze E., Schonfisch B., Dengjel J., Muller M., Stevanovic S. et al. (2004) Quantitative analysis of prion-protein degradation by constitutive and immuno-20S proteasomes indicates differences correlated with disease susceptibility. J. Immunol. 172: 1083-1091
    • (2004) J. Immunol. , vol.172 , pp. 1083-1091
    • Tenzer, S.1    Stoltze, E.2    Schonfisch, B.3    Dengjel, J.4    Muller, M.5    Stevanovic, S.6
  • 28
    • 0034647551 scopus 로고    scopus 로고
    • The human 26 S and 20 S proteasomes generate overlapping but different sets of peptide fragments from a model protein substrate
    • Emmerich N. P. N., Nussbaum A. K., Stevanovic S., Priemer M., Toes R. E. M., Rammensee H. G. et al. (2000) The human 26 S and 20 S proteasomes generate overlapping but different sets of peptide fragments from a model protein substrate. J. Biol. Chem. 275: 21140-21148
    • (2000) J. Biol. Chem. , vol.275 , pp. 21140-21148
    • Emmerich, N.P.N.1    Nussbaum, A.K.2    Stevanovic, S.3    Priemer, M.4    Toes, R.E.M.5    Rammensee, H.G.6
  • 29
    • 0035796461 scopus 로고    scopus 로고
    • Discrete cleavage motifs of constitutive and immunoproteasomes revealed by quantitative analysis of cleavage products
    • Toes R. E. M., Nussbaum A. K., Degermann S., Schirle M., Emmerich N. P. N., Kraft M. et al. (2001) Discrete cleavage motifs of constitutive and immunoproteasomes revealed by quantitative analysis of cleavage products. J. Exp. Med. 194: 1-12
    • (2001) J. Exp. Med. , vol.194 , pp. 1-12
    • Toes, R.E.M.1    Nussbaum, A.K.2    Degermann, S.3    Schirle, M.4    Emmerich, N.P.N.5    Kraft, M.6
  • 30
    • 0035182192 scopus 로고    scopus 로고
    • Efficient identification of novel HLA-A(*)0201-presented cytotoxic T lymphocyte epitopes in the widely expressed tumor antigen PRAME by proteasome-mediated digestion analysis
    • Kessler J. H., Beekman N. J., Bres-Vloemans S. A., Verdijk P., Veelen P. A. van, Kloosterman-Joosten A. M. et al. (2001) Efficient identification of novel HLA-A(*)0201-presented cytotoxic T lymphocyte epitopes in the widely expressed tumor antigen PRAME by proteasome-mediated digestion analysis. J. Exp. Med. 193: 73-88
    • (2001) J. Exp. Med. , vol.193 , pp. 73-88
    • Kessler, J.H.1    Beekman, N.J.2    Bres-Vloemans, S.A.3    Verdijk, P.4    Van Veelen, P.A.5    Kloosterman-Joosten, A.M.6
  • 31
    • 0037083354 scopus 로고    scopus 로고
    • Proteasome-assisted identification of a SSX-2-derived epitope recognized by tumor-reactive CTL infiltrating metastatic melanoma
    • Ayyoub M., Stevanovic S., Sahin U., Guillaume P., Servis C., Rimoldi D. et al. (2002) Proteasome-assisted identification of a SSX-2-derived epitope recognized by tumor-reactive CTL infiltrating metastatic melanoma. J.I mmunol. 168: 1717-1722
    • (2002) J. Immunol. , vol.168 , pp. 1717-1722
    • Ayyoub, M.1    Stevanovic, S.2    Sahin, U.3    Guillaume, P.4    Servis, C.5    Rimoldi, D.6
  • 32
    • 0036300868 scopus 로고    scopus 로고
    • Assessment of proteasomal cleavage probabilities from kinetic analysis of time-dependent product formation
    • Peters B., Janek K., Kuckelkorn U. and Holzhutter H. G. (2002) Assessment of proteasomal cleavage probabilities from kinetic analysis of time-dependent product formation. J. Mol. Biol. 318: 847-862
    • (2002) J. Mol. Biol. , vol.318 , pp. 847-862
    • Peters, B.1    Janek, K.2    Kuckelkorn, U.3    Holzhutter, H.G.4
  • 33
    • 0037934475 scopus 로고    scopus 로고
    • Differential proteasomal processing of hydrophobic and hydrophilic protein regions: Contribution to cytotoxic T lymphocyte epitope clustering in HIV-1-Nef
    • Lucchiari-Hartz M., Lindo V., Hitziger N., Gaedicke S., Saveanu L., Endert P. M. van et al. (2003) Differential proteasomal processing of hydrophobic and hydrophilic protein regions: contribution to cytotoxic T lymphocyte epitope clustering in HIV-1-Nef. Proc. Natl. Acad. Sci. USA 100: 7755-7760
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 7755-7760
    • Lucchiari-Hartz, M.1    Lindo, V.2    Hitziger, N.3    Gaedicke, S.4    Saveanu, L.5    Van Endert, P.M.6
  • 34
    • 0141617555 scopus 로고    scopus 로고
    • Examining the independent binding assumption for binding of peptide epitopes to MHC-1 molecules
    • Peters B., Tong W. W., Sidney J., Sette A. and Weng Z. P. (2003) Examining the independent binding assumption for binding of peptide epitopes to MHC-1 molecules. Bioinformatics 19: 1765-1772
    • (2003) Bioinformatics , vol.19 , pp. 1765-1772
    • Peters, B.1    Tong, W.W.2    Sidney, J.3    Sette, A.4    Weng, Z.P.5
  • 35
  • 36
    • 0028807964 scopus 로고
    • Prominent roles of secondary anchor residues in peptide binding to HLA-A24 human class I molecules
    • Kondo A., Sidney J., Southwood S., Guercio M. F. del, Appella E., Sakamoto H. et al. (1995) Prominent roles of secondary anchor residues in peptide binding to HLA-A24 human class I molecules. J. Immunol. 155: 4307-4312
    • (1995) J. Immunol. , vol.155 , pp. 4307-4312
    • Kondo, A.1    Sidney, J.2    Southwood, S.3    Del Guercio, M.F.4    Appella, E.5    Sakamoto, H.6
  • 37
    • 0345016413 scopus 로고    scopus 로고
    • Simultaneous prediction of binding capacity for multiple molecules of the HLA B44 supertype
    • Sidney J., Southwood S., Pasquetto V. and Sette A. (2003) Simultaneous prediction of binding capacity for multiple molecules of the HLA B44 supertype. J.Immunol. 171: 5964-5974
    • (2003) J.Immunol. , vol.171 , pp. 5964-5974
    • Sidney, J.1    Southwood, S.2    Pasquetto, V.3    Sette, A.4
  • 39
    • 0029933388 scopus 로고    scopus 로고
    • Definition of an HLA-A3-like supermotif demonstrates the overlapping peptide-binding repertoires of common HLA molecules
    • Sidney J., Grey H. M., Southwood S., Celis E., Wentworth P. A., Guercio M. F. del et al. (1996) Definition of an HLA-A3-like supermotif demonstrates the overlapping peptide-binding repertoires of common HLA molecules. Hum. Immunol. 45: 79-93
    • (1996) Hum. Immunol. , vol.45 , pp. 79-93
    • Sidney, J.1    Grey, H.M.2    Southwood, S.3    Celis, E.4    Wentworth, P.A.5    Del Guercio, M.F.6
  • 40
    • 0031191630 scopus 로고    scopus 로고
    • The use of the area under the ROC curve in the evaluation of machine learning algorithms
    • Bradley A. P. (1997) The use of the area under the ROC curve in the evaluation of machine learning algorithms. Pattern Recogn. 30: 1145-1159
    • (1997) Pattern Recogn. , vol.30 , pp. 1145-1159
    • Bradley, A.P.1
  • 41
    • 0345291184 scopus 로고    scopus 로고
    • A theoretical approach towards the identification of cleavage-determining amino acid motifs of the 20 S proteasome
    • Holzhutter H. G., Frommel C. and Kloetzel P. M. (1999) A theoretical approach towards the identification of cleavage-determining amino acid motifs of the 20 S proteasome. J. Mol. Biol. 286: 1251-1265
    • (1999) J. Mol. Biol. , vol.286 , pp. 1251-1265
    • Holzhutter, H.G.1    Frommel, C.2    Kloetzel, P.M.3
  • 42
    • 0033849945 scopus 로고    scopus 로고
    • A kinetic model of vertebrate 20S proteasome accounting for the generation of major proteolytic fragments from oligomeric peptide substrates
    • Holzhutter H. G. and Kloetzel P. M. (2000) A kinetic model of vertebrate 20S proteasome accounting for the generation of major proteolytic fragments from oligomeric peptide substrates. Biophys.J. 79: 1196-1205
    • (2000) Biophys. J. , vol.79 , pp. 1196-1205
    • Holzhutter, H.G.1    Kloetzel, P.M.2
  • 46
    • 0028819781 scopus 로고
    • The peptide-binding motif for the human transporter associated with antigen processing
    • Endert P. M. van, Riganelli D., Greco G., Fleischhauer K., Sidney J., Sette A. et al. (1995) The peptide-binding motif for the human transporter associated with antigen processing. J. Exp. Med. 182: 1883-1895
    • (1995) J. Exp. Med. , vol.182 , pp. 1883-1895
    • Van Endert, P.M.1    Riganelli, D.2    Greco, G.3    Fleischhauer, K.4    Sidney, J.5    Sette, A.6
  • 47
    • 0028052724 scopus 로고
    • Scheme for ranking potential HLA-A2 binding peptides based on independent binding of individual peptide side-chains
    • Parker K. C., Bednarek M. A. and Coligan J. E. (1994) Scheme for ranking potential HLA-A2 binding peptides based on independent binding of individual peptide side-chains. J. Immunol. 152: 163-175
    • (1994) J. Immunol. , vol.152 , pp. 163-175
    • Parker, K.C.1    Bednarek, M.A.2    Coligan, J.E.3
  • 48
    • 0036776745 scopus 로고    scopus 로고
    • Antigen degradation or presentation by MHC class I molecules via classical and non-classical pathways
    • Gromme M. and Neefjes J. (2002) Antigen degradation or presentation by MHC class I molecules via classical and non-classical pathways. Mol. Immunol. 39: 181-202
    • (2002) Mol. Immunol. , vol.39 , pp. 181-202
    • Gromme, M.1    Neefjes, J.2
  • 49
    • 0037386260 scopus 로고    scopus 로고
    • An essential role for tripeptidyl peptidase in the generation of an MHC class I epitope
    • Seifert U., Maranon C., Shmueli A., Desoutter J. F., Wesoloski L., Janek K. et al. (2003) An essential role for tripeptidyl peptidase in the generation of an MHC class I epitope. Nat. Immunol. 4: 375-379
    • (2003) Nat. Immunol. , vol.4 , pp. 375-379
    • Seifert, U.1    Maranon, C.2    Shmueli, A.3    Desoutter, J.F.4    Wesoloski, L.5    Janek, K.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.