메뉴 건너뛰기




Volumn 164, Issue 12, 2000, Pages 6147-6157

The selective proteasome inhibitors lactacystin and epoxomicin can be used to either up- or down-regulate antigen presentation at nontoxic doses

Author keywords

[No Author keywords available]

Indexed keywords

LACTACYSTIN; PROTEASOME INHIBITOR;

EID: 0034659804     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: 10.4049/jimmunol.164.12.6147     Document Type: Article
Times cited : (88)

References (52)
  • 1
    • 0032971227 scopus 로고    scopus 로고
    • Degradation of cell proteins and the generation of MHC class I-presented peptides
    • Rock, K. L., and A. L. Goldberg. 1999. Degradation of cell proteins and the generation of MHC class I-presented peptides. Annu. Rev. Immunol. 17:739.
    • (1999) Annu. Rev. Immunol. , vol.17 , pp. 739
    • Rock, K.L.1    Goldberg, A.L.2
  • 2
    • 0033179885 scopus 로고    scopus 로고
    • Discrete proteolytic intermediates in the MHC class I antigen processing pathway and MHC I-dependent peptide trimming in the ER
    • Paz, P., N. Brouwenstijn, R. Perry, and N. Shastri. 1999. Discrete proteolytic intermediates in the MHC class I antigen processing pathway and MHC I-dependent peptide trimming in the ER. Immunity 11:241.
    • (1999) Immunity , vol.11 , pp. 241
    • Paz, P.1    Brouwenstijn, N.2    Perry, R.3    Shastri, N.4
  • 3
    • 0032867676 scopus 로고    scopus 로고
    • The 26S proteasome: A molecular machine designed for controlled proteolysis
    • Voges, D., P. Zwickl, and W. Baumeister. 1999. The 26S proteasome: a molecular machine designed for controlled proteolysis. Annu. Rev. Biochem. 68:1015.
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 1015
    • Voges, D.1    Zwickl, P.2    Baumeister, W.3
  • 4
    • 0030248766 scopus 로고    scopus 로고
    • Peptide antigen production by the proteasome: Complexity provides efficiency
    • Groettrup, M., A. Soza, U. Kuckelkorn, and P. M. Kloetzel. 1996. Peptide antigen production by the proteasome: complexity provides efficiency. Immunol. Today 17:429.
    • (1996) Immunol. Today , vol.17 , pp. 429
    • Groettrup, M.1    Soza, A.2    Kuckelkorn, U.3    Kloetzel, P.M.4
  • 6
    • 0030774890 scopus 로고    scopus 로고
    • The active sites of the eukaryotic 20S proteasome and their involvement in subunit precursor processing
    • Heinemeyer, W., M. Fischer, T. Krimmer, U. Stachon, and D. H. Wolf. 1997. The active sites of the eukaryotic 20S proteasome and their involvement in subunit precursor processing. J. Biot. Chem. 272:25200.
    • (1997) J. Biot. Chem. , vol.272 , pp. 25200
    • Heinemeyer, W.1    Fischer, M.2    Krimmer, T.3    Stachon, U.4    Wolf, D.H.5
  • 7
    • 0032543205 scopus 로고    scopus 로고
    • Inactivation of a defined active site in the mouse 20S proteasome complex enhances MHC class I antigen presentation of a mouse cytomegalovirus protein
    • Schmidtke, G., M. Eggers, T. Ruppert, M. Groettrup, U. Koszinowskj, and P. M. Kloetzel. 1998. Inactivation of a defined active site in the mouse 20S proteasome complex enhances MHC class I antigen presentation of a mouse cytomegalovirus protein. J. Exp. Med. 187:1641.
    • (1998) J. Exp. Med. , vol.187 , pp. 1641
    • Schmidtke, G.1    Eggers, M.2    Ruppert, T.3    Groettrup, M.4    Koszinowskj, U.5    Kloetzel, P.M.6
  • 8
    • 0033035759 scopus 로고    scopus 로고
    • Mutational analysis of subunit iβ2 (MECL-1) demonstrates conservation of cleavage specificity between yeast and mammalian proteasomes
    • Salzmann, U., S. Kral, B. Braun, S. Standera, M. Schmidt, P. M. Kloetzel, and A. Sijts. 1999. Mutational analysis of subunit iβ2 (MECL-1) demonstrates conservation of cleavage specificity between yeast and mammalian proteasomes. FEBS Lett. 454:11.
    • (1999) FEBS Lett. , vol.454 , pp. 11
    • Salzmann, U.1    Kral, S.2    Braun, B.3    Standera, S.4    Schmidt, M.5    Kloetzel, P.M.6    Sijts, A.7
  • 9
    • 0032103006 scopus 로고    scopus 로고
    • Substrate binding and sequence preference of the proteasome revealed by active-site-directed affinity probes
    • Bogyo, M., S. Shin, J. S. McMaster, and H. L. Ploegh. 1998. Substrate binding and sequence preference of the proteasome revealed by active-site-directed affinity probes. Chem. Biol. 5:307.
    • (1998) Chem. Biol. , vol.5 , pp. 307
    • Bogyo, M.1    Shin, S.2    McMaster, J.S.3    Ploegh, H.L.4
  • 10
    • 0027980319 scopus 로고
    • Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules
    • Rock, K. L., C. Gramm, L. Rothstein, K. Clark, R. Stein, L. Dick, D. Hwang, and A. L. Goldberg. 1994. Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules. Cell 78:761.
    • (1994) Cell , vol.78 , pp. 761
    • Rock, K.L.1    Gramm, C.2    Rothstein, L.3    Clark, K.4    Stein, R.5    Dick, L.6    Hwang, D.7    Goldberg, A.L.8
  • 11
    • 0031228085 scopus 로고    scopus 로고
    • The effect of the proteasome inhibitor lactacystin on the presentation of transporters associated with antigen processing (TAP)-dependent and TAP-independent peptide epitopes by class I molecules
    • Bai, A., and J. Forman. 1997. The effect of the proteasome inhibitor lactacystin on the presentation of transporters associated with antigen processing (TAP)-dependent and TAP-independent peptide epitopes by class I molecules. J. Immunol. 159:2139.
    • (1997) J. Immunol. , vol.159 , pp. 2139
    • Bai, A.1    Forman, J.2
  • 12
    • 0030926777 scopus 로고    scopus 로고
    • Lactacystin and clasto-lactacystin β-lactone modify multiple proteasome β-subunits and inhibit intracellular protein degradation and major histocompatibility complex class I antigen presentation
    • Craiu, A., M. Gaczynska, T. Akopian, C. F. Gramm, G. Fenteany, A. L. Goldberg, and K. L. Rock. 1997, Lactacystin and clasto-lactacystin β-lactone modify multiple proteasome β-subunits and inhibit intracellular protein degradation and major histocompatibility complex class I antigen presentation. J. Biol. Chem. 272:13437.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13437
    • Craiu, A.1    Gaczynska, M.2    Akopian, T.3    Gramm, C.F.4    Fenteany, G.5    Goldberg, A.L.6    Rock, K.L.7
  • 13
    • 0031032422 scopus 로고    scopus 로고
    • The proteasome-specific inhibitor lactacystin blocks presentation of cytotoxic T lymphocyte epitopes in human and murine cells
    • Cerundolo, V., A. Benham, V. Braud, S. Mukherjee, K. Gould, B. Macino, J. Neefjes, and A. Townsend. 1997. The proteasome-specific inhibitor lactacystin blocks presentation of cytotoxic T lymphocyte epitopes in human and murine cells. Eur. J. Immunol. 27:336.
    • (1997) Eur. J. Immunol. , vol.27 , pp. 336
    • Cerundolo, V.1    Benham, A.2    Braud, V.3    Mukherjee, S.4    Gould, K.5    Macino, B.6    Neefjes, J.7    Townsend, A.8
  • 14
    • 0031790032 scopus 로고    scopus 로고
    • The proteasome inhibitor lactacystin prevents the generation of an endoplasmic reticulum leader-derived T cell epitope
    • Gallimore, A., K. Schwarz, M. van den Broek, H. Hengartner, and M. Groettrup. 1998. The proteasome inhibitor lactacystin prevents the generation of an endoplasmic reticulum leader-derived T cell epitope. Mol. Immunol. 35:581.
    • (1998) Mol. Immunol. , vol.35 , pp. 581
    • Gallimore, A.1    Schwarz, K.2    Van Den Broek, M.3    Hengartner, H.4    Groettrup, M.5
  • 15
    • 0031570893 scopus 로고    scopus 로고
    • The generation of MHC class I-associated peptides is only partially inhibited by proteasome inhibitors: Involvement of nonproteasomal cytosolic proteases in antigen processing?
    • Vinitsky, A., L. C. Anton, H. L. Snyder, M. Orlowski, J. R. Bennink, and J. W. Yewdell. 1997. The generation of MHC class I-associated peptides is only partially inhibited by proteasome inhibitors: involvement of nonproteasomal cytosolic proteases in antigen processing? J. Immunol. 159:554.
    • (1997) J. Immunol. , vol.159 , pp. 554
    • Vinitsky, A.1    Anton, L.C.2    Snyder, H.L.3    Orlowski, M.4    Bennink, J.R.5    Yewdell, J.W.6
  • 17
    • 0033559238 scopus 로고    scopus 로고
    • Modulation of proteasomal activity required for the generation of a cytotoxic T lymphocyte-defined peptide derived from the tumor antigen MAGE-3
    • Valmori, D., U. Gileadi, C. Servis, P. R. Dunbar, J. C. Cerottini, P. Romero, V. Cerundolo, and F. Levy. 1999. Modulation of proteasomal activity required for the generation of a cytotoxic T lymphocyte-defined peptide derived from the tumor antigen MAGE-3. J. Exp. Med. 189:895.
    • (1999) J. Exp. Med. , vol.189 , pp. 895
    • Valmori, D.1    Gileadi, U.2    Servis, C.3    Dunbar, P.R.4    Cerottini, J.C.5    Romero, P.6    Cerundolo, V.7    Levy, F.8
  • 19
    • 0032555922 scopus 로고    scopus 로고
    • Major histocompatibility complex class I viral antigen processing in the secretory pathway defined by the trans-Golgi network protease furin
    • GilTorregrosa, B. C., A. R. Castano, and M. DelVal. 1998. Major histocompatibility complex class I viral antigen processing in the secretory pathway defined by the trans-Golgi network protease furin. J. Exp. Med. 188:1105.
    • (1998) J. Exp. Med. , vol.188 , pp. 1105
    • GilTorregrosa, B.C.1    Castano, A.R.2    DelVal, M.3
  • 22
    • 0029033981 scopus 로고
    • Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin
    • Fenteany, G., R. F. Standaert, W. S. Lane, S. Choi, E. J. Corey, and S. L. Schreiber. 1995. Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin. Science 268:726.
    • (1995) Science , vol.268 , pp. 726
    • Fenteany, G.1    Standaert, R.F.2    Lane, W.S.3    Choi, S.4    Corey, E.J.5    Schreiber, S.L.6
  • 24
    • 0033621047 scopus 로고    scopus 로고
    • Epoxomicin, a potent and selective proteasome inhibitor, exhibits in vivo antiinflammatory activity
    • Meng, L., R. Mohan, B. H. B. Kwok, M. Elofsson, N. Sin, and C. M. Crews. 1999. Epoxomicin, a potent and selective proteasome inhibitor, exhibits in vivo antiinflammatory activity. Proc. Natl. Acad. Sci. USA 96:10403.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 10403
    • Meng, L.1    Mohan, R.2    Kwok, B.H.B.3    Elofsson, M.4    Sin, N.5    Crews, C.M.6
  • 25
    • 0032543212 scopus 로고    scopus 로고
    • Protective immunity does not correlate with the hierarchy of virus-specific cytotoxic T cell responses to naturally processed peptides
    • Gallimore, A., T. Dumrese, H. Hengartner, R. M. Zinkernagel, and H.-G. Rammensee. 1998. Protective immunity does not correlate with the hierarchy of virus-specific cytotoxic T cell responses to naturally processed peptides. J. Exp. Med. 187:1647.
    • (1998) J. Exp. Med. , vol.187 , pp. 1647
    • Gallimore, A.1    Dumrese, T.2    Hengartner, H.3    Zinkernagel, R.M.4    Rammensee, H.-G.5
  • 26
    • 0025784112 scopus 로고
    • Protection against lethal cytomegalovirus infection by a recombinant vaccine containing a single nonameric T-cell epitope
    • Del Val, M., H.-J. Schlicht, H. Volkmer, M. Messerle, M. J. Reddehase, and U. H. Koszinowski. 1991. Protection against lethal cytomegalovirus infection by a recombinant vaccine containing a single nonameric T-cell epitope. J. Virol. 65:3641.
    • (1991) J. Virol. , vol.65 , pp. 3641
    • Del Val, M.1    Schlicht, H.-J.2    Volkmer, H.3    Messerle, M.4    Reddehase, M.J.5    Koszinowski, U.H.6
  • 27
    • 0028970626 scopus 로고
    • The interferon-γ-inducible 11S regulator (PA28) and the LMP2/LMP7 subunits govern the peptide production by the 20S proteasome in vitro
    • Groettrup, M., T. Ruppert, L. Kuehn, M. Seeger, S. Standera, U. Koszinowski, and P. M. Kloetzel. 1995. The interferon-γ-inducible 11S regulator (PA28) and the LMP2/LMP7 subunits govern the peptide production by the 20S proteasome in vitro. J. Biol. Chem. 270:23808.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23808
    • Groettrup, M.1    Ruppert, T.2    Kuehn, L.3    Seeger, M.4    Standera, S.5    Koszinowski, U.6    Kloetzel, P.M.7
  • 28
    • 0017187345 scopus 로고
    • Cell surface antigens coded for by the human chromosome 7
    • Aden, D. P., and B. B. Knowles. 1976. Cell surface antigens coded for by the human chromosome 7. Immunogenetics 3:209.
    • (1976) Immunogenetics , vol.3 , pp. 209
    • Aden, D.P.1    Knowles, B.B.2
  • 29
    • 0027420863 scopus 로고
    • Comparison of the sensitivity of in vivo and in vitro assays for detection of antiviral cytotoxic T cell activity
    • Castelmur, L. C. DiPaolo, M. F. Bachmann, H. Hengartner, R. M. Zinkernagel, and T. M. Kündig. 1993. Comparison of the sensitivity of in vivo and in vitro assays for detection of antiviral cytotoxic T cell activity. Cell. Immunol. 151:460.
    • (1993) Cell. Immunol. , vol.151 , pp. 460
    • Castelmur, L.1    DiPaolo, C.2    Bachmann, M.F.3    Hengartner, H.4    Zinkernagel, R.M.5    Kündig, T.M.6
  • 31
    • 0028224014 scopus 로고
    • LacZ inducible, antigen/MHC-specific T cell hybrids
    • Sanderson, S., and N. Shastri. 1994. LacZ inducible, antigen/MHC-specific T cell hybrids. Int. Immunol. 6:369.
    • (1994) Int. Immunol. , vol.6 , pp. 369
    • Sanderson, S.1    Shastri, N.2
  • 32
    • 0002046199 scopus 로고
    • Lymphocytic choriomeningitis virus
    • Lehmann-Grube, F. 1971. Lymphocytic choriomeningitis virus. Virol. Monogr. 10:1.
    • (1971) Virol. Monogr. , vol.10 , pp. 1
    • Lehmann-Grube, F.1
  • 33
    • 0023601760 scopus 로고
    • Cytolytic T lymphocyte recognition of the murine cytomegalovirus nonstructural immediate-early protein pp89 expressed by recombinant vaccinia virus
    • Volkmer, H., C. Bertholet, S. Jonjic, R. Witter, and U. Koszinowski. 1987. Cytolytic T lymphocyte recognition of the murine cytomegalovirus nonstructural immediate-early protein pp89 expressed by recombinant vaccinia virus. J. Exp. Med. 166:668.
    • (1987) J. Exp. Med. , vol.166 , pp. 668
    • Volkmer, H.1    Bertholet, C.2    Jonjic, S.3    Witter, R.4    Koszinowski, U.5
  • 34
    • 0021035910 scopus 로고
    • Lymphocytic choriomeningitis virus. VI. Isolation of a glycoprotein mediating neutralization
    • Bruns, M., J. Cihak, G. Müller, and F. Lehmann-Grube. 1983. Lymphocytic choriomeningitis virus. VI. Isolation of a glycoprotein mediating neutralization. Virology 130:247.
    • (1983) Virology , vol.130 , pp. 247
    • Bruns, M.1    Cihak, J.2    Müller, G.3    Lehmann-Grube, F.4
  • 35
    • 0025883707 scopus 로고
    • Quantification of lymphocytic choriomeningitis virus with an immunological focus assay in 24- or 96-well plates
    • Battegay, M., S. Cooper, A. Althage, J. Banziger, H. Hengartner, and R. M. Zinkernagel. 1991. Quantification of lymphocytic choriomeningitis virus with an immunological focus assay in 24- or 96-well plates. J. Virol. Methods 31:191.
    • (1991) J. Virol. Methods , vol.31 , pp. 191
    • Battegay, M.1    Cooper, S.2    Althage, A.3    Banziger, J.4    Hengartner, H.5    Zinkernagel, R.M.6
  • 36
    • 0033517032 scopus 로고    scopus 로고
    • Total synthesis of the potent proteasome inhibitor epoxomicin: A useful tool for understanding proteasome biology
    • Sin, N., K. B. Kim, M. Elofsson, L. H. Meng, H. Auth, B. H. B. Kwok, and C. M. Crews. 1999. Total synthesis of the potent proteasome inhibitor epoxomicin: a useful tool for understanding proteasome biology. Bioorg. Med. Chem. Lett. 9:2283.
    • (1999) Bioorg. Med. Chem. Lett. , vol.9 , pp. 2283
    • Sin, N.1    Kim, K.B.2    Elofsson, M.3    Meng, L.H.4    Auth, H.5    Kwok, B.H.B.6    Crews, C.M.7
  • 37
    • 0033197542 scopus 로고    scopus 로고
    • Proteasome active sites allosterically regulate each other, suggesting a cyclical bite-chew mechanism for protein breakdown
    • Kisselev, A. F., T. N. Akopian, V. Castillo, and A. L. Goldberg. 1999. Proteasome active sites allosterically regulate each other, suggesting a cyclical bite-chew mechanism for protein breakdown. Mol. Cell. 4:395.
    • (1999) Mol. Cell. , vol.4 , pp. 395
    • Kisselev, A.F.1    Akopian, T.N.2    Castillo, V.3    Goldberg, A.L.4
  • 38
    • 0034599679 scopus 로고    scopus 로고
    • The use of LCMV-specific T cell hybridomas for the quantitative analysis of MHC class I restricted antigen presentation
    • Schwarz, K., M. van den Broek, R. de Giuli, W. W. Seelentag, N. Shastri, and M. Groettrup. 2000. The use of LCMV-specific T cell hybridomas for the quantitative analysis of MHC class I restricted antigen presentation. J. Immunol. Methods 199:202.
    • (2000) J. Immunol. Methods , vol.199 , pp. 202
    • Schwarz, K.1    Van Den Broek, M.2    De Giuli, R.3    Seelentag, W.W.4    Shastri, N.5    Groettrup, M.6
  • 39
    • 0026744323 scopus 로고
    • Immunodominant T cell epitope from signal sequence
    • Buchmeier, M. J., and R. M. Zinkernagel. 1992. Immunodominant T cell epitope from signal sequence. Science 257:1142.
    • (1992) Science , vol.257 , pp. 1142
    • Buchmeier, M.J.1    Zinkernagel, R.M.2
  • 40
    • 0025908807 scopus 로고
    • Protein-protein interactions in lymphocytic choriomeningitis virus
    • Burns, J. W., and M. J. Buchmeier. 1991. Protein-protein interactions in lymphocytic choriomeningitis virus. Virology 183:620.
    • (1991) Virology , vol.183 , pp. 620
    • Burns, J.W.1    Buchmeier, M.J.2
  • 43
    • 0032502719 scopus 로고    scopus 로고
    • Lactacystin, proteasome function, and cell fate
    • Fenteany, G., and S. L. Schreiber. 1998. Lactacystin, proteasome function, and cell fate. J. Biol. Chem. 273:8545.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8545
    • Fenteany, G.1    Schreiber, S.L.2
  • 44
    • 18744428952 scopus 로고    scopus 로고
    • Lactacystin, a specific inhibitor of the proteasome, inhibits human platelet lysosomal cathepsin A-like enzyme
    • Ostrowska, H., C. Wojcik, S. Omura, and K. Worowski. 1997. Lactacystin, a specific inhibitor of the proteasome, inhibits human platelet lysosomal cathepsin A-like enzyme. Biochem. Biophys. Res. Commun. 234:729.
    • (1997) Biochem. Biophys. Res. Commun. , vol.234 , pp. 729
    • Ostrowska, H.1    Wojcik, C.2    Omura, S.3    Worowski, K.4
  • 45
    • 0032497615 scopus 로고    scopus 로고
    • An efficient total synthesis of a new and highly active analog of lactacystin
    • Corey, E. J., and W. D. Z. Li. 1998. An efficient total synthesis of a new and highly active analog of lactacystin. Tetrahedron Lett. 39:7475.
    • (1998) Tetrahedron Lett. , vol.39 , pp. 7475
    • Corey, E.J.1    Li, W.D.Z.2
  • 46
    • 0033083168 scopus 로고    scopus 로고
    • Selective proteasome inhibitors: Modulators of antigen presentation?
    • Groettrup, M., and G. Schmidtke. 1999. Selective proteasome inhibitors: modulators of antigen presentation? Drug Discovery Today 4:63.
    • (1999) Drug Discovery Today , vol.4 , pp. 63
    • Groettrup, M.1    Schmidtke, G.2
  • 47
    • 0024095276 scopus 로고
    • Defective presentation to class I-restricted cytotoxic T lymphocytes in vaccinia-infected cells is overcome by enhanced degradation of antigen
    • Townsend, A., J. Bastin, K. Gould, G. Brownlee, M. Andrew, B. Coupar, D. Boyle, S. Chan, and G. Smith. 1988. Defective presentation to class I-restricted cytotoxic T lymphocytes in vaccinia-infected cells is overcome by enhanced degradation of antigen. J. Exp. Med. 168:1211.
    • (1988) J. Exp. Med. , vol.168 , pp. 1211
    • Townsend, A.1    Bastin, J.2    Gould, K.3    Brownlee, G.4    Andrew, M.5    Coupar, B.6    Boyle, D.7    Chan, S.8    Smith, G.9
  • 48
    • 0030040594 scopus 로고    scopus 로고
    • CTL epitopes generation is tightly linked to cellular proteolysis of a Listeria monocytogenes antigen
    • Sijts, A. J. A. M., M. S. Villanueva, and E. G. Pamer. 1996. CTL epitopes generation is tightly linked to cellular proteolysis of a Listeria monocytogenes antigen. J. Immunol. 156:1497.
    • (1996) J. Immunol. , vol.156 , pp. 1497
    • Sijts, A.J.A.M.1    Villanueva, M.S.2    Pamer, E.G.3
  • 49
    • 0030812840 scopus 로고    scopus 로고
    • DNA immunization: Ubiquitination of a viral protein enhances cytotoxic T-lymphocyte induction and antiviral protection but abrogates antibody induction
    • Rodriguez, F., J. Zhang, and J. L. Whitton. 1997. DNA immunization: ubiquitination of a viral protein enhances cytotoxic T-lymphocyte induction and antiviral protection but abrogates antibody induction. J. Virol. 71:8497.
    • (1997) J. Virol. , vol.71 , pp. 8497
    • Rodriguez, F.1    Zhang, J.2    Whitton, J.L.3
  • 50
    • 0030240571 scopus 로고    scopus 로고
    • Generation of naturally processed peptide/MHC class I complexes is independent of the stability of endogenously synthesized precursors
    • Goth. S., V. Nguyen, and N. Shastri. 1996. Generation of naturally processed peptide/MHC class I complexes is independent of the stability of endogenously synthesized precursors. J. Immunol. 157:1894.
    • (1996) J. Immunol. , vol.157 , pp. 1894
    • Goth, S.1    Nguyen, V.2    Shastri, N.3
  • 51
    • 0030239693 scopus 로고    scopus 로고
    • Defective ribosomal products (DRiPs): A major source of antigenic peptides for MHC class I molecules
    • Yewdell, J. W., L. C. Anton, and J. R. Bennink. 1996. Defective ribosomal products (DRiPs): a major source of antigenic peptides for MHC class I molecules. J. Immunol. 157:1823.
    • (1996) J. Immunol. , vol.157 , pp. 1823
    • Yewdell, J.W.1    Anton, L.C.2    Bennink, J.R.3
  • 52
    • 0031858602 scopus 로고    scopus 로고
    • Allelic differences in the relationship between proteasome activity and MHC class I peptide loading
    • Benham, A. M., M. Gromme, and J. Neefjes. 1998. Allelic differences in the relationship between proteasome activity and MHC class I peptide loading. J. Immunol. 161:83.
    • (1998) J. Immunol. , vol.161 , pp. 83
    • Benham, A.M.1    Gromme, M.2    Neefjes, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.