메뉴 건너뛰기




Volumn 161, Issue 1, 1998, Pages 112-121

Proteasomes can either generate or destroy MHC class I epitopes: Evidence for nonproteasomal epitope generation in the cytosol

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME INHIBITOR; EPITOPE; HLA A ANTIGEN; LACTACYSTIN; MAJOR HISTOCOMPATIBILITY ANTIGEN; N ACETYLLEUCYLLEUCYLNORLEUCINAL; PROTEASOME; UNCLASSIFIED DRUG;

EID: 7144223429     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (104)

References (77)
  • 1
    • 0029001515 scopus 로고
    • Generation, translocation, and presentation of MHC class I-restricted peptides
    • Heemels, M. T., and H. Ploegh. 1995. Generation, translocation, and presentation of MHC class I-restricted peptides. Annu. Rev. Biochem. 64:463.
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 463
    • Heemels, M.T.1    Ploegh, H.2
  • 2
    • 0029917002 scopus 로고    scopus 로고
    • Processing and delivery of peptides presented by MHC class I molecules
    • Lehner, P. J., and P. Cresswell. 1996. Processing and delivery of peptides presented by MHC class I molecules. Curr. Opin. Immunol. 8:59.
    • (1996) Curr. Opin. Immunol. , vol.8 , pp. 59
    • Lehner, P.J.1    Cresswell, P.2
  • 3
    • 0028901108 scopus 로고
    • Pathways for the processing and presentation of antigens to T cells
    • Monaco, J. J. 1995. Pathways for the processing and presentation of antigens to T cells. J. Leukocyte Biol. 57:543.
    • (1995) J. Leukocyte Biol. , vol.57 , pp. 543
    • Monaco, J.J.1
  • 4
    • 0028157771 scopus 로고
    • Structure of peptides associated with MHC class I molecules
    • Engelhard, V. H. 1994. Structure of peptides associated with MHC class I molecules. Curr. Opin. Immunol. 6:13.
    • (1994) Curr. Opin. Immunol. , vol.6 , pp. 13
    • Engelhard, V.H.1
  • 5
    • 0029920469 scopus 로고    scopus 로고
    • Antigen processing and presentation by the class I major histocompatibility complex
    • York, I. A., and K. L. Rock. 1996. Antigen processing and presentation by the class I major histocompatibility complex. Annu. Rev. Immunol. 14:369.
    • (1996) Annu. Rev. Immunol. , vol.14 , pp. 369
    • York, I.A.1    Rock, K.L.2
  • 6
    • 0028798015 scopus 로고
    • Getting the inside out: The transporter associated with antigen processing (TAP) and the presentation of viral antigen
    • Hill, A., and H. Ploegh. 1995. Getting the inside out: the transporter associated with antigen processing (TAP) and the presentation of viral antigen. Proc. Natl. Acad. Sci. USA 92:341.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 341
    • Hill, A.1    Ploegh, H.2
  • 8
    • 0028282108 scopus 로고
    • 2-microglobulin complexes associate with TAP transporters before peptide binding
    • 2-microglobulin complexes associate with TAP transporters before peptide binding. Nature 368:864.
    • (1994) Nature , vol.368 , pp. 864
    • Ortmann, B.1    Androlewicz, M.J.2    Cresswell, P.3
  • 9
    • 0028239443 scopus 로고
    • Interaction of MHC class I molecules with the transporter associated with antigen processing
    • Sun, W. K., M. F. Cohen-Doyle, K. Fruh, K. Wang, P. A. Peterson, and D. B. Williams. 1994. Interaction of MHC class I molecules with the transporter associated with antigen processing. Science 264:1322.
    • (1994) Science , vol.264 , pp. 1322
    • Sun, W.K.1    Cohen-Doyle, M.F.2    Fruh, K.3    Wang, K.4    Peterson, P.A.5    Williams, D.B.6
  • 10
    • 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., P. J. Lehner, B. Ortmann, T. Spies, and P. Cresswell. 1996. Roles for calreticulin and a novel glycoprotein, tapasin, in the interaction of MHC class I molecules with TAP. Immunity 5:103.
    • (1996) Immunity , vol.5 , pp. 103
    • Sadasivan, B.1    Lehner, P.J.2    Ortmann, B.3    Spies, T.4    Cresswell, P.5
  • 12
    • 0026576422 scopus 로고
    • HLA-A2 molecules in an antigen-processing mutant cell contain signal sequence-derived peptides
    • Wei, M. L., and P. Cresswell. 1992. HLA-A2 molecules in an antigen-processing mutant cell contain signal sequence-derived peptides. Nature 356:443.
    • (1992) Nature , vol.356 , pp. 443
    • Wei, M.L.1    Cresswell, P.2
  • 14
    • 0029811941 scopus 로고    scopus 로고
    • Transporter (TAP)-independent processing of a multiple membrane-spanning protein, the Epstein-Barr virus latent membrane protein 2
    • Lee, S. P., W. A. Thomas, N. W. Blake, and A. B. Rickinson. 1996. Transporter (TAP)-independent processing of a multiple membrane-spanning protein, the Epstein-Barr virus latent membrane protein 2. Eur. J. Immunol. 26: 1875.
    • (1996) Eur. J. Immunol. , vol.26 , pp. 1875
    • Lee, S.P.1    Thomas, W.A.2    Blake, N.W.3    Rickinson, A.B.4
  • 16
    • 0028925556 scopus 로고
    • Processing of major histocompatibility class I-restricted antigens in the endoplasmic reticulum
    • Elliott, T., A. Willis, V. Cerundolo, and A. Townsend. 1995. Processing of major histocompatibility class I-restricted antigens in the endoplasmic reticulum. J. Exp. Med. 181:1481.
    • (1995) J. Exp. Med. , vol.181 , pp. 1481
    • Elliott, T.1    Willis, A.2    Cerundolo, V.3    Townsend, A.4
  • 17
    • 0028208970 scopus 로고
    • TAP (transporter associated with antigen processing)-independent presentation of endogenousiy synthesized peptides is enhanced by endoplasmic reticulum insertion sequences located at the amino- But not carboxyl-terminus of the peptide
    • Bacik, I., J. H. Cox, R. Anderson, J. W. Yewdell, and J. R. Bennink. 1994. TAP (transporter associated with antigen processing)-independent presentation of endogenousiy synthesized peptides is enhanced by endoplasmic reticulum insertion sequences located at the amino- but not carboxyl-terminus of the peptide. J. Immunol. 152:381.
    • (1994) J. Immunol. , vol.152 , pp. 381
    • Bacik, I.1    Cox, J.H.2    Anderson, R.3    Yewdell, J.W.4    Bennink, J.R.5
  • 18
    • 0025879780 scopus 로고
    • Endogenously synthesized peptide with an endoplasmic reticulum signal sequence sensitizes antigen processing mutant cells to class I-restricted cell-mediated lysis
    • Anderson, K., P. Cresswell, M. Gammon, J. Hermes, A. Williamson, and H. Zweerink. 1991. Endogenously synthesized peptide with an endoplasmic reticulum signal sequence sensitizes antigen processing mutant cells to class I-restricted cell-mediated lysis. J. Exp. Med. 174:489.
    • (1991) J. Exp. Med. , vol.174 , pp. 489
    • Erson, K.1    Cresswell, P.2    Gammon, M.3    Hermes, J.4    Williamson, A.5    Zweerink, H.6
  • 19
    • 0028096715 scopus 로고
    • Trimming of antigenic peptides in an early secretory compartment
    • Snyder, H. L., J. W. Yewdell, and J. R. Bennink. 1994. Trimming of antigenic peptides in an early secretory compartment. J. Exp. Med. 180:2389.
    • (1994) J. Exp. Med. , vol.180 , pp. 2389
    • Snyder, H.L.1    Yewdell, J.W.2    Bennink, J.R.3
  • 20
    • 0026762981 scopus 로고
    • Measles virus transmembrane fusion protein synthesized de novo or presented in immunostimulating complexes is endogenously processed for HLA class I- And class II-restricted cytotoxic T cell recognition
    • van Binnendijk, R. S., C. A. van Baalen, M. C. Poelen, P. de Vries, J. Boes, V. Cerundolo, A. D. Osterhaus, and F. G. UytdeHaag. 1992. Measles virus transmembrane fusion protein synthesized de novo or presented in immunostimulating complexes is endogenously processed for HLA class I- and class II-restricted cytotoxic T cell recognition. J. Exp. Med. 176:119.
    • (1992) J. Exp. Med. , vol.176 , pp. 119
    • Binnendijk, R.S.1    Van Baalen, C.A.2    Poelen, M.C.3    De Vries, P.4    Boes, J.5    Cerundolo, V.6    Osterhaus, A.D.7    Uytdehaag, F.G.8
  • 23
    • 0028034194 scopus 로고
    • Identification of a TAP-dependent leader peptide recognized by alloreactive T cells specific for a class Ib antigen
    • Aldrich, C. J., A. DeCloux, A. S. Woods, R. J. Cotter, M. J. Soloski, and J. Forman. 1994. Identification of a TAP-dependent leader peptide recognized by alloreactive T cells specific for a class Ib antigen. Cell 79:649.
    • (1994) Cell , vol.79 , pp. 649
    • Aldrich, C.J.1    Decloux, A.2    Woods, A.S.3    Cotter, R.J.4    Soloski, M.J.5    Forman, J.6
  • 24
    • 0028783818 scopus 로고
    • Strictly transporter of antigen presentation (TAP)-dependent presentation of an immunodominant cytotoxic T lymphocyte epitope in the signal sequence of a virus protein
    • Hombach, J., H. Pircher, S. Tonegawa, and R. M. Zinkernagel. 1995. Strictly transporter of antigen presentation (TAP)-dependent presentation of an immunodominant cytotoxic T lymphocyte epitope in the signal sequence of a virus protein. J. Exp. Med. 182:1615.
    • (1995) J. Exp. Med. , vol.182 , pp. 1615
    • Hombach, J.1    Pircher, H.2    Tonegawa, S.3    Zinkernagel, R.M.4
  • 25
    • 0030248766 scopus 로고    scopus 로고
    • Peptide antigen production by the proteasome: Complexity provides efficiency
    • Groettrup, M., A. Soza, U. Kuckelkora, 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    Kuckelkora, U.3    Kloetzel, P.M.4
  • 26
    • 0030016595 scopus 로고    scopus 로고
    • Structure and functions of the 20S and 26S proteasomes
    • Coux, O., K. Tanaka, and A. L. Goldberg. 1996. Structure and functions of the 20S and 26S proteasomes. Annu. Rev. Biochem. 65:801.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 801
    • Coux, O.1    Tanaka, K.2    Goldberg, A.L.3
  • 27
    • 0026040535 scopus 로고
    • Homology of proteasome subunits to a major histocompatibility complex-linked LMP gene
    • Martinez, C. K., and J. J. Monaco. 1991. Homology of proteasome subunits to a major histocompatibility complex-linked LMP gene. Nature 353:664.
    • (1991) Nature , vol.353 , pp. 664
    • Martinez, C.K.1    Monaco, J.J.2
  • 28
  • 29
    • 0025998206 scopus 로고
    • Subunit of the "20S" proteasome (multlcatalytic proteinase) encoded by the major histocompatibility complex
    • Ortiz-Navarrete, V., A. Seelig, M. Gernold, S. Frentzel, P. M. Kloetzel, and G. J. Hammerling. 1991. Subunit of the "20S" proteasome (multlcatalytic proteinase) encoded by the major histocompatibility complex. Nature 353:662.
    • (1991) Nature , vol.353 , pp. 662
    • Ortiz-Navarrete, V.1    Seelig, A.2    Gernold, M.3    Frentzel, S.4    Kloetzel, P.M.5    Hammerling, G.J.6
  • 31
    • 0028346277 scopus 로고
    • MHC-encoded proteasome subunits LMP2 and LMP7 are not required for efficient antigen presentation
    • Yewdell, J., C. Lapham, I. Bacik, T. Spies, and J. Bennink. 1994. MHC-encoded proteasome subunits LMP2 and LMP7 are not required for efficient antigen presentation. J. Immunol. 152:1163.
    • (1994) J. Immunol. , vol.152 , pp. 1163
    • Yewdell, J.1    Lapham, C.2    Bacik, I.3    Spies, T.4    Bennink, J.5
  • 32
    • 0028107066 scopus 로고
    • Presentation of viral antigens restricted by H-2Kb, Db or Kd in proteasome subunit LMP2- And LMP7-deficient cells
    • Zhou, X., F. Momburg, T. Liu, U. M. Abdel Motal, M. Jondal, G. J. Hammerling, and H. G. Ljunggren. 1994. Presentation of viral antigens restricted by H-2Kb, Db or Kd in proteasome subunit LMP2- and LMP7-deficient cells. Eur. J. Immunol. 24:1863.
    • (1994) Eur. J. Immunol. , vol.24 , pp. 1863
    • Zhou, X.1    Momburg, F.2    Liu, T.3    Abdel Motal, U.M.4    Jondal, M.5    Hammerling, G.J.6    Ljunggren, H.G.7
  • 36
    • 0027263157 scopus 로고
    • A role for the ubiquitin-dependent proteolytic pathway in MHC class J-restricted antigen presentation
    • Michalek, M. T., E. P. Grant, C. Gramm, A. L. Goldberg, and K. L. Rock. 1993. A role for the ubiquitin-dependent proteolytic pathway in MHC class J-restricted antigen presentation. Nature 363:552.
    • (1993) Nature , vol.363 , pp. 552
    • Michalek, M.T.1    Grant, E.P.2    Gramm, C.3    Goldberg, A.L.4    Rock, K.L.5
  • 37
    • 0028872334 scopus 로고
    • Presentation of endogenous and exogenous antigens is not affected by inactivation of E1 ubiquitin-activating enzyme in temperature-sensitive cell lines
    • Cox, J. H., P. Galardy, J. R. Bennink, and J. W. Yewdell. 1995. Presentation of endogenous and exogenous antigens is not affected by inactivation of E1 ubiquitin-activating enzyme in temperature-sensitive cell lines. J. Immunol. 154:511.
    • (1995) J. Immunol. , vol.154 , pp. 511
    • Cox, J.H.1    Galardy, P.2    Bennink, J.R.3    Yewdell, J.W.4
  • 38
    • 0029987724 scopus 로고    scopus 로고
    • Chemical denaturation and modification of ovalbumin alters its dependence on ubiquitin conjugation for class I antigen presentation
    • Michalek, M. T., E. P. Grant, and K. L. Rock. 1996. Chemical denaturation and modification of ovalbumin alters its dependence on ubiquitin conjugation for class I antigen presentation. J. Immunol. 157:617.
    • (1996) J. Immunol. , vol.157 , pp. 617
    • Michalek, M.T.1    Grant, E.P.2    Rock, K.L.3
  • 39
    • 0029120173 scopus 로고
    • Rate of antigen degradation by the ubiquitin-proteasome pathway influences MHC class I presentation
    • Grant, E. P., M. T. Michalek, A. L. Goldberg, and K. L. Rock. 1995. Rate of antigen degradation by the ubiquitin-proteasome pathway influences MHC class I presentation. J. Immunol. 155:3750.
    • (1995) J. Immunol. , vol.155 , pp. 3750
    • Grant, E.P.1    Michalek, M.T.2    Goldberg, A.L.3    Rock, K.L.4
  • 40
    • 0030805140 scopus 로고    scopus 로고
    • The listeria monocytogenes-secreted p60 protein is an n-end rule substrate in the cytosol of infected cells: Implications for major histocompatibility complex class I antigen processing of bacterial proteins
    • Sijts, A. M., I. Pilip, and E. G. Pamer. 1997. The listeria monocytogenes-secreted p60 protein is an n-end rule substrate in the cytosol of infected cells: implications for major histocompatibility complex class I antigen processing of bacterial proteins. J. Biol. Chem. 272:1926:1.
    • (1997) J. Biol. Chem. , vol.272 , Issue.1926 , pp. 1
    • Sijts, A.M.1    Pilip, I.2    Pamer, E.G.3
  • 41
    • 0028178515 scopus 로고
    • 20 S proteasomes are assembled via distinct precursor complexes: Processing of LMP2 and LMP7 proproteins takes place in 13-16 S preproteasome complexes
    • Frentzel, S., B. Pesold-Hurt, A. Seelig, and P. M. Kloetzel. 1994. 20 S proteasomes are assembled via distinct precursor complexes: processing of LMP2 and LMP7 proproteins takes place in 13-16 S preproteasome complexes. J. Mol. Biol. 236:975.
    • (1994) J. Mol. Biol. , vol.236 , pp. 975
    • Frentzel, S.1    Pesold-Hurt, B.2    Seelig, A.3    Kloetzel, P.M.4
  • 42
    • 0029781734 scopus 로고    scopus 로고
    • The proteolytic fragments generated by vertebrate proteasomes: Structural relationships to major histocompatibility complex class I binding peptides
    • Niedermann, G., G. King, S. Butz, U. Birsner, R. Grimm, J. Shabanowitz, D. F. Hunt, and K. Eichmann. 1996. The proteolytic fragments generated by vertebrate proteasomes: structural relationships to major histocompatibility complex class I binding peptides. Proc. Natl. Acad. Sci. USA 93:8572.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 8572
    • Niedermann, G.1    King, G.2    Butz, S.3    Birsner, U.4    Grimm, R.5    Shabanowitz, J.6    Hunt, D.F.7    Eichmann, K.8
  • 43
    • 0028968217 scopus 로고
    • Contribution of proteasome-mediated proteolysis to the hierarchy of epitopes presented by major histocompatibility complex class I molecules
    • Niedermann, G., S. Butz, H. G. Ihlenfeldt, R. Grimm, M. Lucchiari, H. Hoschutzky, G. Jung, B. Maier, and K. Eichmann. 1995. Contribution of proteasome-mediated proteolysis to the hierarchy of epitopes presented by major histocompatibility complex class I molecules. Immunity 2:289.
    • (1995) Immunity , vol.2 , pp. 289
    • Niedermann, G.1    Butz, S.2    Ihlenfeldt, H.G.3    Grimm, R.4    Lucchiari, M.5    Hoschutzky, H.6    Jung, G.7    Maier, B.8    Eichmann, K.9
  • 44
    • 0028097823 scopus 로고
    • Interferon gamma stimulation modulates the proteolytic activity and cleavage site preference of 20S mouse proteasomes
    • Boes, B., H. Hengel, T. Ruppert, G. Multhaup, U. H. Koszinowski, and P. M. Kloetzel. 1994. Interferon gamma stimulation modulates the proteolytic activity and cleavage site preference of 20S mouse proteasomes. J. Exp. Med. 179:901.
    • (1994) J. Exp. Med. , vol.179 , pp. 901
    • Boes, B.1    Hengel, H.2    Ruppert, T.3    Multhaup, G.4    Koszinowski, U.H.5    Kloetzel, P.M.6
  • 46
    • 0030061052 scopus 로고    scopus 로고
    • Effects of major-histocompatibility-complex-encoded subunits on the peptidase and proteolytic activities of human 20S proteasomes: Cleavage of proteins and antigenic peptides
    • Ehring, B., T. H. Meyer, C. Eckerskorn, F. Lottspeich, and R. Tampe. 1996. Effects of major-histocompatibility-complex-encoded subunits on the peptidase and proteolytic activities of human 20S proteasomes: cleavage of proteins and antigenic peptides. Eur. J. Biochem. 235:404.
    • (1996) Eur. J. Biochem. , vol.235 , pp. 404
    • Ehring, B.1    Meyer, T.H.2    Eckerskorn, C.3    Lottspeich, F.4    Tampe, R.5
  • 49
    • 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., T. Ruppert, L. Kuehn, M. Seeger, S. Standera, U. Koszinowski, and P. M. Kloetzel. 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. 270:2380:8.
    • (1995) J. Biol. Chem. , vol.270 , Issue.2380 , pp. 8
    • Groettrup, M.1    Ruppert, T.2    Kuehn, L.3    Seeger, M.4    Standera, S.5    Koszinowski, U.6    Kloetzel, P.M.7
  • 51
    • 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
  • 52
    • 0030926777 scopus 로고    scopus 로고
    • Lactacystin and clasto-lactacystin beta- Lactone modify multiple proteasome beta-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 beta- lactone modify multiple proteasome beta-subunits and inhibit intracellular protein degradation and major histocompatibility complex class I antigen presentation. J. Biol. Chem. 272:1343:7.
    • (1997) J. Biol. Chem. , vol.272 , Issue.1343 , pp. 7
    • Craiu, A.1    Gaczynska, M.2    Akopian, T.3    Gramm, C.F.4    Fenteany, G.5    Goldberg, A.L.6    Rock, K.L.7
  • 53
    • 0031228085 scopus 로고    scopus 로고
    • The effect of the proteasome inhibitor lactacystin on the presentation of transporter associated with antigen processing (TAP)-dependentand 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 transporter associated with antigen processing (TAP)-dependentand 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
  • 54
    • 0029123827 scopus 로고
    • Novel dipeptide aldehydes are proteasome inhibitors and block the MHC-I antigen-processing pathway
    • Harding, C. V., J. France, R. Song, J. M. Farah, S. Chatterjee, M. Iqbal, and R. Siman. 1995. Novel dipeptide aldehydes are proteasome inhibitors and block the MHC-I antigen-processing pathway. J. Immunol. 155:1767.
    • (1995) J. Immunol. , vol.155 , pp. 1767
    • Harding, C.V.1    France, J.2    Song, R.3    Farah, J.M.4    Chatterjee, S.5    Iqbal, M.6    Siman, R.7
  • 55
    • 0030040594 scopus 로고    scopus 로고
    • CTL epitope generation is tightly linked to cellular proteolysis of a Listeria monocytogenes antigen
    • Sijts, A. J., M. S. Villanueva, and E. G. Pamer. 1996. CTL epitope 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.1    Villanueva, M.S.2    Pamer, E.G.3
  • 56
    • 0029966286 scopus 로고    scopus 로고
    • The requirement for proteasome activity class I major histocompatibility complex antigen presentation is dictated by the length of preprocessed antigen
    • Yang, B., Y. S. Hahn, C. S. Hahn, and T. J. Braciale. 1996. The requirement for proteasome activity class I major histocompatibility complex antigen presentation is dictated by the length of preprocessed antigen. J. Exp. Med. 183:1545.
    • (1996) J. Exp. Med. , vol.183 , pp. 1545
    • Yang, B.1    Hahn, Y.S.2    Hahn, C.S.3    Braciale, T.J.4
  • 57
    • 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
  • 58
    • 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, E. A., B. Ortmann, M. Surman and P. Cresswell. 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.
    • (1996) J. Exp. Med. , vol.183 , pp. 1569
    • Hughes, E.A.1    Ortmann, B.2    Surman, M.3    Cresswell, P.4
  • 59
    • 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
  • 60
    • 0031114456 scopus 로고    scopus 로고
    • Point mutation flanking a CTL epitope ablates in vitro and in vivo recognition of a full-length viral protein
    • Yellen-Shaw, A. J., E. J. Wherry, G. C. Dubois, and L. C. Eisenlohr. 1997. Point mutation flanking a CTL epitope ablates in vitro and in vivo recognition of a full-length viral protein. J. Immunol. 158:3227.
    • (1997) J. Immunol. , vol.158 , pp. 3227
    • Yellen-Shaw, A.J.1    Wherry, E.J.2    Dubois, G.C.3    Eisenlohr, L.C.4
  • 61
    • 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
  • 62
    • 0024338401 scopus 로고
    • Brefeldin A specifically inhibits presentation of protein antigens to cytotoxic T lymphocytes
    • Yewdell, J. W., and J. R. Bennink. 1989. Brefeldin A specifically inhibits presentation of protein antigens to cytotoxic T lymphocytes. Science 244:1072.
    • (1989) Science , vol.244 , pp. 1072
    • Yewdell, J.W.1    Bennink, J.R.2
  • 63
    • 0024500652 scopus 로고
    • Brefeldin A implicates egress from endoplasmic reticulum in class I restricted antigen presentation
    • Nuchtern, J. G., J. S. Bonifacino, W. E. Biddison, and R. D. Klausner. 1989. Brefeldin A implicates egress from endoplasmic reticulum in class I restricted antigen presentation. Nature 339:223.
    • (1989) Nature , vol.339 , pp. 223
    • Nuchtern, J.G.1    Bonifacino, J.S.2    Biddison, W.E.3    Klausner, R.D.4
  • 64
    • 0024591235 scopus 로고
    • Rapid redistribution of Golgi proteins in the ER in cells treated with brefeldin A: Evidence for membrane cycling from Golgi to ER
    • Uppincolt-Schwartz, J., L. C. Yuan, J. S. Bonifacino, and R. D. Klausner. 1989. Rapid redistribution of Golgi proteins in the ER in cells treated with brefeldin A: evidence for membrane cycling from Golgi to ER. Cell 56:801.
    • (1989) Cell , vol.56 , pp. 801
    • Uppincolt-Schwartz, J.1    Yuan, L.C.2    Bonifacino, J.S.3    Klausner, R.D.4
  • 65
    • 0023692865 scopus 로고
    • Identification by site-directed mutagenesis of amino acid residues contributing to serologic and CTL-defined epitope differences between HLA-A2.1 and HLA-A2.3
    • Hogan, K. T., C. Clayberger, E. J. Bernhard, S. F. Walk, J. P. Ridge, P. Parham, A. M. Krensky, and V. H. Engelhard. 1988. Identification by site-directed mutagenesis of amino acid residues contributing to serologic and CTL-defined epitope differences between HLA-A2.1 and HLA-A2.3. J. Immunol. 141:2519.
    • (1988) J. Immunol. , vol.141 , pp. 2519
    • Hogan, K.T.1    Clayberger, C.2    Bernhard, E.J.3    Walk, S.F.4    Ridge, J.P.5    Parham, P.6    Krensky, A.M.7    Engelhard, V.H.8
  • 66
    • 7144221576 scopus 로고
    • T-cell recognition of class I MHC molecules studied using gene transfection, mutagenesis, and class I transgenic mice. In
    • R. Srivastava, B. P. Ram, and P. Tyle, eds. VCH Publishers, New York
    • Engelhard, V. H., E. J. Bernhard, M. J. Holterman, A.-X. T. Le, R. Henderson, J. P. Ridge, S. Strub, J. A. Barbosa, and E. Lacy. 1991. T-cell recognition of class I MHC molecules studied using gene transfection, mutagenesis, and class I transgenic mice. In Molecular Mechanisms of Immune Regulation. R. Srivastava, B. P. Ram, and P. Tyle, eds. VCH Publishers, New York, p. 107.
    • (1991) Molecular Mechanisms of Immune Regulation , pp. 107
    • Engelhard, V.H.1    Bernhard, E.J.2    Holterman, M.J.3    Le, A.-X.T.4    Henderson, R.5    Ridge, J.P.6    Strub, S.7    Barbosa, J.A.8    Lacy, E.9
  • 69
    • 0029968531 scopus 로고    scopus 로고
    • Importance of MHC class I α2 and α3 domains in the recognition of self and non-self MHC molecules
    • Newberg, M. H., D. H. Smith, S. B. Haertel, D. R. Vining, E. Lacy, and V. H. Engelhard. 1996. Importance of MHC class I α2 and α3 domains in the recognition of self and non-self MHC molecules. J. Immunol. 156:2473.
    • (1996) J. Immunol. , vol.156 , pp. 2473
    • Newberg, M.H.1    Smith, D.H.2    Haertel, S.B.3    Vining, D.R.4    Lacy, E.5    Engelhard, V.H.6
  • 71
    • 0028136465 scopus 로고
    • Peptidase activities of proteasomes are differentially regulated by the major histocompatibility complex-encoded genes for LMP2 and LMP7
    • Gaczynska, M., K. L. Rock, T. Spies, and A. L. Goldberg. 1994. Peptidase activities of proteasomes are differentially regulated by the major histocompatibility complex-encoded genes for LMP2 and LMP7. Proc. Natl. Acad. Sci. USA 91: 9213.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 9213
    • Gaczynska, M.1    Rock, K.L.2    Spies, T.3    Goldberg, A.L.4
  • 72
    • 0031973735 scopus 로고    scopus 로고
    • The class I antigen processing pathway for the membrane protein tyrosinase involves translation in the endoplasmic reticulum and processing in the cytosol
    • Mosse, C. A., L. Meadows, C. J. Luckey, D. J. Kittlesen, E. L. Huczko, C. L. Slingluff, Jr., J. Shabanowitz, D. F. Hunt, and V. H. Engelhard. 1998. The class I antigen processing pathway for the membrane protein tyrosinase involves translation in the endoplasmic reticulum and processing in the cytosol. J. Exp. Med. 187:37.
    • (1998) J. Exp. Med. , vol.187 , pp. 37
    • Mosse, C.A.1    Meadows, L.2    Luckey, C.J.3    Kittlesen, D.J.4    Huczko, E.L.5    Slingluff Jr., C.L.6    Shabanowitz, J.7    Hunt, D.F.8    Engelhard, V.H.9
  • 73
    • 0028130237 scopus 로고
    • T cell recognition of an HLA-A2-restricted epitope derived from a cleaved signal sequence
    • Gueguen, M., W. E. Biddison, and E. O. Long. 1994. T cell recognition of an HLA-A2-restricted epitope derived from a cleaved signal sequence. J. Exp. Med. 180:1989.
    • (1994) J. Exp. Med. , vol.180 , pp. 1989
    • Gueguen, M.1    Biddison, W.E.2    Long, E.O.3
  • 75
    • 0031010398 scopus 로고    scopus 로고
    • Covalent modification of the active site threonine of proteasomal beta subunits and the Escherichia coli homolog HslV by a new class of inhibitors
    • Bogyo, M., J. S. McMaster, M. Gaczynska, D. Tortorella, A. L. Goldberg, and H. Ploegh. 1997. Covalent modification of the active site threonine of proteasomal beta subunits and the Escherichia coli homolog HslV by a new class of inhibitors. Proc. Natl. Acad. Sci. USA 94:6629.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 6629
    • Bogyo, M.1    McMaster, J.S.2    Gaczynska, M.3    Tortorella, D.4    Goldberg, A.L.5    Ploegh, H.6
  • 76
    • 1842290406 scopus 로고    scopus 로고
    • Introduction of a glycosylation site into a secreted protein provides evidence for an alternative antigen processing pathway: Transport of precursors of major histocompatibility complex class I-restricted peptides from the endoplasmic reticulum to the cytosol
    • Bacik, I., H. L. Snyder, L. C. Anton, G. Russ, W. Chen, J. R. Bennink, L. Urge, L. Otvos, B. Dudkowska, L. Eisenlohr, and J. W. Yewdell. 1997. Introduction of a glycosylation site into a secreted protein provides evidence for an alternative antigen processing pathway: transport of precursors of major histocompatibility complex class I-restricted peptides from the endoplasmic reticulum to the cytosol. J. Exp. Med. 186:479.
    • (1997) J. Exp. Med. , vol.186 , pp. 479
    • Bacik, I.1    Snyder, H.L.2    Anton, L.C.3    Russ, G.4    Chen, W.5    Bennink, J.R.6    Urge, L.7    Otvos, L.8    Dudkowska, B.9    Eisenlohr, L.10    Yewdell, J.W.11
  • 77
    • 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, W. K., E. K. Mitchell, Y. Yang, P. A. Peterson, G. L. Waneck, and D. B. Williams. 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.
    • (1996) J. Exp. Med. , vol.184 , pp. 337
    • Suh, W.K.1    Mitchell, E.K.2    Yang, Y.3    Peterson, P.A.4    Waneck, G.L.5    Williams, D.B.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.