메뉴 건너뛰기




Volumn 158, Issue 4, 1997, Pages 1727-1733

Regulation of Class I-Restricted Epitope Processing by Local or Distal Flanking Sequence

Author keywords

[No Author keywords available]

Indexed keywords

CORE PROTEIN; EPITOPE; H2 ANTIGEN; NP PROTEIN, INFLUENZA A VIRUS; NUCLEOPROTEIN; PROTEINASE; RNA BINDING PROTEIN;

EID: 0031568385     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (40)

References (52)
  • 1
    • 0026484826 scopus 로고
    • Cell biology of antigen processing and presentation to major histocompatibility complex class I molecule-restricted T lymphocytes
    • Yewdell, J. W., and J. R. Bennink. 1992. Cell biology of antigen processing and presentation to major histocompatibility complex class I molecule-restricted T lymphocytes. Adv. Immunol. 52:1.
    • (1992) Adv. Immunol. , vol.52 , pp. 1
    • Yewdell, J.W.1    Bennink, J.R.2
  • 2
    • 0027468145 scopus 로고
    • The biochemistry and cell biology of antigen processing and presentation
    • Germain, R. N., and D. H. Margulies. 1993. The biochemistry and cell biology of antigen processing and presentation. Annu. Rev. Immunol. 11:403.
    • (1993) Annu. Rev. Immunol. , vol.11 , pp. 403
    • Germain, R.N.1    Margulies, D.H.2
  • 3
    • 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
  • 4
    • 0025155682 scopus 로고
    • Cellular peptide composition governed by major histocompatibility complex class I molecules
    • Falk, K., O. Rötzschke, and H.-G. Rammensee. 1990. Cellular peptide composition governed by major histocompatibility complex class I molecules. Nature 348:248.
    • (1990) Nature , vol.348 , pp. 248
    • Falk, K.1    Rötzschke, O.2    Rammensee, H.-G.3
  • 5
    • 0028018268 scopus 로고
    • The ubiquitin-proteasome proteolytic pathway
    • Ciechanover, A. 1994. The ubiquitin-proteasome proteolytic pathway. Cell 79:13.
    • (1994) Cell , vol.79 , pp. 13
    • Ciechanover, A.1
  • 6
    • 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
  • 8
    • 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. Hoschützky, 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    Hoschützky, H.6    Jung, G.7    Maier, B.8    Eichmann, K.9
  • 9
  • 10
    • 0027263157 scopus 로고
    • A role for the ubiquitin-dependent proteolytic pathway in MHC class I-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 I-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
  • 12
    • 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
  • 13
    • 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
  • 15
    • 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
    • 0027943180 scopus 로고
    • Trimming of TAP-translocated peptides in the endoplasmic reticulum and in the cytosol during recycling
    • Roelse, J., M. Grommé, F. Momburg, G. Hämmerling, and J. Neefjes. 1994. Trimming of TAP-translocated peptides in the endoplasmic reticulum and in the cytosol during recycling. J. Exp. Med. 180:1591.
    • (1994) J. Exp. Med. , vol.180 , pp. 1591
    • Roelse, J.1    Grommé, M.2    Momburg, F.3    Hämmerling, G.4    Neefjes, J.5
  • 17
    • 0024530961 scopus 로고
    • Recognition of oligonucleotide-encoded T cell epitopes introduced into a gene unrelated to the original antigen
    • Chimini, G., P. Pala, J. Sire, B. R. Jordan, and J. L. Maryanski. 1989. Recognition of oligonucleotide-encoded T cell epitopes introduced into a gene unrelated to the original antigen. J. Exp. Med. 169:297.
    • (1989) J. Exp. Med. , vol.169 , pp. 297
    • Chimini, G.1    Pala, P.2    Sire, J.3    Jordan, B.R.4    Maryanski, J.L.5
  • 18
    • 0025916341 scopus 로고
    • Presentation of viral antigen to class I major histocompatibility complex-restricted cytotoxic T lymphocytes: Recognition of an immunodominant influenza hemagglutinin site by cytotoxic T lymphocytes is independent of the position of the site in the hemagglutinin translation product
    • Hahn, Y. S., V. L. Braciale, and T. J. Braciale. 1991. Presentation of viral antigen to class I major histocompatibility complex-restricted cytotoxic T lymphocytes: recognition of an immunodominant influenza hemagglutinin site by cytotoxic T lymphocytes is independent of the position of the site in the hemagglutinin translation product. J. Exp. Med. 174:733.
    • (1991) J. Exp. Med. , vol.174 , pp. 733
    • Hahn, Y.S.1    Braciale, V.L.2    Braciale, T.J.3
  • 19
    • 0026582620 scopus 로고
    • Cells expressing an H chain Ig gene carrying a viral T cell epitope are lysed by specific cytolytic T cells
    • Zaghouani, H., M. Krystal, H. Kuzu, T. Moran, H. Shah, Y. Kuzu, J. Schulman, and C. Bona. 1992. Cells expressing an H chain Ig gene carrying a viral T cell epitope are lysed by specific cytolytic T cells. J. Immunol. 148:3604.
    • (1992) J. Immunol. , vol.148 , pp. 3604
    • Zaghouani, H.1    Krystal, M.2    Kuzu, H.3    Moran, T.4    Shah, H.5    Kuzu, Y.6    Schulman, J.7    Bona, C.8
  • 20
    • 0027507633 scopus 로고
    • Simian virus 40 T antigen as a carrier for the expression of cytotoxic T-lymphocyte recognition epitopes
    • Fu, T.-M., R. H. Bonneau, M. J. Tevethia, and S. S. Tevethia. 1993. Simian virus 40 T antigen as a carrier for the expression of cytotoxic T-lymphocyte recognition epitopes. J. Virol. 67:6866.
    • (1993) J. Virol. , vol.67 , pp. 6866
    • Fu, T.-M.1    Bonneau, R.H.2    Tevethia, M.J.3    Tevethia, S.S.4
  • 21
    • 0026599764 scopus 로고
    • Flanking sequences influence the presentation of an endogenously synthesized peptide to cytotoxic T lymphocytes
    • Eisenlohr, L. C., J. W. Yewdell, and J. R. Bennink. 1992. Flanking sequences influence the presentation of an endogenously synthesized peptide to cytotoxic T lymphocytes. J. Exp. Med. 175:481.
    • (1992) J. Exp. Med. , vol.175 , pp. 481
    • Eisenlohr, L.C.1    Yewdell, J.W.2    Bennink, J.R.3
  • 22
    • 0026524347 scopus 로고
    • Extracellular processing of antigens that bind class I major histocompatibility molecules
    • Sherman, L. A., T. A. Burke, and J. A. Biggs. 1992. Extracellular processing of antigens that bind class I major histocompatibility molecules. J. Exp. Med. 175:1221.
    • (1992) J. Exp. Med. , vol.175 , pp. 1221
    • Sherman, L.A.1    Burke, T.A.2    Biggs, J.A.3
  • 23
    • 0026455159 scopus 로고
    • Expression of a membrane protease enhances presentation ot endogenous antigens to MHC class I-restricted T lymphocytes
    • Eisenlohr, L. C., I. Bacik, J. R. Bennink, K. Bernstein, and J. W. Yewdell. 1992. Expression of a membrane protease enhances presentation ot endogenous antigens to MHC class I-restricted T lymphocytes. Cell 71:963.
    • (1992) Cell , vol.71 , pp. 963
    • Eisenlohr, L.C.1    Bacik, I.2    Bennink, J.R.3    Bernstein, K.4    Yewdell, J.W.5
  • 25
    • 0025200973 scopus 로고
    • The specificities of yeast methionine aminopeptidase and acelylation of amino-terminal methionine in vivo
    • Moerschell, R. P., Y. Hosokawa, S. Tsunasawa, and F. Sherman. 1990. The specificities of yeast methionine aminopeptidase and acelylation of amino-terminal methionine in vivo. J. Biol. Chem. 265:19638.
    • (1990) J. Biol. Chem. , vol.265 , pp. 19638
    • Moerschell, R.P.1    Hosokawa, Y.2    Tsunasawa, S.3    Sherman, F.4
  • 26
    • 0025643362 scopus 로고
    • A general method for rapid site-directed mutagenesis using the polymerase chain reaction
    • Landt O., H.-P., Grunert, and U. A. Hahn. 1990. A general method for rapid site-directed mutagenesis using the polymerase chain reaction. Gene 96:125.
    • (1990) Gene , vol.96 , pp. 125
    • Landt, O.1    Grunert, H.-P.2    Hahn, U.A.3
  • 27
    • 0023860006 scopus 로고
    • Enhanced recognition of a modified peptide antigen by cytotoxic T cells specific for influenza nucleoprotein
    • Bodmer, H. C., R. M. Pemberton, J. B. Rothbard, and B. A. Askonas. 1988. Enhanced recognition of a modified peptide antigen by cytotoxic T cells specific for influenza nucleoprotein. Cell 52:253.
    • (1988) Cell , vol.52 , pp. 253
    • Bodmer, H.C.1    Pemberton, R.M.2    Rothbard, J.B.3    Askonas, B.A.4
  • 28
    • 0026766091 scopus 로고
    • The N-end rule
    • Varshavsky, A. 1992. The N-end rule. Cell 69:725.
    • (1992) Cell , vol.69 , pp. 725
    • Varshavsky, A.1
  • 29
    • 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
  • 30
    • 0029854328 scopus 로고    scopus 로고
    • Ribosomal scanning past the primary initiation codon as a mechanism for expression of CTL epitopes encoded in alternative reading frames
    • Bullock, T. N. J., and L. C. Eisenlohr. 1996. Ribosomal scanning past the primary initiation codon as a mechanism for expression of CTL epitopes encoded in alternative reading frames. J. Exp. Med. 184:1319.
    • (1996) J. Exp. Med. , vol.184 , pp. 1319
    • Bullock, T.N.J.1    Eisenlohr, L.C.2
  • 31
    • 0027239749 scopus 로고
    • Selective and ATP-dependent translocation of peptides by the MHC-encoded transporter
    • Neefjes, J. J., F. Momburg, and G. J. Hämmerling. 1993. Selective and ATP-dependent translocation of peptides by the MHC-encoded transporter. Science 261:769.
    • (1993) Science , vol.261 , pp. 769
    • Neefjes, J.J.1    Momburg, F.2    Hämmerling, G.J.3
  • 35
    • 0028829908 scopus 로고
    • Major differences in transporter associated with antigen presentation (TAP)-dependent translocation of MHC class I-presentable peptides and the effect of flanking sequences
    • Neisig, A., J. Roelse, A. J. A. M. Sijts, F. Ossendorp, M. C. W. Feltkamp, M. Kast, C. J. M. Melief, and J. J. Neefjes. 1995. Major differences in transporter associated with antigen presentation (TAP)-dependent translocation of MHC class I-presentable peptides and the effect of flanking sequences. J. Immunol. 154:1273.
    • (1995) J. Immunol. , vol.154 , pp. 1273
    • Neisig, A.1    Roelse, J.2    Sijts, A.J.A.M.3    Ossendorp, F.4    Feltkamp, M.C.W.5    Kast, M.6    Melief, C.J.M.7    Neefjes, J.J.8
  • 37
    • 0026500826 scopus 로고
    • Presentation of viral antigen by MHC class I molecules is dependent on a putative peptide transporter heterodimer
    • Spies, T., V. Cerundolo, M. Colonna, P. Cresswell, A. Townsend, and R. DeMars. 1992. Presentation of viral antigen by MHC class I molecules is dependent on a putative peptide transporter heterodimer. Nature 355:644.
    • (1992) Nature , vol.355 , pp. 644
    • Spies, T.1    Cerundolo, V.2    Colonna, M.3    Cresswell, P.4    Townsend, A.5    DeMars, R.6
  • 39
    • 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
  • 40
    • 0023505078 scopus 로고
    • Ubiquitin-mediated pathways for intracellular proteolysis
    • Rechsteiner, M. 1987. Ubiquitin-mediated pathways for intracellular proteolysis. Annu. Rev. Cell Biol. 3:1.
    • (1987) Annu. Rev. Cell Biol. , vol.3 , pp. 1
    • Rechsteiner, M.1
  • 41
    • 0028303252 scopus 로고
    • Activation-dependent ubiquitination of a T cell antigen receptor subunit on multiple intracellular lysines
    • Hou, D., C. Cenciarelli, J. P. Jensen, H. B. Nguyen, and A. M. Weissman. 1994. Activation-dependent ubiquitination of a T cell antigen receptor subunit on multiple intracellular lysines. J. Biol. Chem. 269:14244.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14244
    • Hou, D.1    Cenciarelli, C.2    Jensen, J.P.3    Nguyen, H.B.4    Weissman, A.M.5
  • 42
    • 0026503828 scopus 로고
    • The mechanism and functions of ATP-dependent proteases in bacterial and animal cells
    • Goldberg, A. L. 1992. The mechanism and functions of ATP-dependent proteases in bacterial and animal cells. Eur. J. Biochem. 203:9.
    • (1992) Eur. J. Biochem. , vol.203 , pp. 9
    • Goldberg, A.L.1
  • 44
    • 0029123827 scopus 로고
    • Novel dipeptide aldehydes are proteasome inhibitors and block the MHC-1 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-1 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
  • 45
    • 0030040594 scopus 로고    scopus 로고
    • CTL epitope 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 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.A.M.1    Villanueva, M.S.2    Pamer, E.G.3
  • 46
    • 0029930418 scopus 로고    scopus 로고
    • The rat cim effect: TAP allele-dependent changes in a class I MHC anchor motif and evidence against C-terminal trimming of peptides in the ER
    • Powis, S. J., L. L. Young, E. Joly, P. J. Barker, L. Richardson, R. P. Brandy, C. J. Melief, J. C. Howard, and G. W. Butcher. 1996. The rat cim effect: TAP allele-dependent changes in a class I MHC anchor motif and evidence against C-terminal trimming of peptides in the ER. Immunity 4:159.
    • (1996) Immunity , vol.4 , pp. 159
    • Powis, S.J.1    Young, L.L.2    Joly, E.3    Barker, P.J.4    Richardson, L.5    Brandy, R.P.6    Melief, C.J.7    Howard, J.C.8    Butcher, G.W.9
  • 48
    • 0025930898 scopus 로고
    • Both cyclin AD60 and BD97 are stable and arrest cells in M-phase, but only cyclin BD97 turns on cyclin destruction
    • Luca, F. C., E. K. Shibuya, C. E. Dohrmann, and J. V. Ruderman. 1991. Both cyclin AD60 and BD97 are stable and arrest cells in M-phase, but only cyclin BD97 turns on cyclin destruction. EMBO J. 10:4311.
    • (1991) EMBO J. , vol.10 , pp. 4311
    • Luca, F.C.1    Shibuya, E.K.2    Dohrmann, C.E.3    Ruderman, J.V.4
  • 49
    • 0026089183 scopus 로고
    • Cyclin is degraded by the ubiquitin pathway
    • Glotzer, M., A. W. Murray, and M. W. Kirschner. 1991. Cyclin is degraded by the ubiquitin pathway. Nature 349:132.
    • (1991) Nature , vol.349 , pp. 132
    • Glotzer, M.1    Murray, A.W.2    Kirschner, M.W.3
  • 50
    • 0028027308 scopus 로고
    • Ubiquitin-dependent c-Jun degradation in vivo is mediated by the d domain
    • Treier, M., L. M. Staszewski, and D. Bohmann. 1994. Ubiquitin-dependent c-Jun degradation in vivo is mediated by the d domain. Cell 78:787.
    • (1994) Cell , vol.78 , pp. 787
    • Treier, M.1    Staszewski, L.M.2    Bohmann, D.3
  • 51
    • 0025331090 scopus 로고
    • In vivo degradation of a transcriptional regulator: The yeast a2 repressor
    • Hochstrasser, M., and A. Varshavsky. 1990. In vivo degradation of a transcriptional regulator: the yeast a2 repressor. Cell 61:697.
    • (1990) Cell , vol.61 , pp. 697
    • Hochstrasser, M.1    Varshavsky, A.2
  • 52
    • 0029965803 scopus 로고    scopus 로고
    • The protease inhibitor, N-actyl-L-leucyl-L-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-actyl-L-leucyl-L-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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.