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Volumn 37, Issue 3, 2007, Pages 798-806

Potent T cell agonism mediated by a very rapid TCR/pMHG interaction

Author keywords

Biophysics; Protein protein interactions; TCR

Indexed keywords

GLYCOPROTEIN GP 33; MAJOR HISTOCOMPATIBILITY ANTIGEN; T LYMPHOCYTE RECEPTOR; UNCLASSIFIED DRUG; VIRUS GLYCOPROTEIN; GLYCOPROTEIN; GLYCOPROTEIN PEPTIDE 33 41, LYMPHOCYTIC CHORIOMENINGITIS VIRUS; GLYCOPROTEIN PEPTIDE 33-41, LYMPHOCYTIC CHORIOMENINGITIS VIRUS; H2 ANTIGEN; HISTOCOMPATIBILITY ANTIGEN H 2D(B); HISTOCOMPATIBILITY ANTIGEN H-2D(B); LIGAND; LYMPHOCYTE ANTIGEN RECEPTOR; PEPTIDE; PEPTIDE FRAGMENT; VIRUS ANTIGEN; VIRUS PROTEIN;

EID: 34147094622     PISSN: 00142980     EISSN: None     Source Type: Journal    
DOI: 10.1002/eji.200636743     Document Type: Article
Times cited : (26)

References (30)
  • 2
    • 0038725685 scopus 로고    scopus 로고
    • Negative selection - clearing out the bad apples from the T-cell repertoire
    • Palmer, E., Negative selection - clearing out the bad apples from the T-cell repertoire. Nat. Rev. Immunol. 2003. 3: 383-391.
    • (2003) Nat. Rev. Immunol , vol.3 , pp. 383-391
    • Palmer, E.1
  • 3
    • 16844371602 scopus 로고    scopus 로고
    • T cell homeostasis: Keeping useful T cells alive and live T cells useful
    • Jameson, S. C., T cell homeostasis: Keeping useful T cells alive and live T cells useful. Semin. Immunol. 2005. 17: 231-237.
    • (2005) Semin. Immunol , vol.17 , pp. 231-237
    • Jameson, S.C.1
  • 4
    • 0030772120 scopus 로고    scopus 로고
    • Peptide-induced T cell receptor down-regulation on naive T cells predicts agonist/ partial agonist properties and strictly correlates with T cell activation
    • Bachmann, M. F., Oxenius, A., Speiser, D. E., Mariathasan, S., Hengartner, H., Zinkernagel, R. M. and Ohashi, P. S., Peptide-induced T cell receptor down-regulation on naive T cells predicts agonist/ partial agonist properties and strictly correlates with T cell activation. Eur. J. Immunol. 1997. 27: 2195-2203.
    • (1997) Eur. J. Immunol , vol.27 , pp. 2195-2203
    • Bachmann, M.F.1    Oxenius, A.2    Speiser, D.E.3    Mariathasan, S.4    Hengartner, H.5    Zinkernagel, R.M.6    Ohashi, P.S.7
  • 6
    • 0034948337 scopus 로고    scopus 로고
    • The TCR triggering puzzle
    • van der Merwe, P. A., The TCR triggering puzzle. Immunity 2001. 14: 665-668.
    • (2001) Immunity , vol.14 , pp. 665-668
    • van der Merwe, P.A.1
  • 7
    • 0029037210 scopus 로고
    • Serial triggering of many T-cell receptors by a few peptide-MHC complexes
    • Valitutti, S., Muller, S., Cella, M., Padovan, E. and Lanzavecchia, A., Serial triggering of many T-cell receptors by a few peptide-MHC complexes. Nature 1995. 375: 148-151.
    • (1995) Nature , vol.375 , pp. 148-151
    • Valitutti, S.1    Muller, S.2    Cella, M.3    Padovan, E.4    Lanzavecchia, A.5
  • 8
    • 0348047600 scopus 로고    scopus 로고
    • Evidence that structural rearrangements and/or flexibility during TCR binding can contribute to T cell activation
    • Krogsgaard, M., Prado, N., Adams, E. J., He, X. L., Chow, D. C., Wilson, D. B., Garcia, K. C. and Davis, M. M., Evidence that structural rearrangements and/or flexibility during TCR binding can contribute to T cell activation. Mol. Cell 2003. 12: 1367-1378.
    • (2003) Mol. Cell , vol.12 , pp. 1367-1378
    • Krogsgaard, M.1    Prado, N.2    Adams, E.J.3    He, X.L.4    Chow, D.C.5    Wilson, D.B.6    Garcia, K.C.7    Davis, M.M.8
  • 9
    • 0041929446 scopus 로고    scopus 로고
    • TCR binding kinetics measured with MHC class I tetramers reveal a positive selecting peptide with relatively high affinity for TCR
    • Holmberg, K., Mariathasan, S., Ohteki, T., Ohashi, P. S. and Gascoigne, N. R., TCR binding kinetics measured with MHC class I tetramers reveal a positive selecting peptide with relatively high affinity for TCR. J. Immunol. 2003. 171: 2427-2434.
    • (2003) J. Immunol , vol.171 , pp. 2427-2434
    • Holmberg, K.1    Mariathasan, S.2    Ohteki, T.3    Ohashi, P.S.4    Gascoigne, N.R.5
  • 10
    • 0028832613 scopus 로고
    • Emergence of virus escape mutants after immunization with epitope vaccine
    • Weidt, G., Deppert, W., Utermohlen, O., Heukeshoven, J. and Lehmann-Grube, F., Emergence of virus escape mutants after immunization with epitope vaccine. J. Virol. 1995. 69: 7147-7151.
    • (1995) J. Virol , vol.69 , pp. 7147-7151
    • Weidt, G.1    Deppert, W.2    Utermohlen, O.3    Heukeshoven, J.4    Lehmann-Grube, F.5
  • 12
    • 0030848578 scopus 로고    scopus 로고
    • Self antigens expressed by solid tumors do not efficiently stimulate naive or activated T cells: Implications for immunotherapy
    • Speiser, D. E., Miranda, R., Zakarian, A., Bachmann, M. F., McKall-Faienza, K., Odermatt, B., Hanahan, D. et al., Self antigens expressed by solid tumors do not efficiently stimulate naive or activated T cells: Implications for immunotherapy. J. Exp. Med. 1997 186: 645-653.
    • (1997) J. Exp. Med , vol.186 , pp. 645-653
    • Speiser, D.E.1    Miranda, R.2    Zakarian, A.3    Bachmann, M.F.4    McKall-Faienza, K.5    Odermatt, B.6    Hanahan, D.7
  • 14
    • 0030003476 scopus 로고    scopus 로고
    • Mature T cell reactivity altered by peptide agonist that induces positive selection
    • Sebzda, E., Kundig, T. M., Thomson, C. T., Aoki, K., Mak, S. Y., Mayer, J. P., Zamborelli, T. et al., Mature T cell reactivity altered by peptide agonist that induces positive selection. J. Exp. Med. 1996. 183: 1093-1104.
    • (1996) J. Exp. Med , vol.183 , pp. 1093-1104
    • Sebzda, E.1    Kundig, T.M.2    Thomson, C.T.3    Aoki, K.4    Mak, S.Y.5    Mayer, J.P.6    Zamborelli, T.7
  • 18
    • 0034730372 scopus 로고    scopus 로고
    • Viral escape at the molecular level explained by quantitative T-cell receptor/peptide/MHC interactions and the crystal structure of a peptide/MHC complex
    • Tissot, A. C., Ciatto, C., Mittl, P. R., Grutter, M. G. and Pluckthun, A., Viral escape at the molecular level explained by quantitative T-cell receptor/peptide/MHC interactions and the crystal structure of a peptide/MHC complex. J. Mol. Biol. 2000. 302: 873-885.
    • (2000) J. Mol. Biol , vol.302 , pp. 873-885
    • Tissot, A.C.1    Ciatto, C.2    Mittl, P.R.3    Grutter, M.G.4    Pluckthun, A.5
  • 22
    • 0033613074 scopus 로고    scopus 로고
    • Thermodynamics of T cell receptor binding to peptide-MHC: Evidence for a general mechanism of molecular scanning
    • Boniface, J. J., Reich, Z., Lyons, D. S. and Davis, M. M., Thermodynamics of T cell receptor binding to peptide-MHC: Evidence for a general mechanism of molecular scanning. Proc. Natl. Acad. Sci. USA 1999. 96: 11446-11451.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 11446-11451
    • Boniface, J.J.1    Reich, Z.2    Lyons, D.S.3    Davis, M.M.4
  • 23
    • 0042971650 scopus 로고    scopus 로고
    • Molecular interactions mediating T cell antigen recognition
    • van der Merwe, P. A. and Davis, S. J., Molecular interactions mediating T cell antigen recognition. Annu. Rev. Immunol. 2003. 21: 659-684.
    • (2003) Annu. Rev. Immunol , vol.21 , pp. 659-684
    • van der Merwe, P.A.1    Davis, S.J.2
  • 25
    • 33747092261 scopus 로고    scopus 로고
    • Altered peptide ligands induce delayed CD8-T cell receptor interaction - a role for CD8 in distinguishing antigen quality
    • Yachi, P. P., Ampudia, J., Zal, T. and Gascoigne, N. R., Altered peptide ligands induce delayed CD8-T cell receptor interaction - a role for CD8 in distinguishing antigen quality. Immunity 2006. 25: 203-211.
    • (2006) Immunity , vol.25 , pp. 203-211
    • Yachi, P.P.1    Ampudia, J.2    Zal, T.3    Gascoigne, N.R.4
  • 27
    • 21444445173 scopus 로고    scopus 로고
    • Directed evolution of human T-cell receptors with picomolar affinities by phage display
    • Li, Y., Moysey, R., Molloy, P. E., Vuidepot, A. L., Mahon, T., Baston, E., Dunn, S. et al., Directed evolution of human T-cell receptors with picomolar affinities by phage display. Nat. Biotechnol. 2005. 23: 349-354.
    • (2005) Nat. Biotechnol , vol.23 , pp. 349-354
    • Li, Y.1    Moysey, R.2    Molloy, P.E.3    Vuidepot, A.L.4    Mahon, T.5    Baston, E.6    Dunn, S.7
  • 28
    • 0025006862 scopus 로고
    • Direct binding of peptide to empty MHC class I molecules on intact cells and in vitro
    • Schumacher, T. N., Heemels, M. T., Neefjes, J. J., Kast, W. M., Melief, C. J. and Ploegh, H. L., Direct binding of peptide to empty MHC class I molecules on intact cells and in vitro. Cell 1990. 62: 563-567.
    • (1990) Cell , vol.62 , pp. 563-567
    • Schumacher, T.N.1    Heemels, M.T.2    Neefjes, J.J.3    Kast, W.M.4    Melief, C.J.5    Ploegh, H.L.6
  • 29
    • 0026529908 scopus 로고
    • HLA-A2-peptide complexes: Refolding and crystallization of molecules expressed in Escherichia coli and complexed with single antigenic peptides
    • Garboczi, D. N., Hung, D. T. and Wiley, D. C., HLA-A2-peptide complexes: Refolding and crystallization of molecules expressed in Escherichia coli and complexed with single antigenic peptides. Proc. Natl. Acad. Sci. USA 1992. 89: 3429-3433.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 3429-3433
    • Garboczi, D.N.1    Hung, D.T.2    Wiley, D.C.3
  • 30
    • 0032924825 scopus 로고    scopus 로고
    • BirA enzyme: Production and application in the study of membrane receptor-ligand interactions by site-specific biotinylation
    • O'Callaghan, C. A., Byford, M. F., Wyer, J. R., Willcox, B. E., Jakobsen, B. K., McMichael, A. J. and Bell, J. I., BirA enzyme: Production and application in the study of membrane receptor-ligand interactions by site-specific biotinylation. Anal. Biochem. 1999. 266: 9-15.
    • (1999) Anal. Biochem , vol.266 , pp. 9-15
    • O'Callaghan, C.A.1    Byford, M.F.2    Wyer, J.R.3    Willcox, B.E.4    Jakobsen, B.K.5    McMichael, A.J.6    Bell, J.I.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.