메뉴 건너뛰기




Volumn 162, Issue 8, 1999, Pages 4657-4662

Role of peptide backbone in T cell recognition

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID SUBSTITUTION; ANIMAL CELL; ANTIGENICITY; ARTICLE; CELL FUNCTION; CRYSTAL STRUCTURE; EFFECTOR CELL; HYBRIDOMA; MAJOR HISTOCOMPATIBILITY COMPLEX; MOLECULAR RECOGNITION; NONHUMAN; PEPTIDE SYNTHESIS; PRIORITY JOURNAL; RECEPTOR AFFINITY; RECEPTOR BINDING; T LYMPHOCYTE ACTIVATION;

EID: 0033561631     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (14)

References (47)
  • 1
    • 0024383535 scopus 로고
    • Antigen recognition by class I-restricted T lymphocytes
    • Townsend, A., and H. Bodmer. 1989. Antigen recognition by class I-restricted T lymphocytes. Annu. Rev. Immunol. 7:601.
    • (1989) Annu. Rev. Immunol. , vol.7 , pp. 601
    • Townsend, A.1    Bodmer, H.2
  • 2
    • 0028157771 scopus 로고
    • Structure of peptides associated with MHC class I molecules
    • Engelhard, V. 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.1
  • 3
    • 0028198644 scopus 로고
    • Peptide size selection by the major histocompatibility complex-encoded peptide transporter
    • Momburg, F., J. Roelse, G. J. Hammerling, and J. J. Neefjes. 1994. Peptide size selection by the major histocompatibility complex-encoded peptide transporter J. Exp. Med. 179:1613.
    • (1994) J. Exp. Med. , vol.179 , pp. 1613
    • Momburg, F.1    Roelse, J.2    Hammerling, G.J.3    Neefjes, J.J.4
  • 5
    • 0026618817 scopus 로고
    • Different length peptides bind to HLA-Aw68 similarly at their ends but bulge out in the middle
    • Guo, H. C., T. S. Jardetzky, T. P. Garrett, W. S. Lane, J. L. Strominger, and D. C. Wiley. 1992. Different length peptides bind to HLA-Aw68 similarly at their ends but bulge out in the middle. Nature 360:364.
    • (1992) Nature , vol.360 , pp. 364
    • Guo, H.C.1    Jardetzky, T.S.2    Garrett, T.P.3    Lane, W.S.4    Strominger, J.L.5    Wiley, D.C.6
  • 6
    • 0026728457 scopus 로고
    • Emerging principles for the recognition of peptide antigens by MHC class 1 molecules
    • Matsumura, M., D. H. Fremont, P. A. Peterson, and I. A. Wilson. 1992. Emerging principles for the recognition of peptide antigens by MHC class 1 molecules Science 257:927.
    • (1992) Science , vol.257 , pp. 927
    • Matsumura, M.1    Fremont, D.H.2    Peterson, P.A.3    Wilson, I.A.4
  • 8
    • 0026641803 scopus 로고
    • A critical role for conserved residues in the cleft of HLA-A2 in presentation of a nonapeptide to T cells
    • Latron, F., L. Pazmany, J. Morrison, R. Moots, M. A. Saper, A. McMichael, and J. L. Strominger. 1992. A critical role for conserved residues in the cleft of HLA-A2 in presentation of a nonapeptide to T cells. Science 257:964.
    • (1992) Science , vol.257 , pp. 964
    • Latron, F.1    Pazmany, L.2    Morrison, J.3    Moots, R.4    Saper, M.A.5    McMichael, A.6    Strominger, J.L.7
  • 9
    • 0028855951 scopus 로고
    • Efficient binding of reduced peptide bond pseudopeptides to major histocompatibility complex class I molecule
    • Guichard, G., S. Calbo, S. Muller, P. Kourilsky, J. P. Briand, and J. P. Abastado. 1995. Efficient binding of reduced peptide bond pseudopeptides to major histocompatibility complex class I molecule. J. Biol. Chem. 270:26057.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26057
    • Guichard, G.1    Calbo, S.2    Muller, S.3    Kourilsky, P.4    Briand, J.P.5    Abastado, J.P.6
  • 10
    • 0028032155 scopus 로고
    • Positive selection of lymphocytes
    • von Boehmer, H. 1994. Positive selection of lymphocytes. Cell 76:219.
    • (1994) Cell , vol.76 , pp. 219
    • Von Boehmer, H.1
  • 14
    • 18344405559 scopus 로고    scopus 로고
    • Two human T cell receptors bind in a similar diagonal mode to the HLA-A2/Tax peptide complex using different TCR amino acids
    • Ding, Y. H., K. J. Smith, D. N. Garboczi, U. Utz, W. E. Biddison, and D. C. Wiley. 1998. Two human T cell receptors bind in a similar diagonal mode to the HLA-A2/Tax peptide complex using different TCR amino acids. Immunity 8:403.
    • (1998) Immunity , vol.8 , pp. 403
    • Ding, Y.H.1    Smith, K.J.2    Garboczi, D.N.3    Utz, U.4    Biddison, W.E.5    Wiley, D.C.6
  • 15
    • 0029855347 scopus 로고    scopus 로고
    • Structure of the complex between human T-cell receptor, viral peptide and HLA-A2
    • Garboczi, D. N., P. Ghosh, U. Utz, Q. R. Fan, W. E. Biddison, and D. C. Wiley. 1996. Structure of the complex between human T-cell receptor, viral peptide and HLA-A2. Nature 384:134.
    • (1996) Nature , vol.384 , pp. 134
    • Garboczi, D.N.1    Ghosh, P.2    Utz, U.3    Fan, Q.R.4    Biddison, W.E.5    Wiley, D.C.6
  • 17
    • 0032549142 scopus 로고    scopus 로고
    • Structural basis of plasticity in T cell receptor recognition of a self peptide-MHC antigen
    • Garcia, K. C., M. Degano, L. R. Pease, M. Huang, P. A. Peterson, L. Teyton, and I. A. Wilson. 1998. Structural basis of plasticity in T cell receptor recognition of a self peptide-MHC antigen. Science 279:1166.
    • (1998) Science , vol.279 , pp. 1166
    • Garcia, K.C.1    Degano, M.2    Pease, L.R.3    Huang, M.4    Peterson, P.A.5    Teyton, L.6    Wilson, I.A.7
  • 20
    • 0027632992 scopus 로고
    • Development of a fully automated multichannel peptide synthesizer with integrated TFA cleavage capability
    • Neimark, J., and J. P. Briand. 1993. Development of a fully automated multichannel peptide synthesizer with integrated TFA cleavage capability. Pept. Res. 6:219.
    • (1993) Pept. Res. , vol.6 , pp. 219
    • Neimark, J.1    Briand, J.P.2
  • 21
    • 0029100015 scopus 로고
    • Dimerization of soluble MHC-peptide complexes is sufficient for activation of T-cell hybridoma and induction of unresponsiveness
    • Abastado, J. P., Y. C. Lone, A. Casrouge, G. Boulot, and P. Kourilsky. 1995. Dimerization of soluble MHC-peptide complexes is sufficient for activation of T-cell hybridoma and induction of unresponsiveness. J. Exp. Med. 182:439.
    • (1995) J. Exp. Med. , vol.182 , pp. 439
    • Abastado, J.P.1    Lone, Y.C.2    Casrouge, A.3    Boulot, G.4    Kourilsky, P.5
  • 24
    • 0028177527 scopus 로고
    • The Vβ CDR1 region of an MHC class I-restricted TCR is involved in the recognition of peptide/MHC I and superantigen/MHC II complex
    • Bellio, M., Y.-C. Lone, O. de la Calle-Martin, B. Malissen, J.-P. Abastado, and P. Kourilsky. 1994. The Vβ CDR1 region of an MHC Class I-restricted TCR is involved in the recognition of peptide/MHC I and superantigen/MHC II complex. J. Exp. Med. 179:1087.
    • (1994) J. Exp. Med. , vol.179 , pp. 1087
    • Bellio, M.1    Lone, Y.-C.2    De La Calle-Martin, O.3    Malissen, B.4    Abastado, J.-P.5    Kourilsky, P.6
  • 26
    • 0024845198 scopus 로고
    • Derivation of a T cell hybridoma variant deprived of functional T cell receptor α and β chain transcripts reveals a non-functional α-mRNA of BW5147 origin
    • Letourneur, F., and B. Malissen. 1989. Derivation of a T cell hybridoma variant deprived of functional T cell receptor α and β chain transcripts reveals a non-functional α-mRNA of BW5147 origin. Eur. J. Immunol. 19:2269.
    • (1989) Eur. J. Immunol. , vol.19 , pp. 2269
    • Letourneur, F.1    Malissen, B.2
  • 27
    • 0016301248 scopus 로고
    • Generation of cytotoxic T lymphocytes in vitro. I. Response of normal and immune mouse spleen cells in mixed leukocyte cultures
    • Cerottini, J. C., H. D. Engers, H. R. Macdonald, and T. Brunner. 1974. Generation of cytotoxic T lymphocytes in vitro. I. Response of normal and immune mouse spleen cells in mixed leukocyte cultures. J. Exp. Med. 140:703.
    • (1974) J. Exp. Med. , vol.140 , pp. 703
    • Cerottini, J.C.1    Engers, H.D.2    Macdonald, H.R.3    Brunner, T.4
  • 29
    • 0026529908 scopus 로고
    • HLA-A2-peptide complexes: Refolding and crystallization of molecules expressed in Escherichia coli and complexed with single antigenic peplides
    • Garboczi, D. N., D. T. Hung, and D. C. Wiley. 1992. HLA-A2-peptide complexes: refolding and crystallization of molecules expressed in Escherichia coli and complexed with single antigenic peplides. Proc. Natl. Acad. Sci. USA 89: 3429.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 3429
    • Garboczi, D.N.1    Hung, D.T.2    Wiley, D.C.3
  • 31
    • 0032143604 scopus 로고    scopus 로고
    • Individual variations in the murine T cell response to a specific peptide reflect variability in naive repertoires
    • Bousso, P., A. Casrouge, J. D. Altman, M. Haury, J. Kanellopoulos, J.-P. Abastado, and P. Kourilsky. 1998. Individual variations in the murine T cell response to a specific peptide reflect variability in naive repertoires. Immunity 9:169.
    • (1998) Immunity , vol.9 , pp. 169
    • Bousso, P.1    Casrouge, A.2    Altman, J.D.3    Haury, M.4    Kanellopoulos, J.5    Abastado, J.-P.6    Kourilsky, P.7
  • 32
    • 0023150034 scopus 로고
    • Solid phase synthesis of peptides containing the CH2NH peptide bond isostere
    • Sasaki, Y., and D. H. Coy. 1987. Solid phase synthesis of peptides containing the CH2NH peptide bond isostere. Peptides 8:119.
    • (1987) Peptides , vol.8 , pp. 119
    • Sasaki, Y.1    Coy, D.H.2
  • 36
    • 0026621224 scopus 로고
    • Atomic structure of a human MHC molecule presenting an influenza virus peptide
    • Silver, M., H.-C. Guo, J. Strominger, and D. Wiley. 1992. Atomic structure of a human MHC molecule presenting an influenza virus peptide. Nature 360:367.
    • (1992) Nature , vol.360 , pp. 367
    • Silver, M.1    Guo, H.-C.2    Strominger, J.3    Wiley, D.4
  • 38
    • 0027525106 scopus 로고
    • The antigenic identity of peptide-MHC complexes: A comparison of the conformations of five viral peptides presented by HLA-A2
    • Madden, D., D. Garboczi, and D. Wiley. 1993. The antigenic identity of peptide-MHC complexes: a comparison of the conformations of five viral peptides presented by HLA-A2. Cell 75:693.
    • (1993) Cell , vol.75 , pp. 693
    • Madden, D.1    Garboczi, D.2    Wiley, D.3
  • 39
    • 0026531092 scopus 로고
    • Structural diversity of the classical H-2 genes: K, D, and L
    • Pullen, J. K., R. M. Horton, Z. L. Cai, and L. R. Pease. 1992. Structural diversity of the classical H-2 genes: K, D, and L. J. Immunol. 148:953.
    • (1992) J. Immunol. , vol.148 , pp. 953
    • Pullen, J.K.1    Horton, R.M.2    Cai, Z.L.3    Pease, L.R.4
  • 40
    • 0028987607 scopus 로고
    • The origins of HLA-A,B,C polymorphism
    • Parham, P., E. J. Adams, and K. L. Arnett. 1995. The origins of HLA-A,B,C polymorphism. Immunol. Rev. 143:141.
    • (1995) Immunol. Rev. , vol.143 , pp. 141
    • Parham, P.1    Adams, E.J.2    Arnett, K.L.3
  • 41
    • 0027242282 scopus 로고
    • Differential role of conserved and polymorphic residues of the binding groove of MHC class I molecules in the selection of peptides
    • Abastado, J.-P., A. Casrouge, and P. Kourilsky. 1993. Differential role of conserved and polymorphic residues of the binding groove of MHC class I molecules in the selection of peptides. J. Immunol. 151:3569.
    • (1993) J. Immunol. , vol.151 , pp. 3569
    • Abastado, J.-P.1    Casrouge, A.2    Kourilsky, P.3
  • 42
    • 0028797801 scopus 로고
    • CD8 modulation of T-cell antigen receptor-ligand interactions on living cytotoxic T lymphocytes
    • Luescher, I. F., E. Vivier, A. Layer, J. Mahiou, F. Godeau, B. Malissen, and P. Romero. 1995. CD8 modulation of T-cell antigen receptor-ligand interactions on living cytotoxic T lymphocytes. Nature 373:353.
    • (1995) Nature , vol.373 , pp. 353
    • Luescher, I.F.1    Vivier, E.2    Layer, A.3    Mahiou, J.4    Godeau, F.5    Malissen, B.6    Romero, P.7
  • 44
    • 0032101405 scopus 로고    scopus 로고
    • Detection of antigen-specific T cells with multivalent soluble class 11 MHC covalent peptide complexes
    • Crawford, F., H. Kozono, J. White, P. Marrack, and J. Kappler. 1998. Detection of antigen-specific T cells with multivalent soluble class 11 MHC covalent peptide complexes. Immunity 8:675.
    • (1998) Immunity , vol.8 , pp. 675
    • Crawford, F.1    Kozono, H.2    White, J.3    Marrack, P.4    Kappler, J.5
  • 45
    • 0027321544 scopus 로고
    • Crystal structure of human immunodeficiency virus (HIV) type 2 protease in complex with a reduced amide inhibitor and comparison with HIV-1 protease structures
    • Tong, L., S. Pav, C. Pargellis, F. Do, D. Lamarre, and P. C. Anderson. 1993. Crystal structure of human immunodeficiency virus (HIV) type 2 protease in complex with a reduced amide inhibitor and comparison with HIV-1 protease structures. Proc. Natl. Acad. Sci. USA 90:8387.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 8387
    • Tong, L.1    Pav, S.2    Pargellis, C.3    Do, F.4    Lamarre, D.5    Anderson, P.C.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.