메뉴 건너뛰기




Volumn 19, Issue 4, 2007, Pages 262-271

TCR recognition of peptide/MHC class II complexes and superantigens

Author keywords

Major histocompatibility complex; Peptide antigen; Superantigen; T cell activity; T cell receptor

Indexed keywords

BACTERIAL TOXIN; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 2; PEPTIDE DERIVATIVE; SUPERANTIGEN; T LYMPHOCYTE RECEPTOR;

EID: 34447278825     PISSN: 10445323     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.smim.2007.04.006     Document Type: Review
Times cited : (87)

References (68)
  • 1
    • 0035902080 scopus 로고    scopus 로고
    • Progress in human tumour immunology and immunotherapy
    • Rosenberg S.A. Progress in human tumour immunology and immunotherapy. Nature 411 6835 (2001) 380-384
    • (2001) Nature , vol.411 , Issue.6835 , pp. 380-384
    • Rosenberg, S.A.1
  • 2
    • 4344705662 scopus 로고    scopus 로고
    • Immune recognition of self in immunity against cancer
    • Houghton A.N., and Guevara-Patino J.A. Immune recognition of self in immunity against cancer. J Clin Invest 114 4 (2004) 468-471
    • (2004) J Clin Invest , vol.114 , Issue.4 , pp. 468-471
    • Houghton, A.N.1    Guevara-Patino, J.A.2
  • 3
    • 32244444211 scopus 로고    scopus 로고
    • Autoimmunity and tumor immunity induced by immune responses to mutations in self
    • Engelhorn M.E., Guevara-Patino J.A., Noffz G., Hooper A.T., Lou O., Gold J.S., et al. Autoimmunity and tumor immunity induced by immune responses to mutations in self. Nat Med 12 2 (2006) 198-206
    • (2006) Nat Med , vol.12 , Issue.2 , pp. 198-206
    • Engelhorn, M.E.1    Guevara-Patino, J.A.2    Noffz, G.3    Hooper, A.T.4    Lou, O.5    Gold, J.S.6
  • 5
    • 17644396349 scopus 로고    scopus 로고
    • Immunology of multiple sclerosis
    • Sospedra M., and Martin R. Immunology of multiple sclerosis. Annu Rev Immunol 23 (2005) 683-747
    • (2005) Annu Rev Immunol , vol.23 , pp. 683-747
    • Sospedra, M.1    Martin, R.2
  • 6
    • 18744385526 scopus 로고    scopus 로고
    • Expanded T cells from pancreatic lymph nodes of type 1 diabetic subjects recognize an insulin epitope
    • Kent S.C., Chen Y., Bregoli L., Clemmings S.M., Kenyon N.S., Ricordi C., et al. Expanded T cells from pancreatic lymph nodes of type 1 diabetic subjects recognize an insulin epitope. Nature 435 7039 (2005) 224-228
    • (2005) Nature , vol.435 , Issue.7039 , pp. 224-228
    • Kent, S.C.1    Chen, Y.2    Bregoli, L.3    Clemmings, S.M.4    Kenyon, N.S.5    Ricordi, C.6
  • 7
    • 0035852674 scopus 로고    scopus 로고
    • Identification and modulation of a naturally processed T cell epitope from the diabetes-associated autoantigen human glutamic acid decarboxylase 65 (hGAD65)
    • Nepom G.T., Lippolis J.D., White F.M., Masewicz S., Marto J.A., Herman A., et al. Identification and modulation of a naturally processed T cell epitope from the diabetes-associated autoantigen human glutamic acid decarboxylase 65 (hGAD65). Proc Natl Acad Sci USA 98 4 (2001) 1763-1768
    • (2001) Proc Natl Acad Sci USA , vol.98 , Issue.4 , pp. 1763-1768
    • Nepom, G.T.1    Lippolis, J.D.2    White, F.M.3    Masewicz, S.4    Marto, J.A.5    Herman, A.6
  • 8
    • 0242491039 scopus 로고    scopus 로고
    • Negative selection and autoimmunity
    • Ohashi P.S. Negative selection and autoimmunity. Curr Opin Immunol 15 6 (2003) 668-676
    • (2003) Curr Opin Immunol , vol.15 , Issue.6 , pp. 668-676
    • Ohashi, P.S.1
  • 9
    • 0035171545 scopus 로고    scopus 로고
    • Promiscuous gene expression in medullary thymic epithelial cells mirrors the peripheral self
    • Derbinski J., Schulte A., Kyewski B., and Klein L. Promiscuous gene expression in medullary thymic epithelial cells mirrors the peripheral self. Nat Immunol 2 11 (2001) 1032-1039
    • (2001) Nat Immunol , vol.2 , Issue.11 , pp. 1032-1039
    • Derbinski, J.1    Schulte, A.2    Kyewski, B.3    Klein, L.4
  • 10
    • 0033984067 scopus 로고    scopus 로고
    • Shaping of the autoreactive T-cell repertoire by a splice variant of self protein expressed in thymic epithelial cells
    • Klein L., Klugmann M., Nave K.A., Tuohy V.K., and Kyewski B. Shaping of the autoreactive T-cell repertoire by a splice variant of self protein expressed in thymic epithelial cells. Nat Med 6 1 (2000) 56-61
    • (2000) Nat Med , vol.6 , Issue.1 , pp. 56-61
    • Klein, L.1    Klugmann, M.2    Nave, K.A.3    Tuohy, V.K.4    Kyewski, B.5
  • 11
    • 0023663430 scopus 로고
    • T cell tolerance by clonal elimination in the thymus
    • Kappler J.W., Roehm N., and Marrack P. T cell tolerance by clonal elimination in the thymus. Cell 49 2 (1987) 273-280
    • (1987) Cell , vol.49 , Issue.2 , pp. 273-280
    • Kappler, J.W.1    Roehm, N.2    Marrack, P.3
  • 13
    • 0035176638 scopus 로고    scopus 로고
    • Negative selection during the peripheral immune response to antigen
    • Anderton S.M., Radu C.G., Lowrey P.A., Ward E.S., and Wraith D.C. Negative selection during the peripheral immune response to antigen. J Exp Med 193 1 (2001) 1-11
    • (2001) J Exp Med , vol.193 , Issue.1 , pp. 1-11
    • Anderton, S.M.1    Radu, C.G.2    Lowrey, P.A.3    Ward, E.S.4    Wraith, D.C.5
  • 14
    • 0033103147 scopus 로고    scopus 로고
    • Biochemical identification of a mutated human melanoma antigen recognized by CD4(+) T cells
    • Pieper R., Christian R.E., Gonzales M.I., Nishimura M.I., Gupta G., Settlage R.E., et al. Biochemical identification of a mutated human melanoma antigen recognized by CD4(+) T cells. J Exp Med 189 5 (1999) 757-766
    • (1999) J Exp Med , vol.189 , Issue.5 , pp. 757-766
    • Pieper, R.1    Christian, R.E.2    Gonzales, M.I.3    Nishimura, M.I.4    Gupta, G.5    Settlage, R.E.6
  • 15
    • 26644447982 scopus 로고    scopus 로고
    • Unusual features of self-peptide/MHC binding by autoimmune T cell receptors
    • Nicholson M.J., Hahn M., and Wucherpfennig K.W. Unusual features of self-peptide/MHC binding by autoimmune T cell receptors. Immunity 23 4 (2005) 351-360
    • (2005) Immunity , vol.23 , Issue.4 , pp. 351-360
    • Nicholson, M.J.1    Hahn, M.2    Wucherpfennig, K.W.3
  • 16
    • 12444298109 scopus 로고    scopus 로고
    • Structure of an autoimmune T cell receptor complexed with class II peptide-MHC: insights into MHC bias and antigen specificity
    • Maynard J., Petersson K., Wilson D.H., Adams E.J., Blondelle S.E., Boulanger M.J., et al. Structure of an autoimmune T cell receptor complexed with class II peptide-MHC: insights into MHC bias and antigen specificity. Immunity 22 1 (2005) 81-92
    • (2005) Immunity , vol.22 , Issue.1 , pp. 81-92
    • Maynard, J.1    Petersson, K.2    Wilson, D.H.3    Adams, E.J.4    Blondelle, S.E.5    Boulanger, M.J.6
  • 17
    • 26644468528 scopus 로고    scopus 로고
    • Structure of a human autoimmune TCR bound to a myelin basic protein self-peptide and a multiple sclerosis-associated MHC class II molecule
    • Li Y., Huang Y., Lue J., Quandt J.A., Martin R., and Mariuzza R.A. Structure of a human autoimmune TCR bound to a myelin basic protein self-peptide and a multiple sclerosis-associated MHC class II molecule. EMBO J 24 17 (2005) 2968-2979
    • (2005) EMBO J , vol.24 , Issue.17 , pp. 2968-2979
    • Li, Y.1    Huang, Y.2    Lue, J.3    Quandt, J.A.4    Martin, R.5    Mariuzza, R.A.6
  • 18
    • 18244392426 scopus 로고    scopus 로고
    • Unconventional topology of self peptide-major histocompatibility complex binding by a human autoimmune T cell receptor
    • Hahn M., Nicholson M.J., Pyrdol J., and Wucherpfennig K.W. Unconventional topology of self peptide-major histocompatibility complex binding by a human autoimmune T cell receptor. Nat Immunol 6 5 (2005) 490-496
    • (2005) Nat Immunol , vol.6 , Issue.5 , pp. 490-496
    • Hahn, M.1    Nicholson, M.J.2    Pyrdol, J.3    Wucherpfennig, K.W.4
  • 19
    • 34248530182 scopus 로고    scopus 로고
    • Structural basis for the recognition of mutant self by a tumor-specific, MHC class II-restricted T cell receptor
    • Deng L., Langley R.J., Brown P.H., Xu G., Teng L., Wang Q., et al. Structural basis for the recognition of mutant self by a tumor-specific, MHC class II-restricted T cell receptor. Nat Immunol (2007)
    • (2007) Nat Immunol
    • Deng, L.1    Langley, R.J.2    Brown, P.H.3    Xu, G.4    Teng, L.5    Wang, Q.6
  • 21
    • 0034329441 scopus 로고    scopus 로고
    • Structure of a covalently stabilized complex of a human alphabeta T-cell receptor, influenza HA peptide and MHC class II molecule, HLA-DR1
    • Hennecke J., Carfi A., and Wiley D.C. Structure of a covalently stabilized complex of a human alphabeta T-cell receptor, influenza HA peptide and MHC class II molecule, HLA-DR1. EMBO J 19 21 (2000) 5611-5624
    • (2000) EMBO J , vol.19 , Issue.21 , pp. 5611-5624
    • Hennecke, J.1    Carfi, A.2    Wiley, D.C.3
  • 22
    • 0033520962 scopus 로고    scopus 로고
    • The crystal structure of a T cell receptor in complex with peptide and MHC class II
    • Reinherz E.L., Tan K., Tang L., Kern P., Liu J., Xiong Y., et al. The crystal structure of a T cell receptor in complex with peptide and MHC class II. Science 286 5446 (1999) 1913-1921
    • (1999) Science , vol.286 , Issue.5446 , pp. 1913-1921
    • Reinherz, E.L.1    Tan, K.2    Tang, L.3    Kern, P.4    Liu, J.5    Xiong, Y.6
  • 23
    • 0032961752 scopus 로고    scopus 로고
    • Structural features of autoreactive TCR that determine the degree of degeneracy in peptide recognition
    • Hausmann S., Martin M., Gauthier L., and Wucherpfennig K.W. Structural features of autoreactive TCR that determine the degree of degeneracy in peptide recognition. J Immunol 162 1 (1999) 338-344
    • (1999) J Immunol , vol.162 , Issue.1 , pp. 338-344
    • Hausmann, S.1    Martin, M.2    Gauthier, L.3    Wucherpfennig, K.W.4
  • 24
    • 0034650437 scopus 로고    scopus 로고
    • Contribution of individual amino acids within MHC molecule or antigenic peptide to TCR ligand potency
    • Hemmer B., Pinilla C., Gran B., Vergelli M., Ling N., Conlon P., et al. Contribution of individual amino acids within MHC molecule or antigenic peptide to TCR ligand potency. J Immunol 164 2 (2000) 861-871
    • (2000) J Immunol , vol.164 , Issue.2 , pp. 861-871
    • Hemmer, B.1    Pinilla, C.2    Gran, B.3    Vergelli, M.4    Ling, N.5    Conlon, P.6
  • 25
    • 0036337673 scopus 로고    scopus 로고
    • Structural snapshot of aberrant antigen presentation linked to autoimmunity: the immunodominant epitope of MBP complexed with I-Au
    • He X.L., Radu C., Sidney J., Sette A., Ward E.S., and Garcia K.C. Structural snapshot of aberrant antigen presentation linked to autoimmunity: the immunodominant epitope of MBP complexed with I-Au. Immunity 17 1 (2002) 83-94
    • (2002) Immunity , vol.17 , Issue.1 , pp. 83-94
    • He, X.L.1    Radu, C.2    Sidney, J.3    Sette, A.4    Ward, E.S.5    Garcia, K.C.6
  • 26
    • 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 21 (2003) 659-684
    • (2003) Annu Rev Immunol , vol.21 , pp. 659-684
    • van der Merwe, P.A.1    Davis, S.J.2
  • 27
    • 0037290768 scopus 로고    scopus 로고
    • Epitope dominance, competition and T cell affinity maturation
    • Kedl R.M., Kappler J.W., and Marrack P. Epitope dominance, competition and T cell affinity maturation. Curr Opin Immunol 15 1 (2003) 120-127
    • (2003) Curr Opin Immunol , vol.15 , Issue.1 , pp. 120-127
    • Kedl, R.M.1    Kappler, J.W.2    Marrack, P.3
  • 28
    • 20444485767 scopus 로고    scopus 로고
    • Cellular and genetic mechanisms of self tolerance and autoimmunity
    • Goodnow C.C., Sprent J., Fazekas de St Groth B., and Vinuesa C.G. Cellular and genetic mechanisms of self tolerance and autoimmunity. Nature 435 7042 (2005) 590-597
    • (2005) Nature , vol.435 , Issue.7042 , pp. 590-597
    • Goodnow, C.C.1    Sprent, J.2    Fazekas de St Groth, B.3    Vinuesa, C.G.4
  • 30
    • 33747092627 scopus 로고    scopus 로고
    • T cells with low avidity for a tissue-restricted antigen routinely evade central and peripheral tolerance and cause autoimmunity
    • Zehn D., and Bevan M.J. T cells with low avidity for a tissue-restricted antigen routinely evade central and peripheral tolerance and cause autoimmunity. Immunity 25 2 (2006) 261-270
    • (2006) Immunity , vol.25 , Issue.2 , pp. 261-270
    • Zehn, D.1    Bevan, M.J.2
  • 31
  • 32
    • 0036467503 scopus 로고    scopus 로고
    • So many ways of getting in the way: diversity in the molecular architecture of superantigen-dependent T-cell signaling complexes
    • Sundberg E.J., Li Y., and Mariuzza R.A. So many ways of getting in the way: diversity in the molecular architecture of superantigen-dependent T-cell signaling complexes. Curr Opin Immunol 14 1 (2002) 36-44
    • (2002) Curr Opin Immunol , vol.14 , Issue.1 , pp. 36-44
    • Sundberg, E.J.1    Li, Y.2    Mariuzza, R.A.3
  • 33
    • 0041358919 scopus 로고    scopus 로고
    • Bacterial superantigens
    • Proft T., and Fraser J.D. Bacterial superantigens. Clin Exp Immunol 133 3 (2003) 299-306
    • (2003) Clin Exp Immunol , vol.133 , Issue.3 , pp. 299-306
    • Proft, T.1    Fraser, J.D.2
  • 34
    • 33847723413 scopus 로고    scopus 로고
    • Crystal structure of the streptococcal superantigen SpeI and functional role of a novel loop domain in T cell activation by Group V superantigens
    • Brouillard J.N., Gunther S., Varma A.K., Gryski I., Herfst C.A., Rahman A.K., et al. Crystal structure of the streptococcal superantigen SpeI and functional role of a novel loop domain in T cell activation by Group V superantigens. J Mol Biol 367 (2007) 925-934
    • (2007) J Mol Biol , vol.367 , pp. 925-934
    • Brouillard, J.N.1    Gunther, S.2    Varma, A.K.3    Gryski, I.4    Herfst, C.A.5    Rahman, A.K.6
  • 35
    • 0028559548 scopus 로고
    • Toxic shock syndrome toxin-1 complexed with a class II major histocompatibility molecule HLA-DR1
    • Kim J., Urban R.G., Strominger J.L., and Wiley D.C. Toxic shock syndrome toxin-1 complexed with a class II major histocompatibility molecule HLA-DR1. Science 266 5192 (1994) 1870-1874
    • (1994) Science , vol.266 , Issue.5192 , pp. 1870-1874
    • Kim, J.1    Urban, R.G.2    Strominger, J.L.3    Wiley, D.C.4
  • 36
    • 0029963332 scopus 로고    scopus 로고
    • Major histocompatibility complex class II-associated peptides control the presentation of bacterial superantigens to T cells
    • Wen R., Cole G.A., Surman S., Blackman M.A., and Woodland D.L. Major histocompatibility complex class II-associated peptides control the presentation of bacterial superantigens to T cells. J Exp Med 183 3 (1996) 1083-1092
    • (1996) J Exp Med , vol.183 , Issue.3 , pp. 1083-1092
    • Wen, R.1    Cole, G.A.2    Surman, S.3    Blackman, M.A.4    Woodland, D.L.5
  • 37
    • 33847209552 scopus 로고    scopus 로고
    • Structural basis of T cell receptor specificity and activation by the bacterial superantigen TSST-1
    • Moza B., Varma A.K., Zhu P., Buonpane R.A., Herfst C.A., Nicholson M.J., et al. Structural basis of T cell receptor specificity and activation by the bacterial superantigen TSST-1. EMBO J 26 4 (2007) 1187-1197
    • (2007) EMBO J , vol.26 , Issue.4 , pp. 1187-1197
    • Moza, B.1    Varma, A.K.2    Zhu, P.3    Buonpane, R.A.4    Herfst, C.A.5    Nicholson, M.J.6
  • 39
    • 23444454615 scopus 로고
    • Three-dimensional structure of a human class II histocompatibility molecule complexed with superantigen
    • Jardetzky T.S., Brown J.H., Gorga J.C., Stern L.J., Urban R.G., Chi Y.I., et al. Three-dimensional structure of a human class II histocompatibility molecule complexed with superantigen. Nature 368 6473 (1994) 711-718
    • (1994) Nature , vol.368 , Issue.6473 , pp. 711-718
    • Jardetzky, T.S.1    Brown, J.H.2    Gorga, J.C.3    Stern, L.J.4    Urban, R.G.5    Chi, Y.I.6
  • 40
    • 0029985104 scopus 로고    scopus 로고
    • Crystal structure of a T-cell receptor beta-chain complexed with a superantigen
    • Fields B.A., Malchiodi E.L., Li H., Ysern X., Stauffacher C.V., Schlievert P.M., et al. Crystal structure of a T-cell receptor beta-chain complexed with a superantigen. Nature 384 6605 (1996) 188-192
    • (1996) Nature , vol.384 , Issue.6605 , pp. 188-192
    • Fields, B.A.1    Malchiodi, E.L.2    Li, H.3    Ysern, X.4    Stauffacher, C.V.5    Schlievert, P.M.6
  • 41
    • 0032412391 scopus 로고    scopus 로고
    • Three-dimensional structure of the complex between a T cell receptor beta chain and the superantigen staphylococcal enterotoxin B
    • Li H., Llera A., Tsuchiya D., Leder L., Ysern X., Schlievert P.M., et al. Three-dimensional structure of the complex between a T cell receptor beta chain and the superantigen staphylococcal enterotoxin B. Immunity 9 6 (1998) 807-816
    • (1998) Immunity , vol.9 , Issue.6 , pp. 807-816
    • Li, H.1    Llera, A.2    Tsuchiya, D.3    Leder, L.4    Ysern, X.5    Schlievert, P.M.6
  • 42
    • 0036091233 scopus 로고    scopus 로고
    • Structures of two streptococcal superantigens bound to TCR beta chains reveal diversity in the architecture of T cell signaling complexes
    • Sundberg E.J., Li H., Llera A.S., McCormick J.K., Tormo J., Schlievert P.M., et al. Structures of two streptococcal superantigens bound to TCR beta chains reveal diversity in the architecture of T cell signaling complexes. Structure 10 5 (2002) 687-699
    • (2002) Structure , vol.10 , Issue.5 , pp. 687-699
    • Sundberg, E.J.1    Li, H.2    Llera, A.S.3    McCormick, J.K.4    Tormo, J.5    Schlievert, P.M.6
  • 43
    • 0029062894 scopus 로고
    • Characterization of two distinct MHC class II binding sites in the superantigen staphylococcal enterotoxin A
    • Abrahmsen L., Dohlsten M., Segren S., Bjork P., Jonsson E., and Kalland T. Characterization of two distinct MHC class II binding sites in the superantigen staphylococcal enterotoxin A. EMBO J 14 13 (1995) 2978-2986
    • (1995) EMBO J , vol.14 , Issue.13 , pp. 2978-2986
    • Abrahmsen, L.1    Dohlsten, M.2    Segren, S.3    Bjork, P.4    Jonsson, E.5    Kalland, T.6
  • 44
    • 0029147099 scopus 로고
    • Staphylococcal enterotoxin A has two cooperative binding sites on major histocompatibility complex class II
    • Hudson K.R., Tiedemann R.E., Urban R.G., Lowe S.C., Strominger J.L., and Fraser J.D. Staphylococcal enterotoxin A has two cooperative binding sites on major histocompatibility complex class II. J Exp Med 182 3 (1995) 711-720
    • (1995) J Exp Med , vol.182 , Issue.3 , pp. 711-720
    • Hudson, K.R.1    Tiedemann, R.E.2    Urban, R.G.3    Lowe, S.C.4    Strominger, J.L.5    Fraser, J.D.6
  • 45
    • 0036901549 scopus 로고    scopus 로고
    • Crystal structure of a SEA variant in complex with MHC class II reveals the ability of SEA to crosslink MHC molecules
    • Petersson K., Thunnissen M., Forsberg G., and Walse B. Crystal structure of a SEA variant in complex with MHC class II reveals the ability of SEA to crosslink MHC molecules. Structure 10 12 (2002) 1619-1626
    • (2002) Structure , vol.10 , Issue.12 , pp. 1619-1626
    • Petersson, K.1    Thunnissen, M.2    Forsberg, G.3    Walse, B.4
  • 46
    • 0035796399 scopus 로고    scopus 로고
    • Crystal structure of a superantigen bound to MHC class II displays zinc and peptide dependence
    • Petersson K., Hakansson M., Nilsson H., Forsberg G., Svensson L.A., Liljas A., et al. Crystal structure of a superantigen bound to MHC class II displays zinc and peptide dependence. EMBO J 20 13 (2001) 3306-3312
    • (2001) EMBO J , vol.20 , Issue.13 , pp. 3306-3312
    • Petersson, K.1    Hakansson, M.2    Nilsson, H.3    Forsberg, G.4    Svensson, L.A.5    Liljas, A.6
  • 47
    • 0035129453 scopus 로고    scopus 로고
    • Crystal structure of a superantigen bound to the high-affinity, zinc-dependent site on MHC class II
    • Li Y., Li H., Dimasi N., McCormick J.K., Martin R., Schuck P., et al. Crystal structure of a superantigen bound to the high-affinity, zinc-dependent site on MHC class II. Immunity 14 1 (2001) 93-104
    • (2001) Immunity , vol.14 , Issue.1 , pp. 93-104
    • Li, Y.1    Li, H.2    Dimasi, N.3    McCormick, J.K.4    Martin, R.5    Schuck, P.6
  • 48
    • 0036091233 scopus 로고    scopus 로고
    • Structures of two streptococcal superantigens bound to TCR beta chains reveal diversity in the architecture of T cell signaling complexes
    • Sundberg E.J., Li H., Llera A.S., McCormick J.K., Tormo J., Schlievert P.M., et al. Structures of two streptococcal superantigens bound to TCR beta chains reveal diversity in the architecture of T cell signaling complexes. Structure (Camb) 10 5 (2002) 687-699
    • (2002) Structure (Camb) , vol.10 , Issue.5 , pp. 687-699
    • Sundberg, E.J.1    Li, H.2    Llera, A.S.3    McCormick, J.K.4    Tormo, J.5    Schlievert, P.M.6
  • 49
    • 33845454185 scopus 로고    scopus 로고
    • Molecular basis of TCR selectivity, cross-reactivity, and allelic discrimination by a bacterial superantigen: integrative functional and energetic mapping of the SpeC-Vbeta2.1 molecular interface
    • Rahman A.K., Herfst C.A., Moza B., Shames S.R., Chau L.A., Bueno C., et al. Molecular basis of TCR selectivity, cross-reactivity, and allelic discrimination by a bacterial superantigen: integrative functional and energetic mapping of the SpeC-Vbeta2.1 molecular interface. J Immunol 177 12 (2006) 8595-8603
    • (2006) J Immunol , vol.177 , Issue.12 , pp. 8595-8603
    • Rahman, A.K.1    Herfst, C.A.2    Moza, B.3    Shames, S.R.4    Chau, L.A.5    Bueno, C.6
  • 50
    • 33748749713 scopus 로고    scopus 로고
    • Crystal structure of staphylococcal enterotoxin I (SEI) in complex with a human major histocompatibility complex class II molecule
    • Fernandez M.M., Guan R., Swaminathan C.P., Malchiodi E.L., and Mariuzza R.A. Crystal structure of staphylococcal enterotoxin I (SEI) in complex with a human major histocompatibility complex class II molecule. J Biol Chem 281 35 (2006) 25356-25364
    • (2006) J Biol Chem , vol.281 , Issue.35 , pp. 25356-25364
    • Fernandez, M.M.1    Guan, R.2    Swaminathan, C.P.3    Malchiodi, E.L.4    Mariuzza, R.A.5
  • 51
    • 34447099075 scopus 로고    scopus 로고
    • A novel loop domain in superantigens extends their T cell receptor recognition site
    • Gunther S., Varma A.K., Moza B., Kasper K.J., Wyatt A.W., Zhu P., et al. A novel loop domain in superantigens extends their T cell receptor recognition site. J Mol Biol 371 1 (2007) 210-221
    • (2007) J Mol Biol , vol.371 , Issue.1 , pp. 210-221
    • Gunther, S.1    Varma, A.K.2    Moza, B.3    Kasper, K.J.4    Wyatt, A.W.5    Zhu, P.6
  • 52
    • 0037446529 scopus 로고    scopus 로고
    • Staphylococcal enterotoxin H induces V alpha-specific expansion of T cells
    • Petersson K., Pettersson H., Skartved N.J., Walse B., and Forsberg G. Staphylococcal enterotoxin H induces V alpha-specific expansion of T cells. J Immunol 170 8 (2003) 4148-4154
    • (2003) J Immunol , vol.170 , Issue.8 , pp. 4148-4154
    • Petersson, K.1    Pettersson, H.2    Skartved, N.J.3    Walse, B.4    Forsberg, G.5
  • 53
    • 33846977011 scopus 로고    scopus 로고
    • Crystal structure of a complete ternary complex of TCR, superantigen and peptide-MHC
    • Wang L., Zhao Y., Li Z., Guo Y., Jones L.L., Kranz D.M., et al. Crystal structure of a complete ternary complex of TCR, superantigen and peptide-MHC. Nat Struct Mol Biol (2007)
    • (2007) Nat Struct Mol Biol
    • Wang, L.1    Zhao, Y.2    Li, Z.3    Guo, Y.4    Jones, L.L.5    Kranz, D.M.6
  • 54
    • 25144479800 scopus 로고    scopus 로고
    • Characterization of T cell receptors engineered for high affinity against toxic shock syndrome toxin-1
    • Buonpane R.A., Moza B., Sundberg E.J., and Kranz D.M. Characterization of T cell receptors engineered for high affinity against toxic shock syndrome toxin-1. J Mol Biol 353 2 (2005) 308-321
    • (2005) J Mol Biol , vol.353 , Issue.2 , pp. 308-321
    • Buonpane, R.A.1    Moza, B.2    Sundberg, E.J.3    Kranz, D.M.4
  • 55
    • 0033119268 scopus 로고    scopus 로고
    • Role of the T cell receptor alpha chain in stabilizing TCR-superantigen-MHC class II complexes
    • Andersen P.S., Lavoie P.M., Sekaly R.P., Churchill H., Kranz D.M., Schlievert P.M., et al. Role of the T cell receptor alpha chain in stabilizing TCR-superantigen-MHC class II complexes. Immunity 10 4 (1999) 473-483
    • (1999) Immunity , vol.10 , Issue.4 , pp. 473-483
    • Andersen, P.S.1    Lavoie, P.M.2    Sekaly, R.P.3    Churchill, H.4    Kranz, D.M.5    Schlievert, P.M.6
  • 59
    • 33845454185 scopus 로고    scopus 로고
    • Molecular basis of T cell receptor selectivity, cross-reactivity and allelic discrimination by a bacterial superantigen: integrative functional and energetic mapping of the SpeC-Vb2.1 molecular interface
    • Rahman A.K.M.N., Herfst C.A., Moza B., Chau L.A., Bueno C., Madrenas J., et al. Molecular basis of T cell receptor selectivity, cross-reactivity and allelic discrimination by a bacterial superantigen: integrative functional and energetic mapping of the SpeC-Vb2.1 molecular interface. J Immunol 17 12 (2006)
    • (2006) J Immunol , vol.17 , Issue.12
    • Rahman, A.K.M.N.1    Herfst, C.A.2    Moza, B.3    Chau, L.A.4    Bueno, C.5    Madrenas, J.6
  • 60
    • 0032924155 scopus 로고    scopus 로고
    • Intravenous immunoglobulin therapy for streptococcal toxic shock syndrome-a comparative observational study
    • The Canadian Streptococcal Study Group
    • Kaul R., McGeer A., Norrby-Teglund A., Kotb M., Schwartz B., O'Rourke K., et al., The Canadian Streptococcal Study Group. Intravenous immunoglobulin therapy for streptococcal toxic shock syndrome-a comparative observational study. Clin Infect Dis 28 4 (1999) 800-807
    • (1999) Clin Infect Dis , vol.28 , Issue.4 , pp. 800-807
    • Kaul, R.1    McGeer, A.2    Norrby-Teglund, A.3    Kotb, M.4    Schwartz, B.5    O'Rourke, K.6
  • 61
    • 0035139557 scopus 로고    scopus 로고
    • Human antibodies to bacterial superantigens and their ability to inhibit T-cell activation and lethality
    • LeClaire R.D., and Bavari S. Human antibodies to bacterial superantigens and their ability to inhibit T-cell activation and lethality. Antimicrob Agents Chemother 45 2 (2001) 460-463
    • (2001) Antimicrob Agents Chemother , vol.45 , Issue.2 , pp. 460-463
    • LeClaire, R.D.1    Bavari, S.2
  • 62
    • 0028332839 scopus 로고
    • Monoclonal antibodies defining functional sites on the toxin superantigen staphylococcal enterotoxin B
    • Hamad A.R., Herman A., Marrack P., and Kappler J.W. Monoclonal antibodies defining functional sites on the toxin superantigen staphylococcal enterotoxin B. J Exp Med 180 2 (1994) 615-621
    • (1994) J Exp Med , vol.180 , Issue.2 , pp. 615-621
    • Hamad, A.R.1    Herman, A.2    Marrack, P.3    Kappler, J.W.4
  • 63
    • 0034034354 scopus 로고    scopus 로고
    • Inhibition of staphylococcal enterotoxin B-induced lymphocyte proliferation and tumor necrosis factor alpha secretion by MAb5, an anti-toxic shock syndrome toxin 1 monoclonal antibody
    • Pang L.T., Kum W.W., and Chow A.W. Inhibition of staphylococcal enterotoxin B-induced lymphocyte proliferation and tumor necrosis factor alpha secretion by MAb5, an anti-toxic shock syndrome toxin 1 monoclonal antibody. Infect Immun 68 6 (2000) 3261-3268
    • (2000) Infect Immun , vol.68 , Issue.6 , pp. 3261-3268
    • Pang, L.T.1    Kum, W.W.2    Chow, A.W.3
  • 64
    • 23844524089 scopus 로고    scopus 로고
    • Intracellular protein therapy with SOCS3 inhibits inflammation and apoptosis
    • Jo D., Liu D., Yao S., Collins R.D., and Hawiger J. Intracellular protein therapy with SOCS3 inhibits inflammation and apoptosis. Nat Med 11 8 (2005) 892-898
    • (2005) Nat Med , vol.11 , Issue.8 , pp. 892-898
    • Jo, D.1    Liu, D.2    Yao, S.3    Collins, R.D.4    Hawiger, J.5
  • 65
  • 66
    • 0035853281 scopus 로고    scopus 로고
    • High affinity T cell receptors from yeast display libraries block T cell activation by superantigens
    • Kieke M.C., Sundberg E., Shusta E.V., Mariuzza R.A., Wittrup K.D., and Kranz D.M. High affinity T cell receptors from yeast display libraries block T cell activation by superantigens. J Mol Biol 307 5 (2001) 1305-1315
    • (2001) J Mol Biol , vol.307 , Issue.5 , pp. 1305-1315
    • Kieke, M.C.1    Sundberg, E.2    Shusta, E.V.3    Mariuzza, R.A.4    Wittrup, K.D.5    Kranz, D.M.6
  • 67
    • 0034093737 scopus 로고    scopus 로고
    • Signal transduction by the TCR for antigen
    • Kane L.P., Lin J., and Weiss A. Signal transduction by the TCR for antigen. Curr Opin Immunol 12 3 (2000) 242-249
    • (2000) Curr Opin Immunol , vol.12 , Issue.3 , pp. 242-249
    • Kane, L.P.1    Lin, J.2    Weiss, A.3
  • 68
    • 33746025600 scopus 로고    scopus 로고
    • Bacterial superantigens bypass Lck-dependent T cell receptor signaling by activating a Galpha11-dependent, PLC-beta-mediated pathway
    • Bueno C., Lemke C.D., Criado G., Baroja M.L., Ferguson S.S., Rahman A.K., et al. Bacterial superantigens bypass Lck-dependent T cell receptor signaling by activating a Galpha11-dependent, PLC-beta-mediated pathway. Immunity 25 1 (2006) 67-78
    • (2006) Immunity , vol.25 , Issue.1 , pp. 67-78
    • Bueno, C.1    Lemke, C.D.2    Criado, G.3    Baroja, M.L.4    Ferguson, S.S.5    Rahman, A.K.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.