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Volumn 250, Issue 1, 2012, Pages 49-60

T cells and their eons-old obsession with MHC

Author keywords

Comparative immunology; T cells; T cell receptors; Thymus

Indexed keywords

AMINO ACID; CD4 ANTIGEN; CD8 ANTIGEN; MAJOR HISTOCOMPATIBILITY ANTIGEN; T LYMPHOCYTE RECEPTOR;

EID: 84867406318     PISSN: 01052896     EISSN: 1600065X     Source Type: Journal    
DOI: 10.1111/imr.12004     Document Type: Article
Times cited : (58)

References (109)
  • 1
    • 0026505203 scopus 로고
    • The Nobel Prize for Physiology or Medicine, 1980 awarded to Baruj Benacerraf, Jean Daussett & George D. Snell
    • The Nobel Lectures in Immunology.
    • The Nobel Lectures in Immunology. The Nobel Prize for Physiology or Medicine, 1980 awarded to Baruj Benacerraf, Jean Daussett & George D. Snell. Scand J Immunol 1992;35:373-398.
    • (1992) Scand J Immunol , vol.35 , pp. 373-398
  • 2
    • 0004555768 scopus 로고
    • The antigenic structure of tumors
    • Gorer P. The antigenic structure of tumors. Adv Immunol 1961;1:345.
    • (1961) Adv Immunol , vol.1 , pp. 345
    • Gorer, P.1
  • 3
    • 0021968677 scopus 로고
    • Binding of immunogenic peptides to Ia histocompatibility molecules
    • Babbitt BP, Allen PM, Matsueda G, Haber E, Unanue ER. Binding of immunogenic peptides to Ia histocompatibility molecules. Nature 1985;317:359-361.
    • (1985) Nature , vol.317 , pp. 359-361
    • Babbitt, B.P.1    Allen, P.M.2    Matsueda, G.3    Haber, E.4    Unanue, E.R.5
  • 4
    • 0015518021 scopus 로고
    • Histocompatibility-linked immune response genes
    • Benacerraf B, McDevitt HO. Histocompatibility-linked immune response genes. Science 1972;175:273-279.
    • (1972) Science , vol.175 , pp. 273-279
    • Benacerraf, B.1    McDevitt, H.O.2
  • 5
    • 0016821685 scopus 로고
    • Interaction antigens detected by cytotoxic T cells with the major histocompatibility complex as modifier
    • Bevan MJ. Interaction antigens detected by cytotoxic T cells with the major histocompatibility complex as modifier. Nature 1975;256:419-421.
    • (1975) Nature , vol.256 , pp. 419-421
    • Bevan, M.J.1
  • 6
    • 0017080570 scopus 로고
    • Helper T cells recognise antigen and macrophage surface components simultaneously
    • Kappler JW, Marrack PC. Helper T cells recognise antigen and macrophage surface components simultaneously. Nature 1976;262:797-799.
    • (1976) Nature , vol.262 , pp. 797-799
    • Kappler, J.W.1    Marrack, P.C.2
  • 7
    • 0019458092 scopus 로고
    • Antigen-inducible, H-2-restricted, interleukin-2-producing T cell hybridomas. Lack of independent antigen and H-2 recognition
    • Kappler JW, Skidmore B, White J, Marrack P. Antigen-inducible, H-2-restricted, interleukin-2-producing T cell hybridomas. Lack of independent antigen and H-2 recognition. J Exp Med 1981;153:1198-1214.
    • (1981) J Exp Med , vol.153 , pp. 1198-1214
    • Kappler, J.W.1    Skidmore, B.2    White, J.3    Marrack, P.4
  • 8
    • 0015978555 scopus 로고
    • Cell interactions between histoincompatible T and B lymphocytes. V. Failure of histoincompatible T cells to interfere with physiologic cooperation between syngeneic T and B lymphocytes
    • Katz DH, Hamaoka T, Dorf ME, Benacerraf B. Cell interactions between histoincompatible T and B lymphocytes. V. Failure of histoincompatible T cells to interfere with physiologic cooperation between syngeneic T and B lymphocytes. J Immunol 1974;112:855-857.
    • (1974) J Immunol , vol.112 , pp. 855-857
    • Katz, D.H.1    Hamaoka, T.2    Dorf, M.E.3    Benacerraf, B.4
  • 9
    • 0017904954 scopus 로고
    • Interaction between antigen-presenting cells and primed T lymphocytes: an assessment of Ir gene expression in the antigen-presenting cell
    • Schwartz RH, Yano A, Paul WE. Interaction between antigen-presenting cells and primed T lymphocytes: an assessment of Ir gene expression in the antigen-presenting cell. Immunol Rev 1978;40:153-180.
    • (1978) Immunol Rev , vol.40 , pp. 153-180
    • Schwartz, R.H.1    Yano, A.2    Paul, W.E.3
  • 10
    • 0016664131 scopus 로고
    • Mixed lymphocyte reactivity and cell-mediated lympholysis to trinitrophenyl-modified autologous lymphocytes in C57BL/10 congenic and B10-A recombinant mouse strains
    • Shearer GM, Lozner EC, Rehn TG, Schmitt-Verhulst AM. Mixed lymphocyte reactivity and cell-mediated lympholysis to trinitrophenyl-modified autologous lymphocytes in C57BL/10 congenic and B10-A recombinant mouse strains. J Exp Med 1975;141:930-934.
    • (1975) J Exp Med , vol.141 , pp. 930-934
    • Shearer, G.M.1    Lozner, E.C.2    Rehn, T.G.3    Schmitt-Verhulst, A.M.4
  • 11
    • 0015988964 scopus 로고
    • Alloantiserum-induced inhibition of immune response gene product function. II. Genetic analysis of target antigens
    • Shevach EM, Green I, Paul WE. Alloantiserum-induced inhibition of immune response gene product function. II. Genetic analysis of target antigens. J Exp Med 1974;139:679-695.
    • (1974) J Exp Med , vol.139 , pp. 679-695
    • Shevach, E.M.1    Green, I.2    Paul, W.E.3
  • 12
    • 0020601431 scopus 로고
    • Antigen recognition by H-2-restricted T cells. I. Cell-free antigen processing
    • Shimonkevitz R, Kappler J, Marrack P, Grey H. Antigen recognition by H-2-restricted T cells. I. Cell-free antigen processing. J Exp Med 1983;158:303-316.
    • (1983) J Exp Med , vol.158 , pp. 303-316
    • Shimonkevitz, R.1    Kappler, J.2    Marrack, P.3    Grey, H.4
  • 13
    • 0016318314 scopus 로고
    • Immunological surveillance against altered self components by sensitised T lymphocytes in lymphocytic choriomeningitis
    • Zinkernagel RM, Doherty PC. Immunological surveillance against altered self components by sensitised T lymphocytes in lymphocytic choriomeningitis. Nature 1974;251:547-548.
    • (1974) Nature , vol.251 , pp. 547-548
    • Zinkernagel, R.M.1    Doherty, P.C.2
  • 14
    • 0023187442 scopus 로고
    • The foreign antigen binding site and T cell recognition regions of class I histocompatibility antigens
    • Bjorkman PJ, Saper MA, Samraoui B, Bennett WS, Strominger JL, Wiley DC. The foreign antigen binding site and T cell recognition regions of class I histocompatibility antigens. Nature 1987;329:512-518.
    • (1987) Nature , vol.329 , pp. 512-518
    • Bjorkman, P.J.1    Saper, M.A.2    Samraoui, B.3    Bennett, W.S.4    Strominger, J.L.5    Wiley, D.C.6
  • 15
    • 0022409751 scopus 로고
    • Crystallization and X-ray diffraction studies on the histocompatibility antigens HLA-A2 and HLA-A28 from human cell membranes
    • Bjorkman PJ, Strominger JL, Wiley DC. Crystallization and X-ray diffraction studies on the histocompatibility antigens HLA-A2 and HLA-A28 from human cell membranes. J Mol Biol 1985;186:205-210.
    • (1985) J Mol Biol , vol.186 , pp. 205-210
    • Bjorkman, P.J.1    Strominger, J.L.2    Wiley, D.C.3
  • 16
    • 0019915995 scopus 로고
    • Tumor-specific antigen of murine T-lymphoma defined with monoclonal antibody
    • Allison JP, McIntyre BW, Bloch D. Tumor-specific antigen of murine T-lymphoma defined with monoclonal antibody. J Immunol 1982;129:2293-2300.
    • (1982) J Immunol , vol.129 , pp. 2293-2300
    • Allison, J.P.1    McIntyre, B.W.2    Bloch, D.3
  • 18
    • 0020623652 scopus 로고
    • The major histocompatibility complex-restricted antigen receptor on T cells. I. Isolation with a monoclonal antibody
    • Haskins K, Kubo R, White J, Pigeon M, Kappler J, Marrack P. The major histocompatibility complex-restricted antigen receptor on T cells. I. Isolation with a monoclonal antibody. J Exp Med 1983;157:1149-1169.
    • (1983) J Exp Med , vol.157 , pp. 1149-1169
    • Haskins, K.1    Kubo, R.2    White, J.3    Pigeon, M.4    Kappler, J.5    Marrack, P.6
  • 19
    • 0021215865 scopus 로고
    • Isolation of cDNA clones encoding T cell-specific membrane-associated proteins
    • Hedrick SM, Cohen DI, Nielsen EA, Davis MM. Isolation of cDNA clones encoding T cell-specific membrane-associated proteins. Nature 1984;308:149-153.
    • (1984) Nature , vol.308 , pp. 149-153
    • Hedrick, S.M.1    Cohen, D.I.2    Nielsen, E.A.3    Davis, M.M.4
  • 20
    • 0020695943 scopus 로고
    • Clonotypic structures involved in antigen-specific human T cell function. Relationship to the T3 molecular complex
    • Meuer SC, Fitzgerald KA, Hussey RE, Hodgdon JC, Schlossman SF, Reinherz EL. Clonotypic structures involved in antigen-specific human T cell function. Relationship to the T3 molecular complex. J Exp Med 1983;157:705-719.
    • (1983) J Exp Med , vol.157 , pp. 705-719
    • Meuer, S.C.1    Fitzgerald, K.A.2    Hussey, R.E.3    Hodgdon, J.C.4    Schlossman, S.F.5    Reinherz, E.L.6
  • 21
    • 0021196170 scopus 로고
    • A human T cell-specific cDNA clone encodes a protein having extensive homology to immunoglobulin chains
    • Yanagi Y, Yoshikai Y, Leggett K, Clark SP, Aleksander I, Mak TW. A human T cell-specific cDNA clone encodes a protein having extensive homology to immunoglobulin chains. Nature 1984;308:145-149.
    • (1984) Nature , vol.308 , pp. 145-149
    • Yanagi, Y.1    Yoshikai, Y.2    Leggett, K.3    Clark, S.P.4    Aleksander, I.5    Mak, T.W.6
  • 22
  • 23
  • 24
    • 0022967332 scopus 로고
    • Human T-cell receptor genes: organization, diversity, and polymorphism
    • Concannon P, et al. Human T-cell receptor genes: organization, diversity, and polymorphism. Cold Spring Harb Symp Quant Biol 1986;51:785-789.
    • (1986) Cold Spring Harb Symp Quant Biol , vol.51 , pp. 785-789
    • Concannon, P.1
  • 25
    • 0034807024 scopus 로고    scopus 로고
    • Comparative genomics of the human and mouse T cell receptor loci
    • Glusman G, et al. Comparative genomics of the human and mouse T cell receptor loci. Immunity 2001;15:337-349.
    • (2001) Immunity , vol.15 , pp. 337-349
    • Glusman, G.1
  • 26
    • 0021790235 scopus 로고
    • Unusual organization and diversity of T-cell receptor alpha-chain genes
    • Hayday AC, et al. Unusual organization and diversity of T-cell receptor alpha-chain genes. Nature 1985;316:828-832.
    • (1985) Nature , vol.316 , pp. 828-832
    • Hayday, A.C.1
  • 27
    • 0022652647 scopus 로고
    • Non-germ-line elements (NGE) are present in the T cell receptor beta-chain genes isolated from the mutant mouse, motheaten (me/me)
    • Hagiya M, Davis DD, Shultz LD, Sakano H. Non-germ-line elements (NGE) are present in the T cell receptor beta-chain genes isolated from the mutant mouse, motheaten (me/me). J Immunol 1986;136:2697-2700.
    • (1986) J Immunol , vol.136 , pp. 2697-2700
    • Hagiya, M.1    Davis, D.D.2    Shultz, L.D.3    Sakano, H.4
  • 28
    • 0022528948 scopus 로고
    • Generation of diversity of the beta chain of the human T-lymphocyte receptor for antigen
    • Leiden JM, Strominger JL. Generation of diversity of the beta chain of the human T-lymphocyte receptor for antigen. Proc Natl Acad Sci USA 1986;83:4456-4460.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 4456-4460
    • Leiden, J.M.1    Strominger, J.L.2
  • 29
    • 0027499480 scopus 로고
    • Topology and affinity of T-cell receptor mediated recognition of peptide-MHC complexes
    • Davis MM, Chien Y. Topology and affinity of T-cell receptor mediated recognition of peptide-MHC complexes. Curr Opin Immunol 1993;5:45-49.
    • (1993) Curr Opin Immunol , vol.5 , pp. 45-49
    • Davis, M.M.1    Chien, Y.2
  • 30
    • 0029932899 scopus 로고    scopus 로고
    • The specificity and orientation of a TCR to its peptide-MHC class II ligands
    • Sant'Angelo DB, et al. The specificity and orientation of a TCR to its peptide-MHC class II ligands. Immunity 1996;4:367-376.
    • (1996) Immunity , vol.4 , pp. 367-376
    • Sant'Angelo, D.B.1
  • 31
    • 0032549142 scopus 로고    scopus 로고
    • Structural basis of plasticity in T cell receptor recognition of a self peptide-MHC antigen
    • Garcia KC, et al. Structural basis of plasticity in T cell receptor recognition of a self peptide-MHC antigen. Science 1998;279:1166-1172.
    • (1998) Science , vol.279 , pp. 1166-1172
    • Garcia, K.C.1
  • 32
    • 33947726614 scopus 로고    scopus 로고
    • How a single T cell receptor recognizes both self and foreign MHC
    • Colf LA, et al. How a single T cell receptor recognizes both self and foreign MHC. Cell 2007;129:135-146.
    • (2007) Cell , vol.129 , pp. 135-146
    • Colf, L.A.1
  • 33
    • 40249118205 scopus 로고    scopus 로고
    • Crossreactive T Cells spotlight the germline rules for alphabeta T cell-receptor interactions with MHC molecules
    • Dai S, et al. Crossreactive T Cells spotlight the germline rules for alphabeta T cell-receptor interactions with MHC molecules. Immunity 2008;28:324-334.
    • (2008) Immunity , vol.28 , pp. 324-334
    • Dai, S.1
  • 34
    • 0029855347 scopus 로고    scopus 로고
    • Structure of the complex between human T-cell receptor, viral peptide and HLA-A2
    • Garboczi DN, Ghosh P, Utz U, Fan QR, Biddison WE, Wiley DC. Structure of the complex between human T-cell receptor, viral peptide and HLA-A2. Nature 1996;384:134-141.
    • (1996) Nature , vol.384 , pp. 134-141
    • Garboczi, D.N.1    Ghosh, P.2    Utz, U.3    Fan, Q.R.4    Biddison, W.E.5    Wiley, D.C.6
  • 35
    • 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, et al. Structure of an autoimmune T cell receptor complexed with class II peptide-MHC: insights into MHC bias and antigen specificity. Immunity 2005;22:81-92.
    • (2005) Immunity , vol.22 , pp. 81-92
    • Maynard, J.1
  • 36
    • 37549038674 scopus 로고    scopus 로고
    • A new twist in TCR diversity revealed by a forbidden alphabeta TCR
    • McBeth C, et al. A new twist in TCR diversity revealed by a forbidden alphabeta TCR. J Mol Biol 2008;375:1306-1319.
    • (2008) J Mol Biol , vol.375 , pp. 1306-1319
    • McBeth, C.1
  • 37
    • 0033520962 scopus 로고    scopus 로고
    • The crystal structure of a T cell receptor in complex with peptide and MHC class II
    • Reinherz EL, et al. The crystal structure of a T cell receptor in complex with peptide and MHC class II. Science 1999;286:1913-1921.
    • (1999) Science , vol.286 , pp. 1913-1921
    • Reinherz, E.L.1
  • 38
    • 5944249467 scopus 로고    scopus 로고
    • Crystal structure of a T cell receptor bound to an allogeneic MHC molecule
    • Reiser JB, et al. Crystal structure of a T cell receptor bound to an allogeneic MHC molecule. Nat Immunol 2000;1:291-297.
    • (2000) Nat Immunol , vol.1 , pp. 291-297
    • Reiser, J.B.1
  • 39
    • 18344394144 scopus 로고    scopus 로고
    • A T cell receptor CDR3beta loop undergoes conformational changes of unprecedented magnitude upon binding to a peptide/MHC class I complex
    • Reiser JB, et al. A T cell receptor CDR3beta loop undergoes conformational changes of unprecedented magnitude upon binding to a peptide/MHC class I complex. Immunity 2002;16:345-354.
    • (2002) Immunity , vol.16 , pp. 345-354
    • Reiser, J.B.1
  • 40
    • 78651519759 scopus 로고    scopus 로고
    • A highly tilted binding mode by a self-reactive T cell receptor results in altered engagement of peptide and MHC
    • Sethi DK, et al. A highly tilted binding mode by a self-reactive T cell receptor results in altered engagement of peptide and MHC. J Exp Med 2011;208:91-102.
    • (2011) J Exp Med , vol.208 , pp. 91-102
    • Sethi, D.K.1
  • 41
    • 34247154800 scopus 로고    scopus 로고
    • A T cell receptor flattens a bulged antigenic peptide presented by a major histocompatibility complex class I molecule
    • Tynan FE, et al. A T cell receptor flattens a bulged antigenic peptide presented by a major histocompatibility complex class I molecule. Nat Immunol 2007;8:268-276.
    • (2007) Nat Immunol , vol.8 , pp. 268-276
    • Tynan, F.E.1
  • 42
    • 79960462110 scopus 로고    scopus 로고
    • A single T cell receptor bound to major histocompatibility complex class I and class II glycoproteins reveals switchable TCR conformers
    • Yin L, et al. A single T cell receptor bound to major histocompatibility complex class I and class II glycoproteins reveals switchable TCR conformers. Immunity 2011;35:23-33.
    • (2011) Immunity , vol.35 , pp. 23-33
    • Yin, L.1
  • 43
    • 0001937634 scopus 로고
    • The somatic generation of immune recognition
    • Jerne NK. The somatic generation of immune recognition. Eur J Immunol 1971;1:1-9.
    • (1971) Eur J Immunol , vol.1 , pp. 1-9
    • Jerne, N.K.1
  • 44
    • 0010435374 scopus 로고
    • Low frequency of somatic mutation in beta-chain variable region genes of human T-cell receptors
    • Ikuta K, Ogura T, Shimizu A, Honjo T. Low frequency of somatic mutation in beta-chain variable region genes of human T-cell receptors. Proc Natl Acad Sci USA 1985;82:7701-7705.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 7701-7705
    • Ikuta, K.1    Ogura, T.2    Shimizu, A.3    Honjo, T.4
  • 45
    • 0021056264 scopus 로고
    • The major histocompatibility complex-restricted antigen receptor on T cells. IV. An antiidiotypic antibody predicts both antigen and I-specificity
    • Marrack P, Shimonkevitz R, Hannum C, Haskins K, Kappler J. The major histocompatibility complex-restricted antigen receptor on T cells. IV. An antiidiotypic antibody predicts both antigen and I-specificity. J Exp Med 1983;158:1635-1646.
    • (1983) J Exp Med , vol.158 , pp. 1635-1646
    • Marrack, P.1    Shimonkevitz, R.2    Hannum, C.3    Haskins, K.4    Kappler, J.5
  • 46
    • 0018126188 scopus 로고
    • H-2 antigens of the thymus determine lymphocyte specificity
    • Fink PJ, Bevan MJ. H-2 antigens of the thymus determine lymphocyte specificity. J Exp Med 1978;148:766-775.
    • (1978) J Exp Med , vol.148 , pp. 766-775
    • Fink, P.J.1    Bevan, M.J.2
  • 47
    • 0018085532 scopus 로고
    • On the thymus in the differentiation of "H-2 self-recognition" by T cells: evidence for dual recognition?
    • Zinkernagel RM, Callahan GN, Althage A, Cooper S, Klein PA, Klein J. On the thymus in the differentiation of "H-2 self-recognition" by T cells: evidence for dual recognition? J Exp Med 1978;147:882-896.
    • (1978) J Exp Med , vol.147 , pp. 882-896
    • Zinkernagel, R.M.1    Callahan, G.N.2    Althage, A.3    Cooper, S.4    Klein, P.A.5    Klein, J.6
  • 48
    • 0022997960 scopus 로고
    • The T cell repertoire may be biased in favor of MHC recognition
    • Blackman M, et al. The T cell repertoire may be biased in favor of MHC recognition. Cell 1986;47:349-357.
    • (1986) Cell , vol.47 , pp. 349-357
    • Blackman, M.1
  • 50
    • 0030935007 scopus 로고    scopus 로고
    • The MHC reactivity of the T cell repertoire prior to positive and negative selection
    • Zerrahn J, Held W, Raulet DH. The MHC reactivity of the T cell repertoire prior to positive and negative selection. Cell 1997;88:627-636.
    • (1997) Cell , vol.88 , pp. 627-636
    • Zerrahn, J.1    Held, W.2    Raulet, D.H.3
  • 52
    • 34548128306 scopus 로고    scopus 로고
    • Structural evidence for a germline-encoded T cell receptor-major histocompatibility complex interaction 'codon'
    • Feng D, Bond CJ, Ely LK, Maynard J, Garcia KC. Structural evidence for a germline-encoded T cell receptor-major histocompatibility complex interaction 'codon'. Nat Immunol 2007;8:975-983.
    • (2007) Nat Immunol , vol.8 , pp. 975-983
    • Feng, D.1    Bond, C.J.2    Ely, L.K.3    Maynard, J.4    Garcia, K.C.5
  • 53
    • 58649114309 scopus 로고    scopus 로고
    • The molecular basis of TCR germline bias for MHC is surprisingly simple
    • Garcia KC, Adams JJ, Feng D, Ely LK. The molecular basis of TCR germline bias for MHC is surprisingly simple. Nat Immunol 2009;10:143-147.
    • (2009) Nat Immunol , vol.10 , pp. 143-147
    • Garcia, K.C.1    Adams, J.J.2    Feng, D.3    Ely, L.K.4
  • 56
    • 79956221437 scopus 로고    scopus 로고
    • Structural basis of specificity and cross-reactivity in T cell receptors specific for cytochrome c-I-E(k)
    • Newell EW, et al. Structural basis of specificity and cross-reactivity in T cell receptors specific for cytochrome c-I-E(k). J Immunol 2011;186:5823-5832.
    • (2011) J Immunol , vol.186 , pp. 5823-5832
    • Newell, E.W.1
  • 57
    • 67349280397 scopus 로고    scopus 로고
    • Germline-encoded amino acids in the alphabeta T-cell receptor control thymic selection
    • Scott-Browne JP, White J, Kappler JW, Gapin L, Marrack P. Germline-encoded amino acids in the alphabeta T-cell receptor control thymic selection. Nature 2009;458:1043-1046.
    • (2009) Nature , vol.458 , pp. 1043-1046
    • Scott-Browne, J.P.1    White, J.2    Kappler, J.W.3    Gapin, L.4    Marrack, P.5
  • 58
    • 84856291875 scopus 로고    scopus 로고
    • alphabeta T cell receptors that do not undergo major histocompatibility complex-specific thymic selection possess antibody-like recognition specificities
    • Tikhonova AN, et al. alphabeta T cell receptors that do not undergo major histocompatibility complex-specific thymic selection possess antibody-like recognition specificities. Immunity 2012;36:79-91.
    • (2012) Immunity , vol.36 , pp. 79-91
    • Tikhonova, A.N.1
  • 59
  • 60
    • 15844403109 scopus 로고    scopus 로고
    • Shark immunity bites back: affinity maturation and memory response in the nurse shark, Ginglymostoma cirratum
    • Dooley H, Flajnik MF. Shark immunity bites back: affinity maturation and memory response in the nurse shark, Ginglymostoma cirratum. Eur J Immunol 2005;35:936-945.
    • (2005) Eur J Immunol , vol.35 , pp. 936-945
    • Dooley, H.1    Flajnik, M.F.2
  • 61
    • 84861177186 scopus 로고    scopus 로고
    • Evolutionary and functional relationships of B cells from fish and mammals: insights into their novel roles in phagocytosis and presentation of particulate antigen
    • Sunyer JO. Evolutionary and functional relationships of B cells from fish and mammals: insights into their novel roles in phagocytosis and presentation of particulate antigen. Infect Disord Drug Targets 2012;12:200-212.
    • (2012) Infect Disord Drug Targets , vol.12 , pp. 200-212
    • Sunyer, J.O.1
  • 63
    • 79952750632 scopus 로고    scopus 로고
    • Structure of a TCR with high affinity for self-antigen reveals basis for escape from negative selection
    • Yin Y, Li Y, Kerzic MC, Martin R, Mariuzza RA. Structure of a TCR with high affinity for self-antigen reveals basis for escape from negative selection. EMBO J 2011;30:1137-1148.
    • (2011) EMBO J , vol.30 , pp. 1137-1148
    • Yin, Y.1    Li, Y.2    Kerzic, M.C.3    Martin, R.4    Mariuzza, R.A.5
  • 64
    • 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, Wiley DC. 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 2000;19:5611-5624.
    • (2000) EMBO J , vol.19 , pp. 5611-5624
    • Hennecke, J.1    Carfi, A.2    Wiley, D.C.3
  • 65
    • 0037018102 scopus 로고    scopus 로고
    • Structure of a complex of the human alpha/beta T cell receptor (TCR) HA1.7, influenza hemagglutinin peptide, and major histocompatibility complex class II molecule, HLA-DR4 (DRA*0101 and DRB1*0401): insight into TCR cross-restriction and alloreactivity
    • Hennecke J, Wiley DC. Structure of a complex of the human alpha/beta T cell receptor (TCR) HA1.7, influenza hemagglutinin peptide, and major histocompatibility complex class II molecule, HLA-DR4 (DRA*0101 and DRB1*0401): insight into TCR cross-restriction and alloreactivity. J Exp Med 2002;195:571-581.
    • (2002) J Exp Med , vol.195 , pp. 571-581
    • Hennecke, J.1    Wiley, D.C.2
  • 66
    • 0033559563 scopus 로고    scopus 로고
    • Reciprocal expression in CD4 or CD8 subsets of different members of the V alpha 11 gene family correlates with sequence polymorphism
    • Sim BC, Gascoigne NR. Reciprocal expression in CD4 or CD8 subsets of different members of the V alpha 11 gene family correlates with sequence polymorphism. J Immunol 1999;162:3153-3159.
    • (1999) J Immunol , vol.162 , pp. 3153-3159
    • Sim, B.C.1    Gascoigne, N.R.2
  • 67
    • 0031916706 scopus 로고    scopus 로고
    • Polymorphism within a TCRAV family influences the repertoire through class I/II restriction
    • Sim BC, Wung JL, Gascoigne NR. Polymorphism within a TCRAV family influences the repertoire through class I/II restriction. J Immunol 1998;160:1204-1211.
    • (1998) J Immunol , vol.160 , pp. 1204-1211
    • Sim, B.C.1    Wung, J.L.2    Gascoigne, N.R.3
  • 68
    • 0029791413 scopus 로고    scopus 로고
    • Control of MHC restriction by TCR Valpha CDR1 and CDR2
    • Sim BC, Zerva L, Greene MI, Gascoigne NR. Control of MHC restriction by TCR Valpha CDR1 and CDR2. Science 1996;273:963-966.
    • (1996) Science , vol.273 , pp. 963-966
    • Sim, B.C.1    Zerva, L.2    Greene, M.I.3    Gascoigne, N.R.4
  • 69
    • 0029037960 scopus 로고
    • Improved version of a human CD2 minigene based vector for T cell-specific expression in transgenic mice
    • Zhumabekov T, Corbella P, Tolaini M, Kioussis D. Improved version of a human CD2 minigene based vector for T cell-specific expression in transgenic mice. J Immunol Methods 1995;185:133-140.
    • (1995) J Immunol Methods , vol.185 , pp. 133-140
    • Zhumabekov, T.1    Corbella, P.2    Tolaini, M.3    Kioussis, D.4
  • 70
    • 0030670169 scopus 로고    scopus 로고
    • Separately expressed T cell receptor alpha and beta chain transgenes exert opposite effects on T cell differentiation and neoplastic transformation
    • Brabb T, Rubicz R, Mannikko V, Goverman J. Separately expressed T cell receptor alpha and beta chain transgenes exert opposite effects on T cell differentiation and neoplastic transformation. Eur J Immunol 1997;27:3039-3048.
    • (1997) Eur J Immunol , vol.27 , pp. 3039-3048
    • Brabb, T.1    Rubicz, R.2    Mannikko, V.3    Goverman, J.4
  • 71
    • 0035997909 scopus 로고    scopus 로고
    • Early TCRalpha expression generates TCRalphagamma complexes that signal the DN-to-DP transition and impair development
    • Erman B, Feigenbaum L, Coligan JE, Singer A. Early TCRalpha expression generates TCRalphagamma complexes that signal the DN-to-DP transition and impair development. Nat Immunol 2002;3:564-569.
    • (2002) Nat Immunol , vol.3 , pp. 564-569
    • Erman, B.1    Feigenbaum, L.2    Coligan, J.E.3    Singer, A.4
  • 72
    • 3242695397 scopus 로고    scopus 로고
    • Impact of early expression of TCR alpha chain on thymocyte development
    • Huang CY, Kanagawa O. Impact of early expression of TCR alpha chain on thymocyte development. Eur J Immunol 2004;34:1532-1541.
    • (2004) Eur J Immunol , vol.34 , pp. 1532-1541
    • Huang, C.Y.1    Kanagawa, O.2
  • 73
    • 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 YH, Smith KJ, Garboczi DN, Utz U, Biddison WE, Wiley DC. Two human T cell receptors bind in a similar diagonal mode to the HLA-A2/Tax peptide complex using different TCR amino acids. Immunity 1998;8:403-411.
    • (1998) Immunity , vol.8 , pp. 403-411
    • Ding, Y.H.1    Smith, K.J.2    Garboczi, D.N.3    Utz, U.4    Biddison, W.E.5    Wiley, D.C.6
  • 74
    • 81955161800 scopus 로고    scopus 로고
    • A role for differential variable gene pairing in creating T cell receptors specific for unique major histocompatibility ligands
    • Stadinski BD, et al. A role for differential variable gene pairing in creating T cell receptors specific for unique major histocompatibility ligands. Immunity 2011;35:694-6704.
    • (2011) Immunity , vol.35 , pp. 694-6704
    • Stadinski, B.D.1
  • 75
    • 82055208659 scopus 로고    scopus 로고
    • alphabeta T cell receptors come out swinging
    • Turner SJ, Rossjohn J. alphabeta T cell receptors come out swinging. Immunity 2011;35:660-662.
    • (2011) Immunity , vol.35 , pp. 660-662
    • Turner, S.J.1    Rossjohn, J.2
  • 76
    • 84862988475 scopus 로고    scopus 로고
    • A closer look at TCR germline recognition
    • Garcia K, et al. A closer look at TCR germline recognition. Immunity 2012;36:887-887.
    • (2012) Immunity , vol.36 , pp. 887-887
    • Garcia, K.1
  • 77
    • 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 JA, Martin R, Mariuzza RA. 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 2005;24:2968-2979.
    • (2005) EMBO J , vol.24 , pp. 2968-2979
    • Li, Y.1    Huang, Y.2    Lue, J.3    Quandt, J.A.4    Martin, R.5    Mariuzza, R.A.6
  • 78
    • 18244392426 scopus 로고    scopus 로고
    • Unconventional topology of self peptide-major histocompatibility complex binding by a human autoimmune T cell receptor
    • Hahn M, Nicholson MJ, Pyrdol J, Wucherpfennig KW. Unconventional topology of self peptide-major histocompatibility complex binding by a human autoimmune T cell receptor. Nat Immunol 2005;6:490-496.
    • (2005) Nat Immunol , vol.6 , pp. 490-496
    • Hahn, M.1    Nicholson, M.J.2    Pyrdol, J.3    Wucherpfennig, K.W.4
  • 80
    • 76949098835 scopus 로고    scopus 로고
    • Chromogranin A is an autoantigen in type 1 diabetes
    • Stadinski BD, et al. Chromogranin A is an autoantigen in type 1 diabetes. Nat Immunol 2010;11:225-231.
    • (2010) Nat Immunol , vol.11 , pp. 225-231
    • Stadinski, B.D.1
  • 81
    • 66149179356 scopus 로고    scopus 로고
    • Antigen presentation by CD1 lipids, T cells, and NKT cells in microbial immunity
    • Cohen NR, Garg S, Brenner MB. Antigen presentation by CD1 lipids, T cells, and NKT cells in microbial immunity. Adv Immunol 2009;102:1-94.
    • (2009) Adv Immunol , vol.102 , pp. 1-94
    • Cohen, N.R.1    Garg, S.2    Brenner, M.B.3
  • 82
    • 45449103839 scopus 로고    scopus 로고
    • CD1d-restricted iNKT cells, the 'Swiss-Army knife' of the immune system
    • Matsuda JL, Mallevaey T, Scott-Browne J, Gapin L. CD1d-restricted iNKT cells, the 'Swiss-Army knife' of the immune system. Curr Opin Immunol 2008;20:358-368.
    • (2008) Curr Opin Immunol , vol.20 , pp. 358-368
    • Matsuda, J.L.1    Mallevaey, T.2    Scott-Browne, J.3    Gapin, L.4
  • 83
    • 34447131000 scopus 로고    scopus 로고
    • CD1d-lipid-antigen recognition by the semi-invariant NKT T-cell receptor
    • Borg NA, et al. CD1d-lipid-antigen recognition by the semi-invariant NKT T-cell receptor. Nature 2007;448:44-49.
    • (2007) Nature , vol.448 , pp. 44-49
    • Borg, N.A.1
  • 84
    • 78149305888 scopus 로고    scopus 로고
    • The Valpha14 invariant natural killer T cell TCR forces microbial glycolipids and CD1d into a conserved binding mode
    • Li Y, et al. The Valpha14 invariant natural killer T cell TCR forces microbial glycolipids and CD1d into a conserved binding mode. J Exp Med 2010;207:2383-2393.
    • (2010) J Exp Med , vol.207 , pp. 2383-2393
    • Li, Y.1
  • 85
    • 79952752495 scopus 로고    scopus 로고
    • A molecular basis for NKT cell recognition of CD1d-self-antigen
    • Mallevaey T, et al. A molecular basis for NKT cell recognition of CD1d-self-antigen. Immunity 2011;34:315-326.
    • (2011) Immunity , vol.34 , pp. 315-326
    • Mallevaey, T.1
  • 86
    • 34548745246 scopus 로고    scopus 로고
    • Germline-encoded recognition of diverse glycolipids by natural killer T cells
    • Scott-Browne JP, et al. Germline-encoded recognition of diverse glycolipids by natural killer T cells. Nat Immunol 2007;8:1105-1113.
    • (2007) Nat Immunol , vol.8 , pp. 1105-1113
    • Scott-Browne, J.P.1
  • 87
    • 0025764133 scopus 로고
    • Major histocompatibility complex independent T cell receptor-antigen interaction: functional analysis using fluorescein derivatives
    • Diamond DJ, et al. Major histocompatibility complex independent T cell receptor-antigen interaction: functional analysis using fluorescein derivatives. J Exp Med 1991;174:229-241.
    • (1991) J Exp Med , vol.174 , pp. 229-241
    • Diamond, D.J.1
  • 88
    • 0025891021 scopus 로고
    • Analysis of the interaction site for the self superantigen Mls-1a on T cell receptor V beta
    • Pullen AM, Bill J, Kubo RT, Marrack P, Kappler JW. Analysis of the interaction site for the self superantigen Mls-1a on T cell receptor V beta. J Exp Med 1991;173:1183-1192.
    • (1991) J Exp Med , vol.173 , pp. 1183-1192
    • Pullen, A.M.1    Bill, J.2    Kubo, R.T.3    Marrack, P.4    Kappler, J.W.5
  • 89
    • 0025181117 scopus 로고
    • Residues of the variable region of the T-cell-receptor beta-chain that interact with S. aureus toxin superantigens
    • Choi YW, Herman A, DiGiusto D, Wade T, Marrack P, Kappler J. Residues of the variable region of the T-cell-receptor beta-chain that interact with S. aureus toxin superantigens. Nature 1990;346:471-473.
    • (1990) Nature , vol.346 , pp. 471-473
    • Choi, Y.W.1    Herman, A.2    DiGiusto, D.3    Wade, T.4    Marrack, P.5    Kappler, J.6
  • 90
    • 33846977011 scopus 로고    scopus 로고
    • Crystal structure of a complete ternary complex of TCR, superantigen and peptide-MHC
    • Wang L, et al. Crystal structure of a complete ternary complex of TCR, superantigen and peptide-MHC. Nat Struct Mol Biol 2007;14:169-171.
    • (2007) Nat Struct Mol Biol , vol.14 , pp. 169-171
    • Wang, L.1
  • 91
    • 78650074574 scopus 로고    scopus 로고
    • The structure of superantigen complexed with TCR and MHC reveals novel insights into superantigenic T cell activation
    • Saline M, Rodstrom KE, Fischer G, Orekhov VY, Karlsson BG, Lindkvist-Petersson K. The structure of superantigen complexed with TCR and MHC reveals novel insights into superantigenic T cell activation. Nat Commun 2010;1:119.
    • (2010) Nat Commun , vol.1 , pp. 119
    • Saline, M.1    Rodstrom, K.E.2    Fischer, G.3    Orekhov, V.Y.4    Karlsson, B.G.5    Lindkvist-Petersson, K.6
  • 92
    • 0035167967 scopus 로고    scopus 로고
    • The immune dysregulation, polyendocrinopathy, enteropathy, X-linked syndrome (IPEX) is caused by mutations of FOXP3
    • Bennett CL, et al. The immune dysregulation, polyendocrinopathy, enteropathy, X-linked syndrome (IPEX) is caused by mutations of FOXP3. Nat Genet 2001;27:20-21.
    • (2001) Nat Genet , vol.27 , pp. 20-21
    • Bennett, C.L.1
  • 93
    • 0034805277 scopus 로고    scopus 로고
    • Autoimmune lymphoproliferative syndrome: types I, II and beyond
    • Chun HJ, Lenardo MJ. Autoimmune lymphoproliferative syndrome: types I, II and beyond. Adv Exp Med Biol 2001;490:49-57.
    • (2001) Adv Exp Med Biol , vol.490 , pp. 49-57
    • Chun, H.J.1    Lenardo, M.J.2
  • 94
    • 84858750418 scopus 로고    scopus 로고
    • Twin studies in autoimmune disease: genetics, gender and environment
    • Bogdanos DP, et al. Twin studies in autoimmune disease: genetics, gender and environment. J Autoimmun 2012;38:J156-J169.
    • (2012) J Autoimmun , vol.38
    • Bogdanos, D.P.1
  • 95
    • 71649102108 scopus 로고    scopus 로고
    • The genetics of human autoimmune disease
    • Invernizzi P, Gershwin ME. The genetics of human autoimmune disease. J Autoimmun 2009;33:290-299.
    • (2009) J Autoimmun , vol.33 , pp. 290-299
    • Invernizzi, P.1    Gershwin, M.E.2
  • 96
    • 61849115785 scopus 로고    scopus 로고
    • Copy number variation in the human genome and its implication in autoimmunity
    • Schaschl H, Aitman TJ, Vyse TJ. Copy number variation in the human genome and its implication in autoimmunity. Clin Exp Immunol 2009;156:12-16.
    • (2009) Clin Exp Immunol , vol.156 , pp. 12-16
    • Schaschl, H.1    Aitman, T.J.2    Vyse, T.J.3
  • 97
    • 0016400099 scopus 로고
    • HL-A, immune-response genes, and disease
    • McDevitt HO, Bodmer WF. HL-A, immune-response genes, and disease. Lancet 1974;1:1269-1275.
    • (1974) Lancet , vol.1 , pp. 1269-1275
    • McDevitt, H.O.1    Bodmer, W.F.2
  • 98
    • 77951720536 scopus 로고    scopus 로고
    • Antigenic strength controls the generation of antigen-specific IL-10-secreting T regulatory cells
    • Gabrysova L, Wraith DC. Antigenic strength controls the generation of antigen-specific IL-10-secreting T regulatory cells. Eur J Immunol 2010;40:1386-1395.
    • (2010) Eur J Immunol , vol.40 , pp. 1386-1395
    • Gabrysova, L.1    Wraith, D.C.2
  • 99
    • 77955391804 scopus 로고    scopus 로고
    • TCR ligand density and affinity determine peripheral induction of Foxp3 in vivo
    • Gottschalk RA, Corse E, Allison JP. TCR ligand density and affinity determine peripheral induction of Foxp3 in vivo. J Exp Med 2010;207:1701-1711.
    • (2010) J Exp Med , vol.207 , pp. 1701-1711
    • Gottschalk, R.A.1    Corse, E.2    Allison, J.P.3
  • 100
    • 79958251745 scopus 로고    scopus 로고
    • T cell receptor signal strength in Treg and iNKT cell development demonstrated by a novel fluorescent reporter mouse
    • Moran AE, et al. T cell receptor signal strength in Treg and iNKT cell development demonstrated by a novel fluorescent reporter mouse. J Exp Med 2011;208:1279-1289.
    • (2011) J Exp Med , vol.208 , pp. 1279-1289
    • Moran, A.E.1
  • 101
    • 77954104660 scopus 로고    scopus 로고
    • Dominant role of antigen dose in CD4+Foxp3+ regulatory T cell induction and expansion
    • Turner MS, Kane LP, Morel PA. Dominant role of antigen dose in CD4+Foxp3+ regulatory T cell induction and expansion. J Immunol 2009;183:4895-4903.
    • (2009) J Immunol , vol.183 , pp. 4895-4903
    • Turner, M.S.1    Kane, L.P.2    Morel, P.A.3
  • 102
    • 0025021670 scopus 로고
    • Role of self-peptides in positively selecting the T-cell repertoire
    • Nikolic-Zugic J, Bevan MJ. Role of self-peptides in positively selecting the T-cell repertoire. Nature 1990;344:65-67.
    • (1990) Nature , vol.344 , pp. 65-67
    • Nikolic-Zugic, J.1    Bevan, M.J.2
  • 103
    • 84859425494 scopus 로고    scopus 로고
    • Highly diverse TCRalpha chain repertoire of pre-immune CD8(+) T cells reveals new insights in gene recombination
    • Genolet R, Stevenson BJ, Farinelli L, Osteras M, Luescher IF. Highly diverse TCRalpha chain repertoire of pre-immune CD8(+) T cells reveals new insights in gene recombination. EMBO J 2012;31:1666-1678.
    • (2012) EMBO J , vol.31 , pp. 1666-1678
    • Genolet, R.1    Stevenson, B.J.2    Farinelli, L.3    Osteras, M.4    Luescher, I.F.5
  • 104
    • 77956460339 scopus 로고    scopus 로고
    • Overlap and effective size of the human CD8+ T cell receptor repertoire
    • Robins HS, et al. Overlap and effective size of the human CD8+ T cell receptor repertoire. Sci Transl Med 2010;2:47ra64.
    • (2010) Sci Transl Med , vol.2
    • Robins, H.S.1
  • 105
    • 78650596159 scopus 로고    scopus 로고
    • Convergent recombination shapes the clonotypic landscape of the naive T-cell repertoire
    • Quigley MF, et al. Convergent recombination shapes the clonotypic landscape of the naive T-cell repertoire. Proc Natl Acad Sci USA 2010;107:19414-19419.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 19414-19419
    • Quigley, M.F.1
  • 106
    • 79251590221 scopus 로고    scopus 로고
    • Persistent survival of prevalent clonotypes within an immunodominant HIV gag-specific CD8+ T cell response
    • van Bockel DJ, et al. Persistent survival of prevalent clonotypes within an immunodominant HIV gag-specific CD8+ T cell response. J Immunol 2010;186:359-371.
    • (2010) J Immunol , vol.186 , pp. 359-371
    • van Bockel, D.J.1
  • 107
    • 79955022207 scopus 로고    scopus 로고
    • A mechanism for TCR sharing between T cell subsets and individuals revealed by pyrosequencing
    • Venturi V, et al. A mechanism for TCR sharing between T cell subsets and individuals revealed by pyrosequencing. J Immunol 2011;186:4285-4294.
    • (2011) J Immunol , vol.186 , pp. 4285-4294
    • Venturi, V.1
  • 108
    • 0026317875 scopus 로고
    • Creation of a large genomic deletion at the T-cell antigen receptor beta-subunit locus in mouse embryonic stem cells by gene targeting
    • Mombaerts P, Clarke AR, Hooper ML, Tonegawa S. Creation of a large genomic deletion at the T-cell antigen receptor beta-subunit locus in mouse embryonic stem cells by gene targeting. Proc Natl Acad Sci USA 1991;88:3084-3087.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 3084-3087
    • Mombaerts, P.1    Clarke, A.R.2    Hooper, M.L.3    Tonegawa, S.4
  • 109
    • 22744441535 scopus 로고    scopus 로고
    • How the T cell repertoire becomes peptide and MHC specific
    • Huseby ES, et al. How the T cell repertoire becomes peptide and MHC specific. Cell 2005;122:247-260.
    • (2005) Cell , vol.122 , pp. 247-260
    • Huseby, E.S.1


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