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Volumn 11, Issue 6, 1999, Pages 967-977

Characterization of the interaction of a TCR α chain variable domain with MHC II I-A molecules

Author keywords

Fourth hypervariable region; Immunosuppression; MHC class II; TCR; V( ) domain

Indexed keywords

ALANINE; EPITOPE; GLUTAMIC ACID; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 2; MYELIN BASIC PROTEIN; T LYMPHOCYTE RECEPTOR ALPHA CHAIN;

EID: 0033033582     PISSN: 09538178     EISSN: None     Source Type: Journal    
DOI: 10.1093/intimm/11.6.967     Document Type: Article
Times cited : (3)

References (70)
  • 1
    • 0029898565 scopus 로고    scopus 로고
    • Structure and function of the T-cell receptor: Insights from X-ray crystallography
    • Fields, B. A. and Mariuzza, R. A. 1996. Structure and function of the T-cell receptor: insights from X-ray crystallography. Immunol. Today 17:330.
    • (1996) Immunol. Today , vol.17 , pp. 330
    • Fields, B.A.1    Mariuzza, R.A.2
  • 2
    • 0028038426 scopus 로고
    • MHC-dependent antigen processing and peptide presentation: Providing ligands for T lymphocyte activation
    • Germain, R. N. 1994. MHC-dependent antigen processing and peptide presentation: providing ligands for T lymphocyte activation. Cell 76:287.
    • (1994) Cell , vol.76 , pp. 287
    • Germain, R.N.1
  • 3
    • 0029920469 scopus 로고    scopus 로고
    • Antigen processing and presentation by the class I major histocompatibility complex
    • York, I. A. and Rock, K. L. 1996. Antigen processing and presentation by the class I major histocompatibility complex. Annu. Rev. Immunol. 14:369.
    • (1996) Annu. Rev. Immunol. , vol.14 , pp. 369
    • York, I.A.1    Rock, K.L.2
  • 8
    • 0028348369 scopus 로고
    • Crystal structure of the human class II MHC protein HLA-DR1 complexed with an influenza virus peptide
    • Stern, L. J., Brown, J. H., Jardetzky, T. S., Gorga, J. C., Urban, R. G., Strominger, J. L. and Wiley, D. C. 1994. Crystal structure of the human class II MHC protein HLA-DR1 complexed with an influenza virus peptide. Nature 368:215.
    • (1994) Nature , vol.368 , pp. 215
    • Stern, L.J.1    Brown, J.H.2    Jardetzky, T.S.3    Gorga, J.C.4    Urban, R.G.5    Strominger, J.L.6    Wiley, D.C.7
  • 9
    • 0029782111 scopus 로고    scopus 로고
    • Structures of an MHC class II molecule with covalently bound single peptides
    • Fremont, D. H., Hendrickson, W. A., Marrack, P. and Kappler, J. 1996. Structures of an MHC class II molecule with covalently bound single peptides. Science 272:1001.
    • (1996) Science , vol.272 , pp. 1001
    • Fremont, D.H.1    Hendrickson, W.A.2    Marrack, P.3    Kappler, J.4
  • 10
    • 0029965954 scopus 로고    scopus 로고
    • An altered position of the α 2 helix of MHC class I is revealed by the crystal structure of HLA-B*3501
    • Smith, K. J., Reid, S. W., Stuart, D. I., McMichael, A. J., Jones, E. Y. and Bell, J. I. 1996. An altered position of the α 2 helix of MHC class I is revealed by the crystal structure of HLA-B*3501. Immunity 4:203.
    • (1996) Immunity , vol.4 , pp. 203
    • Smith, K.J.1    Reid, S.W.2    Stuart, D.I.3    McMichael, A.J.4    Jones, E.Y.5    Bell, J.I.6
  • 12
    • 0032033678 scopus 로고    scopus 로고
    • d-peptide complexes reveal that high affinity can be achieved without large anchor residues
    • d-peptide complexes reveal that high affinity can be achieved without large anchor residues. Immunity 8:319.
    • (1998) Immunity , vol.8 , pp. 319
    • Scott, C.A.1    Peterson, P.A.2    Teyton, L.3    Wilson, I.A.4
  • 14
    • 0028956603 scopus 로고
    • Crystal structure of the β chain of a T cell antigen receptor
    • Bentley, G. A., Boulot, G., Karjalainen, K. and Mariuzza, R. A. 1995. Crystal structure of the β chain of a T cell antigen receptor. Science 267:1984.
    • (1995) Science , vol.267 , pp. 1984
    • Bentley, G.A.1    Boulot, G.2    Karjalainen, K.3    Mariuzza, R.A.4
  • 17
    • 0029855347 scopus 로고    scopus 로고
    • Structure of the complex between human T-cell receptor, viral peptide and HLA-A2
    • Garboczi, D. N., Ghosh, P., Utz, U., Fan, Q. R., Biddison, W. E. and Wiley, D. C. 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
  • 18
    • 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., Smith, K. J., Garboczi, D. N., Utz, U., Biddison, W. E. and Wiley, D. C. 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
  • 19
    • 0032549142 scopus 로고    scopus 로고
    • Structural basis of plasticity in T cell receptor recognition of a self peptide-MHC antigen
    • Garcia, K. C., Degano, M., Pease, L. R., Huang, M., Peterson, P. A., Teyton, L. and Wilson, I. A. 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
  • 25
    • 0024325672 scopus 로고
    • Antigen recognition in autoimmune encephalomyelitis and the potential for peptide-mediated immunotherapy
    • Wraith, D. C., Smilek, D. E., Mitchell, D. J., Steinman, L. and McDevitt, H. O. 1989. Antigen recognition in autoimmune encephalomyelitis and the potential for peptide-mediated immunotherapy. Cell 59:247.
    • (1989) Cell , vol.59 , pp. 247
    • Wraith, D.C.1    Smilek, D.E.2    Mitchell, D.J.3    Steinman, L.4    McDevitt, H.O.5
  • 27
    • 0028919236 scopus 로고
    • T cell receptor alpha-chain defines the antigen specificity of antigen-specific suppressor factor but does not impart genetic restriction
    • O'Hara, R. M. J., Byrne, M. C., Kuchroo, V. K., Nagelin, A., Whitters, M. J., Jayaraman, S., Henderson, S. L., Dorf, M. E. and Collins, M. 1995. T cell receptor alpha-chain defines the antigen specificity of antigen-specific suppressor factor but does not impart genetic restriction. J. Immunol. 154:2075.
    • (1995) J. Immunol. , vol.154 , pp. 2075
    • O'Hara, R.M.J.1    Byrne, M.C.2    Kuchroo, V.K.3    Nagelin, A.4    Whitters, M.J.5    Jayaraman, S.6    Henderson, S.L.7    Dorf, M.E.8    Collins, M.9
  • 28
    • 0029959442 scopus 로고    scopus 로고
    • Cellular mechanisms for the formation of a soluble form derivative of T-cell receptor alpha chain by suppressor T cells
    • Ishii, Y., Nakano, T. and Ishizaka, K. 1996. Cellular mechanisms for the formation of a soluble form derivative of T-cell receptor alpha chain by suppressor T cells. Proc. Natl Acad Sci. USA 93:7207.
    • (1996) Proc. Natl Acad Sci. USA , vol.93 , pp. 7207
    • Ishii, Y.1    Nakano, T.2    Ishizaka, K.3
  • 29
    • 0028354134 scopus 로고
    • Two processing pathways for the MHC class II-restricted presentation of exogenous influenza virus antigen
    • Pinet, V., Malnati, M. S. and Long, E. O. 1994. Two processing pathways for the MHC class II-restricted presentation of exogenous influenza virus antigen. J. Immunol. 152:4852.
    • (1994) J. Immunol. , vol.152 , pp. 4852
    • Pinet, V.1    Malnati, M.S.2    Long, E.O.3
  • 30
    • 0029055938 scopus 로고
    • Antigen presentation mediated by recycling of surface HLA-DR molecules
    • Pinet, V., Vergelli, M., Martin, R., Bakke, O. and Long, E. O. 1995. Antigen presentation mediated by recycling of surface HLA-DR molecules. Nature 375:603.
    • (1995) Nature , vol.375 , pp. 603
    • Pinet, V.1    Vergelli, M.2    Martin, R.3    Bakke, O.4    Long, E.O.5
  • 31
    • 0026594097 scopus 로고
    • MHC-binding peptides for immunotherapy of experimental autoimmune disease
    • Wraith, D. C., Smilek, D. E. and Webb, S. 1992. MHC-binding peptides for immunotherapy of experimental autoimmune disease. J. Autoimmun. 5 (Suppl. A):103.
    • (1992) J. Autoimmun. , vol.5 , Issue.SUPPL. A , pp. 103
    • Wraith, D.C.1    Smilek, D.E.2    Webb, S.3
  • 34
    • 0024845198 scopus 로고
    • Derivation of a T cell hybridoma variant deprived of functional T cell receptor alpha and beta chain transcripts reveals a nonfunctional alpha-mRNA of BW5147 origin
    • Letourneur, F. and Malissen, B. 1989. Derivation of a T cell hybridoma variant deprived of functional T cell receptor alpha and beta chain transcripts reveals a nonfunctional alpha-mRNA of BW5147 origin. Eur. J. Immunol. 19:2269.
    • (1989) Eur. J. Immunol. , vol.19 , pp. 2269
    • Letourneur, F.1    Malissen, B.2
  • 35
    • 0027215148 scopus 로고
    • Transfer of putative complementarity-determining region loops of T cell receptor V domains confers toxin reactivity but not peptide/MHC specificity
    • Patten, P. A., Rock, E. P., Sonoda, T., Fazekas de St Groth, B., Jorgensen, J. L. and Davis, M. M. 1993. Transfer of putative complementarity-determining region loops of T cell receptor V domains confers toxin reactivity but not peptide/MHC specificity. J. Immunol. 150:2281.
    • (1993) J. Immunol. , vol.150 , pp. 2281
    • Patten, P.A.1    Rock, E.P.2    Sonoda, T.3    Fazekas De St Groth, B.4    Jorgensen, J.L.5    Davis, M.M.6
  • 37
    • 0021814334 scopus 로고
    • Characterization of a murine monoclonal antibody specific for an allotypic determinant on T cell antigen receptor
    • Staerz, U. D., Rammensee, H. G., Benedetto, J. D. and Bevan, M. J. 1985. Characterization of a murine monoclonal antibody specific for an allotypic determinant on T cell antigen receptor. J. Immunol. 134:3994.
    • (1985) J. Immunol. , vol.134 , pp. 3994
    • Staerz, U.D.1    Rammensee, H.G.2    Benedetto, J.D.3    Bevan, M.J.4
  • 38
    • 0021338681 scopus 로고
    • Monoclonal antibodies specific for Ia glycoproteins raised by immunization with activated T cells: Possible role of T cell bound Ia antigens as targets of immunoregulatory T cells
    • Janeway, C. A. J., Conrad, P. J., Lerner, E. A., Babich, J., Wettstein, P. and Murphy, D. B. 1984. Monoclonal antibodies specific for Ia glycoproteins raised by immunization with activated T cells: possible role of T cell bound Ia antigens as targets of immunoregulatory T cells. J. Immunol. 132:662.
    • (1984) J. Immunol. , vol.132 , pp. 662
    • Janeway, C.A.J.1    Conrad, P.J.2    Lerner, E.A.3    Babich, J.4    Wettstein, P.5    Murphy, D.B.6
  • 40
    • 0026572332 scopus 로고
    • Secretion of T cell receptor fragments from recombinant Escherichia coli cells
    • Ward, E. S. 1992. Secretion of T cell receptor fragments from recombinant Escherichia coli cells. J. Mol. Biol. 224:885.
    • (1992) J. Mol. Biol. , vol.224 , pp. 885
    • Ward, E.S.1
  • 41
    • 0023613953 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel, T. A., Roberts, J. D. and Zakour, R. A. 1987. Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol. 154:367.
    • (1987) Methods Enzymol. , vol.154 , pp. 367
    • Kunkel, T.A.1    Roberts, J.D.2    Zakour, R.A.3
  • 43
    • 0026691177 scopus 로고
    • Immunodetection of biotinylated lymphocyte-surface proteins by enhanced chemiluminescence: A nonradioactive method for cell-surface protein analysis
    • Meier, T., Arni, S., Malarkannan, S., Poincelet, M. and Hoessli, D. 1992. Immunodetection of biotinylated lymphocyte-surface proteins by enhanced chemiluminescence: a nonradioactive method for cell-surface protein analysis. Anal. Biochem. 204:220.
    • (1992) Anal. Biochem. , vol.204 , pp. 220
    • Meier, T.1    Arni, S.2    Malarkannan, S.3    Poincelet, M.4    Hoessli, D.5
  • 45
    • 0000702477 scopus 로고    scopus 로고
    • Measurement of human and murine interleukin 2 and interleukin 4
    • Coligan J. E., ed., John Wiley, New York
    • Lipsky P. E. and Bottomly K. 1996. Measurement of human and murine interleukin 2 and interleukin 4. In Coligan J. E., ed., Current Protocols in Immunology, p. 6.3.1. John Wiley, New York.
    • (1996) Current Protocols in Immunology , pp. 631
    • Lipsky, P.E.1    Bottomly, K.2
  • 46
    • 0022519337 scopus 로고
    • Three-dimensional structure of an antigen-antibody complex at 2.8 Å Resolution
    • Amit, A. G., Mariuzza, R. A., Phillips, S. E. V. and Poljak, R. J. 1986. Three-dimensional structure of an antigen-antibody complex at 2.8 Å Resolution. Science 233:747.
    • (1986) Science , vol.233 , pp. 747
    • Amit, A.G.1    Mariuzza, R.A.2    Phillips, S.E.V.3    Poljak, R.J.4
  • 47
  • 48
    • 0022974996 scopus 로고
    • T-cell epitope of the autoantigen myelin basic protein that induces encephalomyelitis
    • Zamvil, S. S., Mitchell, D. J., Moore, A. C., Kitamura, K., Steinman, L. and Rothbard, J. B. 1986. T-cell epitope of the autoantigen myelin basic protein that induces encephalomyelitis. Nature 324:258.
    • (1986) Nature , vol.324 , pp. 258
    • Zamvil, S.S.1    Mitchell, D.J.2    Moore, A.C.3    Kitamura, K.4    Steinman, L.5    Rothbard, J.B.6
  • 49
    • 0024362181 scopus 로고
    • Capacity of intact proteins to bind to MHC class II molecules
    • Sette, A., Adorini, L., Colon, S. M., Buus, S. and Grey, H. M. 1989. Capacity of intact proteins to bind to MHC class II molecules. J. Immunol. 143:1265.
    • (1989) J. Immunol. , vol.143 , pp. 1265
    • Sette, A.1    Adorini, L.2    Colon, S.M.3    Buus, S.4    Grey, H.M.5
  • 50
    • 0030451002 scopus 로고    scopus 로고
    • Distinct antigen MHC class II complexes generated by separate processing pathways
    • Lindner, R. and Unanue, E. R. 1996. Distinct antigen MHC class II complexes generated by separate processing pathways. EMBO J. 15:6910.
    • (1996) EMBO J. , vol.15 , pp. 6910
    • Lindner, R.1    Unanue, E.R.2
  • 51
    • 0027155945 scopus 로고
    • Acidification and disulfide reduction can be sufficient to allow intact proteins to bind class II MHC
    • Jensen, P. E. 1993. Acidification and disulfide reduction can be sufficient to allow intact proteins to bind class II MHC. J. Immunol. 150:3347.
    • (1993) J. Immunol. , vol.150 , pp. 3347
    • Jensen, P.E.1
  • 52
    • 0027441931 scopus 로고
    • Determinant capture as a possible mechanism of protection afforded by major histocompatibility complex class II molecules in autoimmune disease
    • Deng, H., Apple, R., Clare-Salzler, M., Trembleau, S., Mathis, D., Adorini, L. and Sercarz, E. 1993. Determinant capture as a possible mechanism of protection afforded by major histocompatibility complex class II molecules in autoimmune disease. J. Exp. Med. 178:1675.
    • (1993) J. Exp. Med. , vol.178 , pp. 1675
    • Deng, H.1    Apple, R.2    Clare-Salzler, M.3    Trembleau, S.4    Mathis, D.5    Adorini, L.6    Sercarz, E.7
  • 53
    • 0032532038 scopus 로고    scopus 로고
    • Large protein fragments as substrates for endocytic antigen capture by MHC class II molecules
    • Castellino, F., Zappacosta, F., Coligan, J. E. and Germain, R. N. 1998. Large protein fragments as substrates for endocytic antigen capture by MHC class II molecules. J. Immunol. 161:4048.
    • (1998) J. Immunol. , vol.161 , pp. 4048
    • Castellino, F.1    Zappacosta, F.2    Coligan, J.E.3    Germain, R.N.4
  • 54
    • 0030052495 scopus 로고    scopus 로고
    • Invariant chain protects class II histocompatibility antigens from binding intact polypeptides in the endoplasmic reticulum
    • Busch, R., Cloutier, I., Sekaly, R. P. and Hammerling, G. J. 1996. Invariant chain protects class II histocompatibility antigens from binding intact polypeptides in the endoplasmic reticulum. EMBO J. 15:418.
    • (1996) EMBO J. , vol.15 , pp. 418
    • Busch, R.1    Cloutier, I.2    Sekaly, R.P.3    Hammerling, G.J.4
  • 55
    • 0027439013 scopus 로고
    • An autoantigenic T cell epitope forms unstable complexes with class II MHC: A novel route for escape from tolerance induction
    • Fairchild, P. J., Wildgoose, R., Atherton, E., Webb, S. and Wraith, D. C. 1993. An autoantigenic T cell epitope forms unstable complexes with class II MHC: a novel route for escape from tolerance induction. Int. Immunol. 5:1151.
    • (1993) Int. Immunol. , vol.5 , pp. 1151
    • Fairchild, P.J.1    Wildgoose, R.2    Atherton, E.3    Webb, S.4    Wraith, D.C.5
  • 56
    • 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. 1996. Major histocompatibility complex class II-associated peptides control the presentation of bacterial superantigens to T cells. J. Exp. Med. 183:1083.
    • (1996) J. Exp. Med. , vol.183 , pp. 1083
    • Wen, R.1    Cole, G.A.2    Surman, S.3    Blackman, M.A.4    Woodland, D.L.5
  • 58
    • 0028842488 scopus 로고
    • Major histocompatibility complex class II-associated peptides determine the binding of the superantigen toxic shock syndrome toxin-1
    • von Bonin, A., Ehrlich, S., Malcherek, G. and Fleischer, B. 1995. Major histocompatibility complex class II-associated peptides determine the binding of the superantigen toxic shock syndrome toxin-1. Eur J. Immunol. 25:2894.
    • (1995) Eur J. Immunol. , vol.25 , pp. 2894
    • Von Bonin, A.1    Ehrlich, S.2    Malcherek, G.3    Fleischer, B.4
  • 59
    • 0028136262 scopus 로고
    • The CLIP region of invariant chain plays a critical role in regulating major histocompatibility complex class II folding, transport, and peptide occupancy
    • Romagnoli, P. and Germain, R. N. 1994. The CLIP region of invariant chain plays a critical role in regulating major histocompatibility complex class II folding, transport, and peptide occupancy. J. Exp. Med. 180:1107.
    • (1994) J. Exp. Med. , vol.180 , pp. 1107
    • Romagnoli, P.1    Germain, R.N.2
  • 62
    • 0026553367 scopus 로고
    • Specific low-affinity recognition of major histocompatibility complex plus peptide by soluble T-cell receptor
    • Weber, S., Traunecker, A., Oliveri, F., Gerhard, W. and Karjalainen, K. 1992. Specific low-affinity recognition of major histocompatibility complex plus peptide by soluble T-cell receptor. Nature 356:793.
    • (1992) Nature , vol.356 , pp. 793
    • Weber, S.1    Traunecker, A.2    Oliveri, F.3    Gerhard, W.4    Karjalainen, K.5
  • 65
    • 0003104975 scopus 로고    scopus 로고
    • A TCR binds to antagonist ligands with lower affinities and faster dissociation rates than to agonists
    • Lyons, D. S., Lieberman, S. A., Hampl, J., Boniface, J. J., Chien, Y., Berg, L. J. and Davis, M. M. 1996. A TCR binds to antagonist ligands with lower affinities and faster dissociation rates than to agonists. Immunity 5:53.
    • (1996) Immunity , vol.5 , pp. 53
    • Lyons, D.S.1    Lieberman, S.A.2    Hampl, J.3    Boniface, J.J.4    Chien, Y.5    Berg, L.J.6    Davis, M.M.7
  • 66
    • 0026691321 scopus 로고
    • An MHC interaction site maps to the amino-terminal half of the T cell receptor alpha chain variable domain
    • Hong, S. C., Chelouche, A., Lin, R. H., Shaywitz, D., Braunstein, N. S., Glimcher, L. and Janeway, C. A. J. 1992. An MHC interaction site maps to the amino-terminal half of the T cell receptor alpha chain variable domain. Cell 69:999.
    • (1992) Cell , vol.69 , pp. 999
    • Hong, S.C.1    Chelouche, A.2    Lin, R.H.3    Shaywitz, D.4    Braunstein, N.S.5    Glimcher, L.6    Janeway, C.A.J.7
  • 67
    • 0026502380 scopus 로고
    • Mapping T-cell receptor-peptide contacts by variant peptide immunization of single-chain transgenics
    • Jorgensen, J. L., Esser, U., Fazekas de St Groth, B., Reay, P. A. and Davis, M. M. 1992. Mapping T-cell receptor-peptide contacts by variant peptide immunization of single-chain transgenics. Nature 355:224.
    • (1992) Nature , vol.355 , pp. 224
    • Jorgensen, J.L.1    Esser, U.2    Fazekas De St Groth, B.3    Reay, P.A.4    Davis, M.M.5
  • 68
    • 0029896115 scopus 로고    scopus 로고
    • Modulation of promiscuous T cell receptor recognition by mutagenesis of CDR2 residues
    • Brawley, J. V. and Concannon, P. 1996. Modulation of promiscuous T cell receptor recognition by mutagenesis of CDR2 residues. J. Exp. Med. 183:2043.
    • (1996) J. Exp. Med. , vol.183 , pp. 2043
    • Brawley, J.V.1    Concannon, P.2
  • 69
    • 0032213264 scopus 로고    scopus 로고
    • Invariant chain can bind MHC class II at a site other than the peptide binding groove
    • Wilson, N. A., Wolf, P., Ploegh, H., Ignatowicz, L., Kappler, J. and Marrack, P. 1998. Invariant chain can bind MHC class II at a site other than the peptide binding groove. J. Immunol. 161:4777.
    • (1998) J. Immunol. , vol.161 , pp. 4777
    • Wilson, N.A.1    Wolf, P.2    Ploegh, H.3    Ignatowicz, L.4    Kappler, J.5    Marrack, P.6
  • 70
    • 0029923412 scopus 로고    scopus 로고
    • An insulin peptide that binds an alternative site in class II major histocompatibility complex
    • Tompkins, S. M., Moore, J. C. and Jensen, P. E. 1996. An insulin peptide that binds an alternative site in class II major histocompatibility complex. J. Exp. Med. 183:857.
    • (1996) J. Exp. Med. , vol.183 , pp. 857
    • Tompkins, S.M.1    Moore, J.C.2    Jensen, P.E.3


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