메뉴 건너뛰기




Volumn 164, Issue 2, 2000, Pages 861-871

Contribution of individual amino acids within MHC molecule or antigenic peptide to TCR ligand potency

Author keywords

[No Author keywords available]

Indexed keywords

MAJOR HISTOCOMPATIBILITY ANTIGEN; MYELIN BASIC PROTEIN; PEPTIDE DERIVATIVE; T LYMPHOCYTE RECEPTOR;

EID: 0034650437     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: 10.4049/jimmunol.164.2.861     Document Type: Article
Times cited : (62)

References (55)
  • 1
    • 0029966057 scopus 로고    scopus 로고
    • Essential flexibility in the t cell recognition of antigen
    • Kersh, G. J., and P. M. Allen. 1996. Essential flexibility in the T cell recognition of antigen. Nature 380:495.
    • (1996) Nature , vol.380 , pp. 495
    • Kersh, G.J.1    Allen, P.M.2
  • 2
    • 0031966527 scopus 로고    scopus 로고
    • Probing degeneracy in T cell antigen recognition by combinatorial peptide libraries
    • Hemmer, B., M. Vergelli, C. Pinilla, R. Houghten, and R. Martin. 1998. Probing degeneracy in T cell antigen recognition by combinatorial peptide libraries. Immunol. Today 19:163.
    • (1998) Immunol. Today , vol.19 , pp. 163
    • Hemmer, B.1    Vergelli, M.2    Pinilla, C.3    Houghten, R.4    Martin, R.5
  • 3
    • 0030058657 scopus 로고    scopus 로고
    • The repertoire of T cells shaped by a single MHC/peptide ligand
    • Ignatowicz, L., J. Kappler, and P. Marrack. 1996. The repertoire of T cells shaped by a single MHC/peptide ligand. Cell 84:521.
    • (1996) Cell , vol.84 , pp. 521
    • Ignatowicz, L.1    Kappler, J.2    Marrack, P.3
  • 4
    • 0030775139 scopus 로고    scopus 로고
    • Peripheral T cell survival requires continual ligation of the t cell receptor to major histocompatibility complex-encoded molecules
    • Kirberg, J., A. Berns, and H. von Boehmer. 1997. Peripheral T cell survival requires continual ligation of the T cell receptor to major histocompatibility complex-encoded molecules. J. Exp. Med. 186:1269.
    • (1997) J. Exp. Med. , vol.186 , pp. 1269
    • Kirberg, J.1    Berns, A.2    Von Boehmer, H.3
  • 6
    • 0029798722 scopus 로고    scopus 로고
    • New ligands binding to the human leukocyte antigen class II molecule DRB1*0101 based on the activity pattern of an undecapeptide library
    • Fleckenstein, B., H. Kalbacher, C. P. Muller, D. Stoll, T. Halder, G. Jung, and K. H. Wiesmüller. 1996. New ligands binding to the human leukocyte antigen class II molecule DRB1*0101 based on the activity pattern of an undecapeptide library. Eur. J. Biochem. 240:71.
    • (1996) Eur. J. Biochem. , vol.240 , pp. 71
    • Fleckenstein, B.1    Kalbacher, H.2    Muller, C.P.3    Stoll, D.4    Halder, T.5    Jung, G.6    Wiesmüller, K.H.7
  • 7
    • 0029967743 scopus 로고    scopus 로고
    • Specificity and degeneracy of minor histocompatibility antigen-specific MHC-restricted CTL
    • Gundlach, B. R., K.-H. Wiesmüller, T. Junt, S. Kienle, G. Jung, and P. Walden. 1996. Specificity and degeneracy of minor histocompatibility antigen-specific MHC-restricted CTL. J. Immunol. 156:3645.
    • (1996) J. Immunol. , vol.156 , pp. 3645
    • Gundlach, B.R.1    Wiesmüller, K.-H.2    Junt, T.3    Kienle, S.4    Jung, G.5    Walden, P.6
  • 8
    • 0029005514 scopus 로고
    • Decrypting the structure of major histocompatibility complex class I-restricted cytotoxic T lymphocyte epitopes with complex peptide libraries
    • Udaka, K., K.-H. Wiesmüller, S. Kienle, G. Jung, and P. Walden. 1995. Decrypting the structure of major histocompatibility complex class I-restricted cytotoxic T lymphocyte epitopes with complex peptide libraries. J. Exp. Med. 181:2097.
    • (1995) J. Exp. Med. , vol.181 , pp. 2097
    • Udaka, K.1    Wiesmüller, K.-H.2    Kienle, S.3    Jung, G.4    Walden, P.5
  • 9
    • 0030018874 scopus 로고    scopus 로고
    • Use of combinatorial libraries to construct functional mimics of tumor epitopes recognized by MHC class I-restricted cytolytic T lymphocytes
    • Blake, J., J. V. Johnston, K. E. Hellström, H. Marquardt, and L. Chen. 1996. Use of combinatorial libraries to construct functional mimics of tumor epitopes recognized by MHC class I-restricted cytolytic T lymphocytes. J. Exp. Med. 184: 121.
    • (1996) J. Exp. Med. , vol.184 , pp. 121
    • Blake, J.1    Johnston, J.V.2    Hellström, K.E.3    Marquardt, H.4    Chen, L.5
  • 10
    • 0029902364 scopus 로고    scopus 로고
    • Self-MHC-restricted peptides recognized by alloreactive T lymphocyte clone
    • Udaka, K., K.-H. Wiesmüller, S. Kienle, G. Jung, and P. Walden. 1996. Self-MHC-restricted peptides recognized by alloreactive T lymphocyte clone. J. Immunol. 157:670.
    • (1996) J. Immunol. , vol.157 , pp. 670
    • Udaka, K.1    Wiesmüller, K.-H.2    Kienle, S.3    Jung, G.4    Walden, P.5
  • 11
    • 0030925578 scopus 로고    scopus 로고
    • Identification of high potency microbial and self ligands for a human autoreactive class II restricted T cell clone
    • Hemmer, B., B. Fleckenstein, M. Vergelli, G. Jung, H. McFarland, R. Martin, and K. H. Wiesmueller. 1997. Identification of high potency microbial and self ligands for a human autoreactive class II restricted T cell clone. J. Exp. Med. 185:1651.
    • (1997) J. Exp. Med. , vol.185 , pp. 1651
    • Hemmer, B.1    Fleckenstein, B.2    Vergelli, M.3    Jung, G.4    McFarland, H.5    Martin, R.6    Wiesmueller, K.H.7
  • 13
    • 0032433430 scopus 로고    scopus 로고
    • The use of soluble synthetic peptide combinatorial libraries to determine antigen recognition of T cells
    • Hemmer, B., C. Pinilla, J. Appel, J. Pascal, R. Houghten, and R. Martin. 1998. The use of soluble synthetic peptide combinatorial libraries to determine antigen recognition of T cells. J. Pept. Res. 52:338.
    • (1998) J. Pept. Res. , vol.52 , pp. 338
    • Hemmer, B.1    Pinilla, C.2    Appel, J.3    Pascal, J.4    Houghten, R.5    Martin, R.6
  • 16
    • 0027052983 scopus 로고
    • Rapid identification of high affinity peptide ligands using positional scanning synthetic peptide combinatorial libraries
    • Pinilla, C., J. R. Appel, P. Blanc, and R. A. Houghten. 1992. Rapid identification of high affinity peptide ligands using positional scanning synthetic peptide combinatorial libraries. BioTechniques 13:901.
    • (1992) Biotechniques , vol.13 , pp. 901
    • Pinilla, C.1    Appel, J.R.2    Blanc, P.3    Houghten, R.A.4
  • 17
    • 0028067551 scopus 로고
    • Investigation of antigen-antibody interactions using a soluble nonsupport-bound synthetic decapeptide library composed of four trillion sequences
    • Pinilla, C., J. R. Appel, and R. A. Houghten. 1994. Investigation of antigen-antibody interactions using a soluble nonsupport-bound synthetic decapeptide library composed of four trillion sequences. Biochem. J. 301:847.
    • (1994) Biochem. J. , vol.301 , pp. 847
    • Pinilla, C.1    Appel, J.R.2    Houghten, R.A.3
  • 18
    • 0000478940 scopus 로고
    • General method for the rapid solid-phase synthesis of large numbers of peptides: Specificity of antigen-antibody interaction at the level of individual ammo acids
    • Houghten, R. A. 1985. General method for the rapid solid-phase synthesis of large numbers of peptides: specificity of antigen-antibody interaction at the level of individual ammo acids. Proc. Natl. Acad. Sci. USA 82:847.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 847
    • Houghten, R.A.1
  • 19
    • 0028172455 scopus 로고
    • Peptide libraries: Determination of relative reaction rales of protected amino acids in competitive couplings
    • Ostresh, J. M., J. H. Winkle, V. T. Hamashin, and R. A. Houghten. 1994. Peptide libraries: Determination of relative reaction rales of protected amino acids in competitive couplings. Biopolymers 34:1681.
    • (1994) Biopolymers , vol.34 , pp. 1681
    • Ostresh, J.M.1    Winkle, J.H.2    Hamashin, V.T.3    Houghten, R.A.4
  • 20
    • 0026419319 scopus 로고
    • Generation and use of synthetic peptide combinatorial libraries for basic research and drug discovery
    • Houghten, R. A., C. Pinilla, S. E. Blondelle, J. R. Appel, C. T. Dooley, and J. H. Cuervo. 1991. Generation and use of synthetic peptide combinatorial libraries for basic research and drug discovery. Nature 354:84.
    • (1991) Nature , vol.354 , pp. 84
    • Houghten, R.A.1    Pinilla, C.2    Blondelle, S.E.3    Appel, J.R.4    Dooley, C.T.5    Cuervo, J.H.6
  • 21
    • 0344650195 scopus 로고
    • Isolation, primary structure, and synthesis of human hypothalamic somatocrinin: Growth hormone-releasing factor
    • Ling, N., F. Esch, P. Böhlen, P. Brazeau, W. B. Wehrenberg, and R. Guillemin. 1984. Isolation, primary structure, and synthesis of human hypothalamic somatocrinin: growth hormone-releasing factor. Proc. Natl. Acad. Sci. USA 81:4302.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 4302
    • Ling, N.1    Esch, F.2    Böhlen, P.3    Brazeau, P.4    Wehrenberg, W.B.5    Guillemin, R.6
  • 23
    • 0029586024 scopus 로고
    • Fine chemical modilications at N- and C-termini enhance peptide presentation to T cells by increasing the life span of both free and MHC-complexed peptides
    • Maillere, B., G. Mourier, M. Herve, and A. Menez. 1995. Fine chemical modilications at N- and C-termini enhance peptide presentation to T cells by increasing the life span of both free and MHC-complexed peptides. Mol. Immunol. 32:1377.
    • (1995) Mol. Immunol. , vol.32 , pp. 1377
    • Maillere, B.1    Mourier, G.2    Herve, M.3    Menez, A.4
  • 24
    • 0032521903 scopus 로고    scopus 로고
    • Cutting edge: Predictable TCR antigen recognition based on peptide scans leads to the identification of agonist ligands with no sequence homology
    • Hemmer, B., M. Vergelli, B. Gran, N. Ling, C. Pinilla, R. Houghten, P. Conlon, H. F. McFarland, and R. Martin. 1998. Cutting edge: predictable TCR antigen recognition based on peptide scans leads to the identification of agonist ligands with no sequence homology. J. Immunol. 160:3631.
    • (1998) J. Immunol. , vol.160 , pp. 3631
    • Hemmer, B.1    Vergelli, M.2    Gran, B.3    Ling, N.4    Pinilla, C.5    Houghten, R.6    Conlon, P.7    McFarland, H.F.8    Martin, R.9
  • 26
    • 0028120895 scopus 로고
    • Structural requirements for binding of an immunodominant myelin basic protein peptide to DR2 isotypes and for its recognition by human T cell clones
    • Wucherpfennig, K. W., A. Sette, S. Southwood, C. Oseroff, M. Matsui, J. L. Strominger, and D. A. Hafler. 1994. Structural requirements for binding of an immunodominant myelin basic protein peptide to DR2 isotypes and for its recognition by human T cell clones. J. Exp. Med. 179:279.
    • (1994) J. Exp. Med. , vol.179 , pp. 279
    • Wucherpfennig, K.W.1    Sette, A.2    Southwood, S.3    Oseroff, C.4    Matsui, M.5    Strominger, J.L.6    Hafler, D.A.7
  • 27
    • 0027389119 scopus 로고
    • Binding of myelin basic protein peptides to human histocompatibility leukocyte antigen class II molecules and their recognition by T cells from multiple sclerosis patients
    • Valli, A., A. Sette, L. Kappos, C. Oseroff, J. Sidney, G. Miescher, M. Hochberger, E. D. Albert, and L. Adorini. 1993. Binding of myelin basic protein peptides to human histocompatibility leukocyte antigen class II molecules and their recognition by T cells from multiple sclerosis patients. J. Clin. Invest. 91:616.
    • (1993) J. Clin. Invest. , vol.91 , pp. 616
    • Valli, A.1    Sette, A.2    Kappos, L.3    Oseroff, C.4    Sidney, J.5    Miescher, G.6    Hochberger, M.7    Albert, E.D.8    Adorini, L.9
  • 28
    • 0028902752 scopus 로고
    • ζ phosphorylation without ZAP-70 activation induced by TCR antagonists or partial agonists
    • Madrenas, J., R. L. Wange, J. L. Wang, N. Isakov, L. Samelson, and R. N. Germain. 1995. ζ Phosphorylation without ZAP-70 activation induced by TCR antagonists or partial agonists. Science 167:515.
    • (1995) Science , vol.167 , pp. 515
    • Madrenas, J.1    Wange, R.L.2    Wang, J.L.3    Isakov, N.4    Samelson, L.5    Germain, R.N.6
  • 30
    • 0031569454 scopus 로고    scopus 로고
    • Modifications of peptide ligands enhancing T cell responsiveness imply large numbers of stimulatory ligands for autoreactive T cells
    • Vergelli, M., B. Hemmer, M. Kalbus, A. Vogt, N. Ling, P. Conlon, J. E. Coligan, H. F. McFarland, and R. Martin. 1997. Modifications of peptide ligands enhancing T cell responsiveness imply large numbers of stimulatory ligands for autoreactive T cells. J. Immunol. 158:3746.
    • (1997) J. Immunol. , vol.158 , pp. 3746
    • Vergelli, M.1    Hemmer, B.2    Kalbus, M.3    Vogt, A.4    Ling, N.5    Conlon, P.6    Coligan, J.E.7    McFarland, H.F.8    Martin, R.9
  • 31
    • 0028913816 scopus 로고
    • Ligands for the T-cell receptor: Hard times for avidity models
    • Janeway, C. A. 1995. Ligands for the T-cell receptor: hard times for avidity models. Immunol. Today 16:223.
    • (1995) Immunol. Today , vol.16 , pp. 223
    • Janeway, C.A.1
  • 32
    • 0028988331 scopus 로고
    • T cell receptor antagonists and partial agonists
    • Jameson, S. C., and M. J. Bevan. 1995. T cell receptor antagonists and partial agonists. Immunity 2:1.
    • (1995) Immunity , vol.2 , pp. 1
    • Jameson, S.C.1    Bevan, M.J.2
  • 33
    • 0029933309 scopus 로고    scopus 로고
    • Altered peptide ligand-induced partial T cell activation: Molecular mechanisms and role in T cell biology
    • Sloan-Lancaster, J., and P. M. Allen. 1996. Altered peptide ligand-induced partial T cell activation: molecular mechanisms and role in T cell biology. Annu. Rev. Immunol. 14:1.
    • (1996) Annu. Rev. Immunol. , vol.14 , pp. 1
    • Sloan-Lancaster, J.1    Allen, P.M.2
  • 35
    • 0032171644 scopus 로고    scopus 로고
    • A very high level of crossreactivity is an essential feature of the T-cell receptor
    • Mason, D. 1998. A very high level of crossreactivity is an essential feature of the T-cell receptor. Immunol. Today 19:395.
    • (1998) Immunol. Today , vol.19 , pp. 395
    • Mason, D.1
  • 36
    • 0032438551 scopus 로고    scopus 로고
    • High- and low-potency ligands with similar affinities for the TCR: The importance of kinetics in TCR signaling
    • Kersh, G. J., E. N. Kersh, D. H. Fremont, and P. M. Allen. 1998. High- and low-potency ligands with similar affinities for the TCR: the importance of kinetics in TCR signaling. Immunity 9:817.
    • (1998) Immunity , vol.9 , pp. 817
    • Kersh, G.J.1    Kersh, E.N.2    Fremont, D.H.3    Allen, P.M.4
  • 38
    • 0003104975 scopus 로고    scopus 로고
    • A TCR binds to antagonist ligands with lower affinities and faster dissociation rates than agonists
    • Lyons, D. S., S. A. Lieberman, J. Hampl, J. J. Boniface, Y.-h. Chien, L. I. Berg, and M. M. Davis. 1996. A TCR binds to antagonist ligands with lower affinities and faster dissociation rates than 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.-H.5    Berg, L.I.6    Davis, M.M.7
  • 39
    • 0028872616 scopus 로고
    • Development and selection of T cells: Facts and puzzles
    • Kisielow, P., and H. von Boehmer. 1995 Development and selection of T cells: facts and puzzles. Adv. Immunol. 58:87.
    • (1995) Adv. Immunol. , vol.58 , pp. 87
    • Kisielow, P.1    Von Boehmer, H.2
  • 41
    • 0030873556 scopus 로고    scopus 로고
    • Differential requirements for survival and proliferation of CD8 naive or memory T cells
    • Tanchot, C.,F. A. Lemonnier, B. Perarnau, A. A. Freitas, and B. Rocha. 1997. Differential requirements for survival and proliferation of CD8 naive or memory T cells. Science 276:2057.
    • (1997) Science , vol.276 , pp. 2057
    • Tanchot, C.1    Lemonnier, F.A.2    Perarnau, B.3    Freitas, A.A.4    Rocha, B.5
  • 42
    • 0032549142 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. 199S. Structural basis of plasticity in T cell receptor recognition of a self peptide-MHC antigen. Science 279:1166.
    • (1995) 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
  • 44
    • 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    U, U.4    Biddison, W.E.5    Wiley, D.C.6
  • 45
    • 0030589221 scopus 로고    scopus 로고
    • Assembly, specific binding, and crystallization of a human TCR-αβ with an antigenic Tax peptide from human T lymphotropic virus type 1 and the class I MHC molecule HLA-A2
    • Garboczi, D. N., U. U., P. Ghosh, A. Seth, J. Kim, E. A. VanTienhoven, W. E. Biddison, and D. C. Wiley. 1996. Assembly, specific binding, and crystallization of a human TCR-αβ with an antigenic Tax peptide from human T lymphotropic virus type 1 and the class I MHC molecule HLA-A2. J. Immunol. 157:5403.
    • (1996) J. Immunol. , vol.157 , pp. 5403
    • Garboczi, D.N.1    U, U.2    Ghosh, P.3    Seth, A.4    Kim, J.5    VanTienhoven, E.A.6    Biddison, W.E.7    Wiley, D.C.8
  • 47
    • 0030989505 scopus 로고    scopus 로고
    • Peptide-independent recognition by alloreactive cytotoxic T lymphocytes (CTL)
    • Smith, P. A., A. Brunmark, M. R. Jackson, and T. A. Potter. 1997. Peptide-independent recognition by alloreactive cytotoxic T lymphocytes (CTL). J. Exp. Med. 185:1023.
    • (1997) J. Exp. Med. , vol.185 , pp. 1023
    • Smith, P.A.1    Brunmark, A.2    Jackson, M.R.3    Potter, T.A.4
  • 48
    • 0344026273 scopus 로고    scopus 로고
    • + T cell specificity and compensates for loss of T cell receptor contacts with the specific peptide
    • + T cell specificity and compensates for loss of T cell receptor contacts with the specific peptide. J. Exp. Med. 189:883.
    • (1999) J. Exp. Med. , vol.189 , pp. 883
    • Sandberg, J.K.1    Karre, K.2    Glas, R.3
  • 49
    • 0030935007 scopus 로고    scopus 로고
    • The MHC reactivity of the t cell repertoire prior to positive and negative selection
    • Zerrahn, J., W. Held, and D. H. Raulet. 1997. The MHC reactivity of the T cell repertoire prior to positive and negative selection. Cell 88:627.
    • (1997) Cell , vol.88 , pp. 627
    • Zerrahn, J.1    Held, W.2    Raulet, D.H.3
  • 50
    • 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
  • 51
    • 0030465410 scopus 로고    scopus 로고
    • Complementary mutations in an antigenic peptide allow for crossreactivity of autoreactive T-cell clones
    • Ausubel, L. J., C. K. Kwan, A. Sette, V. Kuchroo, and D. A. Hafler. 1996. Complementary mutations in an antigenic peptide allow for crossreactivity of autoreactive T-cell clones. Proc. Natl. Acad. Sci. USA 93:15317.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 15317
    • Ausubel, L.J.1    Kwan, C.K.2    Sette, A.3    Kuchroo, V.4    Hafler, D.A.5
  • 52
    • 0032212310 scopus 로고    scopus 로고
    • The importance of pairwise interactions between peptide residues in the delineation of TCR specificity
    • Leggatt, G. R., A. Hosmalin, C. D. Pendleton, A. Kumar, S. Hoffman, and J. A. Berzofsky. 1998. The importance of pairwise interactions between peptide residues in the delineation of TCR specificity. J. Immunol. 161:4728.
    • (1998) J. Immunol. , vol.161 , pp. 4728
    • Leggatt, G.R.1    Hosmalin, A.2    Pendleton, C.D.3    Kumar, A.4    Hoffman, S.5    Berzofsky, J.A.6
  • 53
    • 0029377109 scopus 로고
    • Elucidation of monoclonal antibody polyspecificity using a synthetic combinatorial library
    • Pinilla, C., S. Chendra, J. R. Appel, and R. A. Houghten. 1995 Elucidation of monoclonal antibody polyspecificity using a synthetic combinatorial library. Pept. Res. 8:250.
    • (1995) Pept. Res. , vol.8 , pp. 250
    • Pinilla, C.1    Chendra, S.2    Appel, J.R.3    Houghten, R.A.4
  • 54
    • 0030184108 scopus 로고    scopus 로고
    • Highly specific, cross-reactive sequences recognized by an anti-HBsAg antibody identified from a positional scanning synthetic combinatorial library
    • Appel, J. R., S. Muller, N. Benkirane, R. A. Houghten, and C. Pinilla. 1996. Highly specific, cross-reactive sequences recognized by an anti-HBsAg antibody identified from a positional scanning synthetic combinatorial library. Pept. Res. 9:174.
    • (1996) Pept. Res. , vol.9 , pp. 174
    • Appel, J.R.1    Muller, S.2    Benkirane, N.3    Houghten, R.A.4    Pinilla, C.5
  • 55
    • 0027505094 scopus 로고
    • Degenerate-recognition of a dissimilar antigenic peptide by mylein-basic protein-reactive T cells
    • Bhardwaj, V., V. Kumar, H. M. Geysen, and E. B. Sercarz. 1993. Degenerate-recognition of a dissimilar antigenic peptide by mylein-basic protein-reactive T cells. J. Immunol. 151:5000.
    • (1993) J. Immunol. , vol.151 , pp. 5000
    • Bhardwaj, V.1    Kumar, V.2    Geysen, H.M.3    Sercarz, E.B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.