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Volumn 10, Issue 6, 1998, Pages 833-845

Co-stimulation of T cells with CD2 augments TCR-CD3-mediated activation of protein tyrosine kinase p72(syk), resulting in increased tyrosine phosphorylation of adapter proteins, Shc and Cbl

Author keywords

Adapter protein; CD2; Cellular activation; Co stimulatory molecules; Protein kinase; Signal transduction; T lymphocytes; TCR

Indexed keywords

ADAPTOR PROTEIN; CD2 ANTIGEN; CD3 ANTIGEN; INTERLEUKIN 2; MYELIN BASIC PROTEIN; PHYTOHEMAGGLUTININ; PROTEIN TYROSINE KINASE; T LYMPHOCYTE RECEPTOR;

EID: 0031864501     PISSN: 09538178     EISSN: None     Source Type: Journal    
DOI: 10.1093/intimm/10.6.833     Document Type: Article
Times cited : (24)

References (68)
  • 2
    • 0024721339 scopus 로고
    • Immunogenicity signals 1,2,3... and 0
    • Janeway, C. 1989. Immunogenicity signals 1,2,3... and 0. Immunol. Today 10:283.
    • (1989) Immunol. Today , vol.10 , pp. 283
    • Janeway, C.1
  • 4
    • 0025836514 scopus 로고
    • Roles of multiple accessory molecules in T-cell activation
    • Van Seventer, G. A., Shimizu, Y. and Shaw, S. 1991. Roles of multiple accessory molecules in T-cell activation. Curr. Opin. Immunol. 3:294.
    • (1991) Curr. Opin. Immunol. , vol.3 , pp. 294
    • Van Seventer, G.A.1    Shimizu, Y.2    Shaw, S.3
  • 5
    • 0023120574 scopus 로고
    • Alternative pathway activation of T cells by binding of CD2 to its cell-surface ligand
    • Hunig, T., Tiefenthaler, K. H., Buschenfelde, M. and Meuer, S. C. 1987. Alternative pathway activation of T cells by binding of CD2 to its cell-surface ligand. Nature 326:298.
    • (1987) Nature , vol.326 , pp. 298
    • Hunig, T.1    Tiefenthaler, K.H.2    Buschenfelde, M.3    Meuer, S.C.4
  • 6
    • 0025044576 scopus 로고
    • CD2 and CD3 TCR T-cell activation pathways function independently?
    • Kabelit, D. 1990. CD2 and CD3 TCR T-cell activation pathways function independently? Immunol. Today 11:44.
    • (1990) Immunol. Today , vol.11 , pp. 44
    • Kabelit, D.1
  • 7
    • 0025339511 scopus 로고
    • A cell culture model for T lymphocyte clonal anergy
    • Schwartz, R. H. 1990. A cell culture model for T lymphocyte clonal anergy. Science 248:1349.
    • (1990) Science , vol.248 , pp. 1349
    • Schwartz, R.H.1
  • 10
    • 0029930984 scopus 로고    scopus 로고
    • The structure and ligand interactions of CD2: Implications for T-cell function
    • Davis, S. J. and van der Merwe, P. A. 1996. The structure and ligand interactions of CD2: implications for T-cell function. Immunol. Today 17:177.
    • (1996) Immunol. Today , vol.17 , pp. 177
    • Davis, S.J.1    Van Der Merwe, P.A.2
  • 13
    • 0025337880 scopus 로고
    • Association of CD2 and CD45 on human T lymphocytes
    • Schraven, B., Samstag, Y. and Altevogt, P. 1990. Association of CD2 and CD45 on human T lymphocytes. Nature 345:71.
    • (1990) Nature , vol.345 , pp. 71
    • Schraven, B.1    Samstag, Y.2    Altevogt, P.3
  • 14
    • 0026590085 scopus 로고
    • CD2/LFA-3 ligation induces phospholipase Cγ1 tyrosine phosphorylation and regulates CD3 signaling
    • Kanner, S. B., Damle, N. K., Blake, J., Aruffo, A. and Ledbetter, J. A. 1992. CD2/LFA-3 ligation induces phospholipase Cγ1 tyrosine phosphorylation and regulates CD3 signaling. J. Immunol. 148:2023.
    • (1992) J. Immunol. , vol.148 , pp. 2023
    • Kanner, S.B.1    Damle, N.K.2    Blake, J.3    Aruffo, A.4    Ledbetter, J.A.5
  • 16
    • 0028014460 scopus 로고
    • Signal transduction by lymphocyte antigen receptors
    • Weiss, A. and Littman, D. R. 1994. Signal transduction by lymphocyte antigen receptors. Cell 76:263.
    • (1994) Cell , vol.76 , pp. 263
    • Weiss, A.1    Littman, D.R.2
  • 17
    • 0028209548 scopus 로고
    • Sequential interactions of the TCR with two distinct cytoplasmic tyrosine kinases
    • Iwashima, M., Irving, B. A., van Oers, N. S. C., Chan, A. C. and Weiss, A. 1993. Sequential interactions of the TCR with two distinct cytoplasmic tyrosine kinases. Science 263:1136.
    • (1993) Science , vol.263 , pp. 1136
    • Iwashima, M.1    Irving, B.A.2    Van Oers, N.S.C.3    Chan, A.C.4    Weiss, A.5
  • 18
    • 0027328526 scopus 로고
    • Tandem SH2 domains of ZAP-70 bind to T cell antigen receptor zeta and CD3 epsilon from activated Jurkat T cells
    • Wange, R. L., Malek, S. N., Desiderio, S. and Samelson, L. E. 1993. Tandem SH2 domains of ZAP-70 bind to T cell antigen receptor zeta and CD3 epsilon from activated Jurkat T cells. J. Biol. Chem. 268:19797.
    • (1993) J. Biol. Chem. , vol.268 , pp. 19797
    • Wange, R.L.1    Malek, S.N.2    Desiderio, S.3    Samelson, L.E.4
  • 19
    • 0028288927 scopus 로고
    • The role of protein tyrosine kinases and protein tyrosine phosphatases in T cell antigen receptor signal transduction
    • Chan, A. C., Desai, D. M. and Weiss, A. 1994. The role of protein tyrosine kinases and protein tyrosine phosphatases in T cell antigen receptor signal transduction. Annu. Rev. Immunol. 12:555.
    • (1994) Annu. Rev. Immunol. , vol.12 , pp. 555
    • Chan, A.C.1    Desai, D.M.2    Weiss, A.3
  • 21
    • 0028216232 scopus 로고
    • Differential expression of ZAP-70 and Syk protein tyrosine kinases, and the role of this family of protein kinases in TCR signaling
    • Chan, A. C., van Oers, N. S. C., Tran, A., Turka, L., Law, C.-L., Ryan, J. C., Clark, E. A. and Weiss, A. 1994. Differential expression of ZAP-70 and Syk protein tyrosine kinases, and the role of this family of protein kinases in TCR signaling. J. Immunol. 152:4758.
    • (1994) J. Immunol. , vol.152 , pp. 4758
    • Chan, A.C.1    Van Oers, N.S.C.2    Tran, A.3    Turka, L.4    Law, C.-L.5    Ryan, J.C.6    Clark, E.A.7    Weiss, A.8
  • 24
    • 0030795305 scopus 로고    scopus 로고
    • Regulation of T-cell antigen receptor signaling by Syk tyrosine protein kinase
    • Latour, S., Fournel, M. and veillette, A. 1997. Regulation of T-cell antigen receptor signaling by Syk tyrosine protein kinase. Mol. Cell. Biol. 17:4434.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 4434
    • Latour, S.1    Fournel, M.2    Veillette, A.3
  • 25
    • 0028596158 scopus 로고
    • An alternative to SH2 domains for binding tyrosine-phosphorylated proteins
    • Kavanaugh, M. W. and Williams, L. T. 1994. An alternative to SH2 domains for binding tyrosine-phosphorylated proteins. Science 266:1862.
    • (1994) Science , vol.266 , pp. 1862
    • Kavanaugh, M.W.1    Williams, L.T.2
  • 26
    • 0028859279 scopus 로고
    • Protein modules and signaling networks
    • Pawson, T. 1995. Protein modules and signaling networks. Nature 373:573.
    • (1995) Nature , vol.373 , pp. 573
    • Pawson, T.1
  • 28
  • 29
    • 0028027169 scopus 로고
    • The protein product of the c-cbl protooncogene is the 120-kDa tyrosine-phosphorylated protein in Jurkat cells activated via the T cell antigen receptor
    • Donovan, J. A., Wange, R. L., Langdon, W. Y. and Samelson, L. E. 1994. The protein product of the c-cbl protooncogene is the 120-kDa tyrosine-phosphorylated protein in Jurkat cells activated via the T cell antigen receptor. J. Biol. Chem. 269:22921.
    • (1994) J. Biol. Chem. , vol.269 , pp. 22921
    • Donovan, J.A.1    Wange, R.L.2    Langdon, W.Y.3    Samelson, L.E.4
  • 30
    • 0029051695 scopus 로고
    • The SH3 domain-binding T cell tyrosyl phosphoprotein p120. Demonstration of its identity with the c-cbl protooncogene product and in vivo complex with Fyn, Grb2, and phosphatidylinositol 3-kinase
    • Fukazawa, T., Reedquist, K. A., Trub, T., Soltoff, S., Panchamoorthy, G., Druker, B., Cantley, L., Shoelson, S. E. and Band, H. 1995. The SH3 domain-binding T cell tyrosyl phosphoprotein p120. Demonstration of its identity with the c-cbl protooncogene product and in vivo complex with Fyn, Grb2, and phosphatidylinositol 3-kinase. J. Biol. Chem. 270:19141.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19141
    • Fukazawa, T.1    Reedquist, K.A.2    Trub, T.3    Soltoff, S.4    Panchamoorthy, G.5    Druker, B.6    Cantley, L.7    Shoelson, S.E.8    Band, H.9
  • 32
    • 0028932614 scopus 로고
    • The proto-oncogene product c-Cbl becomes tyrosine phosphorylated by stimulation with GM-CSF or Epo and constitutively binds to the SH3 domain of Grb2/Ash in human hematopoietic cells
    • Odai, H., Sasaki, K., Iwamatsu, A., Hanazono, Y., Tanaka, T., Mitani, K., Yazaki, Y. and Hirai, H. 1995. The proto-oncogene product c-Cbl becomes tyrosine phosphorylated by stimulation with GM-CSF or Epo and constitutively binds to the SH3 domain of Grb2/Ash in human hematopoietic cells. J. Biol. Chem. 270:10800.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10800
    • Odai, H.1    Sasaki, K.2    Iwamatsu, A.3    Hanazono, Y.4    Tanaka, T.5    Mitani, K.6    Yazaki, Y.7    Hirai, H.8
  • 33
    • 0028901016 scopus 로고
    • Identification of the major tyrosine kinase substrate in signaling complexes formed after engagement of Fcγreceptors
    • Marcilla, A., Rivero-Lezcano, O. M., Agarwal, A. and Robbins, K. C. 1995. Identification of the major tyrosine kinase substrate in signaling complexes formed after engagement of Fcγreceptors. J. Biol. Chem. 270:9115.
    • (1995) J. Biol. Chem. , vol.270 , pp. 9115
    • Marcilla, A.1    Rivero-Lezcano, O.M.2    Agarwal, A.3    Robbins, K.C.4
  • 34
    • 0027506916 scopus 로고
    • Signal transduction via phosphorylated adhesion molecule, LFA-1β (CD18), is increased by culture of natural killer (NK) cells with interleukin (IL)-2, and distinguishes NK from lymphokine-activated killer cells
    • Umehara, H., Takashima, A., Minami, Y. and Bloom, E. T. 1993. Signal transduction via phosphorylated adhesion molecule, LFA-1β (CD18), is increased by culture of natural killer (NK) cells with interleukin (IL)-2, and distinguishes NK from lymphokine-activated killer cells. Int. Immunol. 5:19.
    • (1993) Int. Immunol. , vol.5 , pp. 19
    • Umehara, H.1    Takashima, A.2    Minami, Y.3    Bloom, E.T.4
  • 36
    • 0028260446 scopus 로고
    • Increased processing of lymphocyte function-associated antigen-1 in human natural killer cells stimulated with IL-2
    • Umehara, H., Minami, Y., Domae, N. and Bloom, E. T. 1994. Increased processing of lymphocyte function-associated antigen-1 in human natural killer cells stimulated with IL-2. Int. Immunol. 6:1071.
    • (1994) Int. Immunol. , vol.6 , pp. 1071
    • Umehara, H.1    Minami, Y.2    Domae, N.3    Bloom, E.T.4
  • 37
    • 0028988329 scopus 로고
    • Protein tyrosine kinase Syk is associated with and activated by the IL-2 receptor: Possible link with the c-myc induction pathway
    • Minami, Y., Nakagawa, Y., Kawahara, A., Miyazaki, T., Sada, K., Yamamura, H. and Taniguchi, T. 1995. Protein tyrosine kinase Syk is associated with and activated by the IL-2 receptor: possible link with the c-myc induction pathway. Immunity 2:89.
    • (1995) Immunity , vol.2 , pp. 89
    • Minami, Y.1    Nakagawa, Y.2    Kawahara, A.3    Miyazaki, T.4    Sada, K.5    Yamamura, H.6    Taniguchi, T.7
  • 40
    • 0027724634 scopus 로고
    • Interaction of Shc with the ζ chain of the T cell receptor upon T cell activation
    • Ravichandran, K. S., Lee, K. K., Songyang, Z., Cantley, L. C., Burn, P. and Burakoff, S. J. 1993. Interaction of Shc with the ζ chain of the T cell receptor upon T cell activation. Science 262:902.
    • (1993) Science , vol.262 , pp. 902
    • Ravichandran, K.S.1    Lee, K.K.2    Songyang, Z.3    Cantley, L.C.4    Burn, P.5    Burakoff, S.J.6
  • 43
    • 0028888152 scopus 로고
    • CD28 co-stimulation up-regulates long-term IL-2Rβ expression in human T cells through combined transcriptional and post-transcriptional regulation
    • Cerdan, C., Martin, Y., Courcoul, M., Mawas, C., Birg, F. and Olive, D. 1995. CD28 co-stimulation up-regulates long-term IL-2Rβ expression in human T cells through combined transcriptional and post-transcriptional regulation. J. Immunol. 154:1007.
    • (1995) J. Immunol. , vol.154 , pp. 1007
    • Cerdan, C.1    Martin, Y.2    Courcoul, M.3    Mawas, C.4    Birg, F.5    Olive, D.6
  • 44
    • 0027330043 scopus 로고
    • The role of NF-κB1 (p50/p105) gene expression in activation of human blood T-lymphocytes via CD2 and CD28 adhesion molecules
    • Costello, R., Cerdan, C., Lipcey, C., Algarte, M., Martin,Y., Baeuerle, P. A., Olive, D. and Imbert, J. 1993. The role of NF-κB1 (p50/p105) gene expression in activation of human blood T-lymphocytes via CD2 and CD28 adhesion molecules. Cell Growth Different. 4:947.
    • (1993) Cell Growth Different , vol.4 , pp. 947
    • Costello, R.1    Cerdan, C.2    Lipcey, C.3    Algarte, M.4    Martin, Y.5    Baeuerle, P.A.6    Olive, D.7    Imbert, J.8
  • 45
    • 0030300143 scopus 로고    scopus 로고
    • The role of CD2 as a regulatory of human T-cell cytokine production
    • Holter, W., Schwarz, M., Cerwenka, A. and Knapp, W. 1996. The role of CD2 as a regulatory of human T-cell cytokine production. Immunol. Rev. 153:107.
    • (1996) Immunol. Rev. , vol.153 , pp. 107
    • Holter, W.1    Schwarz, M.2    Cerwenka, A.3    Knapp, W.4
  • 47
    • 0031568534 scopus 로고    scopus 로고
    • Protein tyrosine kinase Syk and ZAP-70 display distinct requirements for src family kinases in immune response receptor signal transduction
    • Zoller, K. E., MacNeil, I. A. and Brugge, J. S. 1997. Protein tyrosine kinase Syk and ZAP-70 display distinct requirements for src family kinases in immune response receptor signal transduction. J. Immunol. 158:1650.
    • (1997) J. Immunol. , vol.158 , pp. 1650
    • Zoller, K.E.1    MacNeil, I.A.2    Brugge, J.S.3
  • 48
    • 1842403200 scopus 로고
    • The T11 glycoprotein is functionally linked to a calcium channel in precursor and mature T-lineage cells
    • Alcover, A., Weiss, M. J., Daley, J. F. and Reinherz, E. L. 1986. The T11 glycoprotein is functionally linked to a calcium channel in precursor and mature T-lineage cells. Proc. Natl Acad. Sci. USA 83:2614.
    • (1986) Proc. Natl Acad. Sci. USA , vol.83 , pp. 2614
    • Alcover, A.1    Weiss, M.J.2    Daley, J.F.3    Reinherz, E.L.4
  • 49
    • 0023137703 scopus 로고
    • Transmembrane signaling via the T11 dependent pathway of human T cell activation: Evidence for the involvement of 1,2 diacylglycerol and inositol phosphate
    • Pantaleo, G., Olive, D., Poggi, A., Kozumbo, W. J., Moretta, L. and Moretta, A. 1987. Transmembrane signaling via the T11 dependent pathway of human T cell activation: evidence for the involvement of 1,2 diacylglycerol and inositol phosphate. Eur. J. Immunol. 17:55.
    • (1987) Eur. J. Immunol. , vol.17 , pp. 55
    • Pantaleo, G.1    Olive, D.2    Poggi, A.3    Kozumbo, W.J.4    Moretta, L.5    Moretta, A.6
  • 50
    • 0023069478 scopus 로고
    • The lymphocyte function-associated LFA-1, CD2 and LFA-3 molecules: Cell adhesion receptors of the immune system
    • Springer, T. A., Dustin, M. L., Kishimoto, T. K. and Marlin, S. D. 1987. The lymphocyte function-associated LFA-1, CD2 and LFA-3 molecules: cell adhesion receptors of the immune system. Annu. Rev. Immunol. 5:223.
    • (1987) Annu. Rev. Immunol. , vol.5 , pp. 223
    • Springer, T.A.1    Dustin, M.L.2    Kishimoto, T.K.3    Marlin, S.D.4
  • 51
    • 0019435154 scopus 로고
    • Does OKT3 monoclonal antibody react with an antigen-recognition structure on human T cells?
    • Chang, T., Kung, P., Gingras, S. and Goldstein, C. 1981. Does OKT3 monoclonal antibody react with an antigen-recognition structure on human T cells? Proc. Natl Acad. Sci. USA 78:1805.
    • (1981) Proc. Natl Acad. Sci. USA , vol.78 , pp. 1805
    • Chang, T.1    Kung, P.2    Gingras, S.3    Goldstein, C.4
  • 54
    • 0027312272 scopus 로고
    • Guanine-nucleotide-releasing factor hSos 1 binds to Grb2 and links receptor tyrosine kinases to Ras signaling
    • Li, N., Batzer, A., Daly, R., Yajmik, V., Skolnik, E., Chardin, P., BarSagi, D., Margolis, B. and Schlessinger, J. 1993. Guanine-nucleotide-releasing factor hSos 1 binds to Grb2 and links receptor tyrosine kinases to Ras signaling. Nature 363:85.
    • (1993) Nature , vol.363 , pp. 85
    • Li, N.1    Batzer, A.2    Daly, R.3    Yajmik, V.4    Skolnik, E.5    Chardin, P.6    Barsagi, D.7    Margolis, B.8    Schlessinger, J.9
  • 55
    • 0030250114 scopus 로고    scopus 로고
    • Complex complexes: Signaling at the TCR
    • Wange, R. L. and Samelson, L. E. 1996. Complex complexes: signaling at the TCR. Immunity 5:197.
    • (1996) Immunity , vol.5 , pp. 197
    • Wange, R.L.1    Samelson, L.E.2
  • 56
    • 0029876948 scopus 로고    scopus 로고
    • Stimulation through the T cell receptor induces Cbl association with Crk proteins and the guanine nucleotide exchange protein C3G
    • Reedquist, K. A., Fukazawa, T., Panchamoorthy, G., Langdon, W. Y., Shoelson, S. E., Druker, B. J. and Band, H. 1996. Stimulation through the T cell receptor induces Cbl association with Crk proteins and the guanine nucleotide exchange protein C3G. J. Biol. Chem. 271:8435.
    • (1996) J. Biol. Chem. , vol.271 , pp. 8435
    • Reedquist, K.A.1    Fukazawa, T.2    Panchamoorthy, G.3    Langdon, W.Y.4    Shoelson, S.E.5    Druker, B.J.6    Band, H.7
  • 57
    • 0029664998 scopus 로고    scopus 로고
    • Interaction of Cbl with two adapter proteins, Grb2 and Crk, upon T cell activation
    • Buday, L., Khwaja, A., Sipeki, S., Farago, A. and Downward, J. 1996. Interaction of Cbl with two adapter proteins, Grb2 and Crk, upon T cell activation. J. Biol. Chem. 271:6159.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6159
    • Buday, L.1    Khwaja, A.2    Sipeki, S.3    Farago, A.4    Downward, J.5
  • 58
    • 0029655999 scopus 로고    scopus 로고
    • The product of the cbl oncogene forms stable complexes in vivo with endogenous Crk in a tyrosine phosphorylation-dependent manner
    • Ribon, N., Hubbelle, S., Herrera, R. and Saltiel, A. R. 1996. The product of the cbl oncogene forms stable complexes in vivo with endogenous Crk in a tyrosine phosphorylation-dependent manner. Mol. Cell. Biol. 16:45.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 45
    • Ribon, N.1    Hubbelle, S.2    Herrera, R.3    Saltiel, A.R.4
  • 60
    • 0029671073 scopus 로고    scopus 로고
    • cbl is a major substrate of tyrosine phosphorylation upon B cell antigen receptor stimulation and interacts in vivo with Fyn and Syk tyrosine kinases, Grb2 and Shc adaptors, and the p85 subunit of phosphatidylinositol 3-kinase
    • cbl is a major substrate of tyrosine phosphorylation upon B cell antigen receptor stimulation and interacts in vivo with Fyn and Syk tyrosine kinases, Grb2 and Shc adaptors, and the p85 subunit of phosphatidylinositol 3-kinase. J. Biol. Chem. 271:3187.
    • (1996) J. Biol. Chem. , vol.271 , pp. 3187
    • Panchamoorthy, G.1    Fukazawa, T.2    Miyake, S.3    Soltoff, S.4    Reedquist, K.5    Druker, B.6    Schoelson, S.7    Cantley, L.8    Band, H.9
  • 61
    • 0029998597 scopus 로고    scopus 로고
    • Specific association of tyrosine-phosphorylated c-Cbl with Fyn tyrosine kinase in T cells
    • Tsygankov, A. Y., Mahajan, S., Fincke, J. E. and Bolen, J. B. 1996. Specific association of tyrosine-phosphorylated c-Cbl with Fyn tyrosine kinase in T cells. J. Biol. Chem. 271:27130.
    • (1996) J. Biol. Chem. , vol.271 , pp. 27130
    • Tsygankov, A.Y.1    Mahajan, S.2    Fincke, J.E.3    Bolen, J.B.4
  • 62
    • 0029034440 scopus 로고
    • Interactions of Cbl with Grb2 and phosphatidylinositol 3′-kinase in activated Jurkat cells
    • Meisner, H., Conway, B. R., Hartley, D. and Czech, M. P. 1995. Interactions of Cbl with Grb2 and phosphatidylinositol 3′-kinase in activated Jurkat cells. Mol. Cell. Biol. 15:3571.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3571
    • Meisner, H.1    Conway, B.R.2    Hartley, D.3    Czech, M.P.4
  • 63
    • 0027403299 scopus 로고
    • The role of the CD28 receptor during T cell responses to antigen
    • Linsley, P. S. and Ledbetter, J. A. 1993. The role of the CD28 receptor during T cell responses to antigen. Annu. Rev. Immunol. 11:191.
    • (1993) Annu. Rev. Immunol. , vol.11 , pp. 191
    • Linsley, P.S.1    Ledbetter, J.A.2
  • 64
    • 0028182749 scopus 로고
    • Binding of phosphatidylinositol-3-OH kinase to CD28 is required for T-cell signaling
    • Pages, F., Ragueneau, M., Rottapel, R., Truneh, A., Nunes, J., Imbert, J. and Olive, D. 1994. Binding of phosphatidylinositol-3-OH kinase to CD28 is required for T-cell signaling. Nature 369:327.
    • (1994) Nature , vol.369 , pp. 327
    • Pages, F.1    Ragueneau, M.2    Rottapel, R.3    Truneh, A.4    Nunes, J.5    Imbert, J.6    Olive, D.7
  • 65
    • 0028146530 scopus 로고
    • CD28 is associated with and induces the immediate tyrosine phosphorylation and activation of the Tec family kinase ITK/EMT in the human Jurkat leukemic T-cell line
    • August, A., Gibson, S., Kawakami, Y., Kawakami, T., Mills, G. B. and Dupont, B. 1994. CD28 is associated with and induces the immediate tyrosine phosphorylation and activation of the Tec family kinase ITK/EMT in the human Jurkat leukemic T-cell line. Proc. Natl Acad. Sci. USA 91:9347.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 9347
    • August, A.1    Gibson, S.2    Kawakami, Y.3    Kawakami, T.4    Mills, G.B.5    Dupont, B.6
  • 67
    • 0024314938 scopus 로고
    • The CD2 antigen associates with the T-cell antigen receptor CD3 antigen complex on the surface of human T lymphocytes
    • Brown, M. H., Cantrell, D. A., Brattsand, G., Crumpton, M. J. and Gullberg, M. 1989. The CD2 antigen associates with the T-cell antigen receptor CD3 antigen complex on the surface of human T lymphocytes. Nature 339:551.
    • (1989) Nature , vol.339 , pp. 551
    • Brown, M.H.1    Cantrell, D.A.2    Brattsand, G.3    Crumpton, M.J.4    Gullberg, M.5
  • 68
    • 0026598252 scopus 로고
    • Molecular associations between the T-lymphocyte antigen receptor complex and the surface antigens CD2, CD4, or CD8 and CD5
    • Beyers, A. D., Spruyt, L. L. and Williams, A. F. 1992. Molecular associations between the T-lymphocyte antigen receptor complex and the surface antigens CD2, CD4, or CD8 and CD5. Proc. Natl Acad. Sci. USA 89:2945.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 2945
    • Beyers, A.D.1    Spruyt, L.L.2    Williams, A.F.3


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