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Volumn 16, Issue 5, 1996, Pages 2255-2263

Characterization of the roles of SH2 domain-containing proteins in T-lymphocyte activation by using dominant negative SH2 domains

Author keywords

[No Author keywords available]

Indexed keywords

CYTOKINE; HYBRID PROTEIN; PHOSPHOLIPASE C; PHOSPHOTYROSINE; PROTEIN P21; T LYMPHOCYTE RECEPTOR;

EID: 0030002817     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/mcb.16.5.2255     Document Type: Article
Times cited : (30)

References (58)
  • 1
    • 0028269436 scopus 로고
    • Defective T cell receptor signaling and CD8+ thymic selection in humans lacking Zap-70 kinase
    • Arpaia, E., M. Shahar, H. Dadi, A. Cohen, and C. M. Roifman. 1994. Defective T cell receptor signaling and CD8+ thymic selection in humans lacking Zap-70 kinase. Cell 76:947-958.
    • (1994) Cell , vol.76 , pp. 947-958
    • Arpaia, E.1    Shahar, M.2    Dadi, H.3    Cohen, A.4    Roifman, C.M.5
  • 2
    • 0026705289 scopus 로고
    • Interleukin-2 promoter activation in T-cells expressing activated Ha-ras
    • Baldari, C. T., G. Macchia, and J. L. Telford. 1992. Interleukin-2 promoter activation in T-cells expressing activated Ha-ras. J. Biol. Chem. 267:4289-4291
    • (1992) J. Biol. Chem. , vol.267 , pp. 4289-4291
    • Baldari, C.T.1    Macchia, G.2    Telford, J.L.3
  • 3
    • 0028944444 scopus 로고
    • Inhibition of CD4/p561ck signalling by a dominant negative mutant of the Shc adaptor protein
    • Baldari, C. T., G. Pelicci, M. M. Di Somma, E. Milia, S. Giuli, P. G. Pelicci, and J. L. Telford. 1995. Inhibition of CD4/p561ck signalling by a dominant negative mutant of the Shc adaptor protein. Oncogene 10:1141-1147.
    • (1995) Oncogene , vol.10 , pp. 1141-1147
    • Baldari, C.T.1    Pelicci, G.2    Di Somma, M.M.3    Milia, E.4    Giuli, S.5    Pelicci, P.G.6    Telford, J.L.7
  • 4
    • 0028568639 scopus 로고
    • A region in Shc distinct from the SH2 domain can bind tyrosine-phosphorylated growth factor receptors
    • Blaikie, P., D. Immanuel, J. Wu, N. Li, V. Yajnik, and B. Margolis. 1994. A region in Shc distinct from the SH2 domain can bind tyrosine-phosphorylated growth factor receptors. J. Biol. Chem. 269:32031-32034
    • (1994) J. Biol. Chem. , vol.269 , pp. 32031-32034
    • Blaikie, P.1    Immanuel, D.2    Wu, J.3    Li, N.4    Yajnik, V.5    Margolis, B.6
  • 5
    • 0027153103 scopus 로고
    • Epidermal growth factor regulates p21ras through the formation of a complex of receptor, Grb2 adapter protein, and Sos nucleotide exchange factor
    • Buday, L., and J. Downward. 1993. Epidermal growth factor regulates p21ras through the formation of a complex of receptor, Grb2 adapter protein, and Sos nucleotide exchange factor Cell 73:611-620
    • (1993) Cell , vol.73 , pp. 611-620
    • Buday, L.1    Downward, J.2
  • 6
    • 0028245832 scopus 로고
    • A complex of Grb2 adaptor protein. Sos exchange factor, and a 36-kDa membrane-hound tyrosine phosphoprotein is implicated in ras activation in T cells
    • Buday, L., S. E. Egan, P. Rodriguez Viciana, D. A. Cantrell, and J. Downward. 1994 A complex of Grb2 adaptor protein. Sos exchange factor, and a 36-kDa membrane-hound tyrosine phosphoprotein is implicated in ras activation in T cells J Biol. Chem 269:9019-9023.
    • (1994) J Biol. Chem , vol.269 , pp. 9019-9023
    • Buday, L.1    Egan, S.E.2    Rodriguez Viciana, P.3    Cantrell, D.A.4    Downward, J.5
  • 7
    • 0028288927 scopus 로고
    • The role of protein tyrosine kinases and protein tyrosine phosphatases in T cell antigen receptor signal transduction
    • Chan, A. C., D. M. Desai, and A. Weiss. 1994 The role of protein tyrosine kinases and protein tyrosine phosphatases in T cell antigen receptor signal transduction. Annu Rev. Immunol. 12:555-592.
    • (1994) Annu Rev. Immunol. , vol.12 , pp. 555-592
    • Chan, A.C.1    Desai, D.M.2    Weiss, A.3
  • 8
    • 0026483786 scopus 로고
    • ZAP-70: A 70 kd protein-tyrosine kinase that associates with the TCR zeta chain
    • Chan, A. C., M. Iwashima, C. W. Turck, and A. Weiss. 1992 ZAP-70: a 70 kd protein-tyrosine kinase that associates with the TCR zeta chain Cell 71: 649-662.
    • (1992) Cell , vol.71 , pp. 649-662
    • Chan, A.C.1    Iwashima, M.2    Turck, C.W.3    Weiss, A.4
  • 10
    • 0028216232 scopus 로고
    • Differential expression of ZAP-70 and Syk protein tyrosine kinases, and the role of this family of protein tyrosine kinases in TCR signaling
    • Chan, A. C., N. S. van Oers, A. Tran, L. Turka, C. L. Law, J. C. Ryan, E. A. Clark, and A. Weiss. 1994. Differential expression of ZAP-70 and Syk protein tyrosine kinases, and the role of this family of protein tyrosine kinases in TCR signaling J. Immunol. 152:4758-4766.
    • (1994) J. Immunol. , vol.152 , pp. 4758-4766
    • Chan, A.C.1    Van Oers, N.S.2    Tran, A.3    Turka, L.4    Law, C.L.5    Ryan, J.C.6    Clark, E.A.7    Weiss, A.8
  • 12
    • 0026643141 scopus 로고
    • Identification of calcineurin as a key signalling enzyme in T-lymphocyte activation
    • Clipstone, N. A., and G. R. Crabtree. 1992. Identification of calcineurin as a key signalling enzyme in T-lymphocyte activation Nature 357:695-697.
    • (1992) Nature , vol.357 , pp. 695-697
    • Clipstone, N.A.1    Crabtree, G.R.2
  • 13
    • 0027456990 scopus 로고
    • In vivo binding properties of SH2 domains from GTPase-activating protein and phosphatidylinositol 3-kinase
    • Cooper, J. A., and A. Kashishian. 1993. In vivo binding properties of SH2 domains from GTPase-activating protein and phosphatidylinositol 3-kinase Mol. Cell. Biol. 13:1737-1745.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 1737-1745
    • Cooper, J.A.1    Kashishian, A.2
  • 16
    • 0027910431 scopus 로고
    • Association of Sos Ras exchange protein with Grb2 is implicated in tyrosine kinase signal transduction and transformation
    • Egan, S. E., B. W. Giddings, M. W. Brooks, L. Buday, A. M. Sizeland, and R. A. Weinberg. 1993. Association of Sos Ras exchange protein with Grb2 is implicated in tyrosine kinase signal transduction and transformation Nature 363:45-51.
    • (1993) Nature , vol.363 , pp. 45-51
    • Egan, S.E.1    Giddings, B.W.2    Brooks, M.W.3    Buday, L.4    Sizeland, A.M.5    Weinberg, R.A.6
  • 17
    • 0028292001 scopus 로고
    • Human severe combined immunodeficiency due to a defect in ZAP-70, a T cell tyrosine kinase
    • Elder, M. E., D. Lin, J. Clever, A. C. Chan, T. J. Hope, A. Weiss, and T. G. Parslow. 1994. Human severe combined immunodeficiency due to a defect in ZAP-70, a T cell tyrosine kinase. Science 264:1596-1599.
    • (1994) Science , vol.264 , pp. 1596-1599
    • Elder, M.E.1    Lin, D.2    Clever, J.3    Chan, A.C.4    Hope, T.J.5    Weiss, A.6    Parslow, T.G.7
  • 18
    • 0028904413 scopus 로고
    • Defective T-cell receptor signalling and positive selection of Vav-deficient CD4+ CD8+ thymocytes
    • Fischer, K.-D., A. Zmuidzinas, S. Gardner, M. Barbacid, A. Bernstein, and C. Guidos. 1995. Defective T-cell receptor signalling and positive selection of Vav-deficient CD4+ CD8+ thymocytes. Nature 374:474-477.
    • (1995) Nature , vol.374 , pp. 474-477
    • Fischer, K.-D.1    Zmuidzinas, A.2    Gardner, S.3    Barbacid, M.4    Bernstein, A.5    Guidos, C.6
  • 19
    • 0027229556 scopus 로고
    • Grb2 mediates the EGF-dependent activation of guanine nucleotide exchange on Ras
    • Gale, N. W., S. Kaplan, E. J. Lowenstein, J. Schlessinger, and D. Bar-Sagi. 1993. Grb2 mediates the EGF-dependent activation of guanine nucleotide exchange on Ras Nature 363:88-92
    • (1993) Nature , vol.363 , pp. 88-92
    • Gale, N.W.1    Kaplan, S.2    Lowenstein, E.J.3    Schlessinger, J.4    Bar-Sagi, D.5
  • 20
    • 0027207287 scopus 로고
    • Tyrosine kinase-stimulated guanine nucleotide exchange activity of Vav in T cell activation
    • Gulbins, E., K. M. Coggeshall, G. Baier, S. Katzav, P. Burn, and A. Altman. 1993. Tyrosine kinase-stimulated guanine nucleotide exchange activity of Vav in T cell activation. Science 260:822-825.
    • (1993) Science , vol.260 , pp. 822-825
    • Gulbins, E.1    Coggeshall, K.M.2    Baier, G.3    Katzav, S.4    Burn, P.5    Altman, A.6
  • 21
    • 0026611481 scopus 로고
    • Fc epsilon RI-mediated tyrosine phosphorylation and activation of the 72-kDa protein-tyrosine kinase, PTK72, in RBL-2H3 rat tumor mast cells
    • Hutchcroft, J. E., R. L. Geahlen, G. G. Deanin, and J. M. Oliver. 1992. Fc epsilon RI-mediated tyrosine phosphorylation and activation of the 72-kDa protein-tyrosine kinase, PTK72, in RBL-2H3 rat tumor mast cells Proc. Natl. Acad. Sci USA 89:9107-9111.
    • (1992) Proc. Natl. Acad. Sci USA , vol.89 , pp. 9107-9111
    • Hutchcroft, J.E.1    Geahlen, R.L.2    Deanin, G.G.3    Oliver, J.M.4
  • 22
    • 0026656317 scopus 로고
    • Association of the 72-kDa protein-tyrosine kinase PTK72 with the B cell antigen receptor
    • Hutchcroft, J. E., M. L. Harrison, and R. L. Geahlen. 1992 Association of the 72-kDa protein-tyrosine kinase PTK72 with the B cell antigen receptor. J. Biol. Chem. 267:8613-8619
    • (1992) J. Biol. Chem. , vol.267 , pp. 8613-8619
    • Hutchcroft, J.E.1    Harrison, M.L.2    Geahlen, R.L.3
  • 23
    • 0027399703 scopus 로고
    • Functional characterization of a signal transducing motif present in the T cell antigen receptor ζ chain
    • Irving, B. A., A. C. Chan, and A. Weiss. 1993. Functional characterization of a signal transducing motif present in the T cell antigen receptor ζ chain. J. Exp. Med. 177:1093-1103
    • (1993) J. Exp. Med. , vol.177 , pp. 1093-1103
    • Irving, B.A.1    Chan, A.C.2    Weiss, A.3
  • 24
    • 0026064305 scopus 로고
    • The cytoplasmic domain of the T cell receptor zeta chain is sufficient to couple to receptor-associated signal transduction pathways
    • Irving, B. A., and A. Weiss. 1991. The cytoplasmic domain of the T cell receptor zeta chain is sufficient to couple to receptor-associated signal transduction pathways. Cell 64:891-901.
    • (1991) Cell , vol.64 , pp. 891-901
    • Irving, B.A.1    Weiss, A.2
  • 25
    • 0028942111 scopus 로고
    • ZAP-70 binding specificity to T cell receptor tyrosine-based activation motifs. the tandem SH2 domains of ZAP-70 bind distinct tyrosine-based activation motifs with varying affinity
    • Isakov, N., R. L. Wange, W. H. Burgess, J. D. Watts, R. Aebersold, and L. E. Samelson. 1995. ZAP-70 binding specificity to T cell receptor tyrosine-based activation motifs. the tandem SH2 domains of ZAP-70 bind distinct tyrosine-based activation motifs with varying affinity. J. Exp. Med. 181:375-380
    • (1995) J. Exp. Med. , vol.181 , pp. 375-380
    • Isakov, N.1    Wange, R.L.2    Burgess, W.H.3    Watts, J.D.4    Aebersold, R.5    Samelson, L.E.6
  • 26
    • 0028209548 scopus 로고
    • Sequential interactions of the TCR with two distinct cytoplasmic tyrosine kinases
    • Iwashima, M., B. A. Irving, N. S. van Oers, A. C. Chan, and A. Weiss. 1994. Sequential interactions of the TCR with two distinct cytoplasmic tyrosine kinases. Science 263:1136-1139.
    • (1994) Science , vol.263 , pp. 1136-1139
    • Iwashima, M.1    Irving, B.A.2    Van Oers, N.S.3    Chan, A.C.4    Weiss, A.5
  • 28
    • 0028595695 scopus 로고
    • The protein tyrosine kinase ZAP-70 can associate with the SH2 domain of proto-Vav
    • Katzav, S., M. Sutherland, G. Packham, T. Yi, and A. Weiss. 1994. The protein tyrosine kinase ZAP-70 can associate with the SH2 domain of proto-Vav J Biol. Chem. 269:32579-32585.
    • (1994) J Biol. Chem. , vol.269 , pp. 32579-32585
    • Katzav, S.1    Sutherland, M.2    Packham, G.3    Yi, T.4    Weiss, A.5
  • 29
    • 0028596158 scopus 로고
    • An alternative to SH2 domains for binding tyrosine-phosphorylated proteins
    • Kavanaugh, W. M., and L. T. Williams. 1994. An alternative to SH2 domains for binding tyrosine-phosphorylated proteins Science 266:1862-1865.
    • (1994) Science , vol.266 , pp. 1862-1865
    • Kavanaugh, W.M.1    Williams, L.T.2
  • 30
    • 0027998631 scopus 로고
    • Src homology 2 domains of Syk and Lyn bind to tyrosine-phosphorylated subunits of the high affinity IgE receptor
    • Kihara, H., and R. P. Siraganian. 1994. Src homology 2 domains of Syk and Lyn bind to tyrosine-phosphorylated subunits of the high affinity IgE receptor. J Biol Chem. 269:22427-22432.
    • (1994) J Biol Chem. , vol.269 , pp. 22427-22432
    • Kihara, H.1    Siraganian, R.P.2
  • 31
    • 0026603817 scopus 로고
    • The C-terminal SH2 domain of p85 accounts for the high affinity and specificity of the binding of phosphatidylinositol 3-kinase to phosphorylated platetet-derived growth factor β receptor
    • Klippel, A., J. A. Escobedo, W. J. Fantl, and L. T. Williams. 1992 The C-terminal SH2 domain of p85 accounts for the high affinity and specificity of the binding of phosphatidylinositol 3-kinase to phosphorylated platetet-derived growth factor β receptor. Mol. Cell. Biol 12:1451-1459.
    • (1992) Mol. Cell. Biol , vol.12 , pp. 1451-1459
    • Klippel, A.1    Escobedo, J.A.2    Fantl, W.J.3    Williams, L.T.4
  • 32
    • 0027185152 scopus 로고
    • T cell activation by clustered tyrosine kinases
    • Kolanus, W., C. Romeo, and B. Seed. 1993. T cell activation by clustered tyrosine kinases. Cell 74:171-183.
    • (1993) Cell , vol.74 , pp. 171-183
    • Kolanus, W.1    Romeo, C.2    Seed, B.3
  • 33
    • 0025998529 scopus 로고
    • T-cell and basophil activation through the cytoplasmic tail of T-cell-receptor ζ family proteins
    • Letourneur, F., and R. D. Klausner. 1991 T-cell and basophil activation through the cytoplasmic tail of T-cell-receptor ζ family proteins. Proc. Natl. Acad Sci. USA 88:8905-8909
    • (1991) Proc. Natl. Acad Sci. USA , vol.88 , pp. 8905-8909
    • Letourneur, F.1    Klausner, R.D.2
  • 34
  • 36
    • 0025892211 scopus 로고
    • HNF-1 α and HNF-1 β (vHNF-1) share dimerization and homeo domains, but not activation domains, and form heterodimers in vitro
    • Mendel, D. B., L. P. Hansen, M. K. Graves, P. B. Conley, and G. R. Crabtree. 1991 HNF-1 α and HNF-1 β (vHNF-1) share dimerization and homeo domains, but not activation domains, and form heterodimers in vitro. Genes Dev 5:1042-1056.
    • (1991) Genes Dev , vol.5 , pp. 1042-1056
    • Mendel, D.B.1    Hansen, L.P.2    Graves, M.K.3    Conley, P.B.4    Crabtree, G.R.5
  • 38
    • 3142639315 scopus 로고    scopus 로고
    • Unpublished data
    • Northrop, J. P. Unpublished data.
    • Northrop, J.P.1
  • 39
    • 0027518679 scopus 로고
    • Characterization of the nuclear and cytoplasmic components of the lymphoid-specific nuclear factor of activated T cells (NF-AT) complex
    • Northrop, J. P., K. S. Ullman, and G. R. Crabtree. 1993. Characterization of the nuclear and cytoplasmic components of the lymphoid-specific nuclear factor of activated T cells (NF-AT) complex. J. Biol. Chem. 268:2917-2923.
    • (1993) J. Biol. Chem. , vol.268 , pp. 2917-2923
    • Northrop, J.P.1    Ullman, K.S.2    Crabtree, G.R.3
  • 40
    • 0027468233 scopus 로고
    • A Drosophila SH2-SH3 adaptor protein implicated in coupling the sevenless tyrosine kinase to an activator of Ras guanine nucleotide exchange, Sos
    • Olivier, J. P., T. Raabe, M. Henkemeyer, B. Dickson, G. Mbamalu, B. Margolis, J. Schlessinger, E. Hafen, and T. Pawson. 1993. A Drosophila SH2-SH3 adaptor protein implicated in coupling the sevenless tyrosine kinase to an activator of Ras guanine nucleotide exchange, Sos. Cell 73: 179-191.
    • (1993) Cell , vol.73 , pp. 179-191
    • Olivier, J.P.1    Raabe, T.2    Henkemeyer, M.3    Dickson, B.4    Mbamalu, G.5    Margolis, B.6    Schlessinger, J.7    Hafen, E.8    Pawson, T.9
  • 41
    • 0029072239 scopus 로고
    • A comparison of the interaction of Shc and the tyrosine kinase ZAP-70 with the T cell antigen receptor ζ chain tyrosine-based activation motif
    • Osman, N., S. C. Lucas, H. Turner, and D. Cantrell. 1995 A comparison of the interaction of Shc and the tyrosine kinase ZAP-70 with the T cell antigen receptor ζ chain tyrosine-based activation motif. J. Biol Chem. 270:13981-13986.
    • (1995) J. Biol Chem. , vol.270 , pp. 13981-13986
    • Osman, N.1    Lucas, S.C.2    Turner, H.3    Cantrell, D.4
  • 42
    • 0027955433 scopus 로고
    • The adapter protein Shc interacts with the interleukin-2 (IL-2) receptor upon IL-2 stimulation
    • Ravichandran, K. S., and S. J. Burakoff. 1994 The adapter protein Shc interacts with the interleukin-2 (IL-2) receptor upon IL-2 stimulation. J. Biol Chem. 269:1599-1602.
    • (1994) J. Biol Chem. , vol.269 , pp. 1599-1602
    • Ravichandran, K.S.1    Burakoff, S.J.2
  • 43
    • 0027724634 scopus 로고
    • Interaction of Shc with the ζ chain of the T cell receptor upon T cell activation
    • Ravichandran, K. S., K. K. Lee, Z. Songyang, L. C. Cantley, P. Burn, and S. J. Burakoff. 1993. Interaction of Shc with the ζ chain of the T cell receptor upon T cell activation. Science 262:902-905.
    • (1993) Science , vol.262 , pp. 902-905
    • Ravichandran, K.S.1    Lee, K.K.2    Songyang, Z.3    Cantley, L.C.4    Burn, P.5    Burakoff, S.J.6
  • 44
    • 0026484267 scopus 로고
    • p21ras mediates control of IL-2 gene promoter function in T cell activation
    • Rayter, S. I., M. Woodrow, S. C. Lucas, D. A. Cantrell, and J. Downward. 1992. p21ras mediates control of IL-2 gene promoter function in T cell activation. EMBO J. 11:4549-4556.
    • (1992) EMBO J. , vol.11 , pp. 4549-4556
    • Rayter, S.I.1    Woodrow, M.2    Lucas, S.C.3    Cantrell, D.A.4    Downward, J.5
  • 45
    • 0028227284 scopus 로고
    • SH3 domains of the adapter molecule Grb2 complex with two proteins in T cells: The guanine nucleotide exchange protein Sos and a 75-kDa protein that is a substrate for T cell antigen receptor-activated tyrosine kinases
    • Reif, K., L. Buday, J. Downward, and D. A. Cantrell. 1994. SH3 domains of the adapter molecule Grb2 complex with two proteins in T cells: the guanine nucleotide exchange protein Sos and a 75-kDa protein that is a substrate for T cell antigen receptor-activated tyrosine kinases. J. Biol. Chem. 269:14081-14087.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14081-14087
    • Reif, K.1    Buday, L.2    Downward, J.3    Cantrell, D.A.4
  • 46
    • 0024980981 scopus 로고
    • Antigen receptor tail clue
    • Reth, M. 1989 Antigen receptor tail clue. Nature 338:383-384.
    • (1989) Nature , vol.338 , pp. 383-384
    • Reth, M.1
  • 47
    • 0026537801 scopus 로고
    • Sequence requirements for induction of cytolysis by the T cell antigen/Fc receptor ζ chain
    • Romeo, C., M. Amiot, and B. Seed. 1992 Sequence requirements for induction of cytolysis by the T cell antigen/Fc receptor ζ chain. Cell 68:889-897.
    • (1992) Cell , vol.68 , pp. 889-897
    • Romeo, C.1    Amiot, M.2    Seed, B.3
  • 48
    • 0027294981 scopus 로고
    • The SH2 and SH3 domains of mammalian Grb2 couple the EGF receptor to the Ras activator mSos1
    • Rozakis-Adcock, M., R. Fernley, J. Wade, T. Pawson, and D. Bowtell. 1993. The SH2 and SH3 domains of mammalian Grb2 couple the EGF receptor to the Ras activator mSos1. Nature 363:83-85.
    • (1993) Nature , vol.363 , pp. 83-85
    • Rozakis-Adcock, M.1    Fernley, R.2    Wade, J.3    Pawson, T.4    Bowtell, D.5
  • 49
    • 0023821516 scopus 로고
    • Identification of a putative regulator of early T cell activation genes
    • Shaw, J.-P., P. J. Utz, D. B. Durand, J. J. Toole, E. A. Emmel, and G. R. Crabtree. 1988. Identification of a putative regulator of early T cell activation genes. Science 241:202-205
    • (1988) Science , vol.241 , pp. 202-205
    • Shaw, J.-P.1    Utz, P.J.2    Durand, D.B.3    Toole, J.J.4    Emmel, E.A.5    Crabtree, G.R.6
  • 51
    • 0028180585 scopus 로고
    • GRB2 and phospholipase C-γ1 associate with a 36- to 38-kilodalton phosphotyrosine protein after T-cell receptor stimulation
    • Sieh, M., A. Batzer, J. Schlessinger, and A. Weiss. 1994 GRB2 and phospholipase C-γ1 associate with a 36- to 38-kilodalton phosphotyrosine protein after T-cell receptor stimulation. Mol. Cell. Biol. 14:4435-4442.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 4435-4442
    • Sieh, M.1    Batzer, A.2    Schlessinger, J.3    Weiss, A.4
  • 52
    • 0027404990 scopus 로고
    • An SH3-SH2-SH3 protein is required for p21Ras activation and binds to sevenless and Sos proteins in vitro
    • Simon, M. A., G. S. Dodson, and G. M. Rubin. 1993. An SH3-SH2-SH3 protein is required for p21Ras activation and binds to sevenless and Sos proteins in vitro. Cell 73:169-177.
    • (1993) Cell , vol.73 , pp. 169-177
    • Simon, M.A.1    Dodson, G.S.2    Rubin, G.M.3
  • 53
    • 0027756895 scopus 로고
    • Controlling signal transduction with synthetic ligands
    • Spencer, D. M., T. J. Wandless, S. L. Schreiber, and G. R. Crabtree. 1993. Controlling signal transduction with synthetic ligands. Science 262:1019-1024.
    • (1993) Science , vol.262 , pp. 1019-1024
    • Spencer, D.M.1    Wandless, T.J.2    Schreiber, S.L.3    Crabtree, G.R.4
  • 54
    • 0026705903 scopus 로고
    • Genetic evidence for the involvement of the Lck tyrosine kinase in signal transduction through the T cell antigen receptor
    • Straus, D. B., and A. Weiss. 1992 Genetic evidence for the involvement of the Lck tyrosine kinase in signal transduction through the T cell antigen receptor. Cell 70:585-593.
    • (1992) Cell , vol.70 , pp. 585-593
    • Straus, D.B.1    Weiss, A.2
  • 56
    • 0028014460 scopus 로고
    • Signal transduction by lymphocyte antigen receptors
    • Weiss, A., and D. R. Littman. 1994. Signal transduction by lymphocyte antigen receptors. Cell 76:263-274.
    • (1994) Cell , vol.76 , pp. 263-274
    • Weiss, A.1    Littman, D.R.2
  • 57
    • 0028577724 scopus 로고
    • Binding of Vav to Grb2 through dimerization of Src homology 3 domains
    • Ye, Z. S., and D. Baltimore. 1994. Binding of Vav to Grb2 through dimerization of Src homology 3 domains. Proc. Natl. Acad. Sci USA 91:12629-12633.
    • (1994) Proc. Natl. Acad. Sci USA , vol.91 , pp. 12629-12633
    • Ye, Z.S.1    Baltimore, D.2
  • 58
    • 0028915948 scopus 로고
    • Defective signalling through the T- and B-cell antigen receptors in lymphoid cells lacking the vav proto-oncogene
    • Zhang, R., F. W. Alt, L. Davidson, S. H. Orkin, and W. Swat. 1995. Defective signalling through the T- and B-cell antigen receptors in lymphoid cells lacking the vav proto-oncogene. Nature 374:470-473.
    • (1995) Nature , vol.374 , pp. 470-473
    • Zhang, R.1    Alt, F.W.2    Davidson, L.3    Orkin, S.H.4    Swat, W.5


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