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Volumn 161, Issue 10, 1998, Pages 5404-5412

Phosphatidylinositol 3-kinase is required for CD28 but not CD3 regulation of the TEC family tyrosine kinase EMT/ITK/TSK: Functional and physical interaction of EMT with phosphatidylinositol 3-kinase

Author keywords

[No Author keywords available]

Indexed keywords

CD28 ANTIGEN; CD3 ANTIGEN; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN TYROSINE KINASE;

EID: 0032533465     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (39)

References (66)
  • 3
    • 0028979466 scopus 로고
    • New perspectives of CD28-B7-mediated T cell costimulation
    • Bluestone, J. A. 1995. New perspectives of CD28-B7-mediated T cell costimulation. Immunity 2:555.
    • (1995) Immunity , vol.2 , pp. 555
    • Bluestone, J.A.1
  • 5
    • 0028237348 scopus 로고
    • CD28-B7 interactions in T-cell activation
    • Allison, J. P. 1994. CD28-B7 interactions in T-cell activation. Curr. Opin. Immunol. 6:414.
    • (1994) Curr. Opin. Immunol. , vol.6 , pp. 414
    • Allison, J.P.1
  • 8
    • 0029031023 scopus 로고
    • Naive CD28-deficient T cells can initiate but not sustain an in vitro antigen-specific immune response
    • Lucas, P. J., I. Negishi, K. Nakayama, L. E. Fields, and D. Y. Loh. 1995. Naive CD28-deficient T cells can initiate but not sustain an in vitro antigen-specific immune response. J. Immunol. 154:5757.
    • (1995) J. Immunol. , vol.154 , pp. 5757
    • Lucas, P.J.1    Negishi, I.2    Nakayama, K.3    Fields, L.E.4    Loh, D.Y.5
  • 9
    • 0028211126 scopus 로고
    • The cytoplasmic domain of CD28 is both necessary and sufficient for costimulation of interleukin-2 secretion and association with phosphatidylinositol 3′-kinase
    • Stern, P. H., J. D. Fraser, and A. Weiss. 1994. The cytoplasmic domain of CD28 is both necessary and sufficient for costimulation of interleukin-2 secretion and association with phosphatidylinositol 3′-kinase. Mol. Cell. Biol. 14:3392.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 3392
    • Stern, P.H.1    Fraser, J.D.2    Weiss, A.3
  • 10
    • 0026537347 scopus 로고
    • CD28-mediated signaling co-stimulates murine T cells and prevents induction of anergy in T-cell clones
    • Harding, F. A., J. G. McArthur, J. A. Gross, D. H. Raulet, and J. P. Allison. 1992. CD28-mediated signaling co-stimulates murine T cells and prevents induction of anergy in T-cell clones. Nature 356:607.
    • (1992) Nature , vol.356 , pp. 607
    • Harding, F.A.1    McArthur, J.G.2    Gross, J.A.3    Raulet, D.H.4    Allison, J.P.5
  • 12
    • 0029118260 scopus 로고
    • CD28-mediated signaling in vivo prevents activation-induced apoptosis in the thymus and alters peripheral lymphocyte homeostasis
    • Shi, Y. F., L. G. Radvanyi, A. Sharma, P. Shaw, D. R. Green, R. G. Miller, and G. B. Mills. 1995. CD28-mediated signaling in vivo prevents activation-induced apoptosis in the thymus and alters peripheral lymphocyte homeostasis. J. Immunol. 155:1829.
    • (1995) J. Immunol. , vol.155 , pp. 1829
    • Shi, Y.F.1    Radvanyi, L.G.2    Sharma, A.3    Shaw, P.4    Green, D.R.5    Miller, R.G.6    Mills, G.B.7
  • 13
    • 0030006733 scopus 로고    scopus 로고
    • CD28 costimulation prevents cell death during primary T cell activation
    • Noel, P. J., L. H. Boise, J. M. Green, and C. B. Thompson. 1996. CD28 costimulation prevents cell death during primary T cell activation. J. Immunol. 157:127.
    • (1996) J. Immunol. , vol.157 , pp. 127
    • Noel, P.J.1    Boise, L.H.2    Green, J.M.3    Thompson, C.B.4
  • 14
    • 0029099662 scopus 로고
    • CD28 and T-cell activation
    • Olive, D., and R. Van Lier. 1995. CD28 and T-cell activation. Res. Immunol. 146:127.
    • (1995) Res. Immunol. , vol.146 , pp. 127
    • Olive, D.1    Van Lier, R.2
  • 16
    • 0023514599 scopus 로고
    • Molecular cloning of a CD28 cDNA by a high-efficiency Cos cell expression systems
    • Aruffo, A., and B. Seed. 1987. Molecular cloning of a CD28 cDNA by a high-efficiency Cos cell expression systems. Proc. Natl. Acad. Sci. USA 84:8573.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 8573
    • Aruffo, A.1    Seed, B.2
  • 17
    • 0028304143 scopus 로고
    • Activation of SRC family kinase LCK following CD28 crosslinking in the Jurkat leukemic cell line
    • August, A., and B. Dupont. 1994. Activation of SRC family kinase LCK following CD28 crosslinking in the Jurkat leukemic cell line. Biochem. Biophys. Res. Commun. 199:1466.
    • (1994) Biochem. Biophys. Res. Commun. , vol.199 , pp. 1466
    • August, A.1    Dupont, B.2
  • 18
    • 0028203261 scopus 로고
    • Activation-dependent phosphorylation of T lymphocyte surface receptor CD28 and associated proteins
    • Hutchcroft, J. E., and B. E. Bierer. 1994. Activation-dependent phosphorylation of T lymphocyte surface receptor CD28 and associated proteins. Proc. Natl. Acad. Sci. USA 91:3260.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 3260
    • Hutchcroft, J.E.1    Bierer, B.E.2
  • 19
    • 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., S. Gibson, Y. Kawakami, T. Kawakami, G. B. Mills, and B. Dupont. 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
  • 20
    • 0029989312 scopus 로고    scopus 로고
    • Functional LCK is required for optimal CD28-mediated activation of the TEC family tyrosine kinase EMT/ITK
    • Gibson, S., A. August, D. Branch, B. Dupont, and G. B. Mills. 1996. Functional LCK is required for optimal CD28-mediated activation of the TEC family tyrosine kinase EMT/ITK. J. Biol. Chem. 271:7079.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7079
    • Gibson, S.1    August, A.2    Branch, D.3    Dupont, B.4    Mills, G.B.5
  • 21
    • 0030798980 scopus 로고    scopus 로고
    • LCK phosphorylates the activation loop tyrosine of the ITK kinase domain and activates ITK kinase activity
    • Heyeck, S. D., H. M. Wilcox, S. C. Bunnell, and L. J. Berg. 1997. LCK phosphorylates the activation loop tyrosine of the ITK kinase domain and activates ITK kinase activity. J. Biol. Chem. 272:25401.
    • (1997) J. Biol. Chem. , vol.272 , pp. 25401
    • Heyeck, S.D.1    Wilcox, H.M.2    Bunnell, S.C.3    Berg, L.J.4
  • 22
    • 0031567886 scopus 로고    scopus 로고
    • Analysis of CD28 cytoplasmic tail tyrosine residues as regulators and substrates for the protein tyrosine kinases EMT and LCK
    • King, P. D., A. Sadra, J. M. C. Teng, X. R. Liu, A. Han, A. Selvakumar, A. August, and B. Dupont. 1997. Analysis of CD28 cytoplasmic tail tyrosine residues as regulators and substrates for the protein tyrosine kinases EMT and LCK. J. Immunol. 158:580.
    • (1997) J. Immunol. , vol.158 , pp. 580
    • King, P.D.1    Sadra, A.2    Teng, J.M.C.3    Liu, X.R.4    Han, A.5    Selvakumar, A.6    August, A.7    Dupont, B.8
  • 24
    • 0028940428 scopus 로고
    • Inhibition of CD28-mediated T cell costimulation by the phosphoinositol 3-kinase inhibitor wortmannin
    • Ward, S. G., A. Wilson, L. Turner, J. Westwick, and D. M. Sansom. 1995. Inhibition of CD28-mediated T cell costimulation by the phosphoinositol 3-kinase inhibitor wortmannin. Eur. J. Immunol. 25:526.
    • (1995) Eur. J. Immunol. , vol.25 , pp. 526
    • Ward, S.G.1    Wilson, A.2    Turner, L.3    Westwick, J.4    Sansom, D.M.5
  • 25
    • 0028956419 scopus 로고
    • Phosphatidylinositol 3-kinase activity is not essential for CD28 costimulatory activity in Jurkat T cells: Studies with a selective inhibitor, wortmannin
    • Lu, Y., C. A. Phillips, and J. M. Trevillyan. 1995. Phosphatidylinositol 3-kinase activity is not essential for CD28 costimulatory activity in Jurkat T cells: studies with a selective inhibitor, wortmannin. Eur. J. Immunol. 25:533.
    • (1995) Eur. J. Immunol. , vol.25 , pp. 533
    • Lu, Y.1    Phillips, C.A.2    Trevillyan, J.M.3
  • 26
    • 0028972712 scopus 로고
    • CD28-mediated costimulation in the absence of phosphatidylinositol 3-kinase association and activation
    • Crooks, M. E. C., D. R. Littman, R. H. Carter, D. T. Fearon, A. Weiss, and P. H. Stein. 1995. CD28-mediated costimulation in the absence of phosphatidylinositol 3-kinase association and activation. Mol. Cell. Biol. 15:6820.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6820
    • Crooks, M.E.C.1    Littman, D.R.2    Carter, R.H.3    Fearon, D.T.4    Weiss, A.5    Stein, P.H.6
  • 27
    • 0028972549 scopus 로고
    • CD28 delivers costimulatory signals independently of its association with phosphatidylinositol 3-kinase
    • Traitt, K. E., J. Shi, S. Gibson, L. G. Segal, G. B. Mills, and J. B. Imboden. 1995. CD28 delivers costimulatory signals independently of its association with phosphatidylinositol 3-kinase. J. Immunol. 155:4702.
    • (1995) J. Immunol. , vol.155 , pp. 4702
    • Traitt, K.E.1    Shi, J.2    Gibson, S.3    Segal, L.G.4    Mills, G.B.5    Imboden, J.B.6
  • 28
    • 0029910720 scopus 로고    scopus 로고
    • Phosphorylation of each of the distal three tyrosines of the CD28 cytoplasmic tail is required for CD28-induced T cell IL-2 secretion
    • Teng, J. M. C., P. D. King, A. Sadra, X. Liu, A. Han, A. Selvakumar, A. August, and B. Dupont. 1996. Phosphorylation of each of the distal three tyrosines of the CD28 cytoplasmic tail is required for CD28-induced T cell IL-2 secretion. Tissue Antigens 48:255.
    • (1996) Tissue Antigens , vol.48 , pp. 255
    • Teng, J.M.C.1    King, P.D.2    Sadra, A.3    Liu, X.4    Han, A.5    Selvakumar, A.6    August, A.7    Dupont, B.8
  • 29
    • 0029885108 scopus 로고    scopus 로고
    • Structural requirements for CD28-mediated costimulation of IL-2 production in Jurkat T cells
    • Traitt, K. E., T. Nagel, L. F. Suen, J. B. Imboden. 1996. Structural requirements for CD28-mediated costimulation of IL-2 production in Jurkat T cells. J. Immunol. 156:4539.
    • (1996) J. Immunol. , vol.156 , pp. 4539
    • Traitt, K.E.1    Nagel, T.2    Suen, L.F.3    Imboden, J.B.4
  • 30
    • 13344270890 scopus 로고
    • Altered T cell receptor signaling and disrupted T cell development in mice lacking ITK
    • Liao, X. C., and D. R. Littman. 1995. Altered T cell receptor signaling and disrupted T cell development in mice lacking ITK. Immunity 3:757.
    • (1995) Immunity , vol.3 , pp. 757
    • Liao, X.C.1    Littman, D.R.2
  • 31
    • 0030865198 scopus 로고    scopus 로고
    • Antiviral immune responses in Itk-deficient mice
    • Bachman, M. F., D. R. Littman, and X. C. Liao. 1997. Antiviral immune responses in Itk-deficient mice. J. Virol. 71:7253.
    • (1997) J. Virol. , vol.71 , pp. 7253
    • Bachman, M.F.1    Littman, D.R.2    Liao, X.C.3
  • 33
    • 0030584837 scopus 로고    scopus 로고
    • The EMT/ITK/TSK (EMT) tyrosine kinase is activated during TCR signaling: LCK is required for optimal activation of EMT
    • Gibson, S., A. August, Y. Kawakami, T. Kawakami, B. Dupont, and G. B. Mills. 1996. The EMT/ITK/TSK (EMT) tyrosine kinase is activated during TCR signaling: LCK is required for optimal activation of EMT. J. Immunol. 156:2716.
    • (1996) J. Immunol. , vol.156 , pp. 2716
    • Gibson, S.1    August, A.2    Kawakami, Y.3    Kawakami, T.4    Dupont, B.5    Mills, G.B.6
  • 34
    • 0030947852 scopus 로고    scopus 로고
    • Itk, a T cell-specific tyrosine kinase is required for CD2-mediated interleukin-2 promoter activation in the human T cell line Jurkat
    • Tanaka, N., H. Abe, H. Yajita, K. Okumura, M. Nakamura, and K. Sugamura. 1997. Itk, a T cell-specific tyrosine kinase is required for CD2-mediated interleukin-2 promoter activation in the human T cell line Jurkat. Eur. J. Immunol. 27:834.
    • (1997) Eur. J. Immunol. , vol.27 , pp. 834
    • Tanaka, N.1    Abe, H.2    Yajita, H.3    Okumura, K.4    Nakamura, M.5    Sugamura, K.6
  • 36
    • 0029165836 scopus 로고
    • Activation and interaction with protein kinase C of a cytoplasmic kinase ITK/TSK/EMT on Fc epsilon RI cross-linking on mast cells
    • Kawakami, Y., L. Yao, M. Tashiro, S. Gibson, G. B. Mills, and T. Kawakami. 1995. Activation and interaction with protein kinase C of a cytoplasmic kinase ITK/TSK/EMT on Fc epsilon RI cross-linking on mast cells. J. Immunol. 155:3556.
    • (1995) J. Immunol. , vol.155 , pp. 3556
    • Kawakami, Y.1    Yao, L.2    Tashiro, M.3    Gibson, S.4    Mills, G.B.5    Kawakami, T.6
  • 37
    • 0030826662 scopus 로고    scopus 로고
    • SRC-induced activation of inducible T cell kinase (ITK) requires phosphatidylinositol 3-kinase activity and pleckstrin homology domain of inducible T cell kinase
    • August, A., A. Sadra, B. Dupont, and H. Hanafusa. 1997. SRC-induced activation of inducible T cell kinase (ITK) requires phosphatidylinositol 3-kinase activity and pleckstrin homology domain of inducible T cell kinase. Proc. Natl. Acad. Sci. USA 94:11227.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 11227
    • August, A.1    Sadra, A.2    Dupont, B.3    Hanafusa, H.4
  • 38
    • 0027980301 scopus 로고
    • Binding of Bruton's tyrosine kinase to Fyn, Lyn, or Hck through a SRC homology 3 domain-mediated interaction
    • Cheng, G., Z. S. Ye, and D. Baltimore. 1994. Binding of Bruton's tyrosine kinase to Fyn, Lyn, or Hck through a SRC homology 3 domain-mediated interaction. Proc. Natl. Acad. Sci. USA 91:8152.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 8152
    • Cheng, G.1    Ye, Z.S.2    Baltimore, D.3
  • 39
    • 0031029781 scopus 로고    scopus 로고
    • Regulatory intramolecular association in a tyrosine kinases of the TEC family
    • Andreotti, A. H., S. C. Bunnell, S. Feng, L. J. Berg, and S. L. Schreiber. 1997. Regulatory intramolecular association in a tyrosine kinases of the TEC family. Nature 385:93.
    • (1997) Nature , vol.385 , pp. 93
    • Andreotti, A.H.1    Bunnell, S.C.2    Feng, S.3    Berg, L.J.4    Schreiber, S.L.5
  • 41
    • 0031255110 scopus 로고    scopus 로고
    • The SH3 domain of Itk/EMT binds to proline-rich sequences in the cytoplasmic domain of the T cell costimulatory receptor CD28
    • Marengere, L. E. M., K. Okkenhaug, A. Clavreull, D. Couez, S. Gibson, G. B. Mills, T. W. Mak, and R. Rottapel. 1997. The SH3 domain of Itk/EMT binds to proline-rich sequences in the cytoplasmic domain of the T cell costimulatory receptor CD28. J. Immunol. 159:3220.
    • (1997) J. Immunol. , vol.159 , pp. 3220
    • Marengere, L.E.M.1    Okkenhaug, K.2    Clavreull, A.3    Couez, D.4    Gibson, S.5    Mills, G.B.6    Mak, T.W.7    Rottapel, R.8
  • 42
    • 0028182749 scopus 로고
    • Binding of phosphatidylinositol-3-OH kinase to CD28 is required for T-cell signaling
    • Pages, F., M. Ragueneau, R. Rottapel, A. Truneh, J. Nunes, J. Imbert, and D. Olive. 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
  • 43
    • 0027429761 scopus 로고
    • Ligation of CD28 receptor by B7 induces formation of D-3-phosphoinositides in T lymphocytes independently of T cell receptor/CD2 activation
    • Ward, S. G., J. Westwick, N. D. Hall, and D. M. Sansom. 1993. Ligation of CD28 receptor by B7 induces formation of D-3-phosphoinositides in T lymphocytes independently of T cell receptor/CD2 activation. Eur. J. Immunol. 23:2572.
    • (1993) Eur. J. Immunol. , vol.23 , pp. 2572
    • Ward, S.G.1    Westwick, J.2    Hall, N.D.3    Sansom, D.M.4
  • 44
    • 0029046768 scopus 로고
    • The phosphoinositide 3-kinase inhibitor wortmannin inhibits CD28-mediates T cell costimulation
    • Wilson, A., D. Sansom, R. Parry, J. Westwick, and S. Ward. 1995. The phosphoinositide 3-kinase inhibitor wortmannin inhibits CD28-mediates T cell costimulation. Biochem. Soc. Trans. 23:2825.
    • (1995) Biochem. Soc. Trans. , vol.23 , pp. 2825
    • Wilson, A.1    Sansom, D.2    Parry, R.3    Westwick, J.4    Ward, S.5
  • 45
    • 0028118512 scopus 로고
    • Stimulation of CD28 triggers an association between CD28 and phosphatidylinositol 3-kinase in Jurkat T cells
    • Truitt, K. E., C. M. Hicks, and J. B. Imboden. 1994. Stimulation of CD28 triggers an association between CD28 and phosphatidylinositol 3-kinase in Jurkat T cells. J. Exp. Med. 179:1071.
    • (1994) J. Exp. Med. , vol.179 , pp. 1071
    • Truitt, K.E.1    Hicks, C.M.2    Imboden, J.B.3
  • 48
    • 0029965232 scopus 로고    scopus 로고
    • PI3-kinase: A pivotal pathway in T-cell activation
    • Ward, S. G., C. H. June, and D. Olive. 1996. PI3-kinase: a pivotal pathway in T-cell activation. Immunol. Today 14:187.
    • (1996) Immunol. Today , vol.14 , pp. 187
    • Ward, S.G.1    June, C.H.2    Olive, D.3
  • 49
    • 0031039024 scopus 로고    scopus 로고
    • Direct regulation of Akt proto-oncogene product by phosphatidylinositol-3.4-bisphosphate
    • Franke, T. F., D. R. Kaplan, L. C. Cantley, and A. Toker. 1997. Direct regulation of Akt proto-oncogene product by phosphatidylinositol-3.4-bisphosphate. Science 275:665.
    • (1997) Science , vol.275 , pp. 665
    • Franke, T.F.1    Kaplan, D.R.2    Cantley, L.C.3    Toker, A.4
  • 50
    • 0028486018 scopus 로고
    • Phosphatidylinositol 3-kinase
    • Kapeller, R., and L. C. Cantley. 1994. Phosphatidylinositol 3-kinase. Bioessays 16:565.
    • (1994) Bioessays , vol.16 , pp. 565
    • Kapeller, R.1    Cantley, L.C.2
  • 53
    • 0028198388 scopus 로고
    • Activation of phosphatidylinositol-3′ kinase by SRC-family kinase SH3 binding to the p85 subunit
    • Pleiman, C. M., W. M. Hertz, and J. C. Gambier. 1994. Activation of phosphatidylinositol-3′ kinase by SRC-family kinase SH3 binding to the p85 subunit. Science 263:1609.
    • (1994) Science , vol.263 , pp. 1609
    • Pleiman, C.M.1    Hertz, W.M.2    Gambier, J.C.3
  • 54
    • 0029753011 scopus 로고    scopus 로고
    • Structural and thermodynamic characterization of the interaction of the SH3 domain from fyn with the proline-rich binding site on the p85 subunit of PI3-kinase
    • Renzoni, D. A., D. J. Pugh, G. Siligardi, P. Das, C. J. Morton, C. Rossi, M. D. Waterfield, I. D. Campbell, and J. E. Ladbury. 1996. Structural and thermodynamic characterization of the interaction of the SH3 domain from fyn with the proline-rich binding site on the p85 subunit of PI3-kinase. Biochemistry 35:15646.
    • (1996) Biochemistry , vol.35 , pp. 15646
    • Renzoni, D.A.1    Pugh, D.J.2    Siligardi, G.3    Das, P.4    Morton, C.J.5    Rossi, C.6    Waterfield, M.D.7    Campbell, I.D.8    Ladbury, J.E.9
  • 55
    • 0028342859 scopus 로고
    • CD28 of T lymphocytes associates with phosphatidylinositol 3-kinase
    • August, A., and B. Dupont. 1994. CD28 of T lymphocytes associates with phosphatidylinositol 3-kinase. Int. Immunol. 6:769.
    • (1994) Int. Immunol. , vol.6 , pp. 769
    • August, A.1    Dupont, B.2
  • 56
    • 0028221022 scopus 로고
    • T-cell antigen CD28 interacts with lipid kinase phosphatidylinositol 3-kinase by a cytoplasmic Tyr(P)-Met-Xaa-Met motif
    • Prasad, K. V., Y. C. Cai, M. Raab, B. Duckworth, L. C. Cantley, S. E. Shoelson, and C. E. Rudd. 1994. T-cell antigen CD28 interacts with lipid kinase phosphatidylinositol 3-kinase by a cytoplasmic Tyr(P)-Met-Xaa-Met motif. Proc. Natl. Acad. Sci. USA 91:2834.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 2834
    • Prasad, K.V.1    Cai, Y.C.2    Raab, M.3    Duckworth, B.4    Cantley, L.C.5    Shoelson, S.E.6    Rudd, C.E.7
  • 57
    • 0028170210 scopus 로고
    • A specific inhibitor of phosphatidylinositol 3-kinase. 2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one (LY294002)
    • Vlahos, C. J., W. F. Matter, K. Y. Hui, and R. F. Brown. 1994. A specific inhibitor of phosphatidylinositol 3-kinase. 2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one (LY294002). J. Biol. Chem. 269:5241.
    • (1994) J. Biol. Chem. , vol.269 , pp. 5241
    • Vlahos, C.J.1    Matter, W.F.2    Hui, K.Y.3    Brown, R.F.4
  • 58
    • 0028146616 scopus 로고
    • Blockage of chemotactic peptide-induced stimulation of neutrophils by wortmannin as a result of selective inhibition of phosphatidylinositol 3-kinase
    • Okada, T., L. Sakuma, Y. Fukui, O. Hazeki, and M. Ui. 1994. Blockage of chemotactic peptide-induced stimulation of neutrophils by wortmannin as a result of selective inhibition of phosphatidylinositol 3-kinase. J. Biol. Chem. 269:3563.
    • (1994) J. Biol. Chem. , vol.269 , pp. 3563
    • Okada, T.1    Sakuma, L.2    Fukui, Y.3    Hazeki, O.4    Ui, M.5
  • 59
    • 0027217937 scopus 로고
    • Identification, cloning and characterization of a novel human T-cell-specific tyrosine kinase located at hematopoietin complex on chromosome 5q
    • Gibson, S., B. Leung, J. A. Squire, M. Hill, N. Arima, P. Goss, D. Hogg, and G. B. Mills. 1993. Identification, cloning and characterization of a novel human T-cell-specific tyrosine kinase located at hematopoietin complex on chromosome 5q. Blood 82:1561.
    • (1993) Blood , vol.82 , pp. 1561
    • Gibson, S.1    Leung, B.2    Squire, J.A.3    Hill, M.4    Arima, N.5    Goss, P.6    Hogg, D.7    Mills, G.B.8
  • 62
    • 0026705903 scopus 로고
    • Genetic evidence for the involvement of the LCK tyrosine kinase in signal transduction through the T cell antigen receptor
    • Straus, D., 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.
    • (1992) Cell , vol.70 , pp. 585
    • Straus, D.1    Weiss, A.2
  • 63
    • 0029097427 scopus 로고
    • Protein kinases: Structure and function
    • Bossemeyer, D. 1995. Protein kinases: structure and function. FEBS Lett. 369:57.
    • (1995) FEBS Lett. , vol.369 , pp. 57
    • Bossemeyer, D.1
  • 64
    • 0029034440 scopus 로고
    • Interactions of Cbl with Grb2 and phosphatidylinositol 3-kinase in activated Jurkat cells
    • Meisner, H., B. R. Conway, D. Hartley, and M. P. Czech. 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
  • 65
  • 66
    • 0030067874 scopus 로고    scopus 로고
    • Human Txk: Genomic organization, structure and contiguous physical linkage with the TEC gene
    • Ohta, Y., R. N. Haire, C. T. Amemiya, R. T. Littman, T. Trager, O. Riesso, G. W. Litman. 1996. Human Txk: genomic organization, structure and contiguous physical linkage with the TEC gene. Oncogene 12:937.
    • (1996) Oncogene , vol.12 , pp. 937
    • Ohta, Y.1    Haire, R.N.2    Amemiya, C.T.3    Littman, R.T.4    Trager, T.5    Riesso, O.6    Litman, G.W.7


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