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Volumn 15, Issue 2, 2014, Pages 186-194

Inhibition of the kinase Csk in thymocytes reveals a requirement for actin remodeling in the initiation of full TCR signaling

Author keywords

[No Author keywords available]

Indexed keywords

4 AMINO 7 TERT BUTYL 5 (4 METHYLPHENYL)PYRAZOLO[3,4 D]PYRIMIDINE; ACTIN; CD28 ANTIGEN; INOSITOL PHOSPHATE; MITOGEN ACTIVATED PROTEIN KINASE; PHOSPHOLIPASE C GAMMA1; PROTEIN TYROSINE KINASE; T LYMPHOCYTE RECEPTOR;

EID: 84892719664     PISSN: 15292908     EISSN: 15292916     Source Type: Journal    
DOI: 10.1038/ni.2772     Document Type: Article
Times cited : (79)

References (53)
  • 2
    • 0028535120 scopus 로고
    • ZAP-70 is constitutively associated with tyrosine-phosphorylated TCR ζ in murine thymocytes and lymph node T cells
    • van Oers, N.S., Killeen, N. & Weiss, A. ZAP-70 is constitutively associated with tyrosine-phosphorylated TCR ζ in murine thymocytes and lymph node T cells. Immunity 1, 675-685 (1994).
    • (1994) Immunity , vol.1 , pp. 675-685
    • Van Oers, N.S.1    Killeen, N.2    Weiss, A.3
  • 3
    • 55449138409 scopus 로고    scopus 로고
    • Regulation of T cell receptor activation by dynamic membrane binding of the CD3ε cytoplasmic tyrosine-based motif
    • Xu, C. et al. Regulation of T cell receptor activation by dynamic membrane binding of the CD3ε cytoplasmic tyrosine-based motif. Cell 135, 702-713 (2008).
    • (2008) Cell , vol.135 , pp. 702-713
    • Xu, C.1
  • 4
    • 84863482471 scopus 로고    scopus 로고
    • Biophysical mechanism of T-cell receptor triggering in a reconstituted system
    • James, J.R. & Vale, R.D. Biophysical mechanism of T-cell receptor triggering in a reconstituted system. Nature 487, 64-69 (2012).
    • (2012) Nature , vol.487 , pp. 64-69
    • James, J.R.1    Vale, R.D.2
  • 5
    • 78650599246 scopus 로고    scopus 로고
    • Mechanisms for T cell receptor triggering
    • van der Merwe, P.A. & Dushek, O. Mechanisms for T cell receptor triggering. Nat. Rev. Immunol. 11, 47-55 (2011).
    • (2011) Nat. Rev. Immunol , vol.11 , pp. 47-55
    • Van Der Merwe, P.A.1    Dushek, O.2
  • 6
    • 7944231534 scopus 로고    scopus 로고
    • Function of the Src-family kinases, Lck and Fyn, in T-cell development and activation
    • Palacios, E.H. & Weiss, A. Function of the Src-family kinases, Lck and Fyn, in T-cell development and activation. Oncogene 23, 7990-8000 (2004).
    • (2004) Oncogene , vol.23 , pp. 7990-8000
    • Palacios, E.H.1    Weiss, A.2
  • 7
    • 0026681275 scopus 로고
    • The human p50csk tyrosine kinase phosphorylates p56lck at Tyr-505 and down regulates its catalytic activity
    • Bergman, M. et al. The human p50csk tyrosine kinase phosphorylates p56lck at Tyr-505 and down regulates its catalytic activity. EMBO J. 11, 2919-2924 (1992).
    • (1992) EMBO J. , vol.11 , pp. 2919-2924
    • Bergman, M.1
  • 8
    • 0036143017 scopus 로고    scopus 로고
    • Reciprocal regulation of lymphocyte activation by tyrosine kinases and phosphatases
    • Hermiston, M.L., Xu, Z., Majeti, R. & Weiss, A. Reciprocal regulation of lymphocyte activation by tyrosine kinases and phosphatases. J. Clin. Invest. 109, 9-14 (2002).
    • (2002) J. Clin. Invest , vol.109 , pp. 9-14
    • Hermiston, M.L.1    Xu, Z.2    Majeti, R.3    Weiss, A.4
  • 9
    • 77953911933 scopus 로고    scopus 로고
    • Constitutively active Lck kinase in T cells drives antigen receptor signal transduction
    • Nika, K. et al. Constitutively active Lck kinase in T cells drives antigen receptor signal transduction. Immunity 32, 766-777 (2010).
    • (2010) Immunity , vol.32 , pp. 766-777
    • Nika, K.1
  • 10
    • 0027289232 scopus 로고
    • Disruption of the csk gene, encoding a negative regulator of Src family tyrosine kinases, leads to neural tube defects and embryonic lethality in mice
    • Imamoto, A. & Soriano, P. Disruption of the csk gene, encoding a negative regulator of Src family tyrosine kinases, leads to neural tube defects and embryonic lethality in mice. Cell 73, 1117-1124 (1993).
    • (1993) Cell , vol.73 , pp. 1117-1124
    • Imamoto, A.1    Soriano, P.2
  • 11
    • 0027176228 scopus 로고
    • Constitutive activation of Src family kinases in mouse embryos that lack Csk
    • Nada, S. et al. Constitutive activation of Src family kinases in mouse embryos that lack Csk. Cell 73, 1125-1135 (1993).
    • (1993) Cell , vol.73 , pp. 1125-1135
    • Nada, S.1
  • 12
    • 0032572720 scopus 로고    scopus 로고
    • Csk controls antigen receptor-mediated development and selection of T-lineage cells
    • Schmedt, C. et al. Csk controls antigen receptor-mediated development and selection of T-lineage cells. Nature 394, 901-904 (1998).
    • (1998) Nature , vol.394 , pp. 901-904
    • Schmedt, C.1
  • 13
    • 0028820120 scopus 로고
    • Requirement of the SH3 and SH2 domains for the inhibitory function of tyrosine protein kinase p50csk in T lymphocytes
    • Cloutier, J.F., Chow, L.M. & Veillette, A. Requirement of the SH3 and SH2 domains for the inhibitory function of tyrosine protein kinase p50csk in T lymphocytes. Mol. Cell. Biol. 15, 5937-5944 (1995).
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 5937-5944
    • Cloutier, J.F.1    Chow, L.M.2    Veillette, A.3
  • 14
    • 0342313755 scopus 로고    scopus 로고
    • Phosphoprotein associated with glycosphingolipid-enriched microdomains (PAG), a novel ubiquitously expressed transmembrane adaptor protein, binds the protein tyrosine kinase csk and is involved in regulation of T cell activation
    • Brdicka, T. et al. Phosphoprotein associated with glycosphingolipid- enriched microdomains (PAG), a novel ubiquitously expressed transmembrane adaptor protein, binds the protein tyrosine kinase csk and is involved in regulation of T cell activation. J. Exp. Med. 191, 1591-1604 (2000).
    • (2000) J. Exp. Med. , vol.191 , pp. 1591-1604
    • Brdicka, T.1
  • 15
    • 0037370491 scopus 로고    scopus 로고
    • Phosphorylation-dependent regulation of T-cell activation by PAG/Cbp, a lipid raft-associated transmembrane adaptor
    • Davidson, D., Bakinowski, M., Thomas, M.L., Horejsi, V. & Veillette, A. Phosphorylation-dependent regulation of T-cell activation by PAG/Cbp, a lipid raft-associated transmembrane adaptor. Mol. Cell. Biol. 23, 2017-2028 (2003).
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 2017-2028
    • Davidson, D.1    Bakinowski, M.2    Thomas, M.L.3    Horejsi, V.4    Veillette, A.5
  • 16
    • 0034720166 scopus 로고    scopus 로고
    • Transmembrane phosphoprotein Cbp regulates the activities of Src-family tyrosine kinases
    • Kawabuchi, M. et al. Transmembrane phosphoprotein Cbp regulates the activities of Src-family tyrosine kinases. Nature 404, 999-1003 (2000).
    • (2000) Nature , vol.404 , pp. 999-1003
    • Kawabuchi, M.1
  • 17
    • 0032101348 scopus 로고    scopus 로고
    • Membrane compartmentation is required for efficient T cell activation
    • Xavier, R., Brennan, T., Li, Q., McCormack, C. & Seed, B. Membrane compartmentation is required for efficient T cell activation. Immunity 8, 723-732 (1998).
    • (1998) Immunity , vol.8 , pp. 723-732
    • Xavier, R.1    Brennan, T.2    Li, Q.3    McCormack, C.4    Seed, B.5
  • 18
    • 27944447718 scopus 로고    scopus 로고
    • The ubiquitously expressed Csk adaptor protein Cbp is dispensable for embryogenesis and T-cell development and function
    • Dobenecker, M.W., Schmedt, C., Okada, M. & Tarakhovsky, A. The ubiquitously expressed Csk adaptor protein Cbp is dispensable for embryogenesis and T-cell development and function. Mol. Cell. Biol. 25, 10533-10542 (2005).
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 10533-10542
    • Dobenecker, M.W.1    Schmedt, C.2    Okada, M.3    Tarakhovsky, A.4
  • 19
    • 25444448196 scopus 로고    scopus 로고
    • Cbp deficiency alters Csk localization in lipid rafts but does not affect T-cell development
    • Xu, S., Huo, J., Tan, J.E. & Lam, K.P. Cbp deficiency alters Csk localization in lipid rafts but does not affect T-cell development. Mol. Cell. Biol. 25, 8486-8495 (2005).
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 8486-8495
    • Xu, S.1    Huo, J.2    Tan, J.E.3    Lam, K.P.4
  • 20
    • 80052946904 scopus 로고    scopus 로고
    • Feedback circuits monitor and adjust basal Lck-dependent events in T cell receptor signaling
    • Schoenborn, J.R., Tan, Y.X., Zhang, C., Shokat, K.M. & Weiss, A. Feedback circuits monitor and adjust basal Lck-dependent events in T cell receptor signaling. Sci. Signal. 4, ra59 (2011).
    • (2011) Sci. Signal. , vol.4
    • Schoenborn, J.R.1    Tan, Y.X.2    Zhang, C.3    Shokat, K.M.4    Weiss, A.5
  • 21
    • 84871483253 scopus 로고    scopus 로고
    • All PI3Kinase signaling is not mTOR: Dissecting mTOR-dependent and independent signaling pathways in T cells
    • Gamper, C.J. & Powell, J.D. All PI3Kinase signaling is not mTOR: dissecting mTOR-dependent and independent signaling pathways in T cells. Front. Immunol. 3, 312 (2012).
    • (2012) Front. Immunol. , vol.3 , pp. 312
    • Gamper, C.J.1    Powell, J.D.2
  • 22
    • 67349159879 scopus 로고    scopus 로고
    • Inositol trisphosphate and calcium signalling mechanisms
    • Berridge, M.J. Inositol trisphosphate and calcium signalling mechanisms. Biochim. Biophys. Acta 1793, 933-940 (2009).
    • (2009) Biochim. Biophys. Acta , vol.1793 , pp. 933-940
    • Berridge, M.J.1
  • 23
    • 84871837348 scopus 로고    scopus 로고
    • A phospholipase C-γ1-independent RasGRP1-ERK-dependent pathway drives lymphoproliferative disease in linker for activation of T cells-Y136F mutant mice
    • Kortum, R.L. et al. A phospholipase C-γ1-independent, RasGRP1-ERK-dependent pathway drives lymphoproliferative disease in linker for activation of T cells-Y136F mutant mice. J. Immunol. 190, 147-158 (2013).
    • (2013) J. Immunol. , vol.190 , pp. 147-158
    • Kortum, R.L.1
  • 24
    • 17844364513 scopus 로고    scopus 로고
    • Paradigm shift of the plasma membrane concept from the two-dimensional continuum fluid to the partitioned fluid: High-speed single-molecule tracking of membrane molecules
    • Kusumi, A. et al. Paradigm shift of the plasma membrane concept from the two-dimensional continuum fluid to the partitioned fluid: high-speed single-molecule tracking of membrane molecules. Annu. Rev. Biophys. Biomol. Struct. 34, 351-378 (2005).
    • (2005) Annu. Rev. Biophys. Biomol. Struct. , vol.34 , pp. 351-378
    • Kusumi, A.1
  • 25
    • 38549106998 scopus 로고    scopus 로고
    • Quantitative analysis of the binding of ezrin to large unilamellar vesicles containing phosphatidylinositol 4,5 bisphosphate
    • Blin, G. et al. Quantitative analysis of the binding of ezrin to large unilamellar vesicles containing phosphatidylinositol 4,5 bisphosphate. Biophys. J. 94, 1021-1033 (2008).
    • (2008) Biophys. J. , vol.94 , pp. 1021-1033
    • Blin, G.1
  • 26
    • 1942519695 scopus 로고    scopus 로고
    • Electrostatic sequestration of PIP2 on phospholipid membranes by basic/aromatic regions of proteins
    • Gambhir, A. et al. Electrostatic sequestration of PIP2 on phospholipid membranes by basic/aromatic regions of proteins. Biophys. J. 86, 2188-2207 (2004).
    • (2004) Biophys. J. , vol.86 , pp. 2188-2207
    • Gambhir, A.1
  • 27
    • 76949108167 scopus 로고    scopus 로고
    • The membrane skeleton controls diffusion dynamics and signaling through the B cell receptor
    • Treanor, B. et al. The membrane skeleton controls diffusion dynamics and signaling through the B cell receptor. Immunity 32, 187-199 (2010).
    • (2010) Immunity , vol.32 , pp. 187-199
    • Treanor, B.1
  • 28
    • 72949104779 scopus 로고    scopus 로고
    • Antigen presentation in the thymus for positive selection and central tolerance induction
    • Klein, L., Hinterberger, M., Wirnsberger, G. & Kyewski, B. Antigen presentation in the thymus for positive selection and central tolerance induction. Nat. Rev. Immunol. 9, 833-844 (2009).
    • (2009) Nat. Rev. Immunol. , vol.9 , pp. 833-844
    • Klein, L.1    Hinterberger, M.2    Wirnsberger, G.3    Kyewski, B.4
  • 29
    • 56249122238 scopus 로고    scopus 로고
    • Distinct functional capacities of mouse thymic and splenic dendritic cell populations
    • Proietto, A.I., Lahoud, M.H. & Wu, L. Distinct functional capacities of mouse thymic and splenic dendritic cell populations. Immunol. Cell Biol. 86, 700-708 (2008).
    • (2008) Immunol. Cell Biol. , vol.86 , pp. 700-708
    • Proietto, A.I.1    Lahoud, M.H.2    Wu, L.3
  • 31
    • 0023737931 scopus 로고
    • The CD4 and CD8 T cell surface antigens are associated with the internal membrane tyrosine-protein kinase p56lck
    • Veillette, A., Bookman, M.A., Horak, E.M. & Bolen, J.B. The CD4 and CD8 T cell surface antigens are associated with the internal membrane tyrosine-protein kinase p56lck. Cell 55, 301-308 (1988).
    • (1988) Cell , vol.55 , pp. 301-308
    • Veillette, A.1    Bookman, M.A.2    Horak, E.M.3    Bolen, J.B.4
  • 32
    • 84857793524 scopus 로고    scopus 로고
    • Decisions about dendritic cells: Past, present, and future
    • Steinman, R.M. Decisions about dendritic cells: past, present, and future. Annu. Rev. Immunol. 30, 1-22 (2012).
    • (2012) Annu. Rev. Immunol. , vol.30 , pp. 1-22
    • Steinman, R.M.1
  • 34
    • 0041929574 scopus 로고    scopus 로고
    • CD28 engagement promotes actin polymerization through the activation of the small Rho GTPase Cdc42 in human T cells
    • Salazar-Fontana, L.I., Barr, V., Samelson, L.E. & Bierer, B.E. CD28 engagement promotes actin polymerization through the activation of the small Rho GTPase Cdc42 in human T cells. J. Immunol. 171, 2225-2232 (2003).
    • (2003) J. Immunol , vol.171 , pp. 2225-2232
    • Salazar-Fontana, L.I.1    Barr, V.2    Samelson, L.E.3    Bierer, B.E.4
  • 35
    • 84880830434 scopus 로고    scopus 로고
    • The lymphoid lineage-specific actin-uncapping protein Rltpr is essential for costimulation via CD28 and the development of regulatory T cells
    • Liang, Y. et al. The lymphoid lineage-specific actin-uncapping protein Rltpr is essential for costimulation via CD28 and the development of regulatory T cells. Nat. Immunol. 14, 858-866 (2013).
    • (2013) Nat. Immunol. , vol.14 , pp. 858-866
    • Liang, Y.1
  • 36
    • 1842631103 scopus 로고    scopus 로고
    • Jurkat T cells and development of the T-cell receptor signalling paradigm
    • Abraham, R.T. & Weiss, A. Jurkat T cells and development of the T-cell receptor signalling paradigm. Nat. Rev. Immunol. 4, 301-308 (2004).
    • (2004) Nat. Rev. Immunol. , vol.4 , pp. 301-308
    • Abraham, R.T.1    Weiss, A.2
  • 37
    • 74949100104 scopus 로고    scopus 로고
    • Regulation of the actin cytoskeleton-plasma membrane interplay by phosphoinositides
    • Saarikangas, J., Zhao, H. & Lappalainen, P. Regulation of the actin cytoskeleton-plasma membrane interplay by phosphoinositides. Physiol. Rev. 90, 259-289 (2010).
    • (2010) Physiol. Rev. , vol.90 , pp. 259-289
    • Saarikangas, J.1    Zhao, H.2    Lappalainen, P.3
  • 38
    • 0028961573 scopus 로고
    • Sustained signaling leading to T cell activation results from prolonged T cell receptor occupancy. Role of T cell actin cytoskeleton
    • Valitutti, S., Dessing, M., Aktories, K., Gallati, H. & Lanzavecchia, A. Sustained signaling leading to T cell activation results from prolonged T cell receptor occupancy. Role of T cell actin cytoskeleton. J. Exp. Med. 181, 577-584 (1995).
    • (1995) J. Exp. Med. , vol.181 , pp. 577-584
    • Valitutti, S.1    Dessing, M.2    Aktories, K.3    Gallati, H.4    Lanzavecchia, A.5
  • 39
    • 2942582913 scopus 로고    scopus 로고
    • Survival of resting mature B lymphocytes depends on BCR signaling via the Igα/β heterodimer
    • Kraus, M., Alimzhanov, M.B., Rajewsky, N. & Rajewsky, K. Survival of resting mature B lymphocytes depends on BCR signaling via the Igα/β heterodimer. Cell 117, 787-800 (2004).
    • (2004) Cell , vol.117 , pp. 787-800
    • Kraus, M.1    Alimzhanov, M.B.2    Rajewsky, N.3    Rajewsky, K.4
  • 41
    • 0026649765 scopus 로고
    • Identification and distribution of the costimulatory receptor CD28 in the mouse
    • Gross, J.A., Callas, E. & Allison, J.P. Identification and distribution of the costimulatory receptor CD28 in the mouse. J. Immunol. 149, 380-388 (1992).
    • (1992) J. Immunol. , vol.149 , pp. 380-388
    • Gross, J.A.1    Callas, E.2    Allison, J.P.3
  • 42
    • 0037514517 scopus 로고    scopus 로고
    • A role for the B7-1/B7-2:CD28/CTLA-4 pathway during negative selection
    • Buhlmann, J.E., Elkin, S.K. & Sharpe, A.H. A role for the B7-1/B7-2:CD28/CTLA-4 pathway during negative selection. J. Immunol. 170, 5421-5428 (2003).
    • (2003) J. Immunol. , vol.170 , pp. 5421-5428
    • Buhlmann, J.E.1    Elkin, S.K.2    Sharpe, A.H.3
  • 43
    • 0033082497 scopus 로고    scopus 로고
    • Timing and casting for actors of thymic negative selection
    • Dautigny, N., Le Campion, A. & Lucas, B. Timing and casting for actors of thymic negative selection. J. Immunol. 162, 1294-1302 (1999).
    • (1999) J. Immunol. , vol.162 , pp. 1294-1302
    • Dautigny, N.1    Le Campion, A.2    Lucas, B.3
  • 44
    • 0033517125 scopus 로고    scopus 로고
    • Proline residues in CD28 and the Src homology (SH)3 domain of Lck are required for T cell costimulation
    • Holdorf, A.D. et al. Proline residues in CD28 and the Src homology (SH)3 domain of Lck are required for T cell costimulation. J. Exp. Med. 190, 375-384 (1999).
    • (1999) J. Exp. Med. , vol.190 , pp. 375-384
    • Holdorf, A.D.1
  • 45
    • 37249000008 scopus 로고    scopus 로고
    • EGF-induced PIP2 hydrolysis releases and activates cofilin locally in carcinoma cells
    • van Rheenen, J. et al. EGF-induced PIP2 hydrolysis releases and activates cofilin locally in carcinoma cells. J. Cell Biol. 179, 1247-1259 (2007).
    • (2007) J. Cell Biol. , vol.179 , pp. 1247-1259
    • Van Rheenen, J.1
  • 46
    • 77950365218 scopus 로고    scopus 로고
    • RIAM regulates the cytoskeletal distribution and activation of PLC-γ1 in T cells
    • Patsoukis, N. et al. RIAM regulates the cytoskeletal distribution and activation of PLC-γ1 in T cells. Sci. Signal. 2, ra79 (2009).
    • (2009) Sci. Signal. , vol.2
    • Patsoukis, N.1
  • 47
    • 33645053126 scopus 로고    scopus 로고
    • Two-step red-mediated recombination for versatile high-efficiency markerless DNA manipulation in Escherichia coli
    • Tischer, B.K., von Einem, J., Kaufer, B. & Osterrieder, N. Two-step red-mediated recombination for versatile high-efficiency markerless DNA manipulation in Escherichia coli. Biotechniques 40, 191-197 (2006).
    • (2006) Biotechniques , vol.40 , pp. 191-197
    • Tischer, B.K.1    Von Einem, J.2    Kaufer, B.3    Osterrieder, N.4
  • 48
    • 0027326544 scopus 로고
    • Inflammatory and immune responses are impaired in mice deficient in intercellular adhesion molecule 1
    • Sligh, J.E. Jr. et al. Inflammatory and immune responses are impaired in mice deficient in intercellular adhesion molecule 1. Proc. Natl. Acad. Sci. USA 90, 8529-8533 (1993).
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 8529-8533
    • Sligh Jr., J.E.1
  • 49
    • 0030936275 scopus 로고    scopus 로고
    • B7-1 and B7-2 have overlapping, critical roles in immunoglobulin class switching and germinal center formation
    • Borriello, F. et al. B7-1 and B7-2 have overlapping, critical roles in immunoglobulin class switching and germinal center formation. Immunity 6, 303-313 (1997).
    • (1997) Immunity , vol.6 , pp. 303-313
    • Borriello, F.1
  • 50
    • 0027240587 scopus 로고
    • Negative regulation of T-cell receptor signalling by tyrosine protein kinase p50csk
    • Chow, L.M., Fournel, M., Davidson, D. & Veillette, A. Negative regulation of T-cell receptor signalling by tyrosine protein kinase p50csk. Nature 365, 156-160 (1993).
    • (1993) Nature , vol.365 , pp. 156-160
    • Chow, L.M.1    Fournel, M.2    Davidson, D.3    Veillette, A.4
  • 51
    • 27144505097 scopus 로고    scopus 로고
    • Protein identification and analysis tools on the ExPASy server
    • ed. Walker, J.M. Humana
    • Gasteiger, E. et al. Protein identification and analysis tools on the ExPASy server. in The Proteomics Protocols Handbook (ed. Walker, J.M.) 571-607 (Humana, 2005).
    • (2005) The Proteomics Protocols Handbook , pp. 571-607
    • Gasteiger, E.1
  • 52
    • 0028973603 scopus 로고
    • Characterization of pp60c-src tyrosine kinase activities using a continuous assay: Autoactivation of the enzyme is an intermolecular autophosphorylation process
    • Barker, S.C. et al. Characterization of pp60c-src tyrosine kinase activities using a continuous assay: autoactivation of the enzyme is an intermolecular autophosphorylation process. Biochemistry 34, 14843-14851 (1995).
    • (1995) Biochemistry , vol.34 , pp. 14843-14851
    • Barker, S.C.1
  • 53
    • 0032488592 scopus 로고    scopus 로고
    • Peptide and protein phosphorylation by protein tyrosine kinase Csk: Insights into specificity and mechanism
    • Sondhi, D., Xu, W., Songyang, Z., Eck, M.J. & Cole, P.A. Peptide and protein phosphorylation by protein tyrosine kinase Csk: insights into specificity and mechanism. Biochemistry 37, 165-172 (1998).
    • (1998) Biochemistry , vol.37 , pp. 165-172
    • Sondhi, D.1    Xu, W.2    Songyang, Z.3    Eck, M.J.4    Cole, P.A.5


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