메뉴 건너뛰기




Volumn 163, Issue 5, 1999, Pages 2508-2516

CD45 is essential for FcεRI signaling by ZAP70, but not Syk, in Syk- negative mast cells

Author keywords

[No Author keywords available]

Indexed keywords

CD45 ANTIGEN; IMMUNOGLOBULIN E; LYMPHOCYTE ANTIGEN RECEPTOR; PROTEIN TYROSINE KINASE; PROTEIN TYROSINE PHOSPHATASE;

EID: 0033198133     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (26)

References (58)
  • 1
    • 0025196012 scopus 로고
    • Tyrosine phosphorylation coupled to IgE receptor-mediated signal transduction and histamine release
    • Benhamou, M., J. S. Gutkind, K. C. Robbins, and R. P. Siraganian. 1990. Tyrosine phosphorylation coupled to IgE receptor-mediated signal transduction and histamine release. Proc. Natl. Acad. Sci. USA 87:5327.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 5327
    • Benhamou, M.1    Gutkind, J.S.2    Robbins, K.C.3    Siraganian, R.P.4
  • 2
    • 0026612253 scopus 로고
    • FcεRI-mediated tyrosine phosphorylation of multiple proteins, including phospholipase Cγ1 and the receptor βγ2 complex, in RBL-2H3 rat basophilic leukemia cells
    • Li, W., G. G. Deanin, B. Margolis, J. Schlessinger, and J. M. Oliver. 1992. FcεRI-mediated tyrosine phosphorylation of multiple proteins, including phospholipase Cγ1 and the receptor βγ2 complex, in RBL-2H3 rat basophilic leukemia cells. Mol. Cell. Biol. 12:3176.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 3176
    • Li, W.1    Deanin, G.G.2    Margolis, B.3    Schlessinger, J.4    Oliver, J.M.5
  • 3
    • 0029347999 scopus 로고
    • The Syk/ZAP-70 protein tyrosine kinase connection to antigen receptor signaling processes
    • Van Oers, N. S., and A. Weiss. 1995. The Syk/ZAP-70 protein tyrosine kinase connection to antigen receptor signaling processes. Semin. Immunol. 7:227.
    • (1995) Semin. Immunol. , vol.7 , pp. 227
    • Van Oers, N.S.1    Weiss, A.2
  • 4
    • 0002803274 scopus 로고    scopus 로고
    • Regulation and function of protein tyrosine Syk in FcεRI-mediated signaling
    • E. Razin and J. Rivera, eds. Springer-Verlag. Berlin
    • Siraganian, R. P., J. Zhang, and T. Kimura. 1999. Regulation and function of protein tyrosine Syk in FcεRI-mediated signaling. In Signal Transduction in Mast Cells and Basophils. E. Razin and J. Rivera, eds. Springer-Verlag. Berlin, pp. 115-133.
    • (1999) Signal Transduction in Mast Cells and Basophils , pp. 115-133
    • Siraganian, R.P.1    Zhang, J.2    Kimura, T.3
  • 5
    • 0028209548 scopus 로고
    • Sequential interactions of the TCR with two distinct cytoplasmic tyrosine kinases
    • Iwashima, M., B. A. Irving, N. S. C. Van Oers, A. C. Chan, and A. Weiss. 1994. Sequential interactions of the TCR with two distinct cytoplasmic tyrosine kinases. Science 263:1136.
    • (1994) 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
  • 7
    • 0027433055 scopus 로고
    • syk in high affinity IgE receptor signaling: Identification as a component of pp72 and association with the receptor γ chain
    • syk in high affinity IgE receptor signaling: identification as a component of pp72 and association with the receptor γ chain. J. Biol. Chem. 268:23318.
    • (1993) J. Biol. Chem. , vol.268 , pp. 23318
    • Benhamou, M.1    Ryba, N.J.P.2    Kihara, H.3    Nishikata, H.4    Siraganian, R.P.5
  • 8
    • 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.
    • (1994) J. Biol. Chem. , vol.269 , pp. 22427
    • Kihara, H.1    Siraganian, R.P.2
  • 9
    • 0029864882 scopus 로고    scopus 로고
    • syk by tyrosine phosphorylation or by binding of phosphorylated immunoreceptor tyrosine-based activation motif peptides
    • syk by tyrosine phosphorylation or by binding of phosphorylated immunoreceptor tyrosine-based activation motif peptides. Mol. Cell. Biol. 16:1471.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 1471
    • Kimura, T.1    Sakamoto, H.2    Appella, E.3    Siraganian, R.P.4
  • 12
    • 0030018183 scopus 로고    scopus 로고
    • Transfection of Syk protein tyrosine kinase reconstitues high affinity IgE receptor mediated degranulation in a Syk negative variant of rat basophilic leukemia RBL-2H3 cells
    • Zhang, J., E. H. Berenstein, R. L. Evans, and R. P. Siraganian. 1996. Transfection of Syk protein tyrosine kinase reconstitues high affinity IgE receptor mediated degranulation in a Syk negative variant of rat basophilic leukemia RBL-2H3 cells. J. Exp. Med. 184:71.
    • (1996) J. Exp. Med. , vol.184 , pp. 71
    • Zhang, J.1    Berenstein, E.H.2    Evans, R.L.3    Siraganian, R.P.4
  • 13
    • 0028783322 scopus 로고
    • Syk tyrosine kinase required for mouse viability and B-cell development
    • Cheng, A. M., B. Rowley, W. Pao, A. Hayday, J. B. Bolen, and T. Pawson. 1995. Syk tyrosine kinase required for mouse viability and B-cell development. Nature 178:303.
    • (1995) Nature , vol.178 , pp. 303
    • Cheng, A.M.1    Rowley, B.2    Pao, W.3    Hayday, A.4    Bolen, J.B.5    Pawson, T.6
  • 15
    • 0029076731 scopus 로고
    • Reconstitution of Syk function by the ZAP-70 protein tyrosine kinase
    • Kong, G. H., J. Y. Bu, T. Kurosaki, A. S. Shaw, and A. C. Chan. 1995. Reconstitution of Syk function by the ZAP-70 protein tyrosine kinase. Immunity 2:485.
    • (1995) Immunity , vol.2 , pp. 485
    • Kong, G.H.1    Bu, J.Y.2    Kurosaki, T.3    Shaw, A.S.4    Chan, A.C.5
  • 16
    • 0028905060 scopus 로고
    • Syk is activated by phosphotyrosine-containing peptides representing the tyrosine-based activation motifs of the high affinity receptor for IgE
    • Shiue, L., M. J. Zoller, and J. S. Brugge. 1995. Syk is activated by phosphotyrosine-containing peptides representing the tyrosine-based activation motifs of the high affinity receptor for IgE. J. Biol. Chem. 270:10498.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10498
    • Shiue, L.1    Zoller, M.J.2    Brugge, J.S.3
  • 17
    • 0029068171 scopus 로고
    • Syk protein-tyrosine kinase is regulated by tyrosine-phosphorylated Igα/ Igβ immunoreceptor tyrosine activation motif binding and autophosphorylation
    • Rowley, R. B., A. L. Burkhardt, H. G. Chao, G. R. Matsueda, and J. B. Bolen. 1995. Syk protein-tyrosine kinase is regulated by tyrosine-phosphorylated Igα/ Igβ immunoreceptor tyrosine activation motif binding and autophosphorylation. J. Biol. Chem. 270:11590.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11590
    • Rowley, R.B.1    Burkhardt, A.L.2    Chao, H.G.3    Matsueda, G.R.4    Bolen, J.B.5
  • 18
    • 0029895645 scopus 로고    scopus 로고
    • Purification and characterization of human ZAP-70 protein-tyrosine kinase from a baculovirus expression system
    • Isakov, N., R. L. Wange, J. D. Watts, R. Aebersold, and L. E. Samelson. 1996. Purification and characterization of human ZAP-70 protein-tyrosine kinase from a baculovirus expression system. J. Biol. Chem. 271:15753.
    • (1996) J. Biol. Chem. , vol.271 , pp. 15753
    • Isakov, N.1    Wange, R.L.2    Watts, J.D.3    Aebersold, R.4    Samelson, L.E.5
  • 19
    • 0029783430 scopus 로고    scopus 로고
    • Distinct tyrosine phosphorylation sites in ZAP-70 mediate activation and negative regulation of antigen receptor function
    • Kong, G. H., M. Dalton, J. B. Wardenburg, D. Straus, T. Kurosaki, and A. C. Chan. 1996. Distinct tyrosine phosphorylation sites in ZAP-70 mediate activation and negative regulation of antigen receptor function Mol. Cell. Biol. 16:5026.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 5026
    • Kong, G.H.1    Dalton, M.2    Wardenburg, J.B.3    Straus, D.4    Kurosaki, T.5    Chan, A.C.6
  • 20
    • 0029952988 scopus 로고    scopus 로고
    • The Syk protein tyrosine kinase can function independently of CD45 or Lck in T cell antigen receptor signaling
    • Chu, D. H., H. Spits, J. F. Peyron, R. B. Rowley, J. B. Bolen, and A. Weiss. 1996. The Syk protein tyrosine kinase can function independently of CD45 or Lck in T cell antigen receptor signaling. EMBO J. 15:6251.
    • (1996) EMBO J. , vol.15 , pp. 6251
    • Chu, D.H.1    Spits, H.2    Peyron, J.F.3    Rowley, R.B.4    Bolen, J.B.5    Weiss, A.6
  • 21
    • 0031912097 scopus 로고    scopus 로고
    • Genetic evidence for differential coupling of Syk family kinases to the T-cell receptor: Reconstitution studies in a ZAP-70-deficient Jurkat T-cell line
    • Williams, B. L., K. L. Schreiber, W. G. Zhang, R. L. Wange, L. E. Samelson, P. J. Leibson, and R. T. Abraham. 1998. Genetic evidence for differential coupling of Syk family kinases to the T-cell receptor: reconstitution studies in a ZAP-70-deficient Jurkat T-cell line. Mol. Cell. Biol. 18:1388.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 1388
    • Williams, B.L.1    Schreiber, K.L.2    Zhang, W.G.3    Wange, R.L.4    Samelson, L.E.5    Leibson, P.J.6    Abraham, R.T.7
  • 22
    • 0030885363 scopus 로고    scopus 로고
    • The role of CD45 in signal transduction
    • Justement, L. B. 1997. The role of CD45 in signal transduction. Adv. Immunol. 66:1.
    • (1997) Adv. Immunol. , vol.66 , pp. 1
    • Justement, L.B.1
  • 23
    • 0028346560 scopus 로고
    • CD45: An emerging role as a protein tyrosine phosphatase required for lymphocyte activation and development
    • Trowbridge, I. S., and M. L. Thomas. 1994. CD45: An emerging role as a protein tyrosine phosphatase required for lymphocyte activation and development. Annu. Rev. Immunol. 12:85.
    • (1994) Annu. Rev. Immunol. , vol.12 , pp. 85
    • Trowbridge, I.S.1    Thomas, M.L.2
  • 25
    • 0027410485 scopus 로고
    • Differential effects of expression of the CD45 tyrosine protein phosphatase on the tyrosine phosphorylation of the Lck, Fyn, and c-Src tyrosine protein kinases
    • Hurley, T. R., R. Hyman, and B. M. Sefton. 1993. Differential effects of expression of the CD45 tyrosine protein phosphatase on the tyrosine phosphorylation of the Lck, Fyn, and c-Src tyrosine protein kinases. Mol. Cell. Biol. 13:1651.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 1651
    • Hurley, T.R.1    Hyman, R.2    Sefton, B.M.3
  • 26
    • 0027389272 scopus 로고
    • CD45 specifically modulates binding of Lck to a phosphopeptide encompassing the negative regulatory tyrosine of Lck
    • Sieh, M., J. B. Bolen, and A. Weiss. 1993. CD45 specifically modulates binding of Lck to a phosphopeptide encompassing the negative regulatory tyrosine of Lck. EMBO J. 12:315.
    • (1993) EMBO J. , vol.12 , pp. 315
    • Sieh, M.1    Bolen, J.B.2    Weiss, A.3
  • 27
    • 0025297050 scopus 로고
    • Tyrosine phosphatase CD45 is essential for coupling T-cell antigen receptor to the phosphatidyl inositol pathway
    • Koretzky, G. A., J. Picus, M. L. Thomas, and A. Weiss. 1990. Tyrosine phosphatase CD45 is essential for coupling T-cell antigen receptor to the phosphatidyl inositol pathway. Nature 346:66.
    • (1990) Nature , vol.346 , pp. 66
    • Koretzky, G.A.1    Picus, J.2    Thomas, M.L.3    Weiss, A.4
  • 28
    • 0026011310 scopus 로고
    • Tyrosine phosphatase CD45 is required for T-cell antigen receptor and CD2-mediated activation of a protein tyrosine kinase and interleukin 2 production
    • Koretzky, G. A., J. Picus, T. Schultz, and A. Weiss. 1991. Tyrosine phosphatase CD45 is required for T-cell antigen receptor and CD2-mediated activation of a protein tyrosine kinase and interleukin 2 production. Proc. Natl. Acad. Sci. USA 88:2037.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 2037
    • Koretzky, G.A.1    Picus, J.2    Schultz, T.3    Weiss, A.4
  • 29
    • 0024416009 scopus 로고
    • Evidence that the leukocyte-common antigen is required for antigen-induced T lymphocyte proliferation
    • Pingel, J. T., and M. L. Thomas. 1989. Evidence that the leukocyte-common antigen is required for antigen-induced T lymphocyte proliferation. Cell 58:1055.
    • (1989) Cell , vol.58 , pp. 1055
    • Pingel, J.T.1    Thomas, M.L.2
  • 31
    • 0026056126 scopus 로고
    • Monoclonal antibodies to the leukocyte common antigen (CD45) inhibit IgE-mediated histamine release from human basophils
    • Hook, W. A., E. H. Berenstein, F. U. Zinsser, C. Fischler, and R. P. Siraganian. 1991. Monoclonal antibodies to the leukocyte common antigen (CD45) inhibit IgE-mediated histamine release from human basophils. J. Immunol. 147:2670.
    • (1991) J. Immunol. , vol.147 , pp. 2670
    • Hook, W.A.1    Berenstein, E.H.2    Zinsser, F.U.3    Fischler, C.4    Siraganian, R.P.5
  • 32
    • 0028358822 scopus 로고
    • Leukocyte common antigen (CD45) is required for immunoglobulin E-mediated degranulation of mast cells
    • Berger, S. A., T. W. Mak, and C. J. Paige. 1994. Leukocyte common antigen (CD45) is required for immunoglobulin E-mediated degranulation of mast cells. J. Exp. Med. 180:471.
    • (1994) J. Exp. Med. , vol.180 , pp. 471
    • Berger, S.A.1    Mak, T.W.2    Paige, C.J.3
  • 33
    • 0028914242 scopus 로고
    • Regulation by CD45 of the tyrosine phosphorylation of high affinity IgE receptor β- and γ-chains
    • Adamczewski, M., R. P. Numerof, G. A. Koretzky, and J. P. Kinet. 1995. Regulation by CD45 of the tyrosine phosphorylation of high affinity IgE receptor β- and γ-chains. J. Immunol. 154:3047.
    • (1995) J. Immunol. , vol.154 , pp. 3047
    • Adamczewski, M.1    Numerof, R.P.2    Koretzky, G.A.3    Kinet, J.P.4
  • 34
    • 0027130696 scopus 로고
    • CD45-deficient RBL-2H3 cells: Cellular response to FcεR- and ionophore-induced stimulation
    • Schneider, H., M. Korn, and D. Haustein. 1993. CD45-deficient RBL-2H3 cells: cellular response to FcεR- and ionophore-induced stimulation. Immunol. Invest. 22:503.
    • (1993) Immunol. Invest. , vol.22 , pp. 503
    • Schneider, H.1    Korn, M.2    Haustein, D.3
  • 35
    • 0028801038 scopus 로고
    • Protein tyrosine phosphatase activity associates with the high affinity IgE receptor and dephosphorylates the receptor subunits, but not Lyn or Syk
    • Swieter, M., E. H. Berenstein, and R. P. Siraganian. 1995. Protein tyrosine phosphatase activity associates with the high affinity IgE receptor and dephosphorylates the receptor subunits, but not Lyn or Syk. J. Immunol. 155:5330.
    • (1995) J. Immunol. , vol.155 , pp. 5330
    • Swieter, M.1    Berenstein, E.H.2    Siraganian, R.P.3
  • 36
    • 0027096402 scopus 로고
    • Expression, purification, and characterization of the functional dimeric cytoplasmic domain of human erythrocyte band 3 in Escherichia coli
    • Wang, C. C., J. A. Badylak, S. E. Lux, R. Moriyama, J. E. Dixon, and P. S. Low. 1992. Expression, purification, and characterization of the functional dimeric cytoplasmic domain of human erythrocyte band 3 in Escherichia coli. Protein Sci. 1:1206.
    • (1992) Protein Sci. , vol.1 , pp. 1206
    • Wang, C.C.1    Badylak, J.A.2    Lux, S.E.3    Moriyama, R.4    Dixon, J.E.5    Low, P.S.6
  • 37
    • 0032532359 scopus 로고    scopus 로고
    • Mutations in the activation loop tyrosines of protein tyrosine kinase Syk abrogate intracellular signaling but not kinase activity
    • Zhang, J., T. Kimura, and R. P. Siraganian. 1998. Mutations in the activation loop tyrosines of protein tyrosine kinase Syk abrogate intracellular signaling but not kinase activity J. Immunol. 161:4366.
    • (1998) J. Immunol. , vol.161 , pp. 4366
    • Zhang, J.1    Kimura, T.2    Siraganian, R.P.3
  • 39
    • 0023116952 scopus 로고
    • Characterization of monoclonal antibodies produced by immunization with partially purified IgE receptor complexes
    • Stracke, M. L., L. K. Basciano, C. Fischler, E. H. Berenstein, and R. P. Siraganian. 1987. Characterization of monoclonal antibodies produced by immunization with partially purified IgE receptor complexes. Mol. Immunol. 24:347.
    • (1987) Mol. Immunol. , vol.24 , pp. 347
    • Stracke, M.L.1    Basciano, L.K.2    Fischler, C.3    Berenstein, E.H.4    Siraganian, R.P.5
  • 41
    • 0032079343 scopus 로고    scopus 로고
    • A unique insert in the linker domain of Syk is necessary for its function in immunoreceptor signalling
    • Latour, S., J. Zhang, R. P. Siraganian, and A. Veillette. 1998. A unique insert in the linker domain of Syk is necessary for its function in immunoreceptor signalling. EMBO J. 17:2584.
    • (1998) EMBO J. , vol.17 , pp. 2584
    • Latour, S.1    Zhang, J.2    Siraganian, R.P.3    Veillette, A.4
  • 42
    • 0029970787 scopus 로고    scopus 로고
    • Downstream signaling molecules bind to different phosphorylaled immunoreceptor tyrosine-based activation motif (ITAM) peptides of the high affinity IgE receptor
    • Kimura, T., H. Kihara, S. Bhattacharyya, H. Sakamoto, E. Appella, and R. P. Siraganian. 1996. Downstream signaling molecules bind to different phosphorylaled immunoreceptor tyrosine-based activation motif (ITAM) peptides of the high affinity IgE receptor. J. Biol. Chem. 271:27962.
    • (1996) J. Biol. Chem. , vol.271 , pp. 27962
    • Kimura, T.1    Kihara, H.2    Bhattacharyya, S.3    Sakamoto, H.4    Appella, E.5    Siraganian, R.P.6
  • 46
    • 0031918006 scopus 로고    scopus 로고
    • Genetic evidence of a role for Lck in T-cell receptor function independent or downstream of ZAP-70/Syk protein tyrosine kinases
    • Wong, J., D. Straus, and A. C. Chan. 1998. Genetic evidence of a role for Lck in T-cell receptor function independent or downstream of ZAP-70/Syk protein tyrosine kinases. Mol. Cell. Biol. 18:2855.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 2855
    • Wong, J.1    Straus, D.2    Chan, A.C.3
  • 47
    • 0031907541 scopus 로고    scopus 로고
    • Harnessing Syk family tyrosine kinases as signaling domains for chimeric single chain of the variable domain receptors: Optimal design for T cell activation
    • Fitzer-Attas, C. J., D. G. Schindler, T. Waks, and Z. Eshhar. 1998. Harnessing Syk family tyrosine kinases as signaling domains for chimeric single chain of the variable domain receptors: optimal design for T cell activation. J. Immunol. 160:145.
    • (1998) J. Immunol. , vol.160 , pp. 145
    • Fitzer-Attas, C.J.1    Schindler, D.G.2    Waks, T.3    Eshhar, Z.4
  • 48
    • 0029063151 scopus 로고
    • Analysis of the interaction of ZAP-70 and Syk protein-tyrosine kinases with the T-cell antigen receptor by plasmon resonance
    • Bu, J. Y., A. S. Shaw, and A. C. Chan. 1995. Analysis of the interaction of ZAP-70 and Syk protein-tyrosine kinases with the T-cell antigen receptor by plasmon resonance. Proc. Natl. Acad. Sci. USA 92:5106.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 5106
    • Bu, J.Y.1    Shaw, A.S.2    Chan, A.C.3
  • 50
    • 0032555744 scopus 로고    scopus 로고
    • Structural basis for Syk tyrosine kinase ubiquity in signal transduction pathways revealed by the crystal structure of ils regulatory SH2 domains bound to a dually phosphorylated ITAM peptide
    • Futterer, K., J. Wong, R. A. Grucza, A. C. Chan, and G. Waksman. 1998. Structural basis for Syk tyrosine kinase ubiquity in signal transduction pathways revealed by the crystal structure of ils regulatory SH2 domains bound to a dually phosphorylated ITAM peptide. J. Mol. Biol. 281:523.
    • (1998) J. Mol. Biol. , vol.281 , pp. 523
    • Futterer, K.1    Wong, J.2    Grucza, R.A.3    Chan, A.C.4    Waksman, G.5
  • 51
    • 0029788103 scopus 로고    scopus 로고
    • Differential intrinsic enzymatic activity of Syk and Zap-70 protein-tyrosine kinases
    • Latour, S., L. M. L. Chow, and A. Veillette. 1996. Differential intrinsic enzymatic activity of Syk and Zap-70 protein-tyrosine kinases. J. Biol. Chem. 271:22782.
    • (1996) J. Biol. Chem. , vol.271 , pp. 22782
    • Latour, S.1    Chow, L.M.L.2    Veillette, A.3
  • 53
    • 0027981910 scopus 로고
    • The catalytic activity of the CD45 membrane-proximal phosphatase domain is required for TCR signaling and regulation
    • Desai, D. M., J. Sap, O. Silvennoinen, J. Schlessinger, and A. Weiss. 1994. The catalytic activity of the CD45 membrane-proximal phosphatase domain is required for TCR signaling and regulation. EMBO J. 13:4002.
    • (1994) EMBO J. , vol.13 , pp. 4002
    • Desai, D.M.1    Sap, J.2    Silvennoinen, O.3    Schlessinger, J.4    Weiss, A.5
  • 54
    • 0028337449 scopus 로고
    • Multiple components of the B cell antigen receptor complex associate with the protein tyrosine phosphatase, CD45
    • Brown, V. K., E. W. Ogle, A. L. Burkhardt, R. B. Rowley, J. B. Bolen, and L. B. Justement. 1994. Multiple components of the B cell antigen receptor complex associate with the protein tyrosine phosphatase, CD45. J. Biol. Chem. 269: 17238.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17238
    • Brown, V.K.1    Ogle, E.W.2    Burkhardt, A.L.3    Rowley, R.B.4    Bolen, J.B.5    Justement, L.B.6
  • 55
    • 0029846429 scopus 로고    scopus 로고
    • CD45 modulates phosphorylation of both autophosphorylation and negative regulatory tyrosines of Lyn in B cells
    • Yanagi, S., H. Sugawara, M. Kurosaki, H. Sabe, H. Yamamura, and T. Kurosaki. 1996. CD45 modulates phosphorylation of both autophosphorylation and negative regulatory tyrosines of Lyn in B cells. J. Biol. Chem. 271:30487.
    • (1996) J. Biol. Chem. , vol.271 , pp. 30487
    • Yanagi, S.1    Sugawara, H.2    Kurosaki, M.3    Sabe, H.4    Yamamura, H.5    Kurosaki, T.6
  • 56
    • 0031568534 scopus 로고    scopus 로고
    • Protein tyrosine kinases Syk and ZAP-70 display distinct requirements for Src family kinases in immune response receptor signal transduction
    • Zoller, K. E., I. A. MacNeil, and J. S. Brugge. 1997. Protein tyrosine kinases 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
  • 57
    • 0028339795 scopus 로고
    • CD45 regulation of tyrosine phosphorylation and enzyme activity of Src family kinases
    • Burns, C. M., K. Sakaguchi, E. Appella, and J. D. Ashwell. 1994. CD45 regulation of tyrosine phosphorylation and enzyme activity of Src family kinases. J. Biol. Chem. 269:13594.
    • (1994) J. Biol. Chem. , vol.269 , pp. 13594
    • Burns, C.M.1    Sakaguchi, K.2    Appella, E.3    Ashwell, J.D.4
  • 58
    • 0029779003 scopus 로고    scopus 로고
    • Mutational analysis of Lck in CD45-negative T cells: Dominant role of tyrosine 394 phosphorylation in kinase activity
    • D'oro, U., K. Sakaguchi, E. Appella, and J. D. Ashwell. 1996. Mutational analysis of Lck in CD45-negative T cells: dominant role of tyrosine 394 phosphorylation in kinase activity. Mol. Cell. Biol. 16:4996.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 4996
    • D'oro, U.1    Sakaguchi, K.2    Appella, E.3    Ashwell, J.D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.