메뉴 건너뛰기




Volumn 1, Issue 2, 2002, Pages 155-163

Regulation of Lck and Fyn tyrosine kinase activities by transmembrane protein tyrosine phosphatase leukocyte common antigen-related molecule

Author keywords

[No Author keywords available]

Indexed keywords

CD45 ANTIGEN; CYSTINE; PROTEIN KINASE FYN; PROTEIN KINASE LCK; PROTEIN TYROSINE KINASE; PROTEIN TYROSINE PHOSPHATASE; SERINE; UNCLASSIFIED DRUG;

EID: 0036923354     PISSN: 15417786     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (27)

References (52)
  • 1
    • 0035313868 scopus 로고    scopus 로고
    • Combinatorial control of the specificity of protein tyrosine phosphatases
    • Tonks, N. K. and Neel, B. G. Combinatorial control of the specificity of protein tyrosine phosphatases. Curr. Opin. Cell Biol., 13: 182-195, 2001.
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 182-195
    • Tonks, N.K.1    Neel, B.G.2
  • 2
    • 0032176512 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases: Mechanisms of catalysis and regulation
    • Denu, J. M. and Dixon, J. E. Protein tyrosine phosphatases: mechanisms of catalysis and regulation. Curr. Opin. Chem. Biol., 2: 633-641, 1998.
    • (1998) Curr. Opin. Chem. Biol. , vol.2 , pp. 633-641
    • Denu, J.M.1    Dixon, J.E.2
  • 3
    • 0030802798 scopus 로고    scopus 로고
    • Protein tyrosine kinases in thymocyte development
    • Cheng, A. M. and Chan, A. C. Protein tyrosine kinases in thymocyte development. Curr. Opin. Immunol., 9: 528-533, 1997.
    • (1997) Curr. Opin. Immunol. , vol.9 , pp. 528-533
    • Cheng, A.M.1    Chan, A.C.2
  • 4
    • 0032986606 scopus 로고    scopus 로고
    • The regulation of antigen-receptor signaling by protein tyrosine phosphatases: A hole in the story
    • Thomas, M. L. The regulation of antigen-receptor signaling by protein tyrosine phosphatases: a hole in the story. Curr. Opin. Immunol., 11: 270-276, 1999.
    • (1999) Curr. Opin. Immunol. , vol.11 , pp. 270-276
    • Thomas, M.L.1
  • 5
    • 0028014460 scopus 로고
    • Signal transduction by lymphocyte antigen receptors
    • Weiss, A. and Littman, D. R. Signal transduction by lymphocyte antigen receptors. Cell, 76: 263-274, 1994.
    • (1994) Cell , vol.76 , pp. 263-274
    • Weiss, A.1    Littman, D.R.2
  • 6
    • 0030250114 scopus 로고    scopus 로고
    • Complex complexes: Signaling at the TCR
    • Wange, R. L. and Samelson, L. E. Complex complexes: signaling at the TCR. Immunity, 5: 197-205, 1996.
    • (1996) Immunity , vol.5 , pp. 197-205
    • Wange, R.L.1    Samelson, L.E.2
  • 7
    • 0028141681 scopus 로고
    • Involvement of the protein tyrosine kinase p56lck in T cell signaling and thymocyte development
    • Anderson, S. J., Levin, S. D., and Perlmutter, R. M. Involvement of the protein tyrosine kinase p56lck in T cell signaling and thymocyte development. Adv. Immunol., 56: 151-178, 1994.
    • (1994) Adv. Immunol. , vol.56 , pp. 151-178
    • Anderson, S.J.1    Levin, S.D.2    Perlmutter, R.M.3
  • 8
    • 0035367576 scopus 로고    scopus 로고
    • Proximal protein tyrosine kinases in immunoreceptor signaling
    • Latour, S. and Veillette, A. Proximal protein tyrosine kinases in immunoreceptor signaling. Curr. Opin. Immunol., 13: 299-306, 2001.
    • (2001) Curr. Opin. Immunol. , vol.13 , pp. 299-306
    • Latour, S.1    Veillette, A.2
  • 10
    • 0027379547 scopus 로고
    • Protein tyrosine kinase p561ck controls allelic exclusion of T-cell receptor β-chain genes
    • Anderson, S. J., Levin, S. D., and Perlmutter, R. M. Protein tyrosine kinase p561ck controls allelic exclusion of T-cell receptor β-chain genes. Nature, 365: 552-554, 1993.
    • (1993) Nature , vol.365 , pp. 552-554
    • Anderson, S.J.1    Levin, S.D.2    Perlmutter, R.M.3
  • 11
    • 0027467796 scopus 로고
    • A dominant-negative transgene defines a role for p56lck in thymopoiesis
    • Levin, S. D., Anderson, S. J., Forbush, K. A., and Perlmutter, R. M. A dominant-negative transgene defines a role for p56lck in thymopoiesis. EMBO J., 12: 1671-1680, 1993.
    • (1993) EMBO J. , vol.12 , pp. 1671-1680
    • Levin, S.D.1    Anderson, S.J.2    Forbush, K.A.3    Perlmutter, R.M.4
  • 12
    • 0030293791 scopus 로고    scopus 로고
    • αβT cell development is abolished in mice lacking both Lck and Fyn protein tyrosine kinases
    • Van Oers, N. S., Lowin-Kropf, B., Finlay, D., Connolly, K., and Weiss, A. αβT cell development is abolished in mice lacking both Lck and Fyn protein tyrosine kinases. Immunity, 5: 429-436, 1996.
    • (1996) Immunity , vol.5 , pp. 429-436
    • Van Oers, N.S.1    Lowin-Kropf, B.2    Finlay, D.3    Connolly, K.4    Weiss, A.5
  • 13
    • 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., Hyman, R., and Sefton, B. M. 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: 1651-1656, 1993.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 1651-1656
    • Hurley, T.R.1    Hyman, R.2    Sefton, B.M.3
  • 14
    • 0025146562 scopus 로고
    • Structural diversity and evolution of human receptor-like protein tyrosine phosphatases
    • Krueger, N. X., Streuli, M., and Saito, H. Structural diversity and evolution of human receptor-like protein tyrosine phosphatases. EMBO J., 9: 3241-3252, 1990.
    • (1990) EMBO J. , vol.9 , pp. 3241-3252
    • Krueger, N.X.1    Streuli, M.2    Saito, H.3
  • 15
    • 0025277449 scopus 로고
    • Distinct functional roles of the two intracellular phosphatase like domains of the receptor-linked protein tyrosine phosphatases LCA and LAR. 1993
    • Streuli, M., Krueger, N. X., Thai, T., Tang, M., and Saito, H. Distinct functional roles of the two intracellular phosphatase like domains of the receptor-linked protein tyrosine phosphatases LCA and LAR. 1993. EMBO J., 9: 2399-2407, 1990.
    • (1990) EMBO J. , vol.9 , pp. 2399-2407
    • Streuli, M.1    Krueger, N.X.2    Thai, T.3    Tang, M.4    Saito, H.5
  • 16
    • 0024211451 scopus 로고
    • A new member of the immunoglobulin superfamily that has a cytoplasmic region homologous to the leukocyte common antigen
    • Streuli, M., Krueger, N. X., Hall, L. R., Schlossman, S. F., and Saito, H. A new member of the immunoglobulin superfamily that has a cytoplasmic region homologous to the leukocyte common antigen. J. Exp. Med., 168: 1523-1530, 1988.
    • (1988) J. Exp. Med. , vol.168 , pp. 1523-1530
    • Streuli, M.1    Krueger, N.X.2    Hall, L.R.3    Schlossman, S.F.4    Saito, H.5
  • 17
    • 0026583744 scopus 로고
    • Expression of the receptor-linked protein tyrosine phosphatase LAR: Proteolytic cleavage and shedding of the CAM-like extracellular region
    • Streuli, M., Krueger, N. X., Ariniello, P. D., Tang, M., Munro, J. M., Blattler, W. A., Adler, D. A., Disteche, C. M., and Saito, H. Expression of the receptor-linked protein tyrosine phosphatase LAR: proteolytic cleavage and shedding of the CAM-like extracellular region. EMBO J., 11: 897-907, 1992.
    • (1992) EMBO J. , vol.11 , pp. 897-907
    • Streuli, M.1    Krueger, N.X.2    Ariniello, P.D.3    Tang, M.4    Munro, J.M.5    Blattler, W.A.6    Adler, D.A.7    Disteche, C.M.8    Saito, H.9
  • 18
    • 0027520197 scopus 로고
    • Leukocyte common antigen-related receptor-linked tyrosine phosphatase. Regulation of mRNA expression
    • Longo, F. M., Martignetti, J. A., Le Beau, J. M., Zhang, J. S., Barnes, J. P., and Brosius, J. Leukocyte common antigen-related receptor-linked tyrosine phosphatase. Regulation of mRNA expression. J. Biol. Chem., 268: 26503-26511, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 26503-26511
    • Longo, F.M.1    Martignetti, J.A.2    Le Beau, J.M.3    Zhang, J.S.4    Barnes, J.P.5    Brosius, J.6
  • 19
    • 0028926584 scopus 로고
    • LAR tyrosine phosphatase receptor: Alternative splicing is preferential to the nervous system, coordinated with cell growth and generates novel isoforms containing extensive CAG repeats
    • Zhang, J. S. and Longo, F. M. LAR tyrosine phosphatase receptor: alternative splicing is preferential to the nervous system, coordinated with cell growth and generates novel isoforms containing extensive CAG repeats. J. Cell Biol., 128: 415-431, 1995.
    • (1995) J. Cell Biol. , vol.128 , pp. 415-431
    • Zhang, J.S.1    Longo, F.M.2
  • 20
    • 0027520197 scopus 로고
    • Leukocyte common antigen-related receptor-linked tyrosine phosphatase. Regulation of mRNA expression
    • Longo, F. M., Martignetti, J. A., Le-Beau, J. M., Zhang, J. S., Barnes, J. P., and Brosius, J. Leukocyte common antigen-related receptor-linked tyrosine phosphatase. Regulation of mRNA expression. J. Biol. Chem., 268: 26503-26511, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 26503-26511
    • Longo, F.M.1    Martignetti, J.A.2    Le-Beau, J.M.3    Zhang, J.S.4    Barnes, J.P.5    Brosius, J.6
  • 21
    • 0028926584 scopus 로고
    • LAR tyrosine phosphatase receptor: Alternative splicing is preferential to the nervous system, coordinated with cell growth and generates novel isoforms containing extensive CAG repeats
    • Zhang, J. S. and Longo, F. M. LAR tyrosine phosphatase receptor: alternative splicing is preferential to the nervous system, coordinated with cell growth and generates novel isoforms containing extensive CAG repeats. J. Cell Biol., 128: 415-431, 1995.
    • (1995) J. Cell Biol. , vol.128 , pp. 415-431
    • Zhang, J.S.1    Longo, F.M.2
  • 23
    • 0032171118 scopus 로고    scopus 로고
    • Developmental expression of the cell adhesion molecule-like protein tyrosine phosphatases LAR, RPTPδ and RPTPσ in the mouse
    • Schaapveld, R. Q., Schepens, J. T., Bachner, D., Attema, J., Wieringa, B., Jap, P. H., and Hendriks, W. J. Developmental expression of the cell adhesion molecule-like protein tyrosine phosphatases LAR, RPTPδ and RPTPσ in the mouse. Mech. Dev., 77: 59-62, 1998.
    • (1998) Mech. Dev. , vol.77 , pp. 59-62
    • Schaapveld, R.Q.1    Schepens, J.T.2    Bachner, D.3    Attema, J.4    Wieringa, B.5    Jap, P.H.6    Hendriks, W.J.7
  • 24
    • 0027992048 scopus 로고
    • Mutational analysis of proprotein processing, subunit association, and shedding of the LAR transmembrane protein tyrosine phosphatase
    • Serra-Pages, C., Saito, H., and Streuli, M. Mutational analysis of proprotein processing, subunit association, and shedding of the LAR transmembrane protein tyrosine phosphatase. J. Biol. Chem., 269: 23632-23641, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 23632-23641
    • Serra-Pages, C.1    Saito, H.2    Streuli, M.3
  • 25
    • 0027984009 scopus 로고
    • Genomic organization of the human LAR protein tyrosine phosphatase gene and alternative splicing in the extracellular fibronectin type-III domains
    • O'Grady, P., Krueger, N. X., Streuli, M., and Saito, H. Genomic organization of the human LAR protein tyrosine phosphatase gene and alternative splicing in the extracellular fibronectin type-III domains. J. Biol. Chem., 269: 25193-25199, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 25193-25199
    • O'Grady, P.1    Krueger, N.X.2    Streuli, M.3    Saito, H.4
  • 26
    • 0031031229 scopus 로고    scopus 로고
    • Deficient LAR expression decreases basal forebrain cholinergic neuronal size and hippocampal cholinergic innervation
    • Yeo, T. T., Yang, T., Massa, S. M., Zhang, J. S., Honkaniemi, J., Butcher, L. L., and Longo, F. M. Deficient LAR expression decreases basal forebrain cholinergic neuronal size and hippocampal cholinergic innervation. J. Neurosci. Res., 47: 348-360, 1997.
    • (1997) J. Neurosci. Res. , vol.47 , pp. 348-360
    • Yeo, T.T.1    Yang, T.2    Massa, S.M.3    Zhang, J.S.4    Honkaniemi, J.5    Butcher, L.L.6    Longo, F.M.7
  • 27
    • 0035857459 scopus 로고    scopus 로고
    • A decrease in size and number of basal forebrain cholinergic neurons is paralleled by diminished hippocampal cholinergic innervation in mice lacking leukocyte common antigen-related protein tyrosine phosphatase activity
    • Van Lieshout, E. M., Van der Heijden, I., Hendriks, W. J., and Van der Zee, C. E. A decrease in size and number of basal forebrain cholinergic neurons is paralleled by diminished hippocampal cholinergic innervation in mice lacking leukocyte common antigen-related protein tyrosine phosphatase activity. Neuroscience, 102: 833-841, 2001.
    • (2001) Neuroscience , vol.102 , pp. 833-841
    • Van Lieshout, E.M.1    Van der Heijden, I.2    Hendriks, W.J.3    Van der Zee, C.E.4
  • 29
    • 0035879191 scopus 로고    scopus 로고
    • The leukocyte common antigen-related protein tyrosine phosphatase receptor regulates regenerative neurite outgrowth in vivo
    • Xie, Y., Yeo T. T., Zhang, C., Yang, T., Tisi, M. A., Massa, S. M., and Longo, F. M. The leukocyte common antigen-related protein tyrosine phosphatase receptor regulates regenerative neurite outgrowth in vivo. J. Neurosci., 21: 5130-5138, 2001.
    • (2001) J. Neurosci. , vol.21 , pp. 5130-5138
    • Xie, Y.1    Yeo, T.T.2    Zhang, C.3    Yang, T.4    Tisi, M.A.5    Massa, S.M.6    Longo, F.M.7
  • 30
    • 0031594367 scopus 로고    scopus 로고
    • Transgenic mice deficient in the LAR protein-tyrosine phosphatase exhibit profound defects in glucose homeostasis
    • Ren, J. M., Li, P. M., Zhang, W. R., Sweet, L. J., Cline, G., Shulman, G. I., Livingston, J. N., and Goldstein, B. J. Transgenic mice deficient in the LAR protein-tyrosine phosphatase exhibit profound defects in glucose homeostasis. Diabetes, 47: 493-497, 1998.
    • (1998) Diabetes , vol.47 , pp. 493-497
    • Ren, J.M.1    Li, P.M.2    Zhang, W.R.3    Sweet, L.J.4    Cline, G.5    Shulman, G.I.6    Livingston, J.N.7    Goldstein, B.J.8
  • 31
    • 0026643477 scopus 로고
    • Insulin receptor protein-tyrosine phosphatases. Leukocyte common antigen-related phosphatase rapidly deactivates the insulin receptor kinase by preferential dephosphorylation of the receptor regulatory domain
    • Hashimoto, N., Feener, E. P., Zhang, W. R., and Goldstein, B. J. Insulin receptor protein-tyrosine phosphatases. Leukocyte common antigen-related phosphatase rapidly deactivates the insulin receptor kinase by preferential dephosphorylation of the receptor regulatory domain. J. Biol. Chem., 267: 13811-13814, 1992.
    • (1992) J. Biol. Chem. , vol.267 , pp. 13811-13814
    • Hashimoto, N.1    Feener, E.P.2    Zhang, W.R.3    Goldstein, B.J.4
  • 32
    • 0029018196 scopus 로고
    • Increased abundance of the receptor-type protein-tyrosine phosphatase LAR accounts for the elevated insulin receptor dephosphorylating activity in adipose tissue of obese human subjects
    • Ahmad, F., Considine, R. V., and Goldstein, B. J. Increased abundance of the receptor-type protein-tyrosine phosphatase LAR accounts for the elevated insulin receptor dephosphorylating activity in adipose tissue of obese human subjects. J. Clin. Invest., 95: 2806-2812, 1995.
    • (1995) J. Clin. Invest. , vol.95 , pp. 2806-2812
    • Ahmad, F.1    Considine, R.V.2    Goldstein, B.J.3
  • 33
    • 0030021432 scopus 로고    scopus 로고
    • The transmembrane protein-tyrosine phosphatase LAR modulates signaling by multiple receptor tyrosine kinases
    • Kulas, D. T., Goldstein, B. J., and Mooney, R. A. The transmembrane protein-tyrosine phosphatase LAR modulates signaling by multiple receptor tyrosine kinases. J. Biol. Chem., 271: 748-754, 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 748-754
    • Kulas, D.T.1    Goldstein, B.J.2    Mooney, R.A.3
  • 34
    • 0035937777 scopus 로고    scopus 로고
    • Differential effects of leukocyte common antigen-related protein on biochemical and biological activities of RET-MEN2A and RET-MEN2B mutant proteins
    • Qiao, S., Iwashita, T., Furukawa, T., Yamamoto, M., Sobue, G., and Takahashi, M. Differential effects of leukocyte common antigen-related protein on biochemical and biological activities of RET-MEN2A and RET-MEN2B mutant proteins. J. Biol. Chem., 276: 9460-9467, 2001.
    • (2001) J. Biol. Chem. , vol.276 , pp. 9460-9467
    • Qiao, S.1    Iwashita, T.2    Furukawa, T.3    Yamamoto, M.4    Sobue, G.5    Takahashi, M.6
  • 35
    • 0035156407 scopus 로고    scopus 로고
    • Distinct functions of the two protein tyrosine phosphatase domains of LAR (leukocyte common antigen-related) on tyrosine dephosphorylation of insulin receptor
    • Tsujikawa, K., Kawakami, N., Uchino, Y., Ichijo, T., Furukawa, T., Saito, H., and Yamamoto, H. Distinct functions of the two protein tyrosine phosphatase domains of LAR (leukocyte common antigen-related) on tyrosine dephosphorylation of insulin receptor. Mol. Endocrinol., 15: 271-280, 2001.
    • (2001) Mol. Endocrinol. , vol.15 , pp. 271-280
    • Tsujikawa, K.1    Kawakami, N.2    Uchino, Y.3    Ichijo, T.4    Furukawa, T.5    Saito, H.6    Yamamoto, H.7
  • 36
    • 15444357989 scopus 로고    scopus 로고
    • The laminin-nidogen complex is a ligand for a specific splice isoform of the transmembrane protein tyrosine phosphatase LAR
    • O'Grady, P., Thai, T. C., and Saito, H. The laminin-nidogen complex is a ligand for a specific splice isoform of the transmembrane protein tyrosine phosphatase LAR. J. Cell Biol., 141: 1675-1684, 1998.
    • (1998) J. Cell Biol. , vol.141 , pp. 1675-1684
    • O'Grady, P.1    Thai, T.C.2    Saito, H.3
  • 37
    • 0035077088 scopus 로고    scopus 로고
    • Within the hemopoietic system, LAR phosphatase is a T cell lineage-specific adhesion receptor-like protein whose phosphatase activity appears dispensable for T cell development, repertoire selection and function
    • Terszowski, G., JanKowski, A., Hendriks, W. J. A., Rolink, A., and Kisielow, P. Within the hemopoietic system, LAR phosphatase is a T cell lineage-specific adhesion receptor-like protein whose phosphatase activity appears dispensable for T cell development, repertoire selection and function. Eur. J. Immunol., 31: 832-840, 2001.
    • (2001) Eur. J. Immunol. , vol.31 , pp. 832-840
    • Terszowski, G.1    JanKowski, A.2    Hendriks, W.J.A.3    Rolink, A.4    Kisielow, P.5
  • 38
    • 0027997103 scopus 로고
    • Specific interaction of the CD45 protein-tyrosine phosphatase with tyrosine-phosphorylated CD3 ζ chain
    • Furukawa, T., Itoh, M., Krueger, N. X., Streuli, M., and Saito, H. Specific interaction of the CD45 protein-tyrosine phosphatase with tyrosine-phosphorylated CD3 ζ chain. Proc. Natl. Acad. Sci. USA, 91: 10928-10932, 1994.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10928-10932
    • Furukawa, T.1    Itoh, M.2    Krueger, N.X.3    Streuli, M.4    Saito, H.5
  • 39
    • 0024751217 scopus 로고
    • Expression of a novel form of the fyn proto-oncogene in hematopoietic cells
    • Cooke, M. P. and Perlmutter, R. M. Expression of a novel form of the fyn proto-oncogene in hematopoietic cells. New Biol., 1: 66-74, 1989.
    • (1989) New Biol. , vol.1 , pp. 66-74
    • Cooke, M.P.1    Perlmutter, R.M.2
  • 40
    • 0033200308 scopus 로고    scopus 로고
    • Positive and negative regulation of Src-family membrane kinases by CD45
    • Thomas, M. L. and Brown, E. J. Positive and negative regulation of Src-family membrane kinases by CD45. Immunol. Today, 20: 406-411, 1999.
    • (1999) Immunol. Today , vol.20 , pp. 406-411
    • Thomas, M.L.1    Brown, E.J.2
  • 42
    • 0029864147 scopus 로고    scopus 로고
    • CD45-null transgenic mice reveal a positive regulatory role for CD45 in early thymocyte development, in the selection of CD4+CD8+ thymocytes, and B cell maturation
    • Byth, K. F., Conroy, L. A., Howlett, S., Smith, A. J., May, J., Alexander, D. R., and Holmes, N. CD45-null transgenic mice reveal a positive regulatory role for CD45 in early thymocyte development, in the selection of CD4+CD8+ thymocytes, and B cell maturation. J. Exp. Med., 183: 1707-1718, 1996.
    • (1996) J. Exp. Med. , vol.183 , pp. 1707-1718
    • Byth, K.F.1    Conroy, L.A.2    Howlett, S.3    Smith, A.J.4    May, J.5    Alexander, D.R.6    Holmes, N.7
  • 43
    • 0026077561 scopus 로고
    • Adhesion of immature thymocytes to thymic stromal cells through fibronectin molecule and its significance for the induction of thymocyte differentiation
    • Utsumi, K., Sawada, M., Narumiya, S., Nagamine, J., Sakata, T., Iwagami, S., Kita, Y., Teraoka, H., Hirano, H., and Ogata, M. Adhesion of immature thymocytes to thymic stromal cells through fibronectin molecule and its significance for the induction of thymocyte differentiation. Proc. Natl. Acad. Sci. USA, 88: 5685-5689, 1991.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 5685-5689
    • Utsumi, K.1    Sawada, M.2    Narumiya, S.3    Nagamine, J.4    Sakata, T.5    Iwagami, S.6    Kita, Y.7    Teraoka, H.8    Hirano, H.9    Ogata, M.10
  • 44
    • 0028858128 scopus 로고
    • Differential expression of integrins on human thymocyte subpopulations
    • Mojcik, C. K., Salomon, D. R., Chang, A. C., and Shevach. E. M. Differential expression of integrins on human thymocyte subpopulations. Blood, 86: 4206-4217, 1995.
    • (1995) Blood , vol.86 , pp. 4206-4217
    • Mojcik, C.K.1    Salomon, D.R.2    Chang, A.C.3    Shevach, E.M.4
  • 45
    • 0028342629 scopus 로고
    • Insulin stimulates the phosphorylation of Tyr538 and the catalytic activity of PTP1C, a protein tyrosine phosphatase with Src homology-2 domains
    • Uchida, T., Matozaki, T., Noguchi, T., Yamao, T., Horita, K., Suzuki, T., Fujioka, Y., Sakamoto, C., and Kasuga, M. Insulin stimulates the phosphorylation of Tyr538 and the catalytic activity of PTP1C, a protein tyrosine phosphatase with Src homology-2 domains. J. Biol. Chem., 269: 12220-12228, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 12220-12228
    • Uchida, T.1    Matozaki, T.2    Noguchi, T.3    Yamao, T.4    Horita, K.5    Suzuki, T.6    Fujioka, Y.7    Sakamoto, C.8    Kasuga, M.9
  • 47
    • 0028295810 scopus 로고
    • Lck-dependent tyrosyl phosphorylation of the phosphotyrosine phosphatase SH-PTPI in murine T cells
    • Lorenz, U., Ravichandran, K. S., Pei, D., Walsh, C. T., Burakoff, S. J., and Neel, B. G. Lck-dependent tyrosyl phosphorylation of the phosphotyrosine phosphatase SH-PTPI in murine T cells. Mol. Cell. Biol., 14: 1824-1834, 1994.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 1824-1834
    • Lorenz, U.1    Ravichandran, K.S.2    Pei, D.3    Walsh, C.T.4    Burakoff, S.J.5    Neel, B.G.6
  • 48
    • 0033617445 scopus 로고    scopus 로고
    • Fyn kinase-directed activation of SH2 domain-containing protein-tyrosine phosphatase SHP-2 by Gi protein-coupled receptors in Madin-Darby canine kidney cells
    • Tang, H., Zhao, Z. J., Huang, X. Y., Landon, E. J., and Inagami, T. Fyn kinase-directed activation of SH2 domain-containing protein-tyrosine phosphatase SHP-2 by Gi protein-coupled receptors in Madin-Darby canine kidney cells. J. Biol. Chem., 274: 12401-12407, 1999.
    • (1999) J. Biol. Chem. , vol.274 , pp. 12401-12407
    • Tang, H.1    Zhao, Z.J.2    Huang, X.Y.3    Landon, E.J.4    Inagami, T.5
  • 51
    • 0033082439 scopus 로고    scopus 로고
    • The tyrosine kinase Ab1 and its substrate enabled collaborate with the receptor phosphatase Dlar to control motor axon guidance
    • Wills, Z., Bateman, J., Korey, C. A., Comer, A., and Van Vactor, D. The tyrosine kinase Ab1 and its substrate enabled collaborate with the receptor phosphatase Dlar to control motor axon guidance. Neuron, 22: 301-312, 1999.
    • (1999) Neuron , vol.22 , pp. 301-312
    • Wills, Z.1    Bateman, J.2    Korey, C.A.3    Comer, A.4    Van Vactor, D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.