메뉴 건너뛰기




Volumn 335, Issue 1, 2005, Pages 232-239

Pleiotrophin stimulates tyrosine phosphorylation of β-adducin through inactivation of the transmembrane receptor protein tyrosine phosphatase β/ζ

Author keywords

Adducin; Pleiotrophin; Receptor protein tyrosine phosphatase

Indexed keywords

ADDUCIN; BETA ADDUCIN; BETA CATENIN; CYTOSKELETON PROTEIN; MEMBRANE PROTEIN; PHOSPHATASE; PLEIOTROPHIN; PROTEIN TYROSINE KINASE; RECEPTOR PROTEIN; TYROSINE PHOSPHATASE BETA; TYROSINE PHOSPHATASE ZETA; UNCLASSIFIED DRUG;

EID: 25144467994     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2005.07.060     Document Type: Article
Times cited : (67)

References (54)
  • 1
    • 0024801855 scopus 로고
    • A novel 17 kD heparin-binding growth factor (HBGF-8) in bovine uterus: Purification and N-terminal amino acid sequence
    • P.G. Milner, Y.S. Li, R.M. Hoffman, C.M. Kodner, N.R. Siegel, and T.F. Deuel A novel 17 kD heparin-binding growth factor (HBGF-8) in bovine uterus: purification and N-terminal amino acid sequence Biochem. Biophys. Res. Commun. 165 1989 1096 1103
    • (1989) Biochem. Biophys. Res. Commun. , vol.165 , pp. 1096-1103
    • Milner, P.G.1    Li, Y.S.2    Hoffman, R.M.3    Kodner, C.M.4    Siegel, N.R.5    Deuel, T.F.6
  • 2
    • 0024317792 scopus 로고
    • An 18-kd heparin-binding protein of developing brain that is distinct from fibroblast growth factors
    • H. Rauvala An 18-kd heparin-binding protein of developing brain that is distinct from fibroblast growth factors Embo J. 8 1989 2933 2941
    • (1989) Embo J. , vol.8 , pp. 2933-2941
    • Rauvala, H.1
  • 3
    • 0025615372 scopus 로고
    • Cloning and expression of a developmentally regulated protein that induces mitogenic and neurite outgrowth activity
    • Y.S. Li, P.G. Milner, A.K. Chauhan, M.A. Watson, R.M. Hoffman, C.M. Kodner, J. Milbrandt, and T.F. Deuel Cloning and expression of a developmentally regulated protein that induces mitogenic and neurite outgrowth activity Science 250 1990 1690 1694
    • (1990) Science , vol.250 , pp. 1690-1694
    • Li, Y.S.1    Milner, P.G.2    Chauhan, A.K.3    Watson, M.A.4    Hoffman, R.M.5    Kodner, C.M.6    Milbrandt, J.7    Deuel, T.F.8
  • 4
    • 0348013060 scopus 로고    scopus 로고
    • HB-GAM/Pleiotrophin and midkine are differently expressed and distributed during retinoic acid-induced neural differentiation of P19 cells
    • N. Brunet-de Carvalho, D. Raulais, H. Rauvala, B. Souttou, and M. Vigny HB-GAM/Pleiotrophin and midkine are differently expressed and distributed during retinoic acid-induced neural differentiation of P19 cells Growth Factors 21 2003 139 149
    • (2003) Growth Factors , vol.21 , pp. 139-149
    • Brunet-De Carvalho, N.1    Raulais, D.2    Rauvala, H.3    Souttou, B.4    Vigny, M.5
  • 7
    • 0032525099 scopus 로고    scopus 로고
    • Upregulation of pleiotrophin gene expression in developing microvasculature, macrophages, and astrocytes after acute ischemic brain injury
    • H.J. Yeh, Y.Y. He, J. Xu, C.Y. Hsu, and T.F. Deuel Upregulation of pleiotrophin gene expression in developing microvasculature, macrophages, and astrocytes after acute ischemic brain injury J. Neurosci. 18 1998 3699 3707
    • (1998) J. Neurosci. , vol.18 , pp. 3699-3707
    • Yeh, H.J.1    He, Y.Y.2    Xu, J.3    Hsu, C.Y.4    Deuel, T.F.5
  • 8
    • 0032951527 scopus 로고    scopus 로고
    • Pleiotrophin and midkine, a family of mitogenic and angiogenic heparin-binding growth and differentiation factors
    • N. Zhang, and T.F. Deuel Pleiotrophin and midkine, a family of mitogenic and angiogenic heparin-binding growth and differentiation factors Curr. Opin. Hematol. 6 1999 44 50
    • (1999) Curr. Opin. Hematol. , vol.6 , pp. 44-50
    • Zhang, N.1    Deuel, T.F.2
  • 9
    • 0027396677 scopus 로고
    • Pleiotrophin transforms NIH 3T3 cells and induces tumors in nude mice
    • A.K. Chauhan, Y.S. Li, and T.F. Deuel Pleiotrophin transforms NIH 3T3 cells and induces tumors in nude mice Proc. Natl. Acad. Sci. USA 90 1993 679 682
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 679-682
    • Chauhan, A.K.1    Li, Y.S.2    Deuel, T.F.3
  • 11
    • 20744438808 scopus 로고    scopus 로고
    • Midkine regulates pleiotrophin organ-specific gene expression: Evidence for transcriptional regulation and functional redundancy within the pleiotrophin/midkine developmental gene family
    • G. Herradon, L. Ezquerra, T. Nguyen, I. Silos-Santiago, and T.F. Deuel Midkine regulates pleiotrophin organ-specific gene expression: evidence for transcriptional regulation and functional redundancy within the pleiotrophin/midkine developmental gene family Biochem. Biophys. Res. Commun. 333 2005 714 721
    • (2005) Biochem. Biophys. Res. Commun. , vol.333 , pp. 714-721
    • Herradon, G.1    Ezquerra, L.2    Nguyen, T.3    Silos-Santiago, I.4    Deuel, T.F.5
  • 12
    • 0029805056 scopus 로고    scopus 로고
    • Localization of pleiotrophin and its mRNA in subpopulations of neurons and their corresponding axonal tracts suggests important roles in neural-glial interactions during development and in maturity
    • I. Silos-Santiago, H.J. Yeh, M.A. Gurrieri, R.P. Guillerman, Y.S. Li, J. Wolf, W. Snider, and T.F. Deuel Localization of pleiotrophin and its mRNA in subpopulations of neurons and their corresponding axonal tracts suggests important roles in neural-glial interactions during development and in maturity J. Neurobiol. 31 1996 283 296
    • (1996) J. Neurobiol. , vol.31 , pp. 283-296
    • Silos-Santiago, I.1    Yeh, H.J.2    Gurrieri, M.A.3    Guillerman, R.P.4    Li, Y.S.5    Wolf, J.6    Snider, W.7    Deuel, T.F.8
  • 14
    • 0026728088 scopus 로고
    • Cellular distribution of the new growth factor pleiotrophin (HB-GAM) mRNA in developing and adult rat tissues
    • J.M. Vanderwinden, P. Mailleux, S.N. Schiffmann, and J.J. Vanderhaeghen Cellular distribution of the new growth factor pleiotrophin (HB-GAM) mRNA in developing and adult rat tissues Anat. Embryol. (Berl) 186 1992 387 406
    • (1992) Anat. Embryol. (Berl) , vol.186 , pp. 387-406
    • Vanderwinden, J.M.1    Mailleux, P.2    Schiffmann, S.N.3    Vanderhaeghen, J.J.4
  • 15
    • 0027076643 scopus 로고
    • Pleiotrophin stimulates fibroblasts and endothelial and epithelial cells and is expressed in human cancer
    • W. Fang, N. Hartmann, D.T. Chow, A.T. Riegel, and A. Wellstein Pleiotrophin stimulates fibroblasts and endothelial and epithelial cells and is expressed in human cancer J. Biol. Chem. 267 1992 25889 25897
    • (1992) J. Biol. Chem. , vol.267 , pp. 25889-25897
    • Fang, W.1    Hartmann, N.2    Chow, D.T.3    Riegel, A.T.4    Wellstein, A.5
  • 16
    • 0029006173 scopus 로고
    • Effect of heparin on bovine epithelial lens cell proliferation induced by heparin affin regulatory peptide
    • J. Delbe, F. Vacherot, K. Laaroubi, D. Barritault, and J. Courty Effect of heparin on bovine epithelial lens cell proliferation induced by heparin affin regulatory peptide J. Cell Physiol. 164 1995 47 54
    • (1995) J. Cell Physiol. , vol.164 , pp. 47-54
    • Delbe, J.1    Vacherot, F.2    Laaroubi, K.3    Barritault, D.4    Courty, J.5
  • 18
    • 0033535988 scopus 로고    scopus 로고
    • A dominant-negative pleiotrophin mutant introduced by homologous recombination leads to germ-cell apoptosis in male mice
    • N. Zhang, H.J. Yeh, R. Zhong, Y.S. Li, and T.F. Deuel A dominant-negative pleiotrophin mutant introduced by homologous recombination leads to germ-cell apoptosis in male mice Proc. Natl. Acad. Sci. USA 96 1999 6734 6738
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 6734-6738
    • Zhang, N.1    Yeh, H.J.2    Zhong, R.3    Li, Y.S.4    Deuel, T.F.5
  • 19
    • 20544469178 scopus 로고    scopus 로고
    • Midkine, a newly discovered regulator of the renin-angiotensin pathway in mouse aorta: Significance of the pleiotrophin/midkine developmental gene family in angiotensin II signaling
    • L. Ezquerra, G. Herradon, T. Nguyen, I. Silos-Santiago, and T.F. Deuel Midkine, a newly discovered regulator of the renin-angiotensin pathway in mouse aorta: significance of the pleiotrophin/midkine developmental gene family in angiotensin II signaling Biochem. Biophys. Res. Commun. 333 2005 636 643
    • (2005) Biochem. Biophys. Res. Commun. , vol.333 , pp. 636-643
    • Ezquerra, L.1    Herradon, G.2    Nguyen, T.3    Silos-Santiago, I.4    Deuel, T.F.5
  • 21
    • 0030878183 scopus 로고    scopus 로고
    • Human breast cancer growth inhibited in vivo by a dominant negative pleiotrophin mutant
    • N. Zhang, R. Zhong, Z.Y. Wang, and T.F. Deuel Human breast cancer growth inhibited in vivo by a dominant negative pleiotrophin mutant J. Biol. Chem. 272 1997 16733 16736
    • (1997) J. Biol. Chem. , vol.272 , pp. 16733-16736
    • Zhang, N.1    Zhong, R.2    Wang, Z.Y.3    Deuel, T.F.4
  • 22
    • 2642666505 scopus 로고    scopus 로고
    • Differential expression and biological activity of the heparin-binding growth-associated molecule (HB-GAM) in lung cancer cell lines
    • R. Jager, K. Noll, K. Havemann, K.H. Pfluger, C. Knabbe, H. Rauvala, and G. Zugmaier Differential expression and biological activity of the heparin-binding growth-associated molecule (HB-GAM) in lung cancer cell lines Int. J. Cancer 73 1997 537 543
    • (1997) Int. J. Cancer , vol.73 , pp. 537-543
    • Jager, R.1    Noll, K.2    Havemann, K.3    Pfluger, K.H.4    Knabbe, C.5    Rauvala, H.6    Zugmaier, G.7
  • 23
    • 0036308840 scopus 로고    scopus 로고
    • Significance of the expression of the growth factor pleiotrophin in pancreatic cancer patients
    • H.J. Klomp, O. Zernial, S. Flachmann, A. Wellstein, and H. Juhl Significance of the expression of the growth factor pleiotrophin in pancreatic cancer patients Clin. Cancer Res. 8 2002 823 827
    • (2002) Clin. Cancer Res. , vol.8 , pp. 823-827
    • Klomp, H.J.1    Zernial, O.2    Flachmann, S.3    Wellstein, A.4    Juhl, H.5
  • 24
    • 0027985605 scopus 로고
    • The potential role of the heparin-binding growth factor pleiotrophin in breast cancer
    • A.T. Riegel, and A. Wellstein The potential role of the heparin-binding growth factor pleiotrophin in breast cancer Breast Cancer Res. Treat 31 1994 309 314
    • (1994) Breast Cancer Res. Treat , vol.31 , pp. 309-314
    • Riegel, A.T.1    Wellstein, A.2
  • 25
    • 0028146336 scopus 로고
    • Ribozyme-targeting elucidates a direct role of pleiotrophin in tumor growth
    • F. Czubayko, A.T. Riegel, and A. Wellstein Ribozyme-targeting elucidates a direct role of pleiotrophin in tumor growth J. Biol. Chem. 269 1994 21358 21363
    • (1994) J. Biol. Chem. , vol.269 , pp. 21358-21363
    • Czubayko, F.1    Riegel, A.T.2    Wellstein, A.3
  • 26
    • 0029855988 scopus 로고    scopus 로고
    • Melanoma angiogenesis and metastasis modulated by ribozyme targeting of the secreted growth factor pleiotrophin
    • F. Czubayko, A.M. Schulte, G.J. Berchem, and A. Wellstein Melanoma angiogenesis and metastasis modulated by ribozyme targeting of the secreted growth factor pleiotrophin Proc. Natl. Acad. Sci. USA 93 1996 14753 14758
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 14753-14758
    • Czubayko, F.1    Schulte, A.M.2    Berchem, G.J.3    Wellstein, A.4
  • 27
    • 0034646459 scopus 로고    scopus 로고
    • Pleiotrophin signals increased tyrosine phosphorylation of beta beta-catenin through inactivation of the intrinsic catalytic activity of the receptor-type protein tyrosine phosphatase beta/zeta
    • K. Meng, A. Rodriguez-Pena, T. Dimitrov, W. Chen, M. Yamin, M. Noda, and T.F. Deuel Pleiotrophin signals increased tyrosine phosphorylation of beta beta-catenin through inactivation of the intrinsic catalytic activity of the receptor-type protein tyrosine phosphatase beta/zeta Proc. Natl. Acad. Sci. USA 97 2000 2603 2608
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 2603-2608
    • Meng, K.1    Rodriguez-Pena, A.2    Dimitrov, T.3    Chen, W.4    Yamin, M.5    Noda, M.6    Deuel, T.F.7
  • 29
    • 0028109453 scopus 로고
    • Multiple receptor-like protein tyrosine phosphatases in the form of chondroitin sulfate proteoglycan
    • N. Maeda, H. Hamanaka, T. Shintani, T. Nishiwaki, and M. Noda Multiple receptor-like protein tyrosine phosphatases in the form of chondroitin sulfate proteoglycan FEBS Lett. 354 1994 67 70
    • (1994) FEBS Lett. , vol.354 , pp. 67-70
    • Maeda, N.1    Hamanaka, H.2    Shintani, T.3    Nishiwaki, T.4    Noda, M.5
  • 30
    • 0026754494 scopus 로고
    • A human transmembrane protein-tyrosine-phosphatase, PTP zeta, is expressed in brain and has an N-terminal receptor domain homologous to carbonic anhydrases
    • N.X. Krueger, and H. Saito A human transmembrane protein-tyrosine- phosphatase, PTP zeta, is expressed in brain and has an N-terminal receptor domain homologous to carbonic anhydrases Proc. Natl. Acad. Sci. USA 89 1992 7417 7421
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 7417-7421
    • Krueger, N.X.1    Saito, H.2
  • 31
    • 0033617313 scopus 로고    scopus 로고
    • A receptor-like protein-tyrosine phosphatase PTPzeta/RPTPbeta binds a heparin-binding growth factor midkine. Involvement of arginine 78 of midkine in the high affinity binding to PTPzeta
    • N. Maeda, K. Ichihara-Tanaka, T. Kimura, K. Kadomatsu, T. Muramatsu, and M. Noda A receptor-like protein-tyrosine phosphatase PTPzeta/RPTPbeta binds a heparin-binding growth factor midkine. Involvement of arginine 78 of midkine in the high affinity binding to PTPzeta J. Biol. Chem. 274 1999 12474 12479
    • (1999) J. Biol. Chem. , vol.274 , pp. 12474-12479
    • Maeda, N.1    Ichihara-Tanaka, K.2    Kimura, T.3    Kadomatsu, K.4    Muramatsu, T.5    Noda, M.6
  • 32
    • 0031970446 scopus 로고    scopus 로고
    • Multi-ligand interactions with receptor-like protein tyrosine phosphatase beta: Implications for intercellular signaling
    • E. Peles, J. Schlessinger, and M. Grumet Multi-ligand interactions with receptor-like protein tyrosine phosphatase beta: implications for intercellular signaling Trends Biochem. Sci. 23 1998 121 124
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 121-124
    • Peles, E.1    Schlessinger, J.2    Grumet, M.3
  • 34
    • 0031890646 scopus 로고    scopus 로고
    • Characterization and developmental regulation of proteoglycan-type protein tyrosine phosphatase zeta/RPTPbeta isoforms
    • T. Nishiwaki, N. Maeda, and M. Noda Characterization and developmental regulation of proteoglycan-type protein tyrosine phosphatase zeta/RPTPbeta isoforms J. Biochem. (Tokyo) 123 1998 458 467
    • (1998) J. Biochem. (Tokyo) , vol.123 , pp. 458-467
    • Nishiwaki, T.1    Maeda, N.2    Noda, M.3
  • 35
    • 0028988519 scopus 로고
    • Purification, characterization and developmental expression of a brain-specific chondroitin sulfate proteoglycan, 6B4 proteoglycan/phosphacan
    • N. Maeda, H. Hamanaka, A. Oohira, and M. Noda Purification, characterization and developmental expression of a brain-specific chondroitin sulfate proteoglycan, 6B4 proteoglycan/phosphacan Neuroscience 67 1995 23 35
    • (1995) Neuroscience , vol.67 , pp. 23-35
    • Maeda, N.1    Hamanaka, H.2    Oohira, A.3    Noda, M.4
  • 36
    • 0031460029 scopus 로고    scopus 로고
    • PDZ domain proteins: Scaffolds for signaling complexes
    • R. Ranganathan, and E.M. Ross PDZ domain proteins: scaffolds for signaling complexes Curr. Biol. 7 1997 R770 R773
    • (1997) Curr. Biol. , vol.7
    • Ranganathan, R.1    Ross, E.M.2
  • 37
    • 0029759927 scopus 로고    scopus 로고
    • Structural basis for inhibition of receptor protein-tyrosine phosphatase-alpha by dimerization
    • A.M. Bilwes, J. den Hertog, T. Hunter, and J.P. Noel Structural basis for inhibition of receptor protein-tyrosine phosphatase-alpha by dimerization Nature 382 1996 555 559
    • (1996) Nature , vol.382 , pp. 555-559
    • Bilwes, A.M.1    Den Hertog, J.2    Hunter, T.3    Noel, J.P.4
  • 38
  • 39
    • 0034987934 scopus 로고    scopus 로고
    • Tyrosine phosphorylation translocates beta-catenin from cell-cell interface to the cytoplasm, but does not significantly enhance the LEF-1-dependent transactivating function
    • K. Kim, and K.Y. Lee Tyrosine phosphorylation translocates beta-catenin from cell-cell interface to the cytoplasm, but does not significantly enhance the LEF-1-dependent transactivating function Cell Biol. Int. 25 2001 421 427
    • (2001) Cell Biol. Int. , vol.25 , pp. 421-427
    • Kim, K.1    Lee, K.Y.2
  • 40
    • 0027507028 scopus 로고
    • Loss of epithelial differentiation and gain of invasiveness correlates with tyrosine phosphorylation of the E-cadherin/beta-catenin complex in cells transformed with a temperature-sensitive v-SRC gene
    • J. Behrens, L. Vakaet, R. Friis, E. Winterhager, F. Van Roy, M.M. Mareel, and W. Birchmeier Loss of epithelial differentiation and gain of invasiveness correlates with tyrosine phosphorylation of the E-cadherin/beta-catenin complex in cells transformed with a temperature-sensitive v-SRC gene J. Cell Biol. 120 1993 757 766
    • (1993) J. Cell Biol. , vol.120 , pp. 757-766
    • Behrens, J.1    Vakaet, L.2    Friis, R.3    Winterhager, E.4    Van Roy, F.5    Mareel, M.M.6    Birchmeier, W.7
  • 41
    • 0031259778 scopus 로고    scopus 로고
    • Tyrosine phosphorylation and cadherin/catenin function
    • J.M. Daniel, and A.B. Reynolds Tyrosine phosphorylation and cadherin/catenin function Bioessays 19 1997 883 891
    • (1997) Bioessays , vol.19 , pp. 883-891
    • Daniel, J.M.1    Reynolds, A.B.2
  • 42
    • 0030773139 scopus 로고    scopus 로고
    • Identification of proteins that interact with a protein of interest: Applications of the yeast two-hybrid system
    • R.D. Gietz, B. Triggs-Raine, A. Robbins, K.C. Graham, and R.A. Woods Identification of proteins that interact with a protein of interest: applications of the yeast two-hybrid system Mol. Cell Biochem. 172 1997 67 79
    • (1997) Mol. Cell Biochem. , vol.172 , pp. 67-79
    • Gietz, R.D.1    Triggs-Raine, B.2    Robbins, A.3    Graham, K.C.4    Woods, R.A.5
  • 43
    • 0023245565 scopus 로고
    • Modulation of spectrin-actin assembly by erythrocyte adducin
    • K. Gardner, and V. Bennett Modulation of spectrin-actin assembly by erythrocyte adducin Nature 328 1987 359 362
    • (1987) Nature , vol.328 , pp. 359-362
    • Gardner, K.1    Bennett, V.2
  • 45
    • 0034958883 scopus 로고    scopus 로고
    • Spectrin and ankyrin-based pathways: Metazoan inventions for integrating cells into tissues
    • V. Bennett, and A.J. Baines Spectrin and ankyrin-based pathways: metazoan inventions for integrating cells into tissues Physiol. Rev. 81 2001 1353 1392
    • (2001) Physiol. Rev. , vol.81 , pp. 1353-1392
    • Bennett, V.1    Baines, A.J.2
  • 46
    • 0024552276 scopus 로고
    • The spectrin-actin junction of erythrocyte membrane skeletons
    • V. Bennett The spectrin-actin junction of erythrocyte membrane skeletons Biochim. Biophys. Acta 988 1989 107 121
    • (1989) Biochim. Biophys. Acta , vol.988 , pp. 107-121
    • Bennett, V.1
  • 47
    • 0029022939 scopus 로고
    • Adducin: A physical model with implications for function in assembly of spectrin-actin complexes
    • C.A. Hughes, and V. Bennett Adducin: a physical model with implications for function in assembly of spectrin-actin complexes J. Biol. Chem. 270 1995 18990 18996
    • (1995) J. Biol. Chem. , vol.270 , pp. 18990-18996
    • Hughes, C.A.1    Bennett, V.2
  • 48
    • 0033929093 scopus 로고    scopus 로고
    • Adducin: Structure, function and regulation
    • Y. Matsuoka, X. Li, and V. Bennett Adducin: structure, function and regulation Cell Mol. Life Sci. 57 2000 884 895
    • (2000) Cell Mol. Life Sci. , vol.57 , pp. 884-895
    • Matsuoka, Y.1    Li, X.2    Bennett, V.3
  • 49
    • 0025987170 scopus 로고
    • Primary structure and domain organization of human alpha and beta adducin
    • R. Joshi, D.M. Gilligan, E. Otto, T. McLaughlin, and V. Bennett Primary structure and domain organization of human alpha and beta adducin J. Cell Biol. 115 1991 665 675
    • (1991) J. Cell Biol. , vol.115 , pp. 665-675
    • Joshi, R.1    Gilligan, D.M.2    Otto, E.3    McLaughlin, T.4    Bennett, V.5
  • 50
    • 0035834638 scopus 로고    scopus 로고
    • Interaction of the SH2 domain of Fyn with a cytoskeletal protein, beta-adducin
    • T. Shima, N. Okumura, T. Takao, Y. Satomi, T. Yagi, M. Okada, and K. Nagai Interaction of the SH2 domain of Fyn with a cytoskeletal protein, beta-adducin J. Biol. Chem. 276 2001 42233 42240
    • (2001) J. Biol. Chem. , vol.276 , pp. 42233-42240
    • Shima, T.1    Okumura, N.2    Takao, T.3    Satomi, Y.4    Yagi, T.5    Okada, M.6    Nagai, K.7
  • 51
    • 0035810942 scopus 로고    scopus 로고
    • Identification of GIT1/Cat-1 as a substrate molecule of protein tyrosine phosphatase zeta /beta by the yeast substrate-trapping system
    • H. Kawachi, A. Fujikawa, N. Maeda, and M. Noda Identification of GIT1/Cat-1 as a substrate molecule of protein tyrosine phosphatase zeta /beta by the yeast substrate-trapping system Proc. Natl. Acad. Sci. USA 98 2001 6593 6598
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 6593-6598
    • Kawachi, H.1    Fujikawa, A.2    Maeda, N.3    Noda, M.4
  • 54
    • 0033529562 scopus 로고    scopus 로고
    • A tyrosine-phosphorylated protein that binds to an important regulatory region on the cool family of p21-activated kinase-binding proteins
    • S. Bagrodia, D. Bailey, Z. Lenard, M. Hart, J.L. Guan, R.T. Premont, S.J. Taylor, and R.A. Cerione A tyrosine-phosphorylated protein that binds to an important regulatory region on the cool family of p21-activated kinase-binding proteins J. Biol. Chem. 274 1999 22393 22400
    • (1999) J. Biol. Chem. , vol.274 , pp. 22393-22400
    • Bagrodia, S.1    Bailey, D.2    Lenard, Z.3    Hart, M.4    Guan, J.L.5    Premont, R.T.6    Taylor, S.J.7    Cerione, R.A.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.