메뉴 건너뛰기




Volumn 7, Issue 2, 1996, Pages 153-159

Signaling via the insulin-like growth factor-I receptor: Does it differ from insulin receptor signaling?

Author keywords

IGF 1 receptor; Insulin receptor; Signaling

Indexed keywords

INSULIN RECEPTOR; SOMATOMEDIN B; SOMATOMEDIN BINDING PROTEIN; SOMATOMEDIN C; SOMATOMEDIN C RECEPTOR;

EID: 0030207118     PISSN: 13596101     EISSN: None     Source Type: Journal    
DOI: 10.1016/1359-6101(96)00015-9     Document Type: Short Survey
Times cited : (157)

References (52)
  • 1
    • 0027953703 scopus 로고
    • Insulin action diabetogenes, and the cause of type II diabetes
    • 1. Kahn CR. Insulin action diabetogenes, and the cause of type II diabetes. Diabetes 1994, 43, 1066-1984.
    • (1994) Diabetes , vol.43 , pp. 1066-1984
    • Kahn, C.R.1
  • 2
    • 0024355048 scopus 로고
    • Insulin-like growth factors I and II. Peptide, messenger ribonucleic acid and gene structures, serum and tissue concentrations
    • 2. Daughaday WH, Rotwein P. Insulin-like growth factors I and II. Peptide, messenger ribonucleic acid and gene structures, serum and tissue concentrations. Endocr Rev 1989, 10, 68-91.
    • (1989) Endocr Rev , vol.10 , pp. 68-91
    • Daughaday, W.H.1    Rotwein, P.2
  • 3
    • 0028958031 scopus 로고
    • Insulin-like growth factors and their binding proteins: Biological actions
    • 3. Jones JJ, Clemmons DR. Insulin-like growth factors and their binding proteins: Biological actions. Endocr Rev 1995, 16, 3-18.
    • (1995) Endocr Rev , vol.16 , pp. 3-18
    • Jones, J.J.1    Clemmons, D.R.2
  • 4
    • 0028957113 scopus 로고
    • Molecular and cellular aspects of the insulin-like growth factor I receptor
    • 4. LeRoith D, Werner H, Beitner-Johnson D, Roberts Jr CT. Molecular and cellular aspects of the insulin-like growth factor I receptor. Endocr Rev 1995, 16, 143-163.
    • (1995) Endocr Rev , vol.16 , pp. 143-163
    • LeRoith, D.1    Werner, H.2    Beitner-Johnson, D.3    Roberts C.T., Jr.4
  • 5
    • 0023942517 scopus 로고
    • Growth factor receptor tyrosine kinases
    • 5. Yarden Y, Ullrich A. Growth factor receptor tyrosine kinases. Ann Rev Biochem 1988, 57, 443-478.
    • (1988) Ann Rev Biochem , vol.57 , pp. 443-478
    • Yarden, Y.1    Ullrich, A.2
  • 6
    • 0025343230 scopus 로고
    • Signal transduction by receptors with tyrosine kinase activity
    • 6. Ullrich A, Schlessinger J. Signal transduction by receptors with tyrosine kinase activity. Cell 1990, 61, 203-212.
    • (1990) Cell , vol.61 , pp. 203-212
    • Ullrich, A.1    Schlessinger, J.2
  • 8
    • 0027944978 scopus 로고
    • The insulin-like growth factor-I receptor. Structure, ligand binding mechanism and signal transduction
    • 8. De Meyts P, Wallach B, Christoffersen CT et al. The insulin-like growth factor-I receptor. Structure, ligand binding mechanism and signal transduction. Horm Res 1994, 42, 152-169.
    • (1994) Horm Res , vol.42 , pp. 152-169
    • De Meyts, P.1    Wallach, B.2    Christoffersen, C.T.3
  • 9
    • 0026558410 scopus 로고
    • Insulin dependence of murine lymphoid T-cell leukemia
    • 9. Pillemer G, Lugasi-Evgi H, Scharovski G et al. Insulin dependence of murine lymphoid T-cell leukemia. Int J Cancer 1992, 50, 80-85.
    • (1992) Int J Cancer , vol.50 , pp. 80-85
    • Pillemer, G.1    Lugasi-Evgi, H.2    Scharovski, G.3
  • 10
    • 0029135003 scopus 로고
    • New frontiers in insulin receptor substrate signaling
    • 10. Myers MG, White MF. New frontiers in insulin receptor substrate signaling. Trends Endocr Metab 1995, 6, 209-215.
    • (1995) Trends Endocr Metab , vol.6 , pp. 209-215
    • Myers, M.G.1    White, M.F.2
  • 11
    • 0028036698 scopus 로고
    • IRS-1 mediates PI-3′ kinase and p70s6k signaling during insulin, IGF-I and IL-4 stimulation
    • 11. Myers MG, Grammer TC, Wang LM et al. IRS-1 mediates PI-3′ kinase and p70S6k signaling during insulin, IGF-I and IL-4 stimulation. J Biol Chem 1994, 269, 28783-28789.
    • (1994) J Biol Chem , vol.269 , pp. 28783-28789
    • Myers, M.G.1    Grammer, T.C.2    Wang, L.M.3
  • 12
    • 0011172717 scopus 로고
    • Insulin structure and biosynthesis
    • Draznin B, Melmed S, LeRoith D, eds. New York, Alan R Liss Inc.
    • 12. Gold G. Insulin structure and biosynthesis. In Draznin B, Melmed S, LeRoith D, eds. Insulin Secretion. New York, Alan R Liss Inc., 1989, pp. 25-35.
    • (1989) Insulin Secretion , pp. 25-35
    • Gold, G.1
  • 13
    • 0026833451 scopus 로고
    • Structure and expression of the human insulin-like growth factor genes
    • 13. Sussenbach JS, Steenbergh PH, Holthuizen P. Structure and expression of the human insulin-like growth factor genes. Growth Regul 1992, 2, 1-9.
    • (1992) Growth Regul , vol.2 , pp. 1-9
    • Sussenbach, J.S.1    Steenbergh, P.H.2    Holthuizen, P.3
  • 14
    • 0021985413 scopus 로고
    • Human insulin receptor and its relationship to the tyrosine kinase family of oncogenes
    • 14. Ullrich A. Bell JR, Chen EY et al. Human insulin receptor and its relationship to the tyrosine kinase family of oncogenes. Nature 1985, 313, 756-759.
    • (1985) Nature , vol.313 , pp. 756-759
    • Ullrich, A.1    Bell, J.R.2    Chen, E.Y.3
  • 15
    • 0021924895 scopus 로고
    • The human insulin receptor cDNA: The structural basis for hormone-activated transmembrane signalling
    • 15. Ebina Y, Ellis L, Jarnagin K et al. The human insulin receptor cDNA: The structural basis for hormone-activated transmembrane signalling. Cell 1985, 40, 747-758.
    • (1985) Cell , vol.40 , pp. 747-758
    • Ebina, Y.1    Ellis, L.2    Jarnagin, K.3
  • 16
    • 0022800838 scopus 로고
    • Insulin-like growth factor I receptor primary structure: Comparison with insulin receptor suggests structural determinants that define functional specificity
    • 16. Ullrich A, Gray A, Tam AW et al. Insulin-like growth factor I receptor primary structure: comparison with insulin receptor suggests structural determinants that define functional specificity. EMBO J 1986, 5, 2503-2512.
    • (1986) EMBO J , vol.5 , pp. 2503-2512
    • Ullrich, A.1    Gray, A.2    Tam, A.W.3
  • 17
    • 0026674185 scopus 로고
    • Insulin-like growth factor I receptor gene structure
    • 17. Abbott AM, Beuno R, Pedrini MT et al. Insulin-like growth factor I receptor gene structure. J Biol Chem 1992, 267, 10759-10763.
    • (1992) J Biol Chem , vol.267 , pp. 10759-10763
    • Abbott, A.M.1    Beuno, R.2    Pedrini, M.T.3
  • 18
    • 0020407615 scopus 로고
    • Structural and functional homologies in the receptors for insulin and the insulin-like growth factors
    • 18. Czech M. Structural and functional homologies in the receptors for insulin and the insulin-like growth factors. Cell 1982, 31, 8-10.
    • (1982) Cell , vol.31 , pp. 8-10
    • Czech, M.1
  • 19
    • 0026642585 scopus 로고
    • Identification of determinants that confer ligand specificity on the insulin receptor
    • 19. Andersen AS, Kjedsen T, Wiberg FC et al. Identification of determinants that confer ligand specificity on the insulin receptor. J Biol Chem 1992, 267, 13681-13686.
    • (1992) J Biol Chem , vol.267 , pp. 13681-13686
    • Andersen, A.S.1    Kjedsen, T.2    Wiberg, F.C.3
  • 20
    • 0025828542 scopus 로고
    • The ligand specificities of the insulin receptor and the insulin-like growth factor-I receptor reside in different regions of a common binding site
    • 20. Kjedsen T, Andersen AS, Wibert FC et al. The ligand specificities of the insulin receptor and the insulin-like growth factor-I receptor reside in different regions of a common binding site. Proc Natl Acad Sci USA 1991, 88, 4404-4408.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 4404-4408
    • Kjedsen, T.1    Andersen, A.S.2    Wibert, F.C.3
  • 21
    • 0026038883 scopus 로고
    • Insulin and insulin-like growth factor-I binding specificity is determined by distinct regions of their cognate receptors
    • 21. Schumacher R, Mosthaf L, Schlessinger J et al. Insulin and insulin-like growth factor-I binding specificity is determined by distinct regions of their cognate receptors. J Biol Chem 1991, 266, 19288-19295.
    • (1991) J Biol Chem , vol.266 , pp. 19288-19295
    • Schumacher, R.1    Mosthaf, L.2    Schlessinger, J.3
  • 22
    • 0025275004 scopus 로고
    • Identification of a ligand-binding region of the human insulin receptor encoded by the second exon of the gene
    • 22. De Meyts P, Gu J-L, Shymko RM et al. Identification of a ligand-binding region of the human insulin receptor encoded by the second exon of the gene. Molec Endocr 1990, 4, 409-416.
    • (1990) Molec Endocr , vol.4 , pp. 409-416
    • De Meyts, P.1    Gu, J.-L.2    Shymko, R.M.3
  • 23
    • 0026042468 scopus 로고
    • A region of the insulin receptor important for ligand binding (residues 450-601) is recognized by patients' autoimmune antibodies and inhibitory monoclonal antibodies
    • 23. Zhang B, Roth RA, A region of the insulin receptor important for ligand binding (residues 450-601) is recognized by patients' autoimmune antibodies and inhibitory monoclonal antibodies. Proc Natl Acad Sci USA 1991, 88, 9858-9862.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 9858-9862
    • Zhang, B.1    Roth, R.A.2
  • 24
    • 0027471973 scopus 로고
    • Signaling competent receptor chimeras allow mapping of major insulin receptor binding domains determinants
    • 24. Schumacher R, Soos MA, Schlessinger J et al. Signaling competent receptor chimeras allow mapping of major insulin receptor binding domains determinants. J Biol Chem 1993, 268, 1087-1094.
    • (1993) J Biol Chem , vol.268 , pp. 1087-1094
    • Schumacher, R.1    Soos, M.A.2    Schlessinger, J.3
  • 25
    • 0028567976 scopus 로고
    • Chimeric receptors indicate that phenylalanine 39 is a major contributor to insulin specificity of the insulin receptor
    • 25. Kjeldsen T, Wiberg FC, Andersen AS. Chimeric receptors indicate that phenylalanine 39 is a major contributor to insulin specificity of the insulin receptor. J Biol Chem 1994, 269, 32942-32946.
    • (1994) J Biol Chem , vol.269 , pp. 32942-32946
    • Kjeldsen, T.1    Wiberg, F.C.2    Andersen, A.S.3
  • 26
    • 0029391379 scopus 로고
    • Role of the time factor in signaling specificity: Application to mitogenic and metabolic signaling by the insulin and insulin-like growth factor-I receptor tyrosine kinases
    • 26. De Meyts P, Christoffersen CT, Urso B et al. Role of the time factor in signaling specificity: Application to mitogenic and metabolic signaling by the insulin and insulin-like growth factor-I receptor tyrosine kinases. Metabolism 1995, 44, 2-11.
    • (1995) Metabolism , vol.44 , pp. 2-11
    • De Meyts, P.1    Christoffersen, C.T.2    Urso, B.3
  • 27
    • 0017224874 scopus 로고
    • Site-site interactions among insulin receptors: Characterization of the negative cooperativity
    • 27. De Meyts P, Bianco AR, Roth J. Site-site interactions among insulin receptors: Characterization of the negative cooperativity. J Biol Chem 1976, 251, 1877-1888.
    • (1976) J Biol Chem , vol.251 , pp. 1877-1888
    • De Meyts, P.1    Bianco, A.R.2    Roth, J.3
  • 28
    • 0027357339 scopus 로고
    • Insulin-like growth factor binding proteins
    • 28. Rechler MM. Insulin-like growth factor binding proteins. Vitam Horm 1993, 47, 1-114.
    • (1993) Vitam Horm , vol.47 , pp. 1-114
    • Rechler, M.M.1
  • 29
    • 0024916155 scopus 로고
    • Binding proteins for the insulin-like growth factors: Structure, regulation, and function
    • 29. Baxter RC, Martin JL. Binding proteins for the insulin-like growth factors: Structure, regulation, and function. Progr Growth Factor Res 1989, 1, 49-68.
    • (1989) Progr Growth Factor Res , vol.1 , pp. 49-68
    • Baxter, R.C.1    Martin, J.L.2
  • 30
    • 0028146822 scopus 로고
    • The structural basis of insulin and insulin-like growth factor-I (IGF-I) receptor binding and negative cooperativity, and its relevance to mitogenic versus metabolic signaling
    • 30. De Meyts P. The structural basis of insulin and insulin-like growth factor-I (IGF-I) receptor binding and negative cooperativity, and its relevance to mitogenic versus metabolic signaling. Diabetologia 1994, 37, S135-S138.
    • (1994) Diabetologia , vol.37
    • De Meyts, P.1
  • 31
    • 0026486878 scopus 로고
    • Sustained activation of the mitogen-activated protein (MAP) kinase cascade may be required for differentiation of PC12 cells. Comparison of the effects of nerve growth factor and epidermal growth factor
    • 31. Traverse S, Gomez N, Paterson H et al. Sustained activation of the mitogen-activated protein (MAP) kinase cascade may be required for differentiation of PC12 cells. Comparison of the effects of nerve growth factor and epidermal growth factor. Biochem J 1992, 288, 351-355.
    • (1992) Biochem J , vol.288 , pp. 351-355
    • Traverse, S.1    Gomez, N.2    Paterson, H.3
  • 32
    • 0027156503 scopus 로고
    • Co-regulation of the mitogen-activated protein kinase, extracellular signal-regulated kinase 1, and the 90 kDa ribsomal s6 kinase in PC12 cells. Distinct effects of the neurotrophic factor, nerve growth factor, and the mitogenic factor, epidermal growth factor
    • 32. Nguyen TT, Scimeca JC, Filloux C et al. Co-regulation of the mitogen-activated protein kinase, extracellular signal-regulated kinase 1, and the 90 kDa ribsomal S6 kinase in PC12 cells. Distinct effects of the neurotrophic factor, nerve growth factor, and the mitogenic factor, epidermal growth factor. J Biol Chem 1993, 268, 9803-9810.
    • (1993) J Biol Chem , vol.268 , pp. 9803-9810
    • Nguyen, T.T.1    Scimeca, J.C.2    Filloux, C.3
  • 33
    • 0028355734 scopus 로고
    • Comparison of the intracellular itineraries of insulin-like growth factor-I and insulin and their receptors in Rat-1 fibroblasts
    • 33. Zapf A, Hsu D, Olefsky JM. Comparison of the intracellular itineraries of insulin-like growth factor-I and insulin and their receptors in Rat-1 fibroblasts. Endocrinology 1994, 134, 2445-2452.
    • (1994) Endocrinology , vol.134 , pp. 2445-2452
    • Zapf, A.1    Hsu, D.2    Olefsky, J.M.3
  • 34
    • 0011171180 scopus 로고
    • Two alternatively spliced forms of the IGF-I receptor have distinct biological activities and hormone-induced internalization rates
    • 34. Condorelli G, Smith RJ. Two alternatively spliced forms of the IGF-I receptor have distinct biological activities and hormone-induced internalization rates. Exp Clin Endocr 1993, 101, 95-97.
    • (1993) Exp Clin Endocr , vol.101 , pp. 95-97
    • Condorelli, G.1    Smith, R.J.2
  • 35
    • 0028244050 scopus 로고
    • Two alternatively spliced forms of the human insulin-like growth factor I receptor have distinct biological activities and internalization kinetics
    • 35. Condorelli G, Bueno R, Smith R. Two alternatively spliced forms of the human insulin-like growth factor I receptor have distinct biological activities and internalization kinetics. J Biol Chem, 1994, 269, 8510-8516.
    • (1994) J Biol Chem , vol.269 , pp. 8510-8516
    • Condorelli, G.1    Bueno, R.2    Smith, R.3
  • 36
    • 0026573303 scopus 로고
    • How distinct are the insulin and insulin-like growth factor I signalling systems?
    • 36. Adamo M, Roberts Jr CT, Le Roith D. How distinct are the insulin and insulin-like growth factor I signalling systems? BioFactors 1992, 3, 151-157.
    • (1992) BioFactors , vol.3 , pp. 151-157
    • Adamo, M.1    Roberts C.T., Jr.2    Le Roith, D.3
  • 37
    • 0025900432 scopus 로고
    • Mutation of the two carboxyl-terminal tyrosines results in an insulin receptor with normal metabolic signalling by enhanced mitogenic signalling properties
    • 37. Takata Y, Webster NJG, Olefsky JM. Mutation of the two carboxyl-terminal tyrosines results in an insulin receptor with normal metabolic signalling by enhanced mitogenic signalling properties. J Biol Chem 1991, 266, 9135-9139.
    • (1991) J Biol Chem , vol.266 , pp. 9135-9139
    • Takata, Y.1    Webster, N.J.G.2    Olefsky, J.M.3
  • 38
    • 0025999981 scopus 로고
    • The carboxyl-terminal domain of the insulin receptor: Its potential role in growth promoting effects
    • 38. Baron V, Gautier N, Kaliman P, Dolais-Kitabgi D, Van Obberghen E. The carboxyl-terminal domain of the insulin receptor: Its potential role in growth promoting effects. Biochemistry 1991, 30, 9365-9370.
    • (1991) Biochemistry , vol.30 , pp. 9365-9370
    • Baron, V.1    Gautier, N.2    Kaliman, P.3    Dolais-Kitabgi, D.4    Van Obberghen, E.5
  • 39
    • 0024358801 scopus 로고
    • Differential signaling potential of insulin and IGF-I receptor cytoplasmic domains
    • 39. Lammers R, Gray A, Schlessinger J, Ullrich A. Differential signaling potential of insulin and IGF-I receptor cytoplasmic domains. EMBO J 1989, 8, 1369-1375.
    • (1989) EMBO J , vol.8 , pp. 1369-1375
    • Lammers, R.1    Gray, A.2    Schlessinger, J.3    Ullrich, A.4
  • 40
    • 0025189619 scopus 로고
    • Overexpression of the human insulin-like growth factor I receptor promotes ligand-dependent neoplastic transformation
    • 40. Kaleko M, Rutter WJ, Miller AD. Overexpression of the human insulin-like growth factor I receptor promotes ligand-dependent neoplastic transformation. Molec Cell Biol 1990, 10, 464-473.
    • (1990) Molec Cell Biol , vol.10 , pp. 464-473
    • Kaleko, M.1    Rutter, W.J.2    Miller, A.D.3
  • 41
    • 0030064571 scopus 로고
    • Tumorigenic and mitogenic capacities are reduced in transfected fibroblasts expressing mutant insulin-like growth factor (IGF)-I receptors. The role of tyrosine residues 1250, 1251 and 1316 in the carboxyl-terminus of the IGF-I receptor
    • 41. Blakesley VA, Kalebic T, Helman LJ et al. Tumorigenic and mitogenic capacities are reduced in transfected fibroblasts expressing mutant insulin-like growth factor (IGF)-I receptors. The role of tyrosine residues 1250, 1251 and 1316 in the carboxyl-terminus of the IGF-I receptor. Endocrinology 1995, 137, 410-417.
    • (1995) Endocrinology , vol.137 , pp. 410-417
    • Blakesley, V.A.1    Kalebic, T.2    Helman, L.J.3
  • 42
    • 0028157211 scopus 로고
    • The role of the IGF-I receptor in growth and transformation of mammalian cells
    • 42. Baserga R, Sell C, Porcu P, Rubini M. The role of the IGF-I receptor in growth and transformation of mammalian cells. Cell Proliferation 1994, 27, 63-71.
    • (1994) Cell Proliferation , vol.27 , pp. 63-71
    • Baserga, R.1    Sell, C.2    Porcu, P.3    Rubini, M.4
  • 43
    • 0027366338 scopus 로고
    • Simian virus 40 large tumor antigen is unable to transform mouse embryonic fibroblasts lacking type-I IGF receptor
    • 43. Sell C, Rubini M, Rubin R, Liu J-P, Efstratiadis A, Baserga R. Simian virus 40 large tumor antigen is unable to transform mouse embryonic fibroblasts lacking type-I IGF receptor. Proc Natl Acad Sci USA 1993, 90, 11217-11221.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 11217-11221
    • Sell, C.1    Rubini, M.2    Rubin, R.3    Liu, J.-P.4    Efstratiadis, A.5    Baserga, R.6
  • 44
    • 0028214152 scopus 로고
    • Role of the carboxy-terminal domains of the insulin and insulin-like growth factor I receptors in receptor function
    • 44. Faria TN, Blakesley VA, Kato H, Stannard B, LeRoith D, Roberts Jr CT. Role of the carboxy-terminal domains of the insulin and insulin-like growth factor I receptors in receptor function. J Biol Chem 1994, 269, 13922-13928.
    • (1994) J Biol Chem , vol.269 , pp. 13922-13928
    • Faria, T.N.1    Blakesley, V.A.2    Kato, H.3    Stannard, B.4    LeRoith, D.5    Roberts C.T., Jr.6
  • 45
    • 0023905461 scopus 로고
    • Properties of a human insulin receptor with a COOH-terminal truncation
    • 45. McClain DA, Maegawa H, Levy J et al. Properties of a human insulin receptor with a COOH-terminal truncation. J Biol Chem 1988, 263, 8904-8911.
    • (1988) J Biol Chem , vol.263 , pp. 8904-8911
    • McClain, D.A.1    Maegawa, H.2    Levy, J.3
  • 46
    • 0026766141 scopus 로고
    • Enhanced insulin-induced mitogenesis and mitogen-activated protein kinase activities in mutant insulin receptors with substitution of two COOH-terminal tyrosine autophosphorylation sites by phenylalanine
    • 46. Ando A, Momomura K, Tobe K et al. Enhanced insulin-induced mitogenesis and mitogen-activated protein kinase activities in mutant insulin receptors with substitution of two COOH-terminal tyrosine autophosphorylation sites by phenylalanine. J Biol Chem, 1992, 267, 12788-12792.
    • (1992) J Biol Chem , vol.267 , pp. 12788-12792
    • Ando, A.1    Momomura, K.2    Tobe, K.3
  • 47
    • 0029145296 scopus 로고
    • Different effects on mutagenesis and transformation of a mutation at tyrosine 1251 of the insulin-like growth factor I receptor
    • 47. Miura M, Surmacz E, Burgaud J-L, Baserga R. Different effects on mutagenesis and transformation of a mutation at tyrosine 1251 of the insulin-like growth factor I receptor. J Biol Chem 1995, 270, 22639-22644.
    • (1995) J Biol Chem , vol.270 , pp. 22639-22644
    • Miura, M.1    Surmacz, E.2    Burgaud, J.-L.3    Baserga, R.4
  • 48
    • 0028953268 scopus 로고
    • Insulin-like growth factor-I stimulates tyrosine phosphorylation of endogenous c-Crk
    • 48. Beitner-Johnson D, LeRoith D. Insulin-like growth factor-I stimulates tyrosine phosphorylation of endogenous c-Crk. J Biol Chem 1995, 270, 5187-5190.
    • (1995) J Biol Chem , vol.270 , pp. 5187-5190
    • Beitner-Johnson, D.1    LeRoith, D.2
  • 49
    • 0029931974 scopus 로고    scopus 로고
    • The proto-oncogene product c-Crk associates with IRS-I and 4PS: Modulation by IGF-I and enhanced IGF-I signaling
    • 49. Beitner-Johnson D, Blakesley VA, Shen-Orr Z et al. The proto-oncogene product c-Crk associates with IRS-I and 4PS: modulation by IGF-I and enhanced IGF-I signaling. J Biol Chem 1996, 271, 9287-9290.
    • (1996) J Biol Chem , vol.271 , pp. 9287-9290
    • Beitner-Johnson, D.1    Blakesley, V.A.2    Shen-Orr, Z.3
  • 50
    • 0028910137 scopus 로고
    • Divergent insulin and platelet-derived growth factor regulation of focal adhesion kinase tyrosine phosphorylation, and rearrangement of actin stress fibers
    • 50. Knight JB, Yamauchi K, Pessin JE. Divergent insulin and platelet-derived growth factor regulation of focal adhesion kinase tyrosine phosphorylation, and rearrangement of actin stress fibers. J Biol Chem 1995, 270, 10199-10203.
    • (1995) J Biol Chem , vol.270 , pp. 10199-10203
    • Knight, J.B.1    Yamauchi, K.2    Pessin, J.E.3
  • 51
    • 0028837993 scopus 로고
    • Insulin stimulates the tyrosine dephosphorylation of pp125 focal adhesion kinase
    • 51. Pillay TS, Sasaoka T, Olefsky JM. Insulin stimulates the tyrosine dephosphorylation of pp125 focal adhesion kinase. J Biol Chem 1995, 270, 991-994.
    • (1995) J Biol Chem , vol.270 , pp. 991-994
    • Pillay, T.S.1    Sasaoka, T.2    Olefsky, J.M.3
  • 52
    • 0029618917 scopus 로고
    • Substrate specificity of the insulin and insulin-like growth factor I receptor tyrosine kinase catalytic domains
    • 52. Xu B, Bird VG, Miller WT. Substrate specificity of the insulin and insulin-like growth factor I receptor tyrosine kinase catalytic domains. J Biol Chem 1995, 270, 29825-29830.
    • (1995) J Biol Chem , vol.270 , pp. 29825-29830
    • Xu, B.1    Bird, V.G.2    Miller, W.T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.