메뉴 건너뛰기




Volumn 64, Issue 1, 1997, Pages 117-127

Effect of tumor necrosis factor-α on the phosphorylation of tyrosine kinase receptors is associated with dynamic alterations in specific protein- tyrosine phosphatases

Author keywords

epidermal growth factor receptor; insulin receptor; insulin resistance; TNF ; tyrosine phosphorylation

Indexed keywords

PROTEIN TYROSINE KINASE; PROTEIN TYROSINE PHOSPHATASE; TUMOR NECROSIS FACTOR ALPHA;

EID: 0031049438     PISSN: 07302312     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-4644(199701)64:1<117::AID-JCB14>3.0.CO;2-I     Document Type: Article
Times cited : (45)

References (57)
  • 1
    • 0027953703 scopus 로고
    • Insulin action, diabetogenes, and the cause of type II diabetes
    • Kahn CR (1994): Insulin action, diabetogenes, and the cause of type II diabetes. Diabetes 43:1066-1084.
    • (1994) Diabetes , vol.43 , pp. 1066-1084
    • Kahn, C.R.1
  • 2
    • 0026091812 scopus 로고
    • Clinical review 26: Insulin resistance in obese and nonobese man
    • Caro JF (1991): Clinical review 26: Insulin resistance in obese and nonobese man. J Clin Endocrinol Metab 73:691-695.
    • (1991) J Clin Endocrinol Metab , vol.73 , pp. 691-695
    • Caro, J.F.1
  • 3
    • 0028918346 scopus 로고
    • Insulin resistance and non-insulin-dependent diabetes mellitus: Cellular and molecular mechanisms
    • Olefsky JM, Nolan JJ (1995): Insulin resistance and non-insulin-dependent diabetes mellitus: Cellular and molecular mechanisms. Am J Clin Nutr 61:S980-S986.
    • (1995) Am J Clin Nutr , vol.61
    • Olefsky, J.M.1    Nolan, J.J.2
  • 4
    • 0028587742 scopus 로고
    • Tumor necrosis factor alpha: A key component of the obesity-diabetes link
    • Hotamisligil GS, Spiegelman BM (1994): Tumor necrosis factor alpha: A key component of the obesity-diabetes link. Diabetes 43:1271-1278.
    • (1994) Diabetes , vol.43 , pp. 1271-1278
    • Hotamisligil, G.S.1    Spiegelman, B.M.2
  • 5
    • 0025234981 scopus 로고
    • Tumor necrosis factor in the pathophysiology of infection and sepsis
    • Fong Y, Lowry SF (1990): Tumor necrosis factor in the pathophysiology of infection and sepsis. Clin Immunol Immunopathol 55:157-170.
    • (1990) Clin Immunol Immunopathol , vol.55 , pp. 157-170
    • Fong, Y.1    Lowry, S.F.2
  • 6
    • 0023220709 scopus 로고
    • Tumor necrosis factor-a stimulates hepatic lipogenesis in the rat in vivo
    • Feingold KR, Grunfeld C (1987): Tumor necrosis factor-a stimulates hepatic lipogenesis in the rat in vivo. J Clin Invest 80:184-190.
    • (1987) J Clin Invest , vol.80 , pp. 184-190
    • Feingold, K.R.1    Grunfeld, C.2
  • 8
    • 0026549669 scopus 로고
    • Tumor necrosis factor impairs insulin action on peripheral glucose disposal and hepatic glucose output
    • Lang CH, Dobrescu C, Bagby GJ (1992): Tumor necrosis factor impairs insulin action on peripheral glucose disposal and hepatic glucose output. Endocrinology 130:43-52.
    • (1992) Endocrinology , vol.130 , pp. 43-52
    • Lang, C.H.1    Dobrescu, C.2    Bagby, G.J.3
  • 9
    • 0026646608 scopus 로고
    • Tumor necrosis factor a-induced glucose transporter (GLUT-1) mRNA stabilization in 3T3-L1 preadipocytes. Regulation by the adenosine-uridine binding factor
    • Stephens JM, Carter BZ, Pekala PH, Malter JS (1992): Tumor necrosis factor a-induced glucose transporter (GLUT-1) mRNA stabilization in 3T3-L1 preadipocytes. Regulation by the adenosine-uridine binding factor. J Biol Chem 267:8336-8341.
    • (1992) J Biol Chem , vol.267 , pp. 8336-8341
    • Stephens, J.M.1    Carter, B.Z.2    Pekala, P.H.3    Malter, J.S.4
  • 10
    • 0141929200 scopus 로고
    • Enhancement of cAMP levels and of protein kinase activity by tumor necrosis factor and interleukin 1 in human fibroblasts: Role in the induction of interleukin 6
    • Zhang YH, Lin JX, Yip YK, Vilcek J (1988): Enhancement of cAMP levels and of protein kinase activity by tumor necrosis factor and interleukin 1 in human fibroblasts: Role in the induction of interleukin 6. Proc Natl Acad Sci U S A 85:6802-6805.
    • (1988) Proc Natl Acad Sci U S A , vol.85 , pp. 6802-6805
    • Zhang, Y.H.1    Lin, J.X.2    Yip, Y.K.3    Vilcek, J.4
  • 11
    • 0025779160 scopus 로고
    • Tumor necrosis factor. New insights into the molecular mechanisms of its multiple actions
    • Vilcek J, Lee TH (1991): Tumor necrosis factor. New insights into the molecular mechanisms of its multiple actions. J Biol Chem 266:7313-7316.
    • (1991) J Biol Chem , vol.266 , pp. 7313-7316
    • Vilcek, J.1    Lee, T.H.2
  • 12
    • 0027076644 scopus 로고
    • Tumor necrosis factor stimulates multiple serine/threonine protein kinases in Swiss 3T3 and L929 cells. Implication of casein kinase-2 and extracellular signal-regulated kinases in the tumor necrosis factor signal transduction pathway
    • Van Lint J, Agostinis P, Vandevoorde V, Haegeman G, Fiers W, Merlevede W, Vandenheede JR (1992): Tumor necrosis factor stimulates multiple serine/threonine protein kinases in Swiss 3T3 and L929 cells. Implication of casein kinase-2 and extracellular signal-regulated kinases in the tumor necrosis factor signal transduction pathway. J Biol Chem 267:25916-25921.
    • (1992) J Biol Chem , vol.267 , pp. 25916-25921
    • Van Lint, J.1    Agostinis, P.2    Vandevoorde, V.3    Haegeman, G.4    Fiers, W.5    Merlevede, W.6    Vandenheede, J.R.7
  • 13
    • 0027426128 scopus 로고
    • Interleukin 1 and tumour necrosis factor activate the mitogen-activated protein (MAP) kinase in cultured cells
    • Saklatvala J, Rawlinson LM, Marshall CJ, Kracht M (1993): Interleukin 1 and tumour necrosis factor activate the mitogen-activated protein (MAP) kinase in cultured cells. FEBS Lett 334:189-192.
    • (1993) FEBS Lett , vol.334 , pp. 189-192
    • Saklatvala, J.1    Rawlinson, L.M.2    Marshall, C.J.3    Kracht, M.4
  • 14
    • 0028031569 scopus 로고
    • Reduced tyrosine kinase activity of the insulin receptor in obesity-diabetes - Central role of tumor necrosis factor-a
    • Hotamisligil GS, Budavari A, Murray D, Spiegelman BM (1994): Reduced tyrosine kinase activity of the insulin receptor in obesity-diabetes - central role of tumor necrosis factor-a. J Clin Invest 94:1543-1549.
    • (1994) J Clin Invest , vol.94 , pp. 1543-1549
    • Hotamisligil, G.S.1    Budavari, A.2    Murray, D.3    Spiegelman, B.M.4
  • 16
    • 0027332738 scopus 로고
    • Tumor necrosis factor-alpha suppresses insulin-induced tyrosine phosphorylation of insulin receptor and its substrates
    • Feinstein R, Kanety H, Papa MZ, Lunenfeld B, Karasik A (1993): Tumor necrosis factor-alpha suppresses insulin-induced tyrosine phosphorylation of insulin receptor and its substrates. J Biol Chem 268:26055-26058.
    • (1993) J Biol Chem , vol.268 , pp. 26055-26058
    • Feinstein, R.1    Kanety, H.2    Papa, M.Z.3    Lunenfeld, B.4    Karasik, A.5
  • 17
    • 0030061922 scopus 로고    scopus 로고
    • IRS-1-mediated inhibition of insulin receptor tyrosine kinase activity in TNF-a and obesity-induced insulin resistance
    • Hotamisligil GS, Peraldi P, Budavari A, Ellis R, White MF, Spiegelman BM (1996): IRS-1-mediated inhibition of insulin receptor tyrosine kinase activity in TNF-a and obesity-induced insulin resistance. Science 271: 665-670.
    • (1996) Science , vol.271 , pp. 665-670
    • Hotamisligil, G.S.1    Peraldi, P.2    Budavari, A.3    Ellis, R.4    White, M.F.5    Spiegelman, B.M.6
  • 18
    • 0027972524 scopus 로고
    • Altered gene expression for tumor necrosis factor-alpha and its receptors during drug and dietary modulation of insulin resistance
    • Hofmann C, Lorenz K, Braithwaite SS, Colca JR, Palazuk BJ, Hotamisligil GS, Spiegelman BM (1994): Altered gene expression for tumor necrosis factor-alpha and its receptors during drug and dietary modulation of insulin resistance. Endocrinology 134:264-270.
    • (1994) Endocrinology , vol.134 , pp. 264-270
    • Hofmann, C.1    Lorenz, K.2    Braithwaite, S.S.3    Colca, J.R.4    Palazuk, B.J.5    Hotamisligil, G.S.6    Spiegelman, B.M.7
  • 19
    • 0028931724 scopus 로고
    • Increased adipose tissue expression of tumor necrosis factor-alpha in human obesity and insulin resistance
    • Hotamisligil GS, Arner P, Caro JF, Atkinson RL, Spiegelman BM (1995): Increased adipose tissue expression of tumor necrosis factor-alpha in human obesity and insulin resistance. J Clin Invest 95:2409-2415.
    • (1995) J Clin Invest , vol.95 , pp. 2409-2415
    • Hotamisligil, G.S.1    Arner, P.2    Caro, J.F.3    Atkinson, R.L.4    Spiegelman, B.M.5
  • 20
    • 0028968879 scopus 로고
    • The expression of tumor necrosis factor in human adipose tissue. Regulation by obesity, weight loss, and relationship to lipoprotein lipase
    • Kern PA, Saghizadeh M, Ong JM, Bosch RJ, Deem R, Simsolo RB (1995): The expression of tumor necrosis factor in human adipose tissue. Regulation by obesity, weight loss, and relationship to lipoprotein lipase. J Clin Invest 95:2111-2119.
    • (1995) J Clin Invest , vol.95 , pp. 2111-2119
    • Kern, P.A.1    Saghizadeh, M.2    Ong, J.M.3    Bosch, R.J.4    Deem, R.5    Simsolo, R.B.6
  • 21
    • 0027569865 scopus 로고
    • Regulation of insulin receptor signalling by protein-tyrosine dephosphorylation
    • Goldstein BJ (1993): Regulation of insulin receptor signalling by protein-tyrosine dephosphorylation. Receptor 3:1-15.
    • (1993) Receptor , vol.3 , pp. 1-15
    • Goldstein, B.J.1
  • 22
    • 1842369216 scopus 로고    scopus 로고
    • Protein-tyrosine phosphatases and the regulation of insulin action
    • LeRoith D, Olefsky JM, Taylor SI (eds): Philadelphia: Lippincott
    • Goldstein BJ (1996): Protein-tyrosine phosphatases and the regulation of insulin action. In LeRoith D, Olefsky JM, Taylor SI (eds): "Diabetes Mellitus: A Fundamental and Clinical Text." Philadelphia: Lippincott, pp 174-186.
    • (1996) Diabetes Mellitus: A Fundamental and Clinical Text , pp. 174-186
    • Goldstein, B.J.1
  • 23
    • 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 EP, Zhang WR, Goldstein BJ (1992): 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) J Biol Chem , vol.267 , pp. 13811-13814
    • Hashimoto, N.1    Feener, E.P.2    Zhang, W.R.3    Goldstein, B.J.4
  • 24
    • 0028085078 scopus 로고
    • The insulin signalling system
    • White MF, Kahn CR (1994): The insulin signalling system. J Biol Chem 269:1-4.
    • (1994) J Biol Chem , vol.269 , pp. 1-4
    • White, M.F.1    Kahn, C.R.2
  • 25
    • 0024211451 scopus 로고
    • A new member of the immunoglobulin superfamily that has a cytoplasmic region homologous to the leukocyte common antigen
    • Streuli M, Krueger NX, Hall LR, Schlossman SF, Saito H (1988): 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) 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
  • 27
    • 0026471539 scopus 로고
    • Identification of a human src homology 2-containing protein-tyrosine-phosphatase - A putative homolog of drosophila cork-screw
    • Freeman RM, Plutzky J, Neel BG (1992): Identification of a human src homology 2-containing protein-tyrosine-phosphatase - a putative homolog of drosophila cork-screw. Proc Natl Acad Sci U S A 89:11239-11243.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 11239-11243
    • Freeman, R.M.1    Plutzky, J.2    Neel, B.G.3
  • 28
    • 0027531954 scopus 로고
    • A widely expressed human protein-tyrosine phosphatase containing src homology-2 domains
    • Ahmad S, Banville D, Zhao ZZ, Fischer EH, Shen SH (1993): A widely expressed human protein-tyrosine phosphatase containing src homology-2 domains. Proc Natl Acad Sci U S A 90:2197-2201.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 2197-2201
    • Ahmad, S.1    Banville, D.2    Zhao, Z.Z.3    Fischer, E.H.4    Shen, S.H.5
  • 29
    • 0028816605 scopus 로고
    • Insulin receptor signalling is augmented by antisense inhibition of the protein-tyrosine phosphatase LAR
    • Kulas DT, Zhang WR, Goldstein BJ, Furlanetto RW, Mooney RA (1995): Insulin receptor signalling is augmented by antisense inhibition of the protein-tyrosine phosphatase LAR. J Biol Chem 270:2435-2438.
    • (1995) J Biol Chem , vol.270 , pp. 2435-2438
    • Kulas, D.T.1    Zhang, W.R.2    Goldstein, B.J.3    Furlanetto, R.W.4    Mooney, R.A.5
  • 30
    • 0029130199 scopus 로고
    • Osmotic loading of neutralizing antibodies defines a role for protein-tyrosine phosphatase 1B in negative regulation of the insulin action pathway
    • Ahmad F, Li PM, Meyerovitch J, Goldstein BJ (1995): Osmotic loading of neutralizing antibodies defines a role for protein-tyrosine phosphatase 1B in negative regulation of the insulin action pathway. J Biol Chem 270:20503-20508.
    • (1995) J Biol Chem , vol.270 , pp. 20503-20508
    • Ahmad, F.1    Li, P.M.2    Meyerovitch, J.3    Goldstein, B.J.4
  • 31
    • 0028896991 scopus 로고
    • Protein-tyrosine-phosphatase SHPTP2 is a required positive effector for insulin downstream signaling
    • Yamauchi K, Milarski KL, Saltiel AR, Pessin JE (1995): Protein-tyrosine-phosphatase SHPTP2 is a required positive effector for insulin downstream signaling. Proc Natl Acad Sci U S A 92:664-668.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 664-668
    • Yamauchi, K.1    Milarski, K.L.2    Saltiel, A.R.3    Pessin, J.E.4
  • 32
    • 0028136280 scopus 로고
    • Expression of catalytically inactive Syp phosphatase in 3T3 cells blocks stimulation of mitogen-activated protein kinase by insulin
    • Milarski KL, Saltiel AR (1994): Expression of catalytically inactive Syp phosphatase in 3T3 cells blocks stimulation of mitogen-activated protein kinase by insulin. J Biol Chem 269:21239-21243.
    • (1994) J Biol Chem , vol.269 , pp. 21239-21243
    • Milarski, K.L.1    Saltiel, A.R.2
  • 33
    • 0028124504 scopus 로고
    • Role of SH-PTP2, a protein-tyrosine phosphatase with Src homology 2 domains, in insulin-stimulated ras activation
    • Noguchi T, Matozaki T, Horita K, Fujioka Y, Kasuga M (1994): Role of SH-PTP2, a protein-tyrosine phosphatase with Src homology 2 domains, in insulin-stimulated ras activation. Mol Cell Biol 14:6674-6682.
    • (1994) Mol Cell Biol , vol.14 , pp. 6674-6682
    • Noguchi, T.1    Matozaki, T.2    Horita, K.3    Fujioka, Y.4    Kasuga, M.5
  • 35
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976): A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 36
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli EK (1970): Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, E.K.1
  • 37
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H, Staehelin T, Gordon J (1979): Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci U S A 76:4350-4354.
    • (1979) Proc Natl Acad Sci U S A , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 38
    • 0026630976 scopus 로고
    • Insulin receptor and epidermal growth factor receptor dephosphorylation by three major rat liver protein-tyrosine phosphatases expressed in a recombinant bacterial system
    • Hashimoto N, Zhang WR, Goldstein BJ (1992): Insulin receptor and epidermal growth factor receptor dephosphorylation by three major rat liver protein-tyrosine phosphatases expressed in a recombinant bacterial system. Biochem J 284:569-576.
    • (1992) Biochem J , vol.284 , pp. 569-576
    • Hashimoto, N.1    Zhang, W.R.2    Goldstein, B.J.3
  • 41
    • 0021893858 scopus 로고
    • Phosphorylation of the insulin receptor in cultured hepatoma cells and a solubilized system
    • Kasuga M, White MF, Kahn CR (1985): Phosphorylation of the insulin receptor in cultured hepatoma cells and a solubilized system. Methods Enzymol 109:609-621.
    • (1985) Methods Enzymol , vol.109 , pp. 609-621
    • Kasuga, M.1    White, M.F.2    Kahn, C.R.3
  • 42
    • 0026038524 scopus 로고
    • Cloning, bacterial expression, purification, and characterization of the cytoplasmic domain of rat LAR, a receptor-like protein tyrosine phosphatase
    • Pot DA, Woodford TA, Remboutsika E, Haun RS, Dixon JE (1991): Cloning, bacterial expression, purification, and characterization of the cytoplasmic domain of rat LAR, a receptor-like protein tyrosine phosphatase. J Biol Chem 266:19688-19696.
    • (1991) J Biol Chem , vol.266 , pp. 19688-19696
    • Pot, D.A.1    Woodford, T.A.2    Remboutsika, E.3    Haun, R.S.4    Dixon, J.E.5
  • 43
    • 0021224540 scopus 로고
    • A comparison of the insulin- and epidermal growth factor-stimulated protein kinases from human placenta
    • Pike LJ, Kuenzel EA, Casnellie JE, Krebs EG (1984): A comparison of the insulin- and epidermal growth factor-stimulated protein kinases from human placenta. J Biol Chem 259:9913-9921.
    • (1984) J Biol Chem , vol.259 , pp. 9913-9921
    • Pike, L.J.1    Kuenzel, E.A.2    Casnellie, J.E.3    Krebs, E.G.4
  • 44
    • 0025945356 scopus 로고
    • Purification of protein-tyrosine phosphatases from human placenta
    • Tonks NK, Diltz CD, Fischer EH (1991): Purification of protein-tyrosine phosphatases from human placenta. Methods Enzymol 201:427-442.
    • (1991) Methods Enzymol , vol.201 , pp. 427-442
    • Tonks, N.K.1    Diltz, C.D.2    Fischer, E.H.3
  • 45
    • 0027992048 scopus 로고
    • Mutational analysis of proprotein processing, subunit association, and shedding of the LAR transmembrane protein tyrosine phosphatase
    • Serra-Pages C, Saito H, Streuli M (1994): Mutational analysis of proprotein processing, subunit association, and shedding of the LAR transmembrane protein tyrosine phosphatase. J Biol Chem 269:23632-23641.
    • (1994) J Biol Chem , vol.269 , pp. 23632-23641
    • Serra-Pages, C.1    Saito, H.2    Streuli, M.3
  • 46
    • 0026534648 scopus 로고
    • The N-terminal and C-terminal domains of a receptor tyrosine phosphatase are associated by non-covalent linkage
    • Yu Q, Lenardo T, Weinberg RA (1992): The N-terminal and C-terminal domains of a receptor tyrosine phosphatase are associated by non-covalent linkage. Oncogene 7:1051-1058.
    • (1992) Oncogene , vol.7 , pp. 1051-1058
    • Yu, Q.1    Lenardo, T.2    Weinberg, R.A.3
  • 47
    • 0026683969 scopus 로고
    • Phosphatase inhibitors modulate the growth-regulatory effects of human tumor necrosis factor on tumor and normal cells
    • Totpal K, Agarwal S, Aggarwal BB (1992): Phosphatase inhibitors modulate the growth-regulatory effects of human tumor necrosis factor on tumor and normal cells. Cancer Res 52:2557-2562.
    • (1992) Cancer Res , vol.52 , pp. 2557-2562
    • Totpal, K.1    Agarwal, S.2    Aggarwal, B.B.3
  • 48
    • 0028293681 scopus 로고
    • Effects of cytokines on epidermal growth factor receptor expression by malignant trophoblast cells in vitro
    • Steller MA, Mok SC, Yeh J, Fulop V, Anderson DJ, Berkowitz RS (1994): Effects of cytokines on epidermal growth factor receptor expression by malignant trophoblast cells in vitro. J Reprod Med 39:209-216.
    • (1994) J Reprod Med , vol.39 , pp. 209-216
    • Steller, M.A.1    Mok, S.C.2    Yeh, J.3    Fulop, V.4    Anderson, D.J.5    Berkowitz, R.S.6
  • 49
    • 0024316852 scopus 로고
    • Tumor necrosis factor modulates epidermal growth factor receptor phosphorylation and kinase activity in human tumor cells. Correlation with cytotoxicity
    • Donato NJ, Gallick GE, Steck PA, Rosenblum MG (1989): Tumor necrosis factor modulates epidermal growth factor receptor phosphorylation and kinase activity in human tumor cells. Correlation with cytotoxicity. J Biol Chem 264:20474-20481.
    • (1989) J Biol Chem , vol.264 , pp. 20474-20481
    • Donato, N.J.1    Gallick, G.E.2    Steck, P.A.3    Rosenblum, M.G.4
  • 50
    • 0026862657 scopus 로고
    • Tumor necrosis factor regulates tyrosine phosphorylation on epidermal growth factor receptors in A431 carcinoma cells: Evidence for a distinct mechanism
    • Donato NJ, Rosenblum MG, Steck PA (1992): Tumor necrosis factor regulates tyrosine phosphorylation on epidermal growth factor receptors in A431 carcinoma cells: Evidence for a distinct mechanism. Cell Growth Differ 3:259-268.
    • (1992) Cell Growth Differ , vol.3 , pp. 259-268
    • Donato, N.J.1    Rosenblum, M.G.2    Steck, P.A.3
  • 51
    • 0027158159 scopus 로고
    • The insulin receptor substrate-1 associates with the SH2-containing phosphotyrosine phosphatase Syp
    • Kuhné MR, Pawson T, Lienhard GE, Feng GS (1993): The insulin receptor substrate-1 associates with the SH2-containing phosphotyrosine phosphatase Syp. J Biol Chem 268:11479-11481.
    • (1993) J Biol Chem , vol.268 , pp. 11479-11481
    • Kuhné, M.R.1    Pawson, T.2    Lienhard, G.E.3    Feng, G.S.4
  • 52
    • 0027490590 scopus 로고
    • Tyrosyl phosphorylation and growth factor receptor association of the human corkscrew homologue, SH-PTP2
    • Lechleider RJ, Freeman RM, Neel BG (1993): Tyrosyl phosphorylation and growth factor receptor association of the human corkscrew homologue, SH-PTP2. J Biol Chem 268:13434-13438.
    • (1993) J Biol Chem , vol.268 , pp. 13434-13438
    • Lechleider, R.J.1    Freeman, R.M.2    Neel, B.G.3
  • 53
    • 0027399168 scopus 로고
    • Activation of a phosphotyrosine phosphatase by tyrosine phosphorylation
    • Vogel W, Lammers R, Huang JT, Ullrich A (1993): Activation of a phosphotyrosine phosphatase by tyrosine phosphorylation. Science 259:1611-1614.
    • (1993) Science , vol.259 , pp. 1611-1614
    • Vogel, W.1    Lammers, R.2    Huang, J.T.3    Ullrich, A.4
  • 55
    • 0029019297 scopus 로고
    • The LAR transmembrane protein tyrosine phosphatase and a coiled-coil LAR-interacting protein colocalize at focal adhesions
    • Serra-Pages C, Kedersha NL, Fazikas L, Medley Q, Debant A, Streuli M (1995): The LAR transmembrane protein tyrosine phosphatase and a coiled-coil LAR-interacting protein colocalize at focal adhesions. EMBO J 14:2827-2838.
    • (1995) EMBO J , vol.14 , pp. 2827-2838
    • Serra-Pages, C.1    Kedersha, N.L.2    Fazikas, L.3    Medley, Q.4    Debant, A.5    Streuli, M.6
  • 56
    • 0028343581 scopus 로고
    • Dynamic regulation of intact and C-terminal truncated insulin receptor phosphorylation in permeabilized cells
    • Bernier M, Liotta AS, Kole HK, Shock DD, Roth J (1994): Dynamic regulation of intact and C-terminal truncated insulin receptor phosphorylation in permeabilized cells. Biochemistry 33:4343-4351.
    • (1994) Biochemistry , vol.33 , pp. 4343-4351
    • Bernier, M.1    Liotta, A.S.2    Kole, H.K.3    Shock, D.D.4    Roth, J.5
  • 57
    • 0024583592 scopus 로고
    • Phosphorylation of the insulin receptor in permeabilized adipocytes is coupled to a rapid dephosphorylation reaction
    • Mooney RA, Anderson DL (1989): Phosphorylation of the insulin receptor in permeabilized adipocytes is coupled to a rapid dephosphorylation reaction. J Biol Chem 264:6850-6857.
    • (1989) J Biol Chem , vol.264 , pp. 6850-6857
    • Mooney, R.A.1    Anderson, D.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.