메뉴 건너뛰기




Volumn 28, Issue 9, 2003, Pages 509-514

Redox regulation of protein tyrosine phosphatases during receptor tyrosine kinase signal transduction

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN TYROSINE KINASE; PROTEIN TYROSINE PHOSPHATASE; REACTIVE OXYGEN METABOLITE;

EID: 0642276003     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0968-0004(03)00174-9     Document Type: Review
Times cited : (307)

References (74)
  • 1
    • 0035371620 scopus 로고    scopus 로고
    • Regulation of receptor tyrosine kinase signaling by protein tyrosine phosphatases
    • Ostman A., et al. Regulation of receptor tyrosine kinase signaling by protein tyrosine phosphatases. Trends Cell Biol. 11:2001;258-266.
    • (2001) Trends Cell Biol. , vol.11 , pp. 258-266
    • Ostman, A.1
  • 2
    • 0034633602 scopus 로고    scopus 로고
    • Hydrogen peroxide: A key messenger that modulates protein phosphorylation through cysteine oxidation
    • Rhee S.G., et al. Hydrogen peroxide: a key messenger that modulates protein phosphorylation through cysteine oxidation. Sci. STKE. 2000:2000;PE1.
    • (2000) Sci. STKE , vol.2000 , pp. 1
    • Rhee, S.G.1
  • 3
    • 0033796250 scopus 로고    scopus 로고
    • Mitochondrial free radical generation, oxidative stress, and aging
    • Cadenas E., et al. Mitochondrial free radical generation, oxidative stress, and aging. Free Radic. Biol. Med. 29:2000;222-230.
    • (2000) Free Radic. Biol. Med. , vol.29 , pp. 222-230
    • Cadenas, E.1
  • 4
    • 0032496143 scopus 로고    scopus 로고
    • Superoxide in apoptosis. Mitochondrial generation triggered by cytochrome c loss
    • Cai J., et al. Superoxide in apoptosis. Mitochondrial generation triggered by cytochrome c loss. J. Biol. Chem. 273:1998;11401-11404.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11401-11404
    • Cai, J.1
  • 5
    • 0040141644 scopus 로고    scopus 로고
    • Tumor necrosis factor-α increases the steady-state reduction of Cytochrome b of the mitochondrial respiratory chain in metabolically inhibited L929 cells
    • Sanchez-Alcazar J.A., et al. Tumor necrosis factor-α increases the steady-state reduction of Cytochrome b of the mitochondrial respiratory chain in metabolically inhibited L929 cells. J. Biol. Chem. 275:2000;13353-13361.
    • (2000) J. Biol. Chem. , vol.275 , pp. 13353-13361
    • Sanchez-Alcazar, J.A.1
  • 6
    • 0031239737 scopus 로고    scopus 로고
    • Significant levels of oxidants are generated by isolated cardiomyocytes during ischemia prior to reperfusion
    • Vanden Hoek T.L., et al. Significant levels of oxidants are generated by isolated cardiomyocytes during ischemia prior to reperfusion. J. Mol. Cell. Cardiol. 29:1997;2571-2583.
    • (1997) J. Mol. Cell. Cardiol. , vol.29 , pp. 2571-2583
    • Vanden Hoek, T.L.1
  • 7
    • 0037157824 scopus 로고    scopus 로고
    • Integrins engage mitochondrial function for signal transduction by a mechanism dependent on Rho GTPases
    • Werner E., et al. Integrins engage mitochondrial function for signal transduction by a mechanism dependent on Rho GTPases. J. Cell Biol. 158:2002;357-368.
    • (2002) J. Cell Biol. , vol.158 , pp. 357-368
    • Werner, E.1
  • 8
    • 0033105874 scopus 로고    scopus 로고
    • NADPH oxidase: An update
    • Babior B.M. NADPH oxidase: an update. Blood. 93:1999;1464-1476.
    • (1999) Blood , vol.93 , pp. 1464-1476
    • Babior, B.M.1
  • 9
    • 0025904386 scopus 로고
    • Identification of a superoxide-generating NADPH oxidase system in human fibroblasts
    • Meier B., et al. Identification of a superoxide-generating NADPH oxidase system in human fibroblasts. Biochem. J. 275:1991;241-245.
    • (1991) Biochem. J. , vol.275 , pp. 241-245
    • Meier, B.1
  • 10
    • 0028015832 scopus 로고
    • Production of hydrogen peroxide by transforming growth factor-β 1 and its involvement in induction of egr-1 in mouse osteoblastic cells
    • Ohba M., et al. Production of hydrogen peroxide by transforming growth factor-β 1 and its involvement in induction of egr-1 in mouse osteoblastic cells. J. Cell Biol. 126:1994;1079-1088.
    • (1994) J. Cell Biol. , vol.126 , pp. 1079-1088
    • Ohba, M.1
  • 11
    • 0029417335 scopus 로고
    • Activation of an H2O2-generating NADH oxidase in human lung fibroblasts by transforming growth factor β 1
    • Thannickal V.J., et al. Activation of an H2O2-generating NADH oxidase in human lung fibroblasts by transforming growth factor β 1. J. Biol. Chem. 270:1995;30334-30338.
    • (1995) J. Biol. Chem. , vol.270 , pp. 30334-30338
    • Thannickal, V.J.1
  • 12
    • 0024425516 scopus 로고
    • Human fibroblasts release reactive oxygen species in response to interleukin-1 or tumor necrosis factor-α
    • Meier B., et al. Human fibroblasts release reactive oxygen species in response to interleukin-1 or tumor necrosis factor-α Biochem. J. 263:1989;539-545.
    • (1989) Biochem. J. , vol.263 , pp. 539-545
    • Meier, B.1
  • 13
    • 0029020218 scopus 로고
    • Involvement of reactive oxygen species in cytokine and growth factor induction of c-fos expression in chondrocytes
    • Lo Y.Y., et al. Involvement of reactive oxygen species in cytokine and growth factor induction of c-fos expression in chondrocytes. J. Biol. Chem. 270:1995;11727-11730.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11727-11730
    • Lo, Y.Y.1
  • 14
    • 0035877633 scopus 로고    scopus 로고
    • Insulin-stimulated hydrogen peroxide reversibly inhibits protein-tyrosine phosphatase 1b in vivo and enhances the early insulin action cascade
    • Mahadev K., et al. Insulin-stimulated hydrogen peroxide reversibly inhibits protein-tyrosine phosphatase 1b in vivo and enhances the early insulin action cascade. J. Biol. Chem. 276:2001;21938-21942.
    • (2001) J. Biol. Chem. , vol.276 , pp. 21938-21942
    • Mahadev, K.1
  • 15
    • 0028973482 scopus 로고
    • Requirement for generation of H2O2 for platelet-derived growth factor signal transduction
    • Sundaresan M., et al. Requirement for generation of H2O2 for platelet-derived growth factor signal transduction. Science. 270:1995;296-299.
    • (1995) Science , vol.270 , pp. 296-299
    • Sundaresan, M.1
  • 16
    • 15144343374 scopus 로고    scopus 로고
    • Epidermal growth factor (EGF)-induced generation of hydrogen peroxide. Role in EGF receptor-mediated tyrosine phosphorylation
    • Bae Y.S., et al. Epidermal growth factor (EGF)-induced generation of hydrogen peroxide. Role in EGF receptor-mediated tyrosine phosphorylation. J. Biol. Chem. 272:1997;217-221.
    • (1997) J. Biol. Chem. , vol.272 , pp. 217-221
    • Bae, Y.S.1
  • 17
    • 0028365310 scopus 로고
    • Angiotensin II stimulates NADH and NADPH oxidase activity in cultured vascular smooth muscle cells
    • Griendling K.K., et al. Angiotensin II stimulates NADH and NADPH oxidase activity in cultured vascular smooth muscle cells. Circ. Res. 74:1994;1141-1148.
    • (1994) Circ. Res. , vol.74 , pp. 1141-1148
    • Griendling, K.K.1
  • 18
    • 0028806450 scopus 로고
    • Participation of reactive oxygen species in the lysophosphatidic acid-stimulated mitogen-activated protein kinase kinase activation pathway
    • Chen Q., et al. Participation of reactive oxygen species in the lysophosphatidic acid-stimulated mitogen-activated protein kinase kinase activation pathway. J. Biol. Chem. 270:1995;28499-28502.
    • (1995) J. Biol. Chem. , vol.270 , pp. 28499-28502
    • Chen, Q.1
  • 19
    • 0001288948 scopus 로고    scopus 로고
    • Platelet-derived growth factor-induced H(2)O(2) production requires the activation of phosphatidylinositol 3-kinase
    • Bae Y.S., et al. Platelet-derived growth factor-induced H(2)O(2) production requires the activation of phosphatidylinositol 3-kinase. J. Biol. Chem. 275:2000;10527-10531.
    • (2000) J. Biol. Chem. , vol.275 , pp. 10527-10531
    • Bae, Y.S.1
  • 20
    • 0029063584 scopus 로고
    • Rac mediates growth factor-induced arachidonic acid release
    • Peppelenbosch M.P., et al. Rac mediates growth factor-induced arachidonic acid release. Cell. 81:1995;849-856.
    • (1995) Cell , vol.81 , pp. 849-856
    • Peppelenbosch, M.P.1
  • 21
    • 0025739254 scopus 로고
    • Reactive oxygen intermediates as apparently widely used messengers in the activation of the NF-κ B transcription factor and HIV-1
    • Schreck R., et al. Reactive oxygen intermediates as apparently widely used messengers in the activation of the NF-κ B transcription factor and HIV-1. EMBO J. 10:1991;2247-2258.
    • (1991) EMBO J. , vol.10 , pp. 2247-2258
    • Schreck, R.1
  • 22
    • 0027506460 scopus 로고
    • Escape from redox regulation enhances the transforming activity of Fos
    • Okuno H., et al. Escape from redox regulation enhances the transforming activity of Fos. Oncogene. 8:1993;695-701.
    • (1993) Oncogene , vol.8 , pp. 695-701
    • Okuno, H.1
  • 23
    • 0028785860 scopus 로고
    • Effect of protein kinase and phosphatase inhibitors on expression of hypoxia-inducible factor 1
    • Wang G.L., et al. Effect of protein kinase and phosphatase inhibitors on expression of hypoxia-inducible factor 1. Biochem. Biophys. Res. Commun. 216:1995;669-675.
    • (1995) Biochem. Biophys. Res. Commun. , vol.216 , pp. 669-675
    • Wang, G.L.1
  • 24
    • 0029013621 scopus 로고
    • Role of cysteine residues in regulation of p53 function
    • Rainwater R., et al. Role of cysteine residues in regulation of p53 function. Mol. Cell. Biol. 15:1995;3892-3903.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3892-3903
    • Rainwater, R.1
  • 25
    • 0028940301 scopus 로고
    • Nitric oxide-stimulated guanine nucleotide exchange on p21ras
    • Lander H.M., et al. Nitric oxide-stimulated guanine nucleotide exchange on p21ras. J. Biol. Chem. 270:1995;7017-7020.
    • (1995) J. Biol. Chem. , vol.270 , pp. 7017-7020
    • Lander, H.M.1
  • 26
    • 0032176512 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases: Mechanisms of catalysis and regulation
    • Denu J.M., et al. Protein tyrosine phosphatases: mechanisms of catalysis and regulation. Curr. Opin. Chem. Biol. 2:1998;633-641.
    • (1998) Curr. Opin. Chem. Biol. , vol.2 , pp. 633-641
    • Denu, J.M.1
  • 27
    • 0001737772 scopus 로고    scopus 로고
    • Reversible regulation of SHP-1 tyrosine phosphatase activity by oxidation
    • Cunnick J.M., et al. Reversible regulation of SHP-1 tyrosine phosphatase activity by oxidation. Biochem. Mol. Biol. Int. 45:1998;887-894.
    • (1998) Biochem. Mol. Biol. Int. , vol.45 , pp. 887-894
    • Cunnick, J.M.1
  • 28
    • 0036366424 scopus 로고    scopus 로고
    • Redox regulation of protein tyrosine phosphatases by hydrogen peroxide: Detecting sulfenic acid intermediates and examining reversible inactivation
    • Denu J.M., et al. Redox regulation of protein tyrosine phosphatases by hydrogen peroxide: detecting sulfenic acid intermediates and examining reversible inactivation. Methods Enzymol. 348:2002;297-305.
    • (2002) Methods Enzymol. , vol.348 , pp. 297-305
    • Denu, J.M.1
  • 29
    • 0032546955 scopus 로고    scopus 로고
    • Reversible inactivation of protein-tyrosine phosphatase 1B in A431 cells stimulated with epidermal growth factor
    • Lee S.R., et al. Reversible inactivation of protein-tyrosine phosphatase 1B in A431 cells stimulated with epidermal growth factor. J. Biol. Chem. 273:1998;15366-15372.
    • (1998) J. Biol. Chem. , vol.273 , pp. 15366-15372
    • Lee, S.R.1
  • 30
    • 0035823539 scopus 로고    scopus 로고
    • Two vicinal cysteines confer a peculiar redox regulation to low molecular weight protein tyrosine phosphatase in response to platelet-derived growth factor receptor stimulation
    • Chiarugi P., et al. Two vicinal cysteines confer a peculiar redox regulation to low molecular weight protein tyrosine phosphatase in response to platelet-derived growth factor receptor stimulation. J. Biol. Chem. 276:2001;33478-33487.
    • (2001) J. Biol. Chem. , vol.276 , pp. 33478-33487
    • Chiarugi, P.1
  • 31
    • 0033580609 scopus 로고    scopus 로고
    • Regulation of PTP1B via glutathionylation of the active site cysteine 215
    • Barrett W.C., et al. Regulation of PTP1B via glutathionylation of the active site cysteine 215. Biochemistry. 38:1999;6699-6705.
    • (1999) Biochemistry , vol.38 , pp. 6699-6705
    • Barrett, W.C.1
  • 33
    • 0036184190 scopus 로고    scopus 로고
    • Reversible oxidation and inactivation of protein tyrosine phosphatases in vivo
    • Meng T.C., et al. Reversible oxidation and inactivation of protein tyrosine phosphatases in vivo. Mol. Cell. 9:2002;387-399.
    • (2002) Mol. Cell , vol.9 , pp. 387-399
    • Meng, T.C.1
  • 35
    • 0037036460 scopus 로고    scopus 로고
    • Redox regulation of Cdc25C
    • Savitsky P.A., et al. Redox regulation of Cdc25C. J. Biol. Chem. 277:2002;20535-20540.
    • (2002) J. Biol. Chem. , vol.277 , pp. 20535-20540
    • Savitsky, P.A.1
  • 36
    • 0037084009 scopus 로고    scopus 로고
    • Regulation of receptor protein-tyrosine phosphatase α by oxidative stress
    • Blanchetot C., et al. Regulation of receptor protein-tyrosine phosphatase α by oxidative stress. EMBO J. 21:2002;493-503.
    • (2002) EMBO J. , vol.21 , pp. 493-503
    • Blanchetot, C.1
  • 37
    • 0032547385 scopus 로고    scopus 로고
    • Signal transduction via platelet-derived growth factor receptors
    • Heldin C.H., et al. Signal transduction via platelet-derived growth factor receptors. Biochim. Biophys. Acta. 1378:1998;F79-113.
    • (1998) Biochim. Biophys. Acta , vol.1378 , pp. 79-113
    • Heldin, C.H.1
  • 38
    • 0035958911 scopus 로고    scopus 로고
    • Ligand stimulation reduces platelet-derived growth factor β-receptor susceptibility to tyrosine dephosphorylation
    • Shimizu A., et al. Ligand stimulation reduces platelet-derived growth factor β-receptor susceptibility to tyrosine dephosphorylation. J. Biol. Chem. 276:2001;27749-27752.
    • (2001) J. Biol. Chem. , vol.276 , pp. 27749-27752
    • Shimizu, A.1
  • 39
    • 0037092501 scopus 로고    scopus 로고
    • New perspectives in PDGF receptor downregulation: The main role of phosphotyrosine phosphatases
    • Chiarugi P., et al. New perspectives in PDGF receptor downregulation: the main role of phosphotyrosine phosphatases. J. Cell Sci. 115:2002;2219-2232.
    • (2002) J. Cell Sci. , vol.115 , pp. 2219-2232
    • Chiarugi, P.1
  • 40
    • 0037020233 scopus 로고    scopus 로고
    • Insight into the role of low molecular weight phosphotyrosine phosphatase (LMW-PTP) on platelet-derived growth factor receptor (PDGF-r) signaling. LMW-PTP controls PDGF-r kinase activity through TYR-857 dephosphorylation
    • Chiarugi P., et al. Insight into the role of low molecular weight phosphotyrosine phosphatase (LMW-PTP) on platelet-derived growth factor receptor (PDGF-r) signaling. LMW-PTP controls PDGF-r kinase activity through TYR-857 dephosphorylation. J. Biol. Chem. 277:2002;37331-37338.
    • (2002) J. Biol. Chem. , vol.277 , pp. 37331-37338
    • Chiarugi, P.1
  • 41
    • 0034507958 scopus 로고    scopus 로고
    • Molecular basis for the dephosphorylation of the activation segment of the insulin receptor by protein tyrosine phosphatase 1B
    • Salmeen A., et al. Molecular basis for the dephosphorylation of the activation segment of the insulin receptor by protein tyrosine phosphatase 1B. Mol. Cell. 6:2000;1401-1412.
    • (2000) Mol. Cell , vol.6 , pp. 1401-1412
    • Salmeen, A.1
  • 42
    • 0034717163 scopus 로고    scopus 로고
    • Site-selective dephosphorylation of the platelet-derived growth factor β -receptor by the receptor-like protein-tyrosine phosphatase DEP-1
    • Kovalenko M., et al. Site-selective dephosphorylation of the platelet-derived growth factor β -receptor by the receptor-like protein-tyrosine phosphatase DEP-1. J. Biol. Chem. 275:2000;16219-16226.
    • (2000) J. Biol. Chem. , vol.275 , pp. 16219-16226
    • Kovalenko, M.1
  • 43
    • 0034655749 scopus 로고    scopus 로고
    • Protein-tyrosine-phosphatase-mediated epidermal growth factor (EGF) receptor transinactivation and EGF receptor-independent stimulation of mitogen-activated protein kinase by bradykinin in A431 cells
    • Graness A., et al. Protein-tyrosine-phosphatase-mediated epidermal growth factor (EGF) receptor transinactivation and EGF receptor-independent stimulation of mitogen-activated protein kinase by bradykinin in A431 cells. Biochem. J. 347:2000;441-447.
    • (2000) Biochem. J. , vol.347 , pp. 441-447
    • Graness, A.1
  • 44
    • 0032554630 scopus 로고    scopus 로고
    • Electrostatic evaluation of the signature motif (H/V)CX5R(S/T) in protein-tyrosine phosphatases
    • Peters G.H., et al. Electrostatic evaluation of the signature motif (H/V)CX5R(S/T) in protein-tyrosine phosphatases. Biochemistry. 37:1998;5383-5393.
    • (1998) Biochemistry , vol.37 , pp. 5383-5393
    • Peters, G.H.1
  • 45
    • 0035966017 scopus 로고    scopus 로고
    • Low molecular weight protein-tyrosine phosphatase is involved in growth inhibition during cell differentiation
    • Fiaschi T., et al. Low molecular weight protein-tyrosine phosphatase is involved in growth inhibition during cell differentiation. J. Biol. Chem. 276:2001;49156-49163.
    • (2001) J. Biol. Chem. , vol.276 , pp. 49156-49163
    • Fiaschi, T.1
  • 46
    • 0036051939 scopus 로고    scopus 로고
    • Determination of intracellular reactive oxygen species as function of cell density
    • Pani G., et al. Determination of intracellular reactive oxygen species as function of cell density. Methods Enzymol. 352:2002;91-100.
    • (2002) Methods Enzymol. , vol.352 , pp. 91-100
    • Pani, G.1
  • 47
    • 0030980641 scopus 로고    scopus 로고
    • Mitogenic signaling mediated by oxidants in Ras-transformed fibroblasts
    • Irani K., et al. Mitogenic signaling mediated by oxidants in Ras-transformed fibroblasts. Science. 275:1997;1649-1652.
    • (1997) Science , vol.275 , pp. 1649-1652
    • Irani, K.1
  • 48
    • 0032499395 scopus 로고    scopus 로고
    • Ras, superoxide and signal transduction
    • Irani K., et al. Ras, superoxide and signal transduction. Biochem. Pharmacol. 55:1998;1339-1346.
    • (1998) Biochem. Pharmacol. , vol.55 , pp. 1339-1346
    • Irani, K.1
  • 49
    • 0031059530 scopus 로고    scopus 로고
    • Novel mechanisms of RTK signal generation
    • Weiss F.U., et al. Novel mechanisms of RTK signal generation. Curr. Opin. Genet. Dev. 7:1997;80-86.
    • (1997) Curr. Opin. Genet. Dev. , vol.7 , pp. 80-86
    • Weiss, F.U.1
  • 50
    • 0008805915 scopus 로고    scopus 로고
    • Inactivation of protein-tyrosine phosphatases as mechanism of UV-induced signal transduction
    • Gross S., et al. Inactivation of protein-tyrosine phosphatases as mechanism of UV-induced signal transduction. J. Biol. Chem. 274:1999;26378- 26386.
    • (1999) J. Biol. Chem. , vol.274 , pp. 26378-26386
    • Gross, S.1
  • 51
    • 0029790979 scopus 로고    scopus 로고
    • Dephosphorylation of receptor tyrosine kinases as target of regulation by radiation, oxidants or alkylating agents
    • Knebel A., et al. Dephosphorylation of receptor tyrosine kinases as target of regulation by radiation, oxidants or alkylating agents. EMBO J. 15:1996;5314-5325.
    • (1996) EMBO J. , vol.15 , pp. 5314-5325
    • Knebel, A.1
  • 52
    • 0037157854 scopus 로고    scopus 로고
    • The metalloprotease Kuzbanian (ADAM10) mediates the transactivation of EGF receptor by G protein-coupled receptors
    • Yan Y., et al. The metalloprotease Kuzbanian (ADAM10) mediates the transactivation of EGF receptor by G protein-coupled receptors. J. Cell Biol. 158:2002;221-226.
    • (2002) J. Cell Biol. , vol.158 , pp. 221-226
    • Yan, Y.1
  • 53
    • 0030044360 scopus 로고    scopus 로고
    • Role of transactivation of the EGF receptor in signalling by G-protein-coupled receptors
    • Daub H., et al. Role of transactivation of the EGF receptor in signalling by G-protein-coupled receptors. Nature. 379:1996;557-560.
    • (1996) Nature , vol.379 , pp. 557-560
    • Daub, H.1
  • 54
    • 0033850587 scopus 로고    scopus 로고
    • Signal transduction pathways of G protein-coupled receptors and their cross-talk with receptor tyrosine kinases: Lessons from bradykinin signaling
    • Liebmann C., et al. Signal transduction pathways of G protein-coupled receptors and their cross-talk with receptor tyrosine kinases: lessons from bradykinin signaling. Curr. Med. Chem. 7:2000;911-943.
    • (2000) Curr. Med. Chem. , vol.7 , pp. 911-943
    • Liebmann, C.1
  • 55
    • 17544370809 scopus 로고    scopus 로고
    • 5-HT(2A) receptors stimulate mitogen-activated protein kinase via H(2)O(2) generation in rat renal mesangial cells
    • Greene E.L., et al. 5-HT(2A) receptors stimulate mitogen-activated protein kinase via H(2)O(2) generation in rat renal mesangial cells. Am. J. Physiol. Renal Physiol. 278:2000;F650-F658.
    • (2000) Am. J. Physiol. Renal Physiol. , vol.278 , pp. 650-F658
    • Greene, E.L.1
  • 56
    • 0032896376 scopus 로고    scopus 로고
    • Angiotensin II receptor coupling to phospholipase D is mediated by the βγ subunits of heterotrimeric G proteins in vascular smooth muscle cells
    • Ushio-Fukai M., et al. Angiotensin II receptor coupling to phospholipase D is mediated by the βγ subunits of heterotrimeric G proteins in vascular smooth muscle cells. Mol. Pharmacol. 55:1999;142-149.
    • (1999) Mol. Pharmacol. , vol.55 , pp. 142-149
    • Ushio-Fukai, M.1
  • 57
    • 0036138276 scopus 로고    scopus 로고
    • Cell compartmentalization in redox signaling
    • Pani G., et al. Cell compartmentalization in redox signaling. IUBMB Life. 52:2001;7-16.
    • (2001) IUBMB Life , vol.52 , pp. 7-16
    • Pani, G.1
  • 58
    • 0029090238 scopus 로고
    • PDGF receptor as a specific in vivo target for low M(r) phosphotyrosine protein phosphatase
    • Chiarugi P., et al. PDGF receptor as a specific in vivo target for low M(r) phosphotyrosine protein phosphatase. FEBS Lett. 372:1995;49-53.
    • (1995) FEBS Lett. , vol.372 , pp. 49-53
    • Chiarugi, P.1
  • 59
    • 18744419610 scopus 로고    scopus 로고
    • HCPTPA, a protein tyrosine phosphatase that regulates vascular endothelial growth factor receptor-mediated signal transduction and biological activity
    • Huang L., et al. HCPTPA, a protein tyrosine phosphatase that regulates vascular endothelial growth factor receptor-mediated signal transduction and biological activity. J. Biol. Chem. 274:1999;38183-38188.
    • (1999) J. Biol. Chem. , vol.274 , pp. 38183-38188
    • Huang, L.1
  • 60
    • 0031577545 scopus 로고    scopus 로고
    • LMW-PTP is a negative regulator of insulin-mediated mitotic and metabolic signalling
    • Chiarugi P., et al. LMW-PTP is a negative regulator of insulin-mediated mitotic and metabolic signalling. Biochem. Biophys. Res. Commun. 238:1997;676-682.
    • (1997) Biochem. Biophys. Res. Commun. , vol.238 , pp. 676-682
    • Chiarugi, P.1
  • 61
    • 0033525870 scopus 로고    scopus 로고
    • Increased insulin sensitivity and obesity resistance in mice lacking the protein tyrosine phosphatase-1B gene
    • Elchebly M., et al. Increased insulin sensitivity and obesity resistance in mice lacking the protein tyrosine phosphatase-1B gene. Science. 283:1999;1544-1548.
    • (1999) Science , vol.283 , pp. 1544-1548
    • Elchebly, M.1
  • 62
    • 0030668521 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase 1B interacts with and is tyrosine phosphorylated by the epidermal growth factor receptor
    • Liu F., et al. Protein tyrosine phosphatase 1B interacts with and is tyrosine phosphorylated by the epidermal growth factor receptor. Biochem. J. 327:1997;139-145.
    • (1997) Biochem. J. , vol.327 , pp. 139-145
    • Liu, F.1
  • 63
    • 0029810614 scopus 로고    scopus 로고
    • Protein-tyrosine phosphatase 1B is a negative regulator of insulin- and insulin-like growth factor-I-stimulated signaling
    • Kenner K.A., et al. Protein-tyrosine phosphatase 1B is a negative regulator of insulin- and insulin-like growth factor-I-stimulated signaling. J. Biol. Chem. 271:1996;19810-19816.
    • (1996) J. Biol. Chem. , vol.271 , pp. 19810-19816
    • Kenner, K.A.1
  • 64
    • 0032488828 scopus 로고    scopus 로고
    • SHP-1 associates with both platelet-derived growth factor receptor and the p85 subunit of phosphatidylinositol 3-kinase
    • Yu Z., et al. SHP-1 associates with both platelet-derived growth factor receptor and the p85 subunit of phosphatidylinositol 3-kinase. J. Biol. Chem. 273:1998;3687-3694.
    • (1998) J. Biol. Chem. , vol.273 , pp. 3687-3694
    • Yu, Z.1
  • 65
    • 0032544418 scopus 로고    scopus 로고
    • Phosphotyrosine 1173 mediates binding of the protein-tyrosine phosphatase SHP-1 to the epidermal growth factor receptor and attenuation of receptor signaling
    • Keilhack H., et al. Phosphotyrosine 1173 mediates binding of the protein-tyrosine phosphatase SHP-1 to the epidermal growth factor receptor and attenuation of receptor signaling. J. Biol. Chem. 273:1998;24839-24846.
    • (1998) J. Biol. Chem. , vol.273 , pp. 24839-24846
    • Keilhack, H.1
  • 66
    • 0029891236 scopus 로고    scopus 로고
    • Regulation of colony-stimulating factor 1 receptor signaling by the SH2 domain-containing tyrosine phosphatase SHPTP1
    • Chen H.E., et al. Regulation of colony-stimulating factor 1 receptor signaling by the SH2 domain-containing tyrosine phosphatase SHPTP1. Mol. Cell. Biol. 16:1996;3685-3697.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 3685-3697
    • Chen, H.E.1
  • 67
    • 18344374179 scopus 로고    scopus 로고
    • Negative regulation of Ros receptor tyrosine kinase signaling. An epithelial function of the SH2 domain protein tyrosine phosphatase SHP-1
    • Keilhack H., et al. Negative regulation of Ros receptor tyrosine kinase signaling. An epithelial function of the SH2 domain protein tyrosine phosphatase SHP-1. J. Cell Biol. 152:2001;325-334.
    • (2001) J. Cell Biol. , vol.152 , pp. 325-334
    • Keilhack, H.1
  • 68
    • 0029085194 scopus 로고
    • Identification of a putative Syp substrate, the PDGF β receptor
    • Klinghoffer R.A., et al. Identification of a putative Syp substrate, the PDGF β receptor. J. Biol. Chem. 270:1995;22208-22217.
    • (1995) J. Biol. Chem. , vol.270 , pp. 22208-22217
    • Klinghoffer, R.A.1
  • 69
    • 0031935043 scopus 로고    scopus 로고
    • Epidermal growth factor receptor and the adaptor protein p52Shc are specific substrates of T-cell protein tyrosine phosphatase
    • Tiganis T., et al. Epidermal growth factor receptor and the adaptor protein p52Shc are specific substrates of T-cell protein tyrosine phosphatase. Mol. Cell. Biol. 18:1998;1622-1634.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 1622-1634
    • Tiganis, T.1
  • 70
    • 0039619868 scopus 로고    scopus 로고
    • Identification of tyrosine phosphatases that dephosphorylate the insulin receptor. a brute force approach based on "substrate-trapping" mutants
    • Walchli S., et al. Identification of tyrosine phosphatases that dephosphorylate the insulin receptor. A brute force approach based on "substrate-trapping" mutants. J. Biol. Chem. 275:2000;9792-9796.
    • (2000) J. Biol. Chem. , vol.275 , pp. 9792-9796
    • Walchli, S.1
  • 71
    • 0030021432 scopus 로고    scopus 로고
    • The transmembrane protein-tyrosine phosphatase LAR modulates signaling by multiple receptor tyrosine kinases
    • Kulas D.T., et al. The transmembrane protein-tyrosine phosphatase LAR modulates signaling by multiple receptor tyrosine kinases. J. Biol. Chem. 271:1996;748-754.
    • (1996) J. Biol. Chem. , vol.271 , pp. 748-754
    • Kulas, D.T.1
  • 72
    • 0028816605 scopus 로고
    • Insulin receptor signaling is augmented by antisense inhibition of the protein tyrosine phosphatase LAR
    • Kulas D.T., et al. Insulin receptor signaling is augmented by antisense inhibition of the protein tyrosine phosphatase LAR. J. Biol. Chem. 270:1995;2435-2438.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2435-2438
    • Kulas, D.T.1
  • 73
    • 0029117217 scopus 로고
    • Selective down-regulation of the insulin receptor signal by protein-tyrosine phosphatases alpha and epsilon
    • Moller N.P., et al. Selective down-regulation of the insulin receptor signal by protein-tyrosine phosphatases alpha and epsilon. J. Biol. Chem. 270:1995;23126-23131.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23126-23131
    • Moller, N.P.1
  • 74
    • 0033566204 scopus 로고    scopus 로고
    • The transmembrane protein tyrosine phosphatase RPTPσ modulates signaling of the epidermal growth factor receptor in A431 cells
    • Suarez P.E., et al. The transmembrane protein tyrosine phosphatase RPTPσ modulates signaling of the epidermal growth factor receptor in A431 cells. Oncogene. 18:1999;4069-4079.
    • (1999) Oncogene , vol.18 , pp. 4069-4079
    • Suarez, P.E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.