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Volumn 8, Issue 11-12, 2006, Pages 2111-2124

Oxidative stress and growth-regulating intracellular signaling pathways in cardiac myocytes

Author keywords

[No Author keywords available]

Indexed keywords

APOPTOSIS SIGNAL REGULATING KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; MITOGEN ACTIVATED PROTEIN KINASE P38; NEUROHORMONE; PHOSPHATASE; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN KINASE B; PROTEIN KINASE C; RAS PROTEIN; REACTIVE OXYGEN METABOLITE; STRESS ACTIVATED PROTEIN KINASE;

EID: 33947689707     PISSN: 15230864     EISSN: None     Source Type: Journal    
DOI: 10.1089/ars.2006.8.2111     Document Type: Review
Times cited : (108)

References (154)
  • 1
    • 0029896250 scopus 로고    scopus 로고
    • Big mitogen-activated protein kinase 1 (BMK1) is a redox-sensitive kinase
    • Abe J, Kusuhara M, Ulevitch RJ, Berk BC, and Lee J-D. Big mitogen-activated protein kinase 1 (BMK1) is a redox-sensitive kinase. J Biol Chem 271: 16586-16590, 1996.
    • (1996) J Biol Chem , vol.271 , pp. 16586-16590
    • Abe, J.1    Kusuhara, M.2    Ulevitch, R.J.3    Berk, B.C.4    Lee, J.-D.5
  • 2
    • 3142663363 scopus 로고    scopus 로고
    • S-glutathiolation of Ras mediates redox-sensitive signaling by angiotensin II in vascular smooth muscle cells
    • Adachi T, Pimentel DR, Heibeck T, Hou X, Lee YJ, Jiang B, Ido Y, and Cohen RA. S-glutathiolation of Ras mediates redox-sensitive signaling by angiotensin II in vascular smooth muscle cells. J Biol Chem 279: 29857-29862, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 29857-29862
    • Adachi, T.1    Pimentel, D.R.2    Heibeck, T.3    Hou, X.4    Lee, Y.J.5    Jiang, B.6    Ido, Y.7    Cohen, R.A.8
  • 3
    • 0030886770 scopus 로고    scopus 로고
    • Oxidative stress activates extracellular signal-regulated kinases through Src and Ras in cultured cardiac myocytes of neonatal rats
    • Aikawa R, Komuro I, Yamazaki T, Zou Y, Kudoh S, Tanaka M, Shiojima I, Hiroi Y, and Yazaki Y. Oxidative stress activates extracellular signal-regulated kinases through Src and Ras in cultured cardiac myocytes of neonatal rats. J Clin Invest 100: 1813-1821, 1997.
    • (1997) J Clin Invest , vol.100 , pp. 1813-1821
    • Aikawa, R.1    Komuro, I.2    Yamazaki, T.3    Zou, Y.4    Kudoh, S.5    Tanaka, M.6    Shiojima, I.7    Hiroi, Y.8    Yazaki, Y.9
  • 4
    • 0035140827 scopus 로고    scopus 로고
    • Reactive oxygen species mediate alpha-adrenergic receptor-stimulated hypertrophy in adult rat ventricular myocytes
    • Amin JK, Xiao L, Pimental DR, Pagano PJ, Singh K, Sawyer DB, and Colucci WS. Reactive oxygen species mediate alpha-adrenergic receptor-stimulated hypertrophy in adult rat ventricular myocytes. J Mol Cell Cardiol 33: 131-139, 2001.
    • (2001) J Mol Cell Cardiol , vol.33 , pp. 131-139
    • Amin, J.K.1    Xiao, L.2    Pimental, D.R.3    Pagano, P.J.4    Singh, K.5    Sawyer, D.B.6    Colucci, W.S.7
  • 6
    • 0032489871 scopus 로고    scopus 로고
    • Angiotensin II activates RhoA in cardiac myocytes: A critical role of RhoA in angiotensin II-induced premyofibril formation
    • Aoki H, Izumo S, and Sadoshima J. Angiotensin II activates RhoA in cardiac myocytes: a critical role of RhoA in angiotensin II-induced premyofibril formation. Circ Res 82: 666-676, 1998.
    • (1998) Circ Res , vol.82 , pp. 666-676
    • Aoki, H.1    Izumo, S.2    Sadoshima, J.3
  • 7
    • 11144307292 scopus 로고    scopus 로고
    • STRESS signaling pathways that modulate cardiac myocyte apoptosis
    • Baines CP and Molkentin JD. STRESS signaling pathways that modulate cardiac myocyte apoptosis. J Mol Cell Cardiol 38: 47-62, 2005.
    • (2005) J Mol Cell Cardiol , vol.38 , pp. 47-62
    • Baines, C.P.1    Molkentin, J.D.2
  • 8
    • 18044383110 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in cardiovascular disease
    • Ballinger SW. Mitochondrial dysfunction in cardiovascular disease. Free Radic Biol Med 38: 1278-1295, 2005.
    • (2005) Free Radic Biol Med , vol.38 , pp. 1278-1295
    • Ballinger, S.W.1
  • 9
    • 9944235916 scopus 로고    scopus 로고
    • The role of cysteine residues as redox-sensitive regulatory switches
    • Barford D. The role of cysteine residues as redox-sensitive regulatory switches. Curr Opin Struct Biol 14: 679-686, 2004.
    • (2004) Curr Opin Struct Biol , vol.14 , pp. 679-686
    • Barford, D.1
  • 10
    • 17044393948 scopus 로고    scopus 로고
    • Regulation of Akt/PKB Ser473 phosphorylation
    • Bayascas JR and Alessi DR. Regulation of Akt/PKB Ser473 phosphorylation. Mol Cell 18: 143-145, 2005.
    • (2005) Mol Cell , vol.18 , pp. 143-145
    • Bayascas, J.R.1    Alessi, D.R.2
  • 11
    • 1042266632 scopus 로고    scopus 로고
    • On the physiological importance of endoproteolysis of CAAX proteins: Heart-specific RCE1 knockout mice develop a lethal cardiomyopathy
    • Bergo MO, Lieu HD, Gavino BJ, Ambroziak P, Otto JC, Casey PJ, Walker QM, and Young SG. On the physiological importance of endoproteolysis of CAAX proteins: heart-specific RCE1 knockout mice develop a lethal cardiomyopathy. J Biol Chem 279: 4729-4736, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 4729-4736
    • Bergo, M.O.1    Lieu, H.D.2    Gavino, B.J.3    Ambroziak, P.4    Otto, J.C.5    Casey, P.J.6    Walker, Q.M.7    Young, S.G.8
  • 12
    • 17144467725 scopus 로고    scopus 로고
    • Insider information: How palmitoylation of Ras makes it a signaling double agent
    • Berthiaume LG. Insider information: how palmitoylation of Ras makes it a signaling double agent. Sci STKE 2002: PE41, 2002.
    • (2002) Sci STKE , vol.2002
    • Berthiaume, L.G.1
  • 13
    • 0029614706 scopus 로고
    • Peroxovanadium compounds: Biological actions and mechanism of insulin-mimesis
    • Bevan AP, Drake PG, Yale JF, Shaver A, and Posner BI. Peroxovanadium compounds: biological actions and mechanism of insulin-mimesis. Mol Cell Biochem 153: 49-58, 1995.
    • (1995) Mol Cell Biochem , vol.153 , pp. 49-58
    • Bevan, A.P.1    Drake, P.G.2    Yale, J.F.3    Shaver, A.4    Posner, B.I.5
  • 14
    • 4644273095 scopus 로고    scopus 로고
    • Bogoyevitch MA, and Court NW. Counting on mitogen-activated protein kinases-ERKs 3, 4, 5, 6, 7 and 8. Cell Signal 16: 1345-1354, 2004.
    • Bogoyevitch MA, and Court NW. Counting on mitogen-activated protein kinases-ERKs 3, 4, 5, 6, 7 and 8. Cell Signal 16: 1345-1354, 2004.
  • 15
    • 0030036727 scopus 로고    scopus 로고
    • Stimulation of the stress-activated mitogen-activated protein kinases subfamilies in perfused heart. p38/RK mitogen-activated kinases and c-Jun N-terminal kinases are activated by ischemia-reperfusion
    • Bogoyevitch MA, Gillespie-Brown J, Ketterman AJ, Fuller SJ, Ben-Levy R, Ashworth A, Marshall CJ, and Sugden PH. Stimulation of the stress-activated mitogen-activated protein kinases subfamilies in perfused heart. p38/RK mitogen-activated kinases and c-Jun N-terminal kinases are activated by ischemia-reperfusion. Circ Res 79: 161-173, 1996.
    • (1996) Circ Res , vol.79 , pp. 161-173
    • Bogoyevitch, M.A.1    Gillespie-Brown, J.2    Ketterman, A.J.3    Fuller, S.J.4    Ben-Levy, R.5    Ashworth, A.6    Marshall, C.J.7    Sugden, P.H.8
  • 16
    • 0027955166 scopus 로고
    • Endothelin-1 and fibroblast growth factors stimulate the mitogen-activated protein kinase signaling cascade in cardiac myocytes. The potential role of the cascade in the integration of two signaling pathways leading to myocyte hypertrophy
    • Bogoyevitch MA, Glennon PE, Andersson MB, Clerk A, Lazou A, Marshall CJ, Parker PJ, and Sugden PH. Endothelin-1 and fibroblast growth factors stimulate the mitogen-activated protein kinase signaling cascade in cardiac myocytes. The potential role of the cascade in the integration of two signaling pathways leading to myocyte hypertrophy. J Biol Chem 269: 1110-1119, 1994.
    • (1994) J Biol Chem , vol.269 , pp. 1110-1119
    • Bogoyevitch, M.A.1    Glennon, P.E.2    Andersson, M.B.3    Clerk, A.4    Lazou, A.5    Marshall, C.J.6    Parker, P.J.7    Sugden, P.H.8
  • 17
    • 0027528410 scopus 로고
    • Endothelin-1, phorbol esters and phenylephrine stimulate MAP kinase activities in ventricular cardiomyocytes
    • Bogoyevitch MA, Glennon PE, and Sugden PH. Endothelin-1, phorbol esters and phenylephrine stimulate MAP kinase activities in ventricular cardiomyocytes. FEBS Lett 317: 271-275, 1993.
    • (1993) FEBS Lett , vol.317 , pp. 271-275
    • Bogoyevitch, M.A.1    Glennon, P.E.2    Sugden, P.H.3
  • 18
    • 0029591827 scopus 로고
    • Cellular stresses differentially activate c-Jun N-terminal protein kinases and extracellular signal-regulated protein kinases in cultured ventricular myocytes
    • Bogoyevitch MA, Ketterman AJ, and Sugden PH. Cellular stresses differentially activate c-Jun N-terminal protein kinases and extracellular signal-regulated protein kinases in cultured ventricular myocytes. J Biol Chem 270: 29710-29717, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 29710-29717
    • Bogoyevitch, M.A.1    Ketterman, A.J.2    Sugden, P.H.3
  • 19
    • 0028839220 scopus 로고
    • Hypertrophic agonists stimulate the activities of the protein kinases c-Raf and A-Raf in cultured ventricular myocytes
    • Bogoyevitch MA, Marshall CJ, and Sugden PH. Hypertrophic agonists stimulate the activities of the protein kinases c-Raf and A-Raf in cultured ventricular myocytes. J Biol Chem 270: 26303-26310, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 26303-26310
    • Bogoyevitch, M.A.1    Marshall, C.J.2    Sugden, P.H.3
  • 20
    • 0033867612 scopus 로고    scopus 로고
    • Intact mitochondrial electron transport function is essential for signaling by hydrogen peroxide in cardiac myocytes
    • Bogoyevitch MA, Ng DCH, Court NW, Draper KA, Dhillon A, and Abas L. Intact mitochondrial electron transport function is essential for signaling by hydrogen peroxide in cardiac myocytes. J Mol Cell Cardiol 32: 1469-1480, 2000.
    • (2000) J Mol Cell Cardiol , vol.32 , pp. 1469-1480
    • Bogoyevitch, M.A.1    Ng, D.C.H.2    Court, N.W.3    Draper, K.A.4    Dhillon, A.5    Abas, L.6
  • 21
    • 0034062098 scopus 로고    scopus 로고
    • Inactivation of calcineurin by hydrogen peroxide and phenylarsine oxide. Evidence for a dithiol-disulfide equilibrium and implications for redox regulation
    • Bogumil R, Namgaladze D, Schaarschmidt D, Schmachtel T, Hellstern S, Mutzel R, and Ullrich V. Inactivation of calcineurin by hydrogen peroxide and phenylarsine oxide. Evidence for a dithiol-disulfide equilibrium and implications for redox regulation. Eur J Biochem 267: 1407-1415, 2000.
    • (2000) Eur J Biochem , vol.267 , pp. 1407-1415
    • Bogumil, R.1    Namgaladze, D.2    Schaarschmidt, D.3    Schmachtel, T.4    Hellstern, S.5    Mutzel, R.6    Ullrich, V.7
  • 22
    • 0035499454 scopus 로고    scopus 로고
    • Ten years of protein kinase B signaling: A hard Akt to follow
    • Brazil DP and Hemmings BA. Ten years of protein kinase B signaling: a hard Akt to follow. Trends Biochem Sci 26: 657-664, 2001.
    • (2001) Trends Biochem Sci , vol.26 , pp. 657-664
    • Brazil, D.P.1    Hemmings, B.A.2
  • 23
    • 2342565881 scopus 로고    scopus 로고
    • Advances in protein kinase B signaling: AKTion on multiple fronts
    • Brazil DP, Yang ZZ, and Hemmings BA. Advances in protein kinase B signaling: AKTion on multiple fronts. Trends Biochem Sci 29: 233-242, 2004.
    • (2004) Trends Biochem Sci , vol.29 , pp. 233-242
    • Brazil, D.P.1    Yang, Z.Z.2    Hemmings, B.A.3
  • 24
    • 0037246123 scopus 로고    scopus 로고
    • Regulation of cell apoptosis by protein kinase c δ
    • Brodie C and Blumberg PM. Regulation of cell apoptosis by protein kinase c δ. Apoptosis 8: 19-27, 2003.
    • (2003) Apoptosis , vol.8 , pp. 19-27
    • Brodie, C.1    Blumberg, P.M.2
  • 26
    • 0036843158 scopus 로고    scopus 로고
    • Involvement of extracellular signal-regulated kinases 1/2 in cardiac hypertrophy and cell death
    • Bueno OF and Molkentin JD. Involvement of extracellular signal-regulated kinases 1/2 in cardiac hypertrophy and cell death. Circ Res 91: 776-781, 2002.
    • (2002) Circ Res , vol.91 , pp. 776-781
    • Bueno, O.F.1    Molkentin, J.D.2
  • 27
    • 33645096801 scopus 로고    scopus 로고
    • Reactive oxygen species generation is involved in epidermal growth factor receptor transactivation through the transient oxidization of Src homology 2-containing tyrosine phosphatase in endothelin-1 signaling pathway in rat cardiac fibroblasts
    • Chen CH, Cheng TH, Lin H, Shih NL, Chen YL, Chen YS, Cheng CF, Lian WS, Meng TC, Chiu WT, and Chen JJ. Reactive oxygen species generation is involved in epidermal growth factor receptor transactivation through the transient oxidization of Src homology 2-containing tyrosine phosphatase in endothelin-1 signaling pathway in rat cardiac fibroblasts. Mol Pharmacol 69: 1347-1355, 2006.
    • (2006) Mol Pharmacol , vol.69 , pp. 1347-1355
    • Chen, C.H.1    Cheng, T.H.2    Lin, H.3    Shih, N.L.4    Chen, Y.L.5    Chen, Y.S.6    Cheng, C.F.7    Lian, W.S.8    Meng, T.C.9    Chiu, W.T.10    Chen, J.J.11
  • 28
    • 0033963541 scopus 로고    scopus 로고
    • Hydrogen peroxide dose dependent induction of cell death or hypertrophy in cardiac myocytes
    • Chen QM, Tu VC, Wu Y, and Bahl JJ. Hydrogen peroxide dose dependent induction of cell death or hypertrophy in cardiac myocytes. Arch Biochem Biophys 373: 242-248, 2000.
    • (2000) Arch Biochem Biophys , vol.373 , pp. 242-248
    • Chen, Q.M.1    Tu, V.C.2    Wu, Y.3    Bahl, J.J.4
  • 30
    • 0242721091 scopus 로고    scopus 로고
    • Involvement of reactive oxygen species in angiotensin II-induced endothelin-1 gene expression in rat cardiac fibroblasts
    • Cheng T-H, Cheng P-Y, Shih N-L, Chen I-B, Wang DL, and Chen J-J. Involvement of reactive oxygen species in angiotensin II-induced endothelin-1 gene expression in rat cardiac fibroblasts. J Am Coll Cardiol 42: 1845-1854, 2003.
    • (2003) J Am Coll Cardiol , vol.42 , pp. 1845-1854
    • Cheng, T.-H.1    Cheng, P.-Y.2    Shih, N.-L.3    Chen, I.-B.4    Wang, D.L.5    Chen, J.-J.6
  • 31
    • 0033035157 scopus 로고    scopus 로고
    • Reactive oxygen species modulate endothelin-1-induced c-fos gene expression in cardiomyocytes
    • Cheng TH, Shih NL, Chen SY, Wang DL, and Chen JJ. Reactive oxygen species modulate endothelin-1-induced c-fos gene expression in cardiomyocytes. Cardiovasc Res 41: 654-662, 1999.
    • (1999) Cardiovasc Res , vol.41 , pp. 654-662
    • Cheng, T.H.1    Shih, N.L.2    Chen, S.Y.3    Wang, D.L.4    Chen, J.J.5
  • 32
    • 0033538338 scopus 로고    scopus 로고
    • Regulation of Ras.GTP loading and Ras-Raf association in neonatal rat ventricular myocytes by G protein-coupled receptor agonists and phorbol ester. Activation of the ERK cascade by phorbol ester is mediated by Ras
    • Chiloeches A, Paterson HF, Marais R, Clerk A, Marshall CJ, and Sugden PH. Regulation of Ras.GTP loading and Ras-Raf association in neonatal rat ventricular myocytes by G protein-coupled receptor agonists and phorbol ester. Activation of the ERK cascade by phorbol ester is mediated by Ras. J Biol Chem 274: 19762-19770, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 19762-19770
    • Chiloeches, A.1    Paterson, H.F.2    Marais, R.3    Clerk, A.4    Marshall, C.J.5    Sugden, P.H.6
  • 33
    • 32144460477 scopus 로고    scopus 로고
    • C-terminal Src kinase (CSK) and CSK-homologous kinase (CHK)-endogenous negative regulators of Src-family protein kinases
    • Chong Y-P, Mulhern TD, and Cheng H-C. C-terminal Src kinase (CSK) and CSK-homologous kinase (CHK)-endogenous negative regulators of Src-family protein kinases. Growth Factors 23: 233-244, 2005.
    • (2005) Growth Factors , vol.23 , pp. 233-244
    • Chong, Y.-P.1    Mulhern, T.D.2    Cheng, H.-C.3
  • 34
    • 0037325938 scopus 로고    scopus 로고
    • PKC isozyme S-cysteinylation by cystine stimulates the pro-apoptotic isozyme PKCδ and inactivates the oncogenic isozyme PKCε
    • Chu F, Ward NE, and O'Brian CA. PKC isozyme S-cysteinylation by cystine stimulates the pro-apoptotic isozyme PKCδ and inactivates the oncogenic isozyme PKCε. Carcinogenesis 24: 317-325, 2003.
    • (2003) Carcinogenesis , vol.24 , pp. 317-325
    • Chu, F.1    Ward, N.E.2    O'Brian, C.A.3
  • 35
    • 0038482115 scopus 로고    scopus 로고
    • Oxidative stress induces protein phosphatase 2A-dependent dephosphorylation of the pocket proteins pRb, p107, and p130
    • Cicchilliti L, Fasanaro P, Biglioli P, Capogrossi MC, and Martelli F. Oxidative stress induces protein phosphatase 2A-dependent dephosphorylation of the pocket proteins pRb, p107, and p130. J Biol Chem 278: 19509-19517, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 19509-19517
    • Cicchilliti, L.1    Fasanaro, P.2    Biglioli, P.3    Capogrossi, M.C.4    Martelli, F.5
  • 36
    • 33645806282 scopus 로고    scopus 로고
    • S-glutathiolation by peroxynitrite of p21ras at cysteine-118 mediates its direct activation and downstream signaling in endothelial cells
    • Clavreul N, Adachi T, Pimental DR, Ido Y, Schöneich C, and Cohen RA. S-glutathiolation by peroxynitrite of p21ras at cysteine-118 mediates its direct activation and downstream signaling in endothelial cells. FASEB J 20: 518-520, 2006.
    • (2006) FASEB J , vol.20 , pp. 518-520
    • Clavreul, N.1    Adachi, T.2    Pimental, D.R.3    Ido, Y.4    Schöneich, C.5    Cohen, R.A.6
  • 37
    • 27344448911 scopus 로고    scopus 로고
    • Peptide growth factors signal differentially through protein kinase C to extracellular signal-regulated kinase in neonatal cardiomyocytes
    • Clerk A, Aggeli I-K, Stathopoulou K, and Sugden PH. Peptide growth factors signal differentially through protein kinase C to extracellular signal-regulated kinase in neonatal cardiomyocytes. Cell Signal 18: 225-235, 2006.
    • (2006) Cell Signal , vol.18 , pp. 225-235
    • Clerk, A.1    Aggeli, I.-K.2    Stathopoulou, K.3    Sugden, P.H.4
  • 38
    • 0028589299 scopus 로고
    • Differential activation of protein kinase C isoforms by endothelin-1 and phenylephrine and subsequent stimulation of p42 and p44 mitogen-activated protein kinases in ventricular myocytes cultured from neonatal rat hearts
    • Clerk A, Bogoyevitch MA, Andersson MB, and Sugden PH. Differential activation of protein kinase C isoforms by endothelin-1 and phenylephrine and subsequent stimulation of p42 and p44 mitogen-activated protein kinases in ventricular myocytes cultured from neonatal rat hearts. J Biol Chem 269: 32848-32857, 1994.
    • (1994) J Biol Chem , vol.269 , pp. 32848-32857
    • Clerk, A.1    Bogoyevitch, M.A.2    Andersson, M.B.3    Sugden, P.H.4
  • 40
    • 0032571270 scopus 로고    scopus 로고
    • Stimulation of "stress-regulated" mitogen-activated protein kinases (stress-activated protein kinases/c-Jun N-terminal kinases and p38-mitogen-activated protein kinases) by oxidative and other stresses
    • Clerk A, Fuller SJ, Michael A, and Sugden PH. Stimulation of "stress-regulated" mitogen-activated protein kinases (stress-activated protein kinases/c-Jun N-terminal kinases and p38-mitogen-activated protein kinases) by oxidative and other stresses. J Biol Chem 273: 7228-7234, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 7228-7234
    • Clerk, A.1    Fuller, S.J.2    Michael, A.3    Sugden, P.H.4
  • 41
    • 0032572534 scopus 로고    scopus 로고
    • Stimulation of the p38 mitogen-activated protein kinase pathway in neonatal rat ventricular myocytes by the G protein-coupled receptor agonists, endothelin-1 and phenylephrine: A role in cardiac myocyte hypertrophy?
    • Clerk A, Michael A, and Sugden PH. Stimulation of the p38 mitogen-activated protein kinase pathway in neonatal rat ventricular myocytes by the G protein-coupled receptor agonists, endothelin-1 and phenylephrine: a role in cardiac myocyte hypertrophy? J Cell Biol 142: 523-535, 1998.
    • (1998) J Cell Biol , vol.142 , pp. 523-535
    • Clerk, A.1    Michael, A.2    Sugden, P.H.3
  • 42
    • 0032143920 scopus 로고    scopus 로고
    • Stimulation of multiple mitogen-activated protein kinase sub-families by oxidative stress and phosphorylation of the small heat shock protein, HSP25/27, in neonatal ventricular myocytes
    • Clerk A, Michael A, and Sugden PH. Stimulation of multiple mitogen-activated protein kinase sub-families by oxidative stress and phosphorylation of the small heat shock protein, HSP25/27, in neonatal ventricular myocytes. Biochem J 333: 581-589, 1998.
    • (1998) Biochem J , vol.333 , pp. 581-589
    • Clerk, A.1    Michael, A.2    Sugden, P.H.3
  • 44
    • 0034717136 scopus 로고    scopus 로고
    • Small guanine nucleotide-binding proteins and myocardial hypertrophy
    • Clerk A and Sugden PH. Small guanine nucleotide-binding proteins and myocardial hypertrophy. Circ Res 86: 1019-1023, 2000.
    • (2000) Circ Res , vol.86 , pp. 1019-1023
    • Clerk, A.1    Sugden, P.H.2
  • 45
    • 0030783156 scopus 로고    scopus 로고
    • The search for physiological substrates of MAP and SAP kinases in mammalian cells
    • Cohen P. The search for physiological substrates of MAP and SAP kinases in mammalian cells. Trends Cell Biol 7: 353-361, 1997.
    • (1997) Trends Cell Biol , vol.7 , pp. 353-361
    • Cohen, P.1
  • 46
    • 0025181418 scopus 로고
    • Okadaic acid: A new probe for the study of cellular regulation
    • Cohen P, Holmes CF, and Tsukitani Y. Okadaic acid: a new probe for the study of cellular regulation. Trends Biochem Sci 15: 98-102, 1990.
    • (1990) Trends Biochem Sci , vol.15 , pp. 98-102
    • Cohen, P.1    Holmes, C.F.2    Tsukitani, Y.3
  • 47
    • 0032745819 scopus 로고    scopus 로고
    • Regulation of Bcl-2 family proteins during development and in response to oxidative stress in cardiac myocytes: Association with changes in mitochondrial membrane potential
    • Cook SA, Sugden PH, and Clerk A. Regulation of Bcl-2 family proteins during development and in response to oxidative stress in cardiac myocytes: association with changes in mitochondrial membrane potential. Circ Res 85: 940-949, 1999.
    • (1999) Circ Res , vol.85 , pp. 940-949
    • Cook, S.A.1    Sugden, P.H.2    Clerk, A.3
  • 48
    • 0036549872 scopus 로고    scopus 로고
    • Cardiac expression and subcellular localization of the p38 mitogen-activated protein kinase member, stress-activated protein kinase-3 (SAPK3)
    • Court NW, dos Remedies CG, Cordell J, and Bogoyevitch MA. Cardiac expression and subcellular localization of the p38 mitogen-activated protein kinase member, stress-activated protein kinase-3 (SAPK3). J Mol Cell Cardiol 34: 413-426, 2002.
    • (2002) J Mol Cell Cardiol , vol.34 , pp. 413-426
    • Court, N.W.1    dos Remedies, C.G.2    Cordell, J.3    Bogoyevitch, M.A.4
  • 49
    • 0031055415 scopus 로고    scopus 로고
    • Minimal Ras binding domain of Raf1 can be used as an activation-specific probe for Ras
    • de Rooij J and Bos JL. Minimal Ras binding domain of Raf1 can be used as an activation-specific probe for Ras. Oncogene 14: 623-625, 1997.
    • (1997) Oncogene , vol.14 , pp. 623-625
    • de Rooij, J.1    Bos, J.L.2
  • 51
    • 0037086678 scopus 로고    scopus 로고
    • Activation of c-Jun N-terminal kinase promotes survival of cardiac myocytes after oxidative stress
    • Dougherty CJ, Kubasiak LA, Prentice H, Andreka P, Bishopric NH, and Webster KA. Activation of c-Jun N-terminal kinase promotes survival of cardiac myocytes after oxidative stress. Biochem J 362: 561-571, 2002.
    • (2002) Biochem J , vol.362 , pp. 561-571
    • Dougherty, C.J.1    Kubasiak, L.A.2    Prentice, H.3    Andreka, P.4    Bishopric, N.H.5    Webster, K.A.6
  • 52
    • 2042538029 scopus 로고    scopus 로고
    • Structure and regulation of MAPK phosphatases
    • Farooq A and Zhou MM. Structure and regulation of MAPK phosphatases. Cell Signal 16: 769-779, 2004.
    • (2004) Cell Signal , vol.16 , pp. 769-779
    • Farooq, A.1    Zhou, M.M.2
  • 53
    • 0023715225 scopus 로고
    • Inhibition of NIH 3T3 cell proliferation by a mutant ras protein with preferential affinity for GDP
    • Feig LA and Cooper GM. Inhibition of NIH 3T3 cell proliferation by a mutant ras protein with preferential affinity for GDP. Mol Cell Biol 8: 3235-3243, 1988.
    • (1988) Mol Cell Biol , vol.8 , pp. 3235-3243
    • Feig, L.A.1    Cooper, G.M.2
  • 55
    • 0002537440 scopus 로고    scopus 로고
    • Cardiac hypertrophy: The good, the bad, and the ugly
    • Frey N and Olson EN. Cardiac hypertrophy: the good, the bad, and the ugly. Annu Rev Physiol 65: 45-79, 2003.
    • (2003) Annu Rev Physiol , vol.65 , pp. 45-79
    • Frey, N.1    Olson, E.N.2
  • 56
    • 20544472348 scopus 로고    scopus 로고
    • Regulation of protein function by glutathionylation
    • Ghezzi P. Regulation of protein function by glutathionylation. Free Radic Res 39: 573-580, 2005.
    • (2005) Free Radic Res , vol.39 , pp. 573-580
    • Ghezzi, P.1
  • 57
    • 14644442283 scopus 로고    scopus 로고
    • Oxygen, oxidative stress, hypoxia, and heart failure
    • Giordano FJ. Oxygen, oxidative stress, hypoxia, and heart failure. J Clin Invest 115: 500-508, 2005.
    • (2005) J Clin Invest , vol.115 , pp. 500-508
    • Giordano, F.J.1
  • 58
    • 0028332649 scopus 로고
    • Excitation-contraction coupling in single guinea-pig ventricular myocytes exposed to hydrogen peroxide
    • Goldhaber JI and Liu E. Excitation-contraction coupling in single guinea-pig ventricular myocytes exposed to hydrogen peroxide. J Physiol 477: 135-147, 1994.
    • (1994) J Physiol , vol.477 , pp. 135-147
    • Goldhaber, J.I.1    Liu, E.2
  • 59
    • 0032126920 scopus 로고    scopus 로고
    • Redox control of vascular smooth muscle proliferation
    • Griendling KK and Ushio-Fukai M. Redox control of vascular smooth muscle proliferation. J Lab Clin Med 132: 9-15, 1998.
    • (1998) J Lab Clin Med , vol.132 , pp. 9-15
    • Griendling, K.K.1    Ushio-Fukai, M.2
  • 61
    • 0037710311 scopus 로고    scopus 로고
    • The isoform-specific regulation of apoptosis by protein kinase C
    • Gutcher I, Webb PR, and Anderson NG. The isoform-specific regulation of apoptosis by protein kinase C. Cell Mol Life Sci 60: 1061-1070, 2003.
    • (2003) Cell Mol Life Sci , vol.60 , pp. 1061-1070
    • Gutcher, I.1    Webb, P.R.2    Anderson, N.G.3
  • 62
    • 0024388725 scopus 로고
    • Spin-labeling proton NMR study on aromatic amino acid residues in the guanine nucleotide binding site of human c-Ha-ras(1-171) protein
    • Hata-Tanaka A, Kawai G, Yamasaki K, Ito Y, Kajiura H, Ha JM, Miyazawa T, Yokoyama S, and Nishimura S. Spin-labeling proton NMR study on aromatic amino acid residues in the guanine nucleotide binding site of human c-Ha-ras(1-171) protein. Biochemistry 28: 9550-9556, 1989.
    • (1989) Biochemistry , vol.28 , pp. 9550-9556
    • Hata-Tanaka, A.1    Kawai, G.2    Yamasaki, K.3    Ito, Y.4    Kajiura, H.5    Ha, J.M.6    Miyazawa, T.7    Yokoyama, S.8    Nishimura, S.9
  • 63
    • 12444285810 scopus 로고    scopus 로고
    • Role of the BMK1/ERK5 signaling pathway: Lessons from knockout mice
    • Hayashi M and Lee J-D. Role of the BMK1/ERK5 signaling pathway: lessons from knockout mice. J Mol Med 82: 800-808, 2004.
    • (2004) J Mol Med , vol.82 , pp. 800-808
    • Hayashi, M.1    Lee, J.-D.2
  • 64
    • 0035834817 scopus 로고    scopus 로고
    • Differential activation of mitogen-activated protein kinase cascades and apoptosis by protein kinase Cε and δ in neonatal rat ventricular myocytes
    • Heidkamp MC, Bayer AL, Martin JL, and Samarel AM. Differential activation of mitogen-activated protein kinase cascades and apoptosis by protein kinase Cε and δ in neonatal rat ventricular myocytes. Circ Res 89: 882-890, 2001.
    • (2001) Circ Res , vol.89 , pp. 882-890
    • Heidkamp, M.C.1    Bayer, A.L.2    Martin, J.L.3    Samarel, A.M.4
  • 65
    • 1442300935 scopus 로고    scopus 로고
    • Ras S-nitrosylation and kinetics of nitric oxide-mediated guanine nucleotide exchange
    • Ras S-nitrosylation and kinetics of nitric oxide-mediated guanine nucleotide exchange. Biochemistry 43: 2314-2322, 2004.
    • (2004) Biochemistry , vol.43 , pp. 2314-2322
    • Heo, J.1    Campbell, S.L.2
  • 66
    • 16844374922 scopus 로고    scopus 로고
    • Superoxide anion radical modulates the activity of Ras and Ras-related GTPases by a radical mechanism similar to that of nitric oxide
    • Heo J and Campbell SL. Superoxide anion radical modulates the activity of Ras and Ras-related GTPases by a radical mechanism similar to that of nitric oxide. J Biol Chem 280: 12438-12435, 2005.
    • (2005) J Biol Chem , vol.280 , pp. 12438-12435
    • Heo, J.1    Campbell, S.L.2
  • 67
    • 24744433531 scopus 로고    scopus 로고
    • Mechanism of redox-mediated guanine nucleotide exchange on redox-active Rho GTPases
    • Heo J and Campbell SL. Mechanism of redox-mediated guanine nucleotide exchange on redox-active Rho GTPases. J Biol Chem 280: 31003-31010, 2005.
    • (2005) J Biol Chem , vol.280 , pp. 31003-31010
    • Heo, J.1    Campbell, S.L.2
  • 68
    • 33144488804 scopus 로고    scopus 로고
    • Ras regulation by reactive oxygen and nitrogen species
    • Heo J and Campbell SL. Ras regulation by reactive oxygen and nitrogen species. Biochemistry 45: 2200-2210, 2006.
    • (2006) Biochemistry , vol.45 , pp. 2200-2210
    • Heo, J.1    Campbell, S.L.2
  • 69
    • 13844298143 scopus 로고    scopus 로고
    • Mechanism of free radical nitric oxide-mediated Ras guanine nucleotide dissociation
    • Heo J, Prutzman KC, Mocanu V, and Campbell SL. Mechanism of free radical nitric oxide-mediated Ras guanine nucleotide dissociation. J Mol Biol 346: 1423-1440, 2005.
    • (2005) J Mol Biol , vol.346 , pp. 1423-1440
    • Heo, J.1    Prutzman, K.C.2    Mocanu, V.3    Campbell, S.L.4
  • 72
    • 0032571395 scopus 로고    scopus 로고
    • The low molecular weight GTPase Rho regulates myofibril formation and organization in neonatal rat ventricular myocytes. Involvement of Rho kinase
    • Hoshijima M, Sah VP, Wang Y, Chien KR, and Brown JH. The low molecular weight GTPase Rho regulates myofibril formation and organization in neonatal rat ventricular myocytes. Involvement of Rho kinase. J Biol Chem 273: 7725-7730, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 7725-7730
    • Hoshijima, M.1    Sah, V.P.2    Wang, Y.3    Chien, K.R.4    Brown, J.H.5
  • 73
    • 0242266963 scopus 로고    scopus 로고
    • Apoptosis signal-regulating kinase 1 plays a pivotal role in angiotensin 11-induced cardiac hypertrophy and remodeling
    • Izumiya Y, Kim S, Izumi Y, Yoshida K, Yoshiyama M, Matsuzawa A, Ichijo H, and Iwao H. Apoptosis signal-regulating kinase 1 plays a pivotal role in angiotensin 11-induced cardiac hypertrophy and remodeling. Circ Res 93: 874-883, 2003.
    • (2003) Circ Res , vol.93 , pp. 874-883
    • Izumiya, Y.1    Kim, S.2    Izumi, Y.3    Yoshida, K.4    Yoshiyama, M.5    Matsuzawa, A.6    Ichijo, H.7    Iwao, H.8
  • 75
    • 0142200985 scopus 로고    scopus 로고
    • Role of proteolytic activation of protein kinase Cδ in oxidative stress-induced apoptosis
    • Kanthasamy AG, Kitazawa M, Kanthasamy A, and Anantharam V. Role of proteolytic activation of protein kinase Cδ in oxidative stress-induced apoptosis. Antioxid Redox Signal 5: 609-620, 2003.
    • (2003) Antioxid Redox Signal , vol.5 , pp. 609-620
    • Kanthasamy, A.G.1    Kitazawa, M.2    Kanthasamy, A.3    Anantharam, V.4
  • 76
    • 23344444562 scopus 로고    scopus 로고
    • Tyrosine phosphorylation regulates the proteolytic activation of protein kinase Cδ in dopaminergic neuronal cells
    • Kaul S, Anantharam V, Yang Y, Choi CJ, Kanthasamy A, and Kanthasamy AG. Tyrosine phosphorylation regulates the proteolytic activation of protein kinase Cδ in dopaminergic neuronal cells. J Biol Chem 280: 28721-28730, 2005.
    • (2005) J Biol Chem , vol.280 , pp. 28721-28730
    • Kaul, S.1    Anantharam, V.2    Yang, Y.3    Choi, C.J.4    Kanthasamy, A.5    Kanthasamy, A.G.6
  • 77
    • 33746852467 scopus 로고    scopus 로고
    • Using U0126 to dissect the role of the extracellular signal-regulated kinase 1/2 (ERK1/2) cascade in the regulation of gene expression by endothelin-1 in cardiac myocytes
    • Kennedy RA, Kemp TJ, Sugden PH, and Clerk A. Using U0126 to dissect the role of the extracellular signal-regulated kinase 1/2 (ERK1/2) cascade in the regulation of gene expression by endothelin-1 in cardiac myocytes. J Mol Cell Cardiol 41: 236-247, 2006.
    • (2006) J Mol Cell Cardiol , vol.41 , pp. 236-247
    • Kennedy, R.A.1    Kemp, T.J.2    Sugden, P.H.3    Clerk, A.4
  • 79
    • 18244390487 scopus 로고    scopus 로고
    • Myeloperoxidase: Friend and foe
    • Klebanoff SJ. Myeloperoxidase: friend and foe. J Leukoc Biol 77: 598-625, 2005.
    • (2005) J Leukoc Biol , vol.77 , pp. 598-625
    • Klebanoff, S.J.1
  • 82
    • 0031587929 scopus 로고    scopus 로고
    • Novel homologues of CSBP/p38 MAP kinase: Activation, substrate specificity and sensitivity to inhibition by pyridinyl imidazoles
    • Kumar S, McDonnell PC, Gum RJ, Hand AT, Lee JC, and Young PR. Novel homologues of CSBP/p38 MAP kinase: activation, substrate specificity and sensitivity to inhibition by pyridinyl imidazoles. Biochem Biophys Res Commun 235: 533-538, 1997.
    • (1997) Biochem Biophys Res Commun , vol.235 , pp. 533-538
    • Kumar, S.1    McDonnell, P.C.2    Gum, R.J.3    Hand, A.T.4    Lee, J.C.5    Young, P.R.6
  • 83
    • 14944371448 scopus 로고    scopus 로고
    • α-Adrenergic receptor-stimulated hypertrophy in adult rat ventricular myocytes is mediated via thioredoxin-1-sensitive oxidation of thiols on Ras
    • Kuster GM, Pimentel DR, Adachi T, Ido Y, Brenner DA, Cohen RA, Liao R, Siwik DA, and Colucci WS. α-Adrenergic receptor-stimulated hypertrophy in adult rat ventricular myocytes is mediated via thioredoxin-1-sensitive oxidation of thiols on Ras. Circulation 111: 1192-1198, 2005.
    • (2005) Circulation , vol.111 , pp. 1192-1198
    • Kuster, G.M.1    Pimentel, D.R.2    Adachi, T.3    Ido, Y.4    Brenner, D.A.5    Cohen, R.A.6    Liao, R.7    Siwik, D.A.8    Colucci, W.S.9
  • 86
    • 0034975973 scopus 로고    scopus 로고
    • Antioxidants inhibit JNK and p38 MAPK activation but not ERK 1/2 activation by angiotensin II in rat aortic smooth muscle cells
    • Kyaw M, Yoshizumi M, Tsuchiya K, Kirima K, and Tamaki T. Antioxidants inhibit JNK and p38 MAPK activation but not ERK 1/2 activation by angiotensin II in rat aortic smooth muscle cells. Hypertens Res 24: 251-261, 2001.
    • (2001) Hypertens Res , vol.24 , pp. 251-261
    • Kyaw, M.1    Yoshizumi, M.2    Tsuchiya, K.3    Kirima, K.4    Tamaki, T.5
  • 87
    • 0031057890 scopus 로고    scopus 로고
    • Hypoxia/reoxygenation stimulates Jun kinase activity through redox signaling in cardiac myocytes
    • Laderoute KR and Webster KA. Hypoxia/reoxygenation stimulates Jun kinase activity through redox signaling in cardiac myocytes. Circ Res 80: 336-344, 1997.
    • (1997) Circ Res , vol.80 , pp. 336-344
    • Laderoute, K.R.1    Webster, K.A.2
  • 88
    • 1542406446 scopus 로고    scopus 로고
    • NOX enzymes and the biology of reactive oxygen
    • Lambeth JD. NOX enzymes and the biology of reactive oxygen. Nat Rev Immunol 4: 181-189, 2004.
    • (2004) Nat Rev Immunol , vol.4 , pp. 181-189
    • Lambeth, J.D.1
  • 90
    • 0032104249 scopus 로고    scopus 로고
    • Activation of mitogen-activated protein kinases (p38-MAPKs, SAPKs/JNKs and ERKs) by the G protein-coupled receptor agonist phenylephrine in the perfused rat heart
    • Lazou A, Sugden PH, and Clerk A. Activation of mitogen-activated protein kinases (p38-MAPKs, SAPKs/JNKs and ERKs) by the G protein-coupled receptor agonist phenylephrine in the perfused rat heart. Biochem J 332: 459-465, 1998.
    • (1998) Biochem J , vol.332 , pp. 459-465
    • Lazou, A.1    Sugden, P.H.2    Clerk, A.3
  • 92
    • 0034925481 scopus 로고    scopus 로고
    • Decreased p38 MAPK activity in end-stage failing human myocardium: P38 MAPK α is the predominant isoform expressed in human heart
    • Lemke LE, Bloem LJ, Fouts R, Esterman M, Sandusky G, and Vlahos CJ. Decreased p38 MAPK activity in end-stage failing human myocardium: p38 MAPK α is the predominant isoform expressed in human heart. J Mol Cell Cardiol 33: 1527-1540, 2001.
    • (2001) J Mol Cell Cardiol , vol.33 , pp. 1527-1540
    • Lemke, L.E.1    Bloem, L.J.2    Fouts, R.3    Esterman, M.4    Sandusky, G.5    Vlahos, C.J.6
  • 93
    • 0033528695 scopus 로고    scopus 로고
    • Inhibition of p38 mitogen-activated protein kinase decreases cardiomyocyte apoptosis and improves cardiac function after myocardial ischemia and reperfusion
    • Ma XL, Kumar S, Gao F, Louden CS, Lopez BL, Christopher TA, Wang C, Lee JC, Feuerstein GZ, and Yue TL. Inhibition of p38 mitogen-activated protein kinase decreases cardiomyocyte apoptosis and improves cardiac function after myocardial ischemia and reperfusion. Circulation 99: 1685-1691, 1999.
    • (1999) Circulation , vol.99 , pp. 1685-1691
    • Ma, X.L.1    Kumar, S.2    Gao, F.3    Louden, C.S.4    Lopez, B.L.5    Christopher, T.A.6    Wang, C.7    Lee, J.C.8    Feuerstein, G.Z.9    Yue, T.L.10
  • 94
    • 11144253483 scopus 로고    scopus 로고
    • Convergent signal transduction pathways controlling cardiomyocyte survival and function: The role of P1 3-kinase and Akt
    • Matsui T and Rosenzweig A. Convergent signal transduction pathways controlling cardiomyocyte survival and function: the role of P1 3-kinase and Akt. J Mol Cell Cardiol 38: 63-71, 2005.
    • (2005) J Mol Cell Cardiol , vol.38 , pp. 63-71
    • Matsui, T.1    Rosenzweig, A.2
  • 95
    • 0042355181 scopus 로고    scopus 로고
    • Protein prenyl-transferases: Anchor size, pseudogenes and parasites
    • Maurer-Stroh S, Washietl S, and Eisenhaber F. Protein prenyl-transferases: anchor size, pseudogenes and parasites. Biol Chem 384: 977-989, 2003.
    • (2003) Biol Chem , vol.384 , pp. 977-989
    • Maurer-Stroh, S.1    Washietl, S.2    Eisenhaber, F.3
  • 96
    • 0031000742 scopus 로고    scopus 로고
    • Structural and functional analysis of a mutant Ras protein that is insensitive to nitric oxide activation
    • Mott HR, Carpenter JW, and Campbell SL. Structural and functional analysis of a mutant Ras protein that is insensitive to nitric oxide activation. Biochemistry 36: 3640-3644, 1997.
    • (1997) Biochemistry , vol.36 , pp. 3640-3644
    • Mott, H.R.1    Carpenter, J.W.2    Campbell, S.L.3
  • 98
    • 9144256765 scopus 로고    scopus 로고
    • Protein kinase Cδ activation induces apoptosis in response to cardiac ischemia and reperfusion damage: A mechanism involving BAD and the mitochondria
    • Murriel CL, Churchill E, Inagaki K, Szweda LI, and Mochly-Rosen D. Protein kinase Cδ activation induces apoptosis in response to cardiac ischemia and reperfusion damage: a mechanism involving BAD and the mitochondria. J Biol Chem 279: 47985-47991, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 47985-47991
    • Murriel, C.L.1    Churchill, E.2    Inagaki, K.3    Szweda, L.I.4    Mochly-Rosen, D.5
  • 99
    • 0032566405 scopus 로고    scopus 로고
    • Inhibitory effects of antioxidants on neonatal rat cardiac myocyte hypertrophy induced by tumor necrosis factor- and angiotensin II
    • Nakamura K, Fushimi K, Kouchi H, Mihara K, Miyazaki M, Ohe T, and Namba M. Inhibitory effects of antioxidants on neonatal rat cardiac myocyte hypertrophy induced by tumor necrosis factor-" and angiotensin II. Circulation 98: 794-799, 1998.
    • (1998) Circulation , vol.98 , pp. 794-799
    • Nakamura, K.1    Fushimi, K.2    Kouchi, H.3    Mihara, K.4    Miyazaki, M.5    Ohe, T.6    Namba, M.7
  • 100
    • 0035413601 scopus 로고    scopus 로고
    • Protein kinase C: Structural and spatial regulation by phosphorylation, cofactors, and macromolecular interactions
    • Newton AC. Protein kinase C: structural and spatial regulation by phosphorylation, cofactors, and macromolecular interactions. Chem Rev 101: 2353-2364, 2001.
    • (2001) Chem Rev , vol.101 , pp. 2353-2364
    • Newton, A.C.1
  • 101
    • 0037337159 scopus 로고    scopus 로고
    • Regulation of the ABC kinases by phosphorylation: Protein kinase C as a paradigm
    • Newton AC. Regulation of the ABC kinases by phosphorylation: protein kinase C as a paradigm. Biochem J 370: 361-371, 2003.
    • (2003) Biochem J , vol.370 , pp. 361-371
    • Newton, A.C.1
  • 102
    • 0035355360 scopus 로고    scopus 로고
    • Activated MEK5 induces serial assembly of sarcomeres and eccentric cardiac hypertrophy
    • Nicol RL, Frey N, Pearson G, Cobb M, Richardson J, and Olson EN. Activated MEK5 induces serial assembly of sarcomeres and eccentric cardiac hypertrophy. EMBO J 20: 2757-2767, 2001.
    • (2001) EMBO J , vol.20 , pp. 2757-2767
    • Nicol, R.L.1    Frey, N.2    Pearson, G.3    Cobb, M.4    Richardson, J.5    Olson, E.N.6
  • 103
    • 19044381583 scopus 로고    scopus 로고
    • Post-translational disulfide modifications in cell signaling-role of inter-protein, intra-protein, S-glutathionyl, and S-cystaminyl disulfide modifications in signal transmission
    • O'Brian CA and Chu F. Post-translational disulfide modifications in cell signaling-role of inter-protein, intra-protein, S-glutathionyl, and S-cystaminyl disulfide modifications in signal transmission. Free Radic Res 39: 471-480, 2005.
    • (2005) Free Radic Res , vol.39 , pp. 471-480
    • O'Brian, C.A.1    Chu, F.2
  • 104
    • 0042163035 scopus 로고    scopus 로고
    • Reversible inhibition of the protein phosphatase 1 by hydrogen peroxide. Potential regulation of eIF2α phosphorylation in differentiated PC-12 cells
    • O'Loghlen A, Perez-Morgado MI, Salinas M, and Martin ME. Reversible inhibition of the protein phosphatase 1 by hydrogen peroxide. Potential regulation of eIF2α phosphorylation in differentiated PC-12 cells. Arch Biochem Biophys 417: 194-202, 2003.
    • (2003) Arch Biochem Biophys , vol.417 , pp. 194-202
    • O'Loghlen, A.1    Perez-Morgado, M.I.2    Salinas, M.3    Martin, M.E.4
  • 105
    • 0042161933 scopus 로고    scopus 로고
    • Sizing up the heart: Development redux in disease
    • Olson EN and Schneider MD. Sizing up the heart: development redux in disease. Genes Dev 17: 1937-1956, 2003.
    • (2003) Genes Dev , vol.17 , pp. 1937-1956
    • Olson, E.N.1    Schneider, M.D.2
  • 107
    • 1642421710 scopus 로고    scopus 로고
    • Parker PJ and Murray-Rust J. PKC at a glance. J Cell Sci 117: 131-132, 2004.
    • Parker PJ and Murray-Rust J. PKC at a glance. J Cell Sci 117: 131-132, 2004.
  • 109
    • 24144455328 scopus 로고    scopus 로고
    • Role of reactive oxygen species and protein kinase C in ischemic tolerance in the brain
    • Perez-Pinzon MA, Dave KR, and Raval AP. Role of reactive oxygen species and protein kinase C in ischemic tolerance in the brain. Antioxid Redox Signal 7: 1150-1157, 2005.
    • (2005) Antioxid Redox Signal , vol.7 , pp. 1150-1157
    • Perez-Pinzon, M.A.1    Dave, K.R.2    Raval, A.P.3
  • 110
    • 0034705239 scopus 로고    scopus 로고
    • Regulation of protein kinase B and 4E-BP1 by oxidative stress in cardiac myocytes
    • Pham FH, Sugden PH, and Clerk A. Regulation of protein kinase B and 4E-BP1 by oxidative stress in cardiac myocytes. Circ Res 86: 1252-1258, 2000.
    • (2000) Circ Res , vol.86 , pp. 1252-1258
    • Pham, F.H.1    Sugden, P.H.2    Clerk, A.3
  • 112
    • 0029763774 scopus 로고    scopus 로고
    • Hydrogen peroxide induces complex formation of SHC-Grb2-SOS with receptor tyrosine kinase and activates Ras and extracellular signal-regulated protein kinase group of mitogen-activated protein kinases
    • Rao GN. Hydrogen peroxide induces complex formation of SHC-Grb2-SOS with receptor tyrosine kinase and activates Ras and extracellular signal-regulated protein kinase group of mitogen-activated protein kinases. Oncogene 13: 713-719, 1996.
    • (1996) Oncogene , vol.13 , pp. 713-719
    • Rao, G.N.1
  • 113
    • 0036291166 scopus 로고    scopus 로고
    • Regulation of protein phosphatase 2A by hydrogen peroxide and glutathiolation
    • Rao RK and Clayton LW. Regulation of protein phosphatase 2A by hydrogen peroxide and glutathiolation. Biochem Biophys Res Commun 293: 610-616, 2002.
    • (2002) Biochem Biophys Res Commun , vol.293 , pp. 610-616
    • Rao, R.K.1    Clayton, L.W.2
  • 115
    • 0034633602 scopus 로고    scopus 로고
    • Hydrogen peroxide: A key messenger that modulates protein phosphorylation through cysteine oxidation
    • Rhee SG, Bae YS, Lee SR, and Kwon J. Hydrogen peroxide: a key messenger that modulates protein phosphorylation through cysteine oxidation. Sci STKE 2000: PE1: 2000.
    • (2000) Sci STKE , vol.2000
    • Rhee, S.G.1    Bae, Y.S.2    Lee, S.R.3    Kwon, J.4
  • 116
    • 19444375216 scopus 로고    scopus 로고
    • Peroxiredoxins: A historical overview and speculative preview of novel mechanisms and emerging concepts in cell signaling
    • Rhee SG, Chae HZ, and Kim K. Peroxiredoxins: a historical overview and speculative preview of novel mechanisms and emerging concepts in cell signaling. Free Radic Biol Med 38: 1543-1552, 2005.
    • (2005) Free Radic Biol Med , vol.38 , pp. 1543-1552
    • Rhee, S.G.1    Chae, H.Z.2    Kim, K.3
  • 117
    • 15044362438 scopus 로고    scopus 로고
    • Intracellular messenger function of hydrogen peroxide and its regulation by peroxiredoxins
    • Rhee SG, Kang SW, Jeong W, Chang T-S, Yang K-S, and Woo HA. Intracellular messenger function of hydrogen peroxide and its regulation by peroxiredoxins. Curr Opin Cell Biol 17: 183-189, 2005.
    • (2005) Curr Opin Cell Biol , vol.17 , pp. 183-189
    • Rhee, S.G.1    Kang, S.W.2    Jeong, W.3    Chang, T.-S.4    Yang, K.-S.5    Woo, H.A.6
  • 118
    • 13544256790 scopus 로고    scopus 로고
    • Src protein-tyrosine kinase structure and regulation
    • Roskoski R, Jr. Src protein-tyrosine kinase structure and regulation. Biochem Biophys Res Commun 324: 1155-1164, 2004.
    • (2004) Biochem Biophys Res Commun , vol.324 , pp. 1155-1164
    • Roskoski Jr., R.1
  • 119
    • 2442498430 scopus 로고    scopus 로고
    • Stimulus-specific differences in protein kinase Cδ localization and activation mechanisms in cardiomyocytes
    • Rybin VO, Guo J, Sabri A, Elouardighi H, Schaefer E, and Steinberg SF. Stimulus-specific differences in protein kinase Cδ localization and activation mechanisms in cardiomyocytes. J Biol Chem 279: 19350-19361, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 19350-19361
    • Rybin, V.O.1    Guo, J.2    Sabri, A.3    Elouardighi, H.4    Schaefer, E.5    Steinberg, S.F.6
  • 121
    • 0030969371 scopus 로고    scopus 로고
    • The cellular and molecular response of cardiac myocytes to mechanical stress
    • Sadoshima J and Izumo S. The cellular and molecular response of cardiac myocytes to mechanical stress. Annu Rev Physiol 59: 551-571, 1997.
    • (1997) Annu Rev Physiol , vol.59 , pp. 551-571
    • Sadoshima, J.1    Izumo, S.2
  • 122
    • 17644371347 scopus 로고    scopus 로고
    • Functions and mechanisms of redox regulation of cysteine-based phosphatases
    • Salmeen A and Barford D. Functions and mechanisms of redox regulation of cysteine-based phosphatases. Antioxid Redox Signal 7: 560-577, 2005.
    • (2005) Antioxid Redox Signal , vol.7 , pp. 560-577
    • Salmeen, A.1    Barford, D.2
  • 123
    • 0034595828 scopus 로고    scopus 로고
    • Distinct carboxy-termini confer divergent characteristics to the mitogen-activated protein kinase p38α and its splice isoform Mxi2
    • Sanz V, Arozarena I, and Crespo P. Distinct carboxy-termini confer divergent characteristics to the mitogen-activated protein kinase p38α and its splice isoform Mxi2. FEBS Lett 474: 169-174, 2000.
    • (2000) FEBS Lett , vol.474 , pp. 169-174
    • Sanz, V.1    Arozarena, I.2    Crespo, P.3
  • 124
    • 0033748263 scopus 로고    scopus 로고
    • The role of differential activation of p38-mitogen-activated protein kinase in preconditioned ventricular myocytes
    • Saurin AT, Martin JL, Heads RJ, Foley C, Mockridge JW, Wright MJ, Wang Y, and Marber MS. The role of differential activation of p38-mitogen-activated protein kinase in preconditioned ventricular myocytes. FASEB J 14: 2237-2246, 2000.
    • (2000) FASEB J , vol.14 , pp. 2237-2246
    • Saurin, A.T.1    Martin, J.L.2    Heads, R.J.3    Foley, C.4    Mockridge, J.W.5    Wright, M.J.6    Wang, Y.7    Marber, M.S.8
  • 126
    • 0034644539 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • Schlessinger J. Cell signaling by receptor tyrosine kinases. Cell 103: 211-225, 2000.
    • (2000) Cell , vol.103 , pp. 211-225
    • Schlessinger, J.1
  • 128
    • 25144478337 scopus 로고    scopus 로고
    • Biochemical dysfunction in heart mitochondria exposed to ischaemia and reperfusion
    • Solaini G and Harris DA. Biochemical dysfunction in heart mitochondria exposed to ischaemia and reperfusion. Biochem J 390: 377-394, 2005.
    • (2005) Biochem J , vol.390 , pp. 377-394
    • Solaini, G.1    Harris, D.A.2
  • 129
    • 0037102481 scopus 로고    scopus 로고
    • Differential susceptibilities of serine/threonine phosphatases to oxidative and nitrosative stress
    • Sommer D, Coleman S, Swanson SA, and Stemmer PM. Differential susceptibilities of serine/threonine phosphatases to oxidative and nitrosative stress. Arch Biochem Biophys 404: 271-278, 2002.
    • (2002) Arch Biochem Biophys , vol.404 , pp. 271-278
    • Sommer, D.1    Coleman, S.2    Swanson, S.A.3    Stemmer, P.M.4
  • 130
    • 10944238407 scopus 로고    scopus 로고
    • Distinctive activation mechanisms and functions for protein kinase Cδ
    • Steinberg SF. Distinctive activation mechanisms and functions for protein kinase Cδ. Biochem J 384: 449-459, 2004.
    • (2004) Biochem J , vol.384 , pp. 449-459
    • Steinberg, S.F.1
  • 132
    • 0347381135 scopus 로고    scopus 로고
    • Akt, and mechanotransduction in the cardiac myocyte
    • Sugden PH. Ras, Akt, and mechanotransduction in the cardiac myocyte. Circ Res 93: 1179-1192, 2003.
    • (2003) Circ Res , vol.93 , pp. 1179-1192
    • Ras, S.P.H.1
  • 133
    • 0032563677 scopus 로고    scopus 로고
    • Stress-responsive mitogen-activated protein kinases (c-Jun N-terminal kinases and p38 mitogen-activated protein kinases) in the myocardium
    • Sugden PH and Clerk A. "Stress-responsive" mitogen-activated protein kinases (c-Jun N-terminal kinases and p38 mitogen-activated protein kinases) in the myocardium. Circ Res 83: 345-352, 1998.
    • (1998) Circ Res , vol.83 , pp. 345-352
    • Sugden, P.H.1    Clerk, A.2
  • 134
    • 17744364870 scopus 로고    scopus 로고
    • Regulation of MAP kinase-dependent apoptotic pathway: Implication of reactive oxygen and nitrogen species
    • Sumbayev VV and Yasinska IM. Regulation of MAP kinase-dependent apoptotic pathway: implication of reactive oxygen and nitrogen species. Arch Biochem Biophys 436: 406-412, 2005.
    • (2005) Arch Biochem Biophys , vol.436 , pp. 406-412
    • Sumbayev, V.V.1    Yasinska, I.M.2
  • 137
    • 0035136655 scopus 로고    scopus 로고
    • Redox regulation of MAPK pathways and cardiac hypertrophy in adult rat cardiac myocyte
    • Tanaka K, Honda M, and Takabatake T. Redox regulation of MAPK pathways and cardiac hypertrophy in adult rat cardiac myocyte. J Am Coll Cordial 37: 676-685, 2001.
    • (2001) J Am Coll Cordial , vol.37 , pp. 676-685
    • Tanaka, K.1    Honda, M.2    Takabatake, T.3
  • 138
    • 0042525992 scopus 로고    scopus 로고
    • Diverse mechanisms of myocardial p38 mitogen-activated protein kinase activation: Evidence for MKK-independent activation by a TAB1-associated mechanism contributing to injury during myocardial ischemia
    • Tanno M, Bassi R, Gorog DA, Saurin AT, Jiang J, Heads RJ, Martin JL, Davis RJ, Flavell RA, and Marber MS. Diverse mechanisms of myocardial p38 mitogen-activated protein kinase activation: evidence for MKK-independent activation by a TAB1-associated mechanism contributing to injury during myocardial ischemia. Circ Res 93: 254-261, 2003.
    • (2003) Circ Res , vol.93 , pp. 254-261
    • Tanno, M.1    Bassi, R.2    Gorog, D.A.3    Saurin, A.T.4    Jiang, J.5    Heads, R.J.6    Martin, J.L.7    Davis, R.J.8    Flavell, R.A.9    Marber, M.S.10
  • 139
    • 0030461098 scopus 로고    scopus 로고
    • Cell cycle-dependent activation of Ras
    • Taylor SJ and Shalloway D. Cell cycle-dependent activation of Ras. Curr Biol 6: 1621-1627, 1996.
    • (1996) Curr Biol , vol.6 , pp. 1621-1627
    • Taylor, S.J.1    Shalloway, D.2
  • 141
    • 2642551439 scopus 로고    scopus 로고
    • Angiotensin II and endothelin-1 regulate MAP kinases through different redox-dependent mechanisms in human vascular smooth muscle cells
    • Touyz RM, Yao G, Viel E, Amiri F, and Schiffrin EL. Angiotensin II and endothelin-1 regulate MAP kinases through different redox-dependent mechanisms in human vascular smooth muscle cells. J Hypertens 22: 1141-1149, 2004.
    • (2004) J Hypertens , vol.22 , pp. 1141-1149
    • Touyz, R.M.1    Yao, G.2    Viel, E.3    Amiri, F.4    Schiffrin, E.L.5
  • 142
    • 0036176049 scopus 로고    scopus 로고
    • Signals of oxidant-induced cardiomyocyte hypertrophy: Key activation of p70 S6 kinase-1 and phosphoinositide 3-kinase
    • Tu VC, Bahl JJ, and Chen QM. Signals of oxidant-induced cardiomyocyte hypertrophy: key activation of p70 S6 kinase-1 and phosphoinositide 3-kinase. J Pharmacol Exp Ther 300: 1101-1110, 2002.
    • (2002) J Pharmacol Exp Ther , vol.300 , pp. 1101-1110
    • Tu, V.C.1    Bahl, J.J.2    Chen, Q.M.3
  • 143
    • 0034653608 scopus 로고    scopus 로고
    • The PI3K-PDK1 connection: More than just a road to PKB
    • Vanhaesebroeck B and Alessi DR. The PI3K-PDK1 connection: more than just a road to PKB. Biochem J 346: 561-576, 2000.
    • (2000) Biochem J , vol.346 , pp. 561-576
    • Vanhaesebroeck, B.1    Alessi, D.R.2
  • 147
    • 4444382387 scopus 로고    scopus 로고
    • Calcium-calcineurin signaling in the regulation of cardiac hypertrophy
    • Wilkins BJ and Molkentin JD. Calcium-calcineurin signaling in the regulation of cardiac hypertrophy. Biochem Biophys Res Commun 322: 1178-1191, 2004.
    • (2004) Biochem Biophys Res Commun , vol.322 , pp. 1178-1191
    • Wilkins, B.J.1    Molkentin, J.D.2
  • 148
    • 18344394166 scopus 로고    scopus 로고
    • Post-prenylation-processing enzymes as new targets in oncogenesis
    • Winter-Vann AM and Casey PJ. Post-prenylation-processing enzymes as new targets in oncogenesis. Nat Rev Cancer 5: 405-412, 2005.
    • (2005) Nat Rev Cancer , vol.5 , pp. 405-412
    • Winter-Vann, A.M.1    Casey, P.J.2
  • 149
    • 0346850874 scopus 로고    scopus 로고
    • Reversible oxidation of the active site cysteine of peroxiredoxins to cysteine sulphinic acid. Immunoblot detection with antibodies specific for the hyperoxidized cysteine-containing sequence
    • Woo HA, Kang SW, Kim HK, Yang KS, Chae HZ, and Rhee SG. Reversible oxidation of the active site cysteine of peroxiredoxins to cysteine sulphinic acid. Immunoblot detection with antibodies specific for the hyperoxidized cysteine-containing sequence. J Biol Chem 278: 47361-47364, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 47361-47364
    • Woo, H.A.1    Kang, S.W.2    Kim, H.K.3    Yang, K.S.4    Chae, H.Z.5    Rhee, S.G.6
  • 150
    • 15044363028 scopus 로고    scopus 로고
    • Recent advances in the protein kinase B signaling pathway
    • Woodgett JR. Recent advances in the protein kinase B signaling pathway. Curr Opin Cell Biol 17: 150-157, 2005.
    • (2005) Curr Opin Cell Biol , vol.17 , pp. 150-157
    • Woodgett, J.R.1
  • 151
  • 152
    • 0036083322 scopus 로고    scopus 로고
    • Role of reactive oxygen species and NAD(P)H oxidase in α-adrenoceptor signaling in adult rat cardiac myocytes
    • Xiao L, Pimentel DR, Wang J, Singh K, Colucci WS, and Sawyer DB. Role of reactive oxygen species and NAD(P)H oxidase in α-adrenoceptor signaling in adult rat cardiac myocytes. Am J Physiol Cell Physiol 282: C926-C934, 2002.
    • (2002) Am J Physiol Cell Physiol , vol.282
    • Xiao, L.1    Pimentel, D.R.2    Wang, J.3    Singh, K.4    Colucci, W.S.5    Sawyer, D.B.6
  • 154
    • 0346788518 scopus 로고    scopus 로고
    • ROS during the acute phase of Ang 11 hypertension participates in cardiovascular MAPK. activation but not vasoconstriction
    • Zhang GX, Kimura S, Nishiyama A, Shokoji T, Rahman M, and Abe Y. ROS during the acute phase of Ang 11 hypertension participates in cardiovascular MAPK. activation but not vasoconstriction. Hypertension 43: 117-124, 2004.
    • (2004) Hypertension , vol.43 , pp. 117-124
    • Zhang, G.X.1    Kimura, S.2    Nishiyama, A.3    Shokoji, T.4    Rahman, M.5    Abe, Y.6


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