메뉴 건너뛰기




Volumn 1, Issue 1, 2006, Pages 59-72

Oxidative stress and DNA damage - DNA repair system in vascular smooth muscle cells in artery and vein grafts

Author keywords

Apoptosis; Coronary artery bypass graft; DNA damage; DNA repair pathways; Oxidative stress; Vascular smooth muscle cell

Indexed keywords

8 HYDROXYDEOXYGUANOSINE; DNA DIRECTED DNA POLYMERASE BETA; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; MITOCHONDRIAL DNA; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; SUPEROXIDE DISMUTASE;

EID: 32644483898     PISSN: 15740668     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jccr.2005.11.003     Document Type: Review
Times cited : (8)

References (147)
  • 1
    • 0024460865 scopus 로고
    • Endothelium-derived relaxing factor and protection against contractions induced by histamine and serotonin in the internal mammary artery and saphenous vein
    • Z. Yang D. Diederich K. Schneider R. Siebenmann P. Stulz L. vonSegesser et al. Endothelium-derived relaxing factor and protection against contractions induced by histamine and serotonin in the internal mammary artery and saphenous vein Circulation 80 1989 1041-1048
    • (1989) Circulation , vol.80 , pp. 1041-1048
    • Yang, Z.1    Diederich, D.2    Schneider, K.3    Siebenmann, R.4    Stulz, P.5    vonSegesser, L.6
  • 3
    • 0033800351 scopus 로고    scopus 로고
    • Overexpression of CuZnSOD in coronary vascular cells attenuates myocardial ischemia/reperfusion injury
    • Z. Chen T.D. Oberley Y. Ho C.C. Chua B. Siu R.C. Hamdy et al. Overexpression of CuZnSOD in coronary vascular cells attenuates myocardial ischemia/reperfusion injury Free Radic Bio Med 29 2000 589-596
    • (2000) Free Radic Bio Med , vol.29 , pp. 589-596
    • Chen, Z.1    Oberley, T.D.2    Ho, Y.3    Chua, C.C.4    Siu, B.5    Hamdy, R.C.6
  • 4
    • 0037067317 scopus 로고    scopus 로고
    • Mediation of poly(ADP-ribose) polymerase-1-dependent cell death by apoptosis-inducing factor
    • S. Yu H. Wang M.F. Poitras C. Coombs W.J. Bowers H.J. Federoff et al. Mediation of poly(ADP-ribose) polymerase-1-dependent cell death by apoptosis-inducing factor Science 297 2002 259-263
    • (2002) Science , vol.297 , pp. 259-263
    • Yu, S.1    Wang, H.2    Poitras, M.F.3    Coombs, C.4    Bowers, W.J.5    Federoff, H.J.6
  • 5
    • 0023730308 scopus 로고
    • Difference between endothelium-dependent relaxation in arterial and in venous coronary bypass grafts
    • T.F. Luscher D. Diederich R. Siebenmenn K. Lehmann P. Stulz L. vonSegesser et al. Difference between endothelium-dependent relaxation in arterial and in venous coronary bypass grafts N Engl J Med 319 1988 462-467
    • (1988) N Engl J Med , vol.319 , pp. 462-467
    • Luscher, T.F.1    Diederich, D.2    Siebenmenn, R.3    Lehmann, K.4    Stulz, P.5    vonSegesser, L.6
  • 6
    • 0000382970 scopus 로고
    • Comparison of late changes in internal mammary artery and saphenous vein grafts in two consecutive series of patients 10 years after operation
    • C.M. Grondin L. Campeau J. Lesperance M. Enjalbert M.G. Bourassa Comparison of late changes in internal mammary artery and saphenous vein grafts in two consecutive series of patients 10 years after operation Circulation 70 Suppl. I 1984 I208-I212
    • (1984) Circulation , vol.70 , Issue.SUPPL. I
    • Grondin, C.M.1    Campeau, L.2    Lesperance, J.3    Enjalbert, M.4    Bourassa, M.G.5
  • 8
    • 0023034701 scopus 로고
    • Bypass surgery with the internal mammary graft: 15 year follow-up
    • A. Cameron H.G. Kemp G.E. Green Bypass surgery with the internal mammary graft: 15 year follow-up Circulation 74 5 Pt 2 1986 III30-III36
    • (1986) Circulation , vol.74 , Issue.5 PART 2
    • Cameron, A.1    Kemp, H.G.2    Green, G.E.3
  • 9
    • 0036208590 scopus 로고    scopus 로고
    • Improved patency in vein grafts harvested with surrounding tissue: Results of a randomized study using three harvesting techniques
    • D.S. Souza M.R. Dashwood J.C. Tsui D. Filbe L. Bodin B. Johanasson et al. Improved patency in vein grafts harvested with surrounding tissue: results of a randomized study using three harvesting techniques Ann Thorac Surg 73 2002 1189-1195
    • (2002) Ann Thorac Surg , vol.73 , pp. 1189-1195
    • Souza, D.S.1    Dashwood, M.R.2    Tsui, J.C.3    Filbe, D.4    Bodin, L.5    Johanasson, B.6
  • 12
    • 0033059768 scopus 로고    scopus 로고
    • Radial artery in CABG: Could the early results be comparable to internal mammary artery graft?
    • A. Bhan V. Gupta S.K. Choudhary R. Sharma B. Singh R. Aggarwal et al. Radial artery in CABG: Could the early results be comparable to internal mammary artery graft? Ann Thorac Surg 67 1999 1631-1636
    • (1999) Ann Thorac Surg , vol.67 , pp. 1631-1636
    • Bhan, A.1    Gupta, V.2    Choudhary, S.K.3    Sharma, R.4    Singh, B.5    Aggarwal, R.6
  • 13
    • 0037349230 scopus 로고    scopus 로고
    • Complications after radial artery harvesting for coronary artery bypass grafting: Our experience
    • A.M. Budillon F. Nicolini A. Agostinelli C. Beghi G. Pavesi C. Fragnito et al. Complications after radial artery harvesting for coronary artery bypass grafting: Our experience Surgery 133 2003 283-287
    • (2003) Surgery , vol.133 , pp. 283-287
    • Budillon, A.M.1    Nicolini, F.2    Agostinelli, A.3    Beghi, C.4    Pavesi, G.5    Fragnito, C.6
  • 15
    • 0031890233 scopus 로고    scopus 로고
    • Different proliferative properties of smooth muscle cells of human arterial and venous bypass vessels: Role of PDGF receptors, mitogen-activated protein kinase, and cyclin-dependent kinase inhibitors
    • Z. Yang B.S. Oemar T. Carrel B. Kipfer F. Julmy T.F. Luscher Different proliferative properties of smooth muscle cells of human arterial and venous bypass vessels: Role of PDGF receptors, mitogen-activated protein kinase, and cyclin-dependent kinase inhibitors Circulation 97 1998 181-187
    • (1998) Circulation , vol.97 , pp. 181-187
    • Yang, Z.1    Oemar, B.S.2    Carrel, T.3    Kipfer, B.4    Julmy, F.5    Luscher, T.F.6
  • 18
    • 0027508026 scopus 로고
    • Are free radicals involved in the pathobiology of human essential hypertension?
    • K.V. Kumar U.N. Das Are free radicals involved in the pathobiology of human essential hypertension? Free Radic Res Commun 9 1993 59-66
    • (1993) Free Radic Res Commun , vol.9 , pp. 59-66
    • Kumar, K.V.1    Das, U.N.2
  • 19
    • 0025217207 scopus 로고
    • Lipid peroxidation associated with successful thrombolysis
    • [Erratum appears in Lancet 1990;335:1108]
    • S.W. Davies K. Ranjadayalan D.G. Wickens T.L. Dormandy A.D. Timmis Lipid peroxidation associated with successful thrombolysis [Erratum appears in Lancet 1990;335:1108] Lancet 335 1990 741-743
    • (1990) Lancet , vol.335 , pp. 741-743
    • Davies, S.W.1    Ranjadayalan, K.2    Wickens, D.G.3    Dormandy, T.L.4    Timmis, A.D.5
  • 20
  • 21
    • 0000098037 scopus 로고
    • Direct measurement of free radical generation following reperfusion of ischemic myocardium
    • J.L. Zweier J.T. Flaherty M.L. Weisfeldt Direct measurement of free radical generation following reperfusion of ischemic myocardium Proc Natl Acad Sci U S A 84 1987 1404-1407
    • (1987) Proc Natl Acad Sci U S A , vol.84 , pp. 1404-1407
    • Zweier, J.L.1    Flaherty, J.T.2    Weisfeldt, M.L.3
  • 22
    • 0028827252 scopus 로고
    • Dilated cardiomyopathy and neonatal lethality in mutant mice lacking manganese superoxide dismutase
    • Y. Li T.T. Huang E.J. Carlson S. Melov P.C. Ursell J.L. Olson et al. Dilated cardiomyopathy and neonatal lethality in mutant mice lacking manganese superoxide dismutase Nat Genet 11 1995 376-381
    • (1995) Nat Genet , vol.11 , pp. 376-381
    • Li, Y.1    Huang, T.T.2    Carlson, E.J.3    Melov, S.4    Ursell, P.C.5    Olson, J.L.6
  • 23
    • 0033535974 scopus 로고    scopus 로고
    • Signaling pathways in reactive oxygen species-induced cardiomyocyte apoptosis
    • R. von Harsdorf P.F. Li R. Dietz Signaling pathways in reactive oxygen species-induced cardiomyocyte apoptosis Circulation 99 1999 2934-2941
    • (1999) Circulation , vol.99 , pp. 2934-2941
    • von Harsdorf, R.1    Li, P.F.2    Dietz, R.3
  • 24
    • 0033586639 scopus 로고    scopus 로고
    • Increased NADH-oxidase-mediated superoxide production in the early stages of atherosclerosis: Evidence for involvement of the renin-angiotensin system
    • A. Warnholtz G. Nickenig E. Schulz R. Macharzina J.H. Brasen M. Skatchkov et al. Increased NADH-oxidase-mediated superoxide production in the early stages of atherosclerosis: Evidence for involvement of the renin-angiotensin system Circulation 99 1999 2027-2033
    • (1999) Circulation , vol.99 , pp. 2027-2033
    • Warnholtz, A.1    Nickenig, G.2    Schulz, E.3    Macharzina, R.4    Brasen, J.H.5    Skatchkov, M.6
  • 26
    • 0034677947 scopus 로고    scopus 로고
    • NAD(P)H oxidase: Role in cardiovascular biology and disease
    • K.K. Griendling D. Sorescu M. Ushio-Fukai NAD(P)H oxidase: Role in cardiovascular biology and disease Circ Res 86 2000 494-501
    • (2000) Circ Res , vol.86 , pp. 494-501
    • Griendling, K.K.1    Sorescu, D.2    Ushio-Fukai, M.3
  • 28
    • 0030806863 scopus 로고    scopus 로고
    • Superoxide anion radical, superoxide dismutases, and related matters
    • I. Fridovich Superoxide anion radical, superoxide dismutases, and related matters J Biol Chem 272 1997 18515-18517
    • (1997) J Biol Chem , vol.272 , pp. 18515-18517
    • Fridovich, I.1
  • 29
    • 0026515446 scopus 로고
    • Active oxygen species stimulate vascular smooth muscle cell growth and proto-oncogene expression
    • G.N. Rao B.C. Berk Active oxygen species stimulate vascular smooth muscle cell growth and proto-oncogene expression Circ Res 70 1992 593-599
    • (1992) Circ Res , vol.70 , pp. 593-599
    • Rao, G.N.1    Berk, B.C.2
  • 30
    • 0032407020 scopus 로고    scopus 로고
    • Reactive oxygen species are critical in the oleic acid-mediated mitogenic signaling pathway in vascular smooth muscle cells
    • G. Lu E.L. Greene T. Nagai B.M. Egan Reactive oxygen species are critical in the oleic acid-mediated mitogenic signaling pathway in vascular smooth muscle cells Hypertension 32 1998 1003-1010
    • (1998) Hypertension , vol.32 , pp. 1003-1010
    • Lu, G.1    Greene, E.L.2    Nagai, T.3    Egan, B.M.4
  • 31
    • 0032570321 scopus 로고    scopus 로고
    • Hydrogen peroxide induces intracellular calcium oscillations in human aortic endothelial cells
    • Q. Hu S. Corda J.L. Zweier M.C. Capoggrossi R.C. Ziegelstein Hydrogen peroxide induces intracellular calcium oscillations in human aortic endothelial cells Circulation 97 1998 268-275
    • (1998) Circulation , vol.97 , pp. 268-275
    • Hu, Q.1    Corda, S.2    Zweier, J.L.3    Capoggrossi, M.C.4    Ziegelstein, R.C.5
  • 32
    • 0029086511 scopus 로고
    • Reactive oxygen intermediates mediate angiotensin II-induced c-Jun, c-Fos heterodimer DNA binding activity and proliferative hypertrophic responses in myogenic cells
    • P.L. Puri M.L. Avantaggiati V.L. Burgio P. Chirillo D. Collepardo G. Natoli et al. Reactive oxygen intermediates mediate angiotensin II-induced c-Jun, c-Fos heterodimer DNA binding activity and proliferative hypertrophic responses in myogenic cells J Biol Chem 270 1995 22129-22134
    • (1995) J Biol Chem , vol.270 , pp. 22129-22134
    • Puri, P.L.1    Avantaggiati, M.L.2    Burgio, V.L.3    Chirillo, P.4    Collepardo, D.5    Natoli, G.6
  • 35
    • 0036667555 scopus 로고    scopus 로고
    • Superoxide dismutase multigene family: A comparison of the CuZn-SOD (SOD1), Mn-SOD (SOD2), and EC-SOD (SOD3) gene structures, evolution, and expression
    • I.N. Zelko T.J. Mariani R.J. Folz Superoxide dismutase multigene family: A comparison of the CuZn-SOD (SOD1), Mn-SOD (SOD2), and EC-SOD (SOD3) gene structures, evolution, and expression Free Radic Biol Med 33 2002 337-349
    • (2002) Free Radic Biol Med , vol.33 , pp. 337-349
    • Zelko, I.N.1    Mariani, T.J.2    Folz, R.J.3
  • 36
    • 0030044703 scopus 로고    scopus 로고
    • Effect of vitamin E on hydrogen peroxide production by human vascular endothelial cells after hypoxia/reoxygenation
    • A. Martin J. Zulueta P. Hasson J.B. Blumberg M. Meydani Effect of vitamin E on hydrogen peroxide production by human vascular endothelial cells after hypoxia/reoxygenation Free Radic Biol Med 20 1996 99-105
    • (1996) Free Radic Biol Med , vol.20 , pp. 99-105
    • Martin, A.1    Zulueta, J.2    Hasson, P.3    Blumberg, J.B.4    Meydani, M.5
  • 38
    • 0032700284 scopus 로고    scopus 로고
    • Superoxide anion generation, superoxide dismutase activity, and nitric oxide release in human internal mammary artery and saphenous vein segments
    • C.M. Schmalfuss L.Y. Chen J.N. Bott E.D. Staples J.L. Mehta Superoxide anion generation, superoxide dismutase activity, and nitric oxide release in human internal mammary artery and saphenous vein segments J Cardiovasc Pharmacol Ther 4 1999 249-257
    • (1999) J Cardiovasc Pharmacol Ther , vol.4 , pp. 249-257
    • Schmalfuss, C.M.1    Chen, L.Y.2    Bott, J.N.3    Staples, E.D.4    Mehta, J.L.5
  • 39
    • 0035873991 scopus 로고    scopus 로고
    • Oxidative stress and lipid retention in vascular grafts: Comparison between venous and arterial conduits
    • Y. Shi S. Patel K.L. Davenpeck R. Niculescu E. Rodriguez M.G. Magno et al. Oxidative stress and lipid retention in vascular grafts: Comparison between venous and arterial conduits Circulation 103 2001 2408-2413
    • (2001) Circulation , vol.103 , pp. 2408-2413
    • Shi, Y.1    Patel, S.2    Davenpeck, K.L.3    Niculescu, R.4    Rodriguez, E.5    Magno, M.G.6
  • 40
    • 0036781612 scopus 로고    scopus 로고
    • Superoxide radical concentration and superoxide dismutase (SOD) enzyme activity in varicose veins
    • M.A. Wali S.A. Suleiman O.F. Kadoumi M.A. Nasr Superoxide radical concentration and superoxide dismutase (SOD) enzyme activity in varicose veins Ann Thorac Cardiovasc Surg 8 2002 286-290
    • (2002) Ann Thorac Cardiovasc Surg , vol.8 , pp. 286-290
    • Wali, M.A.1    Suleiman, S.A.2    Kadoumi, O.F.3    Nasr, M.A.4
  • 43
    • 0344043305 scopus 로고    scopus 로고
    • Superoxide production in vascular smooth muscle contributes to oxidative stress and impaired relaxation in atherosclerosis
    • F.J. Miller D.D. Gutterman C.D. Rios D.D. Heistad B.L. Davidson Superoxide production in vascular smooth muscle contributes to oxidative stress and impaired relaxation in atherosclerosis Circ Res 82 1998 1298-1305
    • (1998) Circ Res , vol.82 , pp. 1298-1305
    • Miller, F.J.1    Gutterman, D.D.2    Rios, C.D.3    Heistad, D.D.4    Davidson, B.L.5
  • 44
    • 0026746382 scopus 로고
    • PEG-SOD and myocardial antioxidant status during ischaemia and reperfusion: Dose-response studies in the isolated blood perfused rabbit heart
    • M. Galinanes R. Ferrari Y. Qiu A. Cargnoni A. Ezrin D.J. Hearse PEG-SOD and myocardial antioxidant status during ischaemia and reperfusion: Dose-response studies in the isolated blood perfused rabbit heart J Mol Cell Cardiol 24 1992 1021-1030
    • (1992) J Mol Cell Cardiol , vol.24 , pp. 1021-1030
    • Galinanes, M.1    Ferrari, R.2    Qiu, Y.3    Cargnoni, A.4    Ezrin, A.5    Hearse, D.J.6
  • 45
    • 0026495575 scopus 로고
    • PEG-SOD improves postischemic functional recovery and antioxidant status in blood-perfused rabbit hearts
    • Y. Qiu M. Galinanaes R. Ferrari A. Cargnoni A. Ezrin D.J. Hearse PEG-SOD improves postischemic functional recovery and antioxidant status in blood-perfused rabbit hearts Am J Physiol 263 1992 H1243-H1249
    • (1992) Am J Physiol , vol.263
    • Qiu, Y.1    Galinanaes, M.2    Ferrari, R.3    Cargnoni, A.4    Ezrin, A.5    Hearse, D.J.6
  • 46
    • 0033563781 scopus 로고    scopus 로고
    • Reduction of lipid peroxidation with intraoperative superoxide dismutase treatment decreases intimal hyperplasia in experimental vein grafts
    • T.T. Huynh M.G. Davies M.J. Trovato L. Barber H.J. Safi P.O. Hagen Reduction of lipid peroxidation with intraoperative superoxide dismutase treatment decreases intimal hyperplasia in experimental vein grafts J Surg Res 84 1999 223-232
    • (1999) J Surg Res , vol.84 , pp. 223-232
    • Huynh, T.T.1    Davies, M.G.2    Trovato, M.J.3    Barber, L.4    Safi, H.J.5    Hagen, P.O.6
  • 47
    • 0034951734 scopus 로고    scopus 로고
    • Protective effect of PEG-SOD against early reperfusion injury assessed in reperfused and non-reperfused ischaemic areas of the same heart
    • K. Kanamasa N. Ishida K. Ishikawa Protective effect of PEG-SOD against early reperfusion injury assessed in reperfused and non-reperfused ischaemic areas of the same heart Acta Cardiol 56 2001 181-186
    • (2001) Acta Cardiol , vol.56 , pp. 181-186
    • Kanamasa, K.1    Ishida, N.2    Ishikawa, K.3
  • 48
    • 13344279414 scopus 로고    scopus 로고
    • Induction of apoptosis by pyrrolidinedithiocarbamete and N-acetylcysteine in vascular smooth muscle cells
    • J.-C. Tsai M. Jain C.-M. Hsieh W.S. Lee M. Yoshizumi C. Patterson et al. Induction of apoptosis by pyrrolidinedithiocarbamete and N-acetylcysteine in vascular smooth muscle cells J Biol Chem 271 1996 3667-3670
    • (1996) J Biol Chem , vol.271 , pp. 3667-3670
    • Tsai, J.-C.1    Jain, M.2    Hsieh, C.-M.3    Lee, W.S.4    Yoshizumi, M.5    Patterson, C.6
  • 49
    • 0032534623 scopus 로고    scopus 로고
    • Oxidant treatment causes a dose-dependent phenotype of apoptosis in cultured motoneurons
    • E.C. Kaal H. Veldman H. Sodaar E.A. Joosten P.R. Dop Bar Oxidant treatment causes a dose-dependent phenotype of apoptosis in cultured motoneurons J Neurosci Res 54 1998 778-786
    • (1998) J Neurosci Res , vol.54 , pp. 778-786
    • Kaal, E.C.1    Veldman, H.2    Sodaar, H.3    Joosten, E.A.4    Dop Bar, P.R.5
  • 50
    • 0021351203 scopus 로고
    • Oxygen toxicity, oxygen radicals, transition metals and disease
    • B. Hallwell J.M.C. Gutteridge Oxygen toxicity, oxygen radicals, transition metals and disease Biochem J 219 1984 1-14
    • (1984) Biochem J , vol.219 , pp. 1-14
    • Hallwell, B.1    Gutteridge, J.M.C.2
  • 51
    • 0028232804 scopus 로고
    • Excitotoxicity, free radicals, and cell membrane changes
    • L.L. Dugan D.W. Choi Excitotoxicity, free radicals, and cell membrane changes Ann Neurol 35 1994 S17-S21
    • (1994) Ann Neurol , vol.35
    • Dugan, L.L.1    Choi, D.W.2
  • 52
    • 0025373259 scopus 로고
    • Oxidative damage to DNA during aging: 8-Hydroxy-2′-deoxyguanosine in rat organ DNA and urine
    • C.G. Fraga M.K. Shigenaga J.-W. Park P. Degan B.N. Ames Oxidative damage to DNA during aging: 8-Hydroxy-2′-deoxyguanosine in rat organ DNA and urine Proc Natl Acad Sci U S A 87 1990 4533-4537
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 4533-4537
    • Fraga, C.G.1    Shigenaga, M.K.2    Park, J.-W.3    Degan, P.4    Ames, B.N.5
  • 53
    • 0027055332 scopus 로고
    • Age-associated oxygen damage and mutations in mitochondrial DNA in human hearts
    • M. Hayakawa K. Hattori S. Sugiyama T. Ozawa Age-associated oxygen damage and mutations in mitochondrial DNA in human hearts Biochem Biophys Res Commun 189 1992 979-985
    • (1992) Biochem Biophys Res Commun , vol.189 , pp. 979-985
    • Hayakawa, M.1    Hattori, K.2    Sugiyama, S.3    Ozawa, T.4
  • 54
    • 0029973192 scopus 로고    scopus 로고
    • Damage, repair, and mutagenesis in nuclear genes after mouse forebrain ischemia-reperfusion
    • P.K. Liu C.Y. Hsu M. Dizdaroglu R.A. Floyd Y.W. Kow A. Karakaya et al. Damage, repair, and mutagenesis in nuclear genes after mouse forebrain ischemia-reperfusion J Neurosci 16 1996 6795-6806
    • (1996) J Neurosci , vol.16 , pp. 6795-6806
    • Liu, P.K.1    Hsu, C.Y.2    Dizdaroglu, M.3    Floyd, R.A.4    Kow, Y.W.5    Karakaya, A.6
  • 55
    • 0025902273 scopus 로고
    • Endogenous mutagens and the causes of aging and cancer
    • B.N. Ames L.S. Gold Endogenous mutagens and the causes of aging and cancer Mutat Res 250 1991 3-16
    • (1991) Mutat Res , vol.250 , pp. 3-16
    • Ames, B.N.1    Gold, L.S.2
  • 56
    • 0026592966 scopus 로고
    • 8-Hydroxyguanine, an abundant form of oxidative DNA damage, causes G-T and A-C substitutions
    • K.C. Cheng D.S. Cahill H. Kasai S. Nishimura L.A. Loeb 8-Hydroxyguanine, an abundant form of oxidative DNA damage, causes G-T and A-C substitutions J Biol Chem 267 1992 166-172
    • (1992) J Biol Chem , vol.267 , pp. 166-172
    • Cheng, K.C.1    Cahill, D.S.2    Kasai, H.3    Nishimura, S.4    Loeb, L.A.5
  • 57
    • 0026513966 scopus 로고
    • MutT protein specifically hydrolyses a potent mutagenic substrate for DNA synthesis
    • H. Maki M. Sekiguchi MutT protein specifically hydrolyses a potent mutagenic substrate for DNA synthesis Nature 355 1992 273-275
    • (1992) Nature , vol.355 , pp. 273-275
    • Maki, H.1    Sekiguchi, M.2
  • 58
    • 0025981359 scopus 로고
    • Insertion of specific bases during DNA synthesis past the oxidation-damaged base 8-oxodG
    • S. Shibutani M. Takeshita A.P. Grollman Insertion of specific bases during DNA synthesis past the oxidation-damaged base 8-oxodG Nature 349 1991 431-434
    • (1991) Nature , vol.349 , pp. 431-434
    • Shibutani, S.1    Takeshita, M.2    Grollman, A.P.3
  • 59
    • 0027215203 scopus 로고
    • Mutations in the mutY gene of Escherichia coli enhance the frequency of targeted G:C-T:A transversions induced by a single 8-oxoguanine residue in single-stranded DNA
    • M. Moriya A.P. Grollman Mutations in the mutY gene of Escherichia coli enhance the frequency of targeted G:C-T:A transversions induced by a single 8-oxoguanine residue in single-stranded DNA Mol Gen Genet 239 1993 72-76
    • (1993) Mol Gen Genet , vol.239 , pp. 72-76
    • Moriya, M.1    Grollman, A.P.2
  • 60
    • 0025334691 scopus 로고
    • Mechanistic studies of ionizing radiation and oxidative mutagenesis: Genetic effects of a single 8-hydroxyguanine (7-hydro-8-oxoguanine) residue inserted at a unique site in a viral genome
    • M.L. Wood M. Dizdaroglu E. Gajewski J.M. Essigmann Mechanistic studies of ionizing radiation and oxidative mutagenesis: Genetic effects of a single 8-hydroxyguanine (7-hydro-8-oxoguanine) residue inserted at a unique site in a viral genome Biochemistry 29 1990 7024-7032
    • (1990) Biochemistry , vol.29 , pp. 7024-7032
    • Wood, M.L.1    Dizdaroglu, M.2    Gajewski, E.3    Essigmann, J.M.4
  • 62
    • 0028933674 scopus 로고
    • Functional cooperation of MutT MutM and MutY proteins in preventing mutations caused by spontaneous oxidation of guanine nucleotide in Escherichia coli
    • T. Tajiri H. Maki M. Sekiguchi Functional cooperation of MutT MutM and MutY proteins in preventing mutations caused by spontaneous oxidation of guanine nucleotide in Escherichia coli Mutat Res 336 1995 257-267
    • (1995) Mutat Res , vol.336 , pp. 257-267
    • Tajiri, T.1    Maki, H.2    Sekiguchi, M.3
  • 63
    • 0027528412 scopus 로고
    • Repair of DNA containing the oxidatively-damaged base 8-oxoguanine
    • J. Tchou A.P. Grollman Repair of DNA containing the oxidatively-damaged base 8-oxoguanine Mutat Res 299 1993 277-287
    • (1993) Mutat Res , vol.299 , pp. 277-287
    • Tchou, J.1    Grollman, A.P.2
  • 64
    • 0025240665 scopus 로고
    • Homogeneous Escherichia coli FPG protein. A DNA glycosylase which excises imidazole ring-opened purines and nicks DNA at apurinic/ apyrimidinic sites
    • S. Boiteux T.R. O'Connor F. Lederer A. Gouyette J. Laval Homogeneous Escherichia coli FPG protein. A DNA glycosylase which excises imidazole ring-opened purines and nicks DNA at apurinic/apyrimidinic sites J Biol Chem 265 1990 3916-3922
    • (1990) J Biol Chem , vol.265 , pp. 3916-3922
    • Boiteux, S.1    O'Connor, T.R.2    Lederer, F.3    Gouyette, A.4    Laval, J.5
  • 66
    • 0026513966 scopus 로고
    • MutT protein specifically hydrolyses a potent mutagenic substrate for DNA synthesis
    • H. Maki M. Sekiguchi MutT protein specifically hydrolyses a potent mutagenic substrate for DNA synthesis Nature 355 1992 273-275
    • (1992) Nature , vol.355 , pp. 273-275
    • Maki, H.1    Sekiguchi, M.2
  • 67
    • 0030475264 scopus 로고    scopus 로고
    • Specific recognition of A/G and A/7 8-dihydro-8-oxoguanine (8-oxoG0 mismatches by Escherichia coli MutY: Removal of the C-terminal domain preferentially affects A/8-oxoG recognition
    • A. Gogos J. Cillo N.D. Clarke A.L. Lu Specific recognition of A/G and A/ 7 8-dihydro-8-oxoguanine (8-oxoG0 mismatches by Escherichia coli MutY: removal of the C-terminal domain preferentially affects A/8-oxoG recognition Biochemistry 35 1996 16665-16671
    • (1996) Biochemistry , vol.35 , pp. 16665-16671
    • Gogos, A.1    Cillo, J.2    Clarke, N.D.3    Lu, A.L.4
  • 68
    • 0029835339 scopus 로고    scopus 로고
    • Catalytic mechanism and DNA substrate recognition of Escherichia coli MutY protein
    • A.L. Lu D.S. Yuen J. Cillo Catalytic mechanism and DNA substrate recognition of Escherichia coli MutY protein J Biol Chem 271 1996 24138-24143
    • (1996) J Biol Chem , vol.271 , pp. 24138-24143
    • Lu, A.L.1    Yuen, D.S.2    Cillo, J.3
  • 69
    • 0030987556 scopus 로고    scopus 로고
    • Cloning, overexpression, and biochemical characterization of the catalytic domain of MutY
    • R.C. Manuel R.S. Lloyd Cloning, overexpression, and biochemical characterization of the catalytic domain of MutY Biochemistry 36 1997 11140-11152
    • (1997) Biochemistry , vol.36 , pp. 11140-11152
    • Manuel, R.C.1    Lloyd, R.S.2
  • 70
    • 0026703168 scopus 로고
    • Escherichia coli MutY protein has both N-glycosylase and apurinic/ apyrimidinic endonuclease activities on A.C and A.G mispairs
    • J.J. Tsai-Wu H.F. Liu A.L. Lu Escherichia coli MutY protein has both N-glycosylase and apurinic/apyrimidinic endonuclease activities on A.C and A.G mispairs Proc Natl Acad Sci U S A 89 1992 8779-8783
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 8779-8783
    • Tsai-Wu, J.J.1    Liu, H.F.2    Lu, A.L.3
  • 71
    • 0025981359 scopus 로고
    • Insertion of specific bases during DNA synthesis past the oxidation-damaged base 8-oxodG
    • S. Shibutani M. Takeshita A.P. Grollman Insertion of specific bases during DNA synthesis past the oxidation-damaged base 8-oxodG Nature 349 1991 431-434
    • (1991) Nature , vol.349 , pp. 431-434
    • Shibutani, S.1    Takeshita, M.2    Grollman, A.P.3
  • 72
    • 0030004207 scopus 로고    scopus 로고
    • Cloning and sequencing a human homolog (hMYH) of the Escherichia coli mutY gene whose function is required for the repair of oxidative DNA damage
    • M.M. Slupska C. Baikalov W.M. Luther J.H. Chiang Y.F. Wei J.H. Miller Cloning and sequencing a human homolog (hMYH) of the Escherichia coli mutY gene whose function is required for the repair of oxidative DNA damage J Bacteriol 178 1996 3885-3892
    • (1996) J Bacteriol , vol.178 , pp. 3885-3892
    • Slupska, M.M.1    Baikalov, C.2    Luther, W.M.3    Chiang, J.H.4    Wei, Y.F.5    Miller, J.H.6
  • 74
    • 0033568099 scopus 로고    scopus 로고
    • Differential subcellular localization of human MutY homolg (hMYH) and the functional activity of adenine:8-oxoguanine DNA glycosylase
    • M. Takao Q.M. Zhang S. Yonei A. Yasui Differential subcellular localization of human MutY homolg (hMYH) and the functional activity of adenine:8-oxoguanine DNA glycosylase Nucleic Acids Res 27 1999 3638-3644
    • (1999) Nucleic Acids Res , vol.27 , pp. 3638-3644
    • Takao, M.1    Zhang, Q.M.2    Yonei, S.3    Yasui, A.4
  • 75
    • 0034654256 scopus 로고    scopus 로고
    • Identification of human MutY homolog (hMYH) as a repair enzyme for 2-hydroxyadenine in DNA and detection of multiple forms of hMYH located in nuclei and mitochondria
    • T. Ohtsubo K. Nishioka Y. Imaiso S. Iwai H. Shimokawa Oda T. Fujiwara Y. Nakabeppu Identification of human MutY homolog (hMYH) as a repair enzyme for 2-hydroxyadenine in DNA and detection of multiple forms of hMYH located in nuclei and mitochondria Nucleic Acids Res 28 2000 1355-1364
    • (2000) Nucleic Acids Res , vol.28 , pp. 1355-1364
    • Ohtsubo, T.1    Nishioka, K.2    Imaiso, Y.3    Iwai, S.4    Shimokawa, H.5    Oda6    Fujiwara, T.7    Nakabeppu, Y.8
  • 76
    • 0030760240 scopus 로고    scopus 로고
    • Cloning of a human homolog of the yeast OGG1 gene that is involved in the repair of oxidative DNA damage
    • K. Arai K. Morishita K. Shinmura T. Kohno S.R. Kim T. Nohmi et al. Cloning of a human homolog of the yeast OGG1 gene that is involved in the repair of oxidative DNA damage Oncogene 14 1997 2857-2861
    • (1997) Oncogene , vol.14 , pp. 2857-2861
    • Arai, K.1    Morishita, K.2    Shinmura, K.3    Kohno, T.4    Kim, S.R.5    Nohmi, T.6
  • 77
    • 0030816108 scopus 로고    scopus 로고
    • Cloning and characterization of hOGG1, a human homolog of the OGG1 gene of Saccharomyces cerevisiae
    • J.P. Radicella C. Dherin C. Desmaze M.S. Fox S. Boiteux Cloning and characterization of hOGG1, a human homolog of the OGG1 gene of Saccharomyces cerevisiae Proc Natl Acad Sci U S A 94 1997 8010-8015
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 8010-8015
    • Radicella, J.P.1    Dherin, C.2    Desmaze, C.3    Fox, M.S.4    Boiteux, S.5
  • 78
    • 0343353893 scopus 로고    scopus 로고
    • Characterization of the hOGG1 promoter and its expression during the cell cycle
    • A. Dhenaut S. Boiteux J.P. Radicella Characterization of the hOGG1 promoter and its expression during the cell cycle Mutat Res 461 2000 109-118
    • (2000) Mutat Res , vol.461 , pp. 109-118
    • Dhenaut, A.1    Boiteux, S.2    Radicella, J.P.3
  • 79
    • 0032508052 scopus 로고    scopus 로고
    • Mutations of OGG1, a gene involved in the repair of oxidative damage, are found in human lung and kidney tumours
    • S. Chevillard J.P. Radicella C. Levalois J. Lebeau M.F. Poupon S. Oudard et al. Mutations of OGG1, a gene involved in the repair of oxidative damage, are found in human lung and kidney tumours Oncogene 16 1998 3083-3086
    • (1998) Oncogene , vol.16 , pp. 3083-3086
    • Chevillard, S.1    Radicella, J.P.2    Levalois, C.3    Lebeau, J.4    Poupon, M.F.5    Oudard, S.6
  • 80
    • 0031716838 scopus 로고    scopus 로고
    • Infrequent mutations of the hOGG1 gene, that is involved in the excision of 8-hydroxyguanine in damaged DNA, in human gastric cancer
    • K. Shinmura T. Kohno H. Kasai K. Koda H. Sugimura J. Yokota Infrequent mutations of the hOGG1 gene, that is involved in the excision of 8-hydroxyguanine in damaged DNA, in human gastric cancer Jpn J Cancer Res 89 1998 825-828
    • (1998) Jpn J Cancer Res , vol.89 , pp. 825-828
    • Shinmura, K.1    Kohno, T.2    Kasai, H.3    Koda, K.4    Sugimura, H.5    Yokota, J.6
  • 82
    • 0036904776 scopus 로고    scopus 로고
    • Base excision repair capacity in mitochondria and nuclei: Tissue-specific variations
    • B. Karahalil B.A. Hogue N.C. de Souza-Pinto V.A. Bohr Base excision repair capacity in mitochondria and nuclei: Tissue-specific variations FASEB J 16 2002 1895-1902
    • (2002) FASEB J , vol.16 , pp. 1895-1902
    • Karahalil, B.1    Hogue, B.A.2    de Souza-Pinto, N.C.3    Bohr, V.A.4
  • 83
    • 0036270993 scopus 로고    scopus 로고
    • DNA repair/pro-apoptotic dual-role proteins in five major DNA repair pathways: Fail-safe protection against carcinogenesis
    • C. Bernstein H. Bernstein C.M. Payne H. Garewal DNA repair/pro-apoptotic dual-role proteins in five major DNA repair pathways: Fail-safe protection against carcinogenesis Mutat Res 511 2002 145-178
    • (2002) Mutat Res , vol.511 , pp. 145-178
    • Bernstein, C.1    Bernstein, H.2    Payne, C.M.3    Garewal, H.4
  • 84
    • 0030030379 scopus 로고    scopus 로고
    • Requirement of mammalian DNA polymerase-β in base-excision repair
    • R.W. Sobol J.K. Horton R. Juhn H. Gu R.K. Singhal R. Prasad et al. Requirement of mammalian DNA polymerase-β in base-excision repair Nature 379 1996 183-186
    • (1996) Nature , vol.379 , pp. 183-186
    • Sobol, R.W.1    Horton, J.K.2    Juhn, R.3    Gu, H.4    Singhal, R.K.5    Prasad, R.6
  • 85
    • 0034659935 scopus 로고    scopus 로고
    • The lyase activity of the DNA repair protein β-polymerase protects from DNA-damage-induced cytotoxicity
    • R.W. Sobol R. Prasad A. Evenski A. Baker X.P. Yang J.K. Horton et al. The lyase activity of the DNA repair protein β-polymerase protects from DNA-damage-induced cytotoxicity Nature 405 2000 807-810
    • (2000) Nature , vol.405 , pp. 807-810
    • Sobol, R.W.1    Prasad, R.2    Evenski, A.3    Baker, A.4    Yang, X.P.5    Horton, J.K.6
  • 86
    • 0035869014 scopus 로고    scopus 로고
    • Human DNA polymerase β initiates DNA synthesis during long-patch repair of reduced AP sites in DNA
    • A.J. Podlutsky I. Dianova V.N. Podust V.A. Bohr G. Dianov Human DNA polymerase β initiates DNA synthesis during long-patch repair of reduced AP sites in DNA EMBO J 20 2001 1477-1482
    • (2001) EMBO J , vol.20 , pp. 1477-1482
    • Podlutsky, A.J.1    Dianova, I.2    Podust, V.N.3    Bohr, V.A.4    Dianov, G.5
  • 87
    • 0035803497 scopus 로고    scopus 로고
    • DNA polymerase β is the major dRP lyase involved in repair of oxidative base lesions in DNA by mammalian cell extracts
    • S.L. Allinson I.I. Dianova G.L. Dianov DNA polymerase β is the major dRP lyase involved in repair of oxidative base lesions in DNA by mammalian cell extracts EMBO J 20 2001 6919-6926
    • (2001) EMBO J , vol.20 , pp. 6919-6926
    • Allinson, S.L.1    Dianova, I.I.2    Dianov, G.L.3
  • 88
    • 0032509471 scopus 로고    scopus 로고
    • Repair pathways for processing of 8-oxoguanine in DNA by mammalian cell extracts
    • G. Dianov C. Bischoff J. Piotrowski V.A. Bohr Repair pathways for processing of 8-oxoguanine in DNA by mammalian cell extracts J Biol Chem 273 1998 33811-33816
    • (1998) J Biol Chem , vol.273 , pp. 33811-33816
    • Dianov, G.1    Bischoff, C.2    Piotrowski, J.3    Bohr, V.A.4
  • 89
    • 0033553510 scopus 로고    scopus 로고
    • Role of DNA polymerase β in the excision step of long patch mammalian base excision repair
    • G.L. Dianov R. Prasad S.H. Wilson V.A. Bohr Role of DNA polymerase β in the excision step of long patch mammalian base excision repair J Biol Chem 274 1999 13741-13743
    • (1999) J Biol Chem , vol.274 , pp. 13741-13743
    • Dianov, G.L.1    Prasad, R.2    Wilson, S.H.3    Bohr, V.A.4
  • 90
    • 0038449141 scopus 로고    scopus 로고
    • PARP-1, a determinant of cell survival in response to DNA damage
    • V.J. Bouchard M. Rouleu G.G. Poirier PARP-1, a determinant of cell survival in response to DNA damage Exp Hematol 31 2003 446-454
    • (2003) Exp Hematol , vol.31 , pp. 446-454
    • Bouchard, V.J.1    Rouleu, M.2    Poirier, G.G.3
  • 91
    • 0035846899 scopus 로고    scopus 로고
    • XRCC1 stimulates human polymucleotide kinase activity at damaged RNA termini and accelerates DNA single-strand break repair
    • C.J. Whitehouse R.M. Taylor A. Thistlethwite H. Zhang F. Karimi-Busheri D.D. Lasko et al. XRCC1 stimulates human polymucleotide kinase activity at damaged RNA termini and accelerates DNA single-strand break repair Cell 104 2001 107-117
    • (2001) Cell , vol.104 , pp. 107-117
    • Whitehouse, C.J.1    Taylor, R.M.2    Thistlethwite, A.3    Zhang, H.4    Karimi-Busheri, F.5    Lasko, D.D.6
  • 92
    • 0025314841 scopus 로고
    • Mismatch-specific thymine DNA glycosylase and DNA polymerase β mediate the correction of G-T mispairs in nuclear extracts from human cells
    • K. Wiebauer J. Jiricny Mismatch-specific thymine DNA glycosylase and DNA polymerase β mediate the correction of G-T mispairs in nuclear extracts from human cells Proc Natl Acad Sci U S A 87 1990 5842-5845
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 5842-5845
    • Wiebauer, K.1    Jiricny, J.2
  • 93
    • 0033520969 scopus 로고    scopus 로고
    • Quality control by DNA repair
    • T. Lindahl R.D. Wood Quality control by DNA repair Science 286 1999 1897-1905
    • (1999) Science , vol.286 , pp. 1897-1905
    • Lindahl, T.1    Wood, R.D.2
  • 94
    • 0025884701 scopus 로고
    • Inactivation of DNA polymerase β by in vitro phosphorylation with protein kinase C
    • T. Tokui M. Inagaki K. Nishizawa R. Yatani M. Kusagawa K. Ajiro et al. Inactivation of DNA polymerase β by in vitro phosphorylation with protein kinase C J Biol Chem 266 1991 10820-10824
    • (1991) J Biol Chem , vol.266 , pp. 10820-10824
    • Tokui, T.1    Inagaki, M.2    Nishizawa, K.3    Yatani, R.4    Kusagawa, M.5    Ajiro, K.6
  • 95
    • 0032526616 scopus 로고    scopus 로고
    • Mitochondrial targeting of human DNA glycosylases for repair of oxidative DNA damage
    • M. Takao H. Aburatani K. Kobayashi A. Yasui Mitochondrial targeting of human DNA glycosylases for repair of oxidative DNA damage Nucleic Acids Res 26 1998 2917-2922
    • (1998) Nucleic Acids Res , vol.26 , pp. 2917-2922
    • Takao, M.1    Aburatani, H.2    Kobayashi, K.3    Yasui, A.4
  • 96
    • 2542505678 scopus 로고    scopus 로고
    • Mitochondrial DNA mutations and oxidative damage in aging and diseases: An emerging paradigm of gerontology and medicine
    • Y.H. Wei Mitochondrial DNA mutations and oxidative damage in aging and diseases: An emerging paradigm of gerontology and medicine Proc Soc Exp Biol Med 217 1998 53-63
    • (1998) Proc Soc Exp Biol Med , vol.217 , pp. 53-63
    • Wei, Y.H.1
  • 97
    • 0036570012 scopus 로고    scopus 로고
    • Repair of oxidative DNA damage in nuclear and mitochondrial DNA, and some changes with aging in mammalian cells
    • V.A. Bohr Repair of oxidative DNA damage in nuclear and mitochondrial DNA, and some changes with aging in mammalian cells Free Radic Biol Med 32 2002 804-812
    • (2002) Free Radic Biol Med , vol.32 , pp. 804-812
    • Bohr, V.A.1
  • 98
    • 0034640534 scopus 로고    scopus 로고
    • Canaries in the coal mine; Mitochondrial DNA and vascular injury from reactive oxygen species
    • R.S. Williams Canaries in the coal mine; Mitochondrial DNA and vascular injury from reactive oxygen species Circ Res 86 2000 915-916
    • (2000) Circ Res , vol.86 , pp. 915-916
    • Williams, R.S.1
  • 99
    • 0034083227 scopus 로고    scopus 로고
    • Role of oxidative stress in cardiovascular diseases
    • N.S. Dhalla R.M. Temsah T. Netticadan Role of oxidative stress in cardiovascular diseases J Hypertens 18 2000 655-673
    • (2000) J Hypertens , vol.18 , pp. 655-673
    • Dhalla, N.S.1    Temsah, R.M.2    Netticadan, T.3
  • 100
    • 0033520388 scopus 로고    scopus 로고
    • Stress pathways and heart failure
    • K.R. Chien Stress pathways and heart failure Cell 98 1999 555-558
    • (1999) Cell , vol.98 , pp. 555-558
    • Chien, K.R.1
  • 101
    • 0031669940 scopus 로고    scopus 로고
    • Cellular mechanisms of cardiac hypertrophy
    • P.H. Sugden A. Clerk Cellular mechanisms of cardiac hypertrophy J Mol Med 76 1998 725-746
    • (1998) J Mol Med , vol.76 , pp. 725-746
    • Sugden, P.H.1    Clerk, A.2
  • 102
    • 0033570271 scopus 로고    scopus 로고
    • Oxidative stress as a regulator of gene expression in the vasculature
    • C. Kunsch R.M. Medford Oxidative stress as a regulator of gene expression in the vasculature Circ Res 85 1999 753-766
    • (1999) Circ Res , vol.85 , pp. 753-766
    • Kunsch, C.1    Medford, R.M.2
  • 103
    • 0035136655 scopus 로고    scopus 로고
    • Redox regulation of MAPK pathway and cardiac hypertrophy in adult rat cardiac myocyte
    • K. Tanaka M. Honda T. Takabatake Redox regulation of MAPK pathway and cardiac hypertrophy in adult rat cardiac myocyte J Am Coll Cardiol 37 2001 676-685
    • (2001) J Am Coll Cardiol , vol.37 , pp. 676-685
    • Tanaka, K.1    Honda, M.2    Takabatake, T.3
  • 104
    • 0036791698 scopus 로고    scopus 로고
    • Activation of NADPH oxidase during progression of cardiac hypertrophy to failure
    • J.-M. Li N.P. Gall D.J. Grieve M. Chen A.M. Shah Activation of NADPH oxidase during progression of cardiac hypertrophy to failure Hypertension 40 2002 477-484
    • (2002) Hypertension , vol.40 , pp. 477-484
    • Li, J.-M.1    Gall, N.P.2    Grieve, D.J.3    Chen, M.4    Shah, A.M.5
  • 105
    • 0034535088 scopus 로고    scopus 로고
    • Extracellular signal-regulated kinase plays an essential role in hypertrophic agonists, endothelin-1 and phenylephrine-induced cardiomyocyte hypertrophy
    • T.-L. Yue J.-L. Gu C. Wang A.D. Reith J.C. Lee R.C. Mirabile et al. Extracellular signal-regulated kinase plays an essential role in hypertrophic agonists, endothelin-1 and phenylephrine-induced cardiomyocyte hypertrophy J Biol Chem 275 2000 37895-37901
    • (2000) J Biol Chem , vol.275 , pp. 37895-37901
    • Yue, T.-L.1    Gu, J.-L.2    Wang, C.3    Reith, A.D.4    Lee, J.C.5    Mirabile, R.C.6
  • 106
    • 0034794982 scopus 로고    scopus 로고
    • Reactive oxygen species modulate angiotensin II-induced β-myosin heavy chain gene expression via ras/raf/extracellular signal-regulated kinase pathway in neonatal rat cardiomyocytes
    • N.-L. Shih T.-H. Cheng S.-H. Loh P.-Y. Cheng D.L. Wang Y.-S. Chen et al. Reactive oxygen species modulate angiotensin II-induced β-myosin heavy chain gene expression via ras/raf/extracellular signal-regulated kinase pathway in neonatal rat cardiomyocytes Biochem Biophys Res Commun 283 2001 143-148
    • (2001) Biochem Biophys Res Commun , vol.283 , pp. 143-148
    • Shih, N.-L.1    Cheng, T.-H.2    Loh, S.-H.3    Cheng, P.-Y.4    Wang, D.L.5    Chen, Y.-S.6
  • 107
    • 0030782666 scopus 로고    scopus 로고
    • Increased pressure induced sustained protein kinase C-independent hybrimycin A-sensitive activation of extracellular signal-related kinase 1/2 in the rabbit aorta in organ culture
    • K.G. Birukov S. Lehoux A.A. Birukova R. Merval V.A. Tkachuk A. Tedgui Increased pressure induced sustained protein kinase C-independent hybrimycin A-sensitive activation of extracellular signal-related kinase 1/2 in the rabbit aorta in organ culture Circ Res 81 1997 895-903
    • (1997) Circ Res , vol.81 , pp. 895-903
    • Birukov, K.G.1    Lehoux, S.2    Birukova, A.A.3    Merval, R.4    Tkachuk, V.A.5    Tedgui, A.6
  • 109
    • 0033533986 scopus 로고    scopus 로고
    • Differential regulation of p90 ribosomal S6 kinase and big mitogen-activated protein kinase by ischemia/reperfusion and oxidative stress in perfused guinea pig hearts
    • Y. Takeishi J.-I. Abe J.D. Lee H. Kawakatsu R. Walsh B.C. Berk Differential regulation of p90 ribosomal S6 kinase and big mitogen-activated protein kinase by ischemia/reperfusion and oxidative stress in perfused guinea pig hearts Circ Res 85 1999 1164-1172
    • (1999) Circ Res , vol.85 , pp. 1164-1172
    • Takeishi, Y.1    Abe, J.-I.2    Lee, J.D.3    Kawakatsu, H.4    Walsh, R.5    Berk, B.C.6
  • 110
    • 0031939753 scopus 로고    scopus 로고
    • Cardiac muscle cell hypertrophy and apoptosis induced by distinct members of the p38 mitogen-activated protein kinase family
    • Y. Wang S. Huang V.P. Sah J. Ross Jr. J.H. Brown J. Han et al. Cardiac muscle cell hypertrophy and apoptosis induced by distinct members of the p38 mitogen-activated protein kinase family J Biol Chem 273 1998 2161-2168
    • (1998) J Biol Chem , vol.273 , pp. 2161-2168
    • Wang, Y.1    Huang, S.2    Sah, V.P.3    Ross, J.4    Brown, J.H.5    Han, J.6
  • 112
    • 0033216629 scopus 로고    scopus 로고
    • NF-kB as a primary regulator of the stress response
    • F. Mercurio A.M. Manning NF-kB as a primary regulator of the stress response Oncogene 18 1999 6163-6171
    • (1999) Oncogene , vol.18 , pp. 6163-6171
    • Mercurio, F.1    Manning, A.M.2
  • 113
    • 0030615201 scopus 로고    scopus 로고
    • Nuclear factor-kB: A pivotal transcription factor in chronic inflammatory diseases
    • P.J. Barnes M. Karin Nuclear factor-kB: A pivotal transcription factor in chronic inflammatory diseases N Engl J Med 336 1997 1066-1071
    • (1997) N Engl J Med , vol.336 , pp. 1066-1071
    • Barnes, P.J.1    Karin, M.2
  • 114
    • 0035174615 scopus 로고    scopus 로고
    • The transcription factor NF-kB and human diseases
    • A.S. Baldwin Jr. The transcription factor NF-kB and human diseases J Clin Invest 107 2001 3-6
    • (2001) J Clin Invest , vol.107 , pp. 3-6
    • Baldwin Jr., A.S.1
  • 115
    • 0034746919 scopus 로고    scopus 로고
    • NF-kB: A key role in inflammatory diseases
    • P.P. Tak G.S. Firestein NF-kB: A key role in inflammatory diseases J Clin Invest 107 2001 7-11
    • (2001) J Clin Invest , vol.107 , pp. 7-11
    • Tak, P.P.1    Firestein, G.S.2
  • 116
    • 0034084163 scopus 로고    scopus 로고
    • Phosphorylation meets ubiquitination: The control of NF-kB activity
    • M. Karin Y. Ben Neriah Phosphorylation meets ubiquitination: The control of NF-kB activity Annu Rev Immnol 18 2000 621-663
    • (2000) Annu Rev Immnol , vol.18 , pp. 621-663
    • Karin, M.1    Ben Neriah, Y.2
  • 117
    • 0033595893 scopus 로고    scopus 로고
    • How NF-kB is activated: The role of the IkB kinase (IKK) complex
    • M. Karin How NF-kB is activated: The role of the IkB kinase (IKK) complex Oncogene 18 2000 6867-6874
    • (2000) Oncogene , vol.18 , pp. 6867-6874
    • Karin, M.1
  • 118
    • 0030610362 scopus 로고    scopus 로고
    • A cytokine-responsive IkB kinase that activates the transcription factor NF-kB
    • J.A. DiDonato M. Hayakawa D.M. Rothwarf E. Zandi M. Karin A cytokine-responsive IkB kinase that activates the transcription factor NF-kB Nature 388 1997 548-554
    • (1997) Nature , vol.388 , pp. 548-554
    • DiDonato, J.A.1    Hayakawa, M.2    Rothwarf, D.M.3    Zandi, E.4    Karin, M.5
  • 119
    • 0030685825 scopus 로고    scopus 로고
    • IKK-1 and IKK-2: Cytokine-activated IkB kinases essential for NF-kB activation
    • F. Mercurio H. Zhu B.W. Murray A. Shevchenko B.L. Bennett J. Li et al. IKK-1 and IKK-2: Cytokine-activated IkB kinases essential for NF-kB activation Science 278 1997 860-866
    • (1997) Science , vol.278 , pp. 860-866
    • Mercurio, F.1    Zhu, H.2    Murray, B.W.3    Shevchenko, A.4    Bennett, B.L.5    Li, J.6
  • 120
    • 0032583947 scopus 로고    scopus 로고
    • NF-kB-inducing kinase activates IKK-α by phosphorylation of Ser-176
    • L. Ling Z. Cao D.V. Goeddel NF-kB-inducing kinase activates IKK-α by phosphorylation of Ser-176 Proc Natl Acad Sci U S A 95 1998 3792-3797
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 3792-3797
    • Ling, L.1    Cao, Z.2    Goeddel, D.V.3
  • 122
    • 0033537719 scopus 로고    scopus 로고
    • Positive and negative regulation of IkB kinase activity thorugh IKKβ subunit phosphorylation
    • M. Delhase M. Hayakawa Y. Chen M. Karin Positive and negative regulation of IkB kinase activity thorugh IKKβ subunit phosphorylation Science 284 1999 309-313
    • (1999) Science , vol.284 , pp. 309-313
    • Delhase, M.1    Hayakawa, M.2    Chen, Y.3    Karin, M.4
  • 123
    • 0032575752 scopus 로고    scopus 로고
    • Mtochondria and apoptosis
    • D.R. Green J.C. Reed Mtochondria and apoptosis Science 281 1998 1309-1312
    • (1998) Science , vol.281 , pp. 1309-1312
    • Green, D.R.1    Reed, J.C.2
  • 124
    • 0031037897 scopus 로고    scopus 로고
    • The release of cytochrome c from mitochondria: A primary site for Bcl-2 regulation of apoptosis
    • R.M. Kluck E. Bossy-Wetzel D.R. Green D.D. Newmeyer The release of cytochrome c from mitochondria: A primary site for Bcl-2 regulation of apoptosis Science 275 1997 1132-1136
    • (1997) Science , vol.275 , pp. 1132-1136
    • Kluck, R.M.1    Bossy-Wetzel, E.2    Green, D.R.3    Newmeyer, D.D.4
  • 125
    • 0030581151 scopus 로고    scopus 로고
    • Induction of apoptotic program in cell-free extracts: Requirement for dAATP and cytochrome c
    • X. Liu C.N. Kim J. Yang R. Jemmerson X. Wang Induction of apoptotic program in cell-free extracts: Requirement for dAATP and cytochrome c Cell 86 1996 147-157
    • (1996) Cell , vol.86 , pp. 147-157
    • Liu, X.1    Kim, C.N.2    Yang, J.3    Jemmerson, R.4    Wang, X.5
  • 126
    • 0027449187 scopus 로고
    • Induction of apoptosis in fibroblasts by IL-1 beta-converting enzyme, a mammalian homolog of the C. elegans cell death gene ced-3
    • M. Miura H. Zhu R. Rotello E.A. Hartwieg J. Yuan Induction of apoptosis in fibroblasts by IL-1 beta-converting enzyme, a mammalian homolog of the C. elegans cell death gene ced-3 Cell 75 1993 653-660
    • (1993) Cell , vol.75 , pp. 653-660
    • Miura, M.1    Zhu, H.2    Rotello, R.3    Hartwieg, E.A.4    Yuan, J.5
  • 127
    • 0027990778 scopus 로고
    • Induction of apoptosis by the mouse Nedd2 gene, which encodes a protein similar to the product of the Caenorhabditis elegans cell death gene ced-3 and the mammalian IL-1 beta-converting enzyme
    • S. Kumar M. Kinoshita M. Noda N.G. Copeland N.A. Jenkins Induction of apoptosis by the mouse Nedd2 gene, which encodes a protein similar to the product of the Caenorhabditis elegans cell death gene ced-3 and the mammalian IL-1 beta-converting enzyme Genes Dev 8 1994 1613-1626
    • (1994) Genes Dev , vol.8 , pp. 1613-1626
    • Kumar, S.1    Kinoshita, M.2    Noda, M.3    Copeland, N.G.4    Jenkins, N.A.5
  • 128
    • 0028990125 scopus 로고
    • Yama/CPP32 beta, a mammalian homolog of CED-3, is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase
    • M. Tewari L.T. Quan K. Q'Rourke S. Desnoyers Z. Zeng D.R. Beidler et al. Yama/CPP32 beta, a mammalian homolog of CED-3, is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase Cell 81 1995 801-809
    • (1995) Cell , vol.81 , pp. 801-809
    • Tewari, M.1    Quan, L.T.2    Q'Rourke, K.3    Desnoyers, S.4    Zeng, Z.5    Beidler, D.R.6
  • 129
    • 0028920863 scopus 로고
    • Altered cytokine export and apoptosis in mice deficient in interleukin-1 beta converting enzyme
    • K. Kuida J.A. Lippke G. Ku M.W. Harding D.J. Livingston M.S. Su et al. Altered cytokine export and apoptosis in mice deficient in interleukin-1 beta converting enzyme Science 267 1995 2000-2003
    • (1995) Science , vol.267 , pp. 2000-2003
    • Kuida, K.1    Lippke, J.A.2    Ku, G.3    Harding, M.W.4    Livingston, D.J.5    Su, M.S.6
  • 130
    • 0030614952 scopus 로고    scopus 로고
    • Inhibition of interleukin 1beta converting enzyme family proteases reduces ischemic and excitotoxic neuronal damage
    • H. Hara R.M. Friedlander V. Gagliardini C. Ayata K. Fink Z. Huang et al. Inhibition of interleukin 1beta converting enzyme family proteases reduces ischemic and excitotoxic neuronal damage Proc Natl Acad Sci U S A 94 1997 2007-2012
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 2007-2012
    • Hara, H.1    Friedlander, R.M.2    Gagliardini, V.3    Ayata, C.4    Fink, K.5    Huang, Z.6
  • 131
    • 0032570292 scopus 로고    scopus 로고
    • Attenuation of ischemia/reperfusion injury in rats by a caspase inhibitor
    • H. Yaoita K. Ogawa K. Maehara Y. Maruyama Attenuation of ischemia/ reperfusion injury in rats by a caspase inhibitor Circulation 97 1998 276-281
    • (1998) Circulation , vol.97 , pp. 276-281
    • Yaoita, H.1    Ogawa, K.2    Maehara, K.3    Maruyama, Y.4
  • 132
    • 0034016833 scopus 로고    scopus 로고
    • Caspase inhibition and limitation of myocardial infarct size: Protection against lethal reperfusion injury
    • M.M. Mocanu G.F. Baxter D.M. Yellon Caspase inhibition and limitation of myocardial infarct size: Protection against lethal reperfusion injury Br J Pharmacol 130 2000 197-200
    • (2000) Br J Pharmacol , vol.130 , pp. 197-200
    • Mocanu, M.M.1    Baxter, G.F.2    Yellon, D.M.3
  • 133
  • 134
    • 0028943734 scopus 로고
    • Apoptosis in the pathogenesis and treatment of diseases
    • C.B. Thompson Apoptosis in the pathogenesis and treatment of diseases Science 267 1995 1456-1462
    • (1995) Science , vol.267 , pp. 1456-1462
    • Thompson, C.B.1
  • 135
  • 136
    • 0026722655 scopus 로고
    • Cooperative interaction between c-myc and bac-2 proto-oncogenes
    • A. Fanidi E.A. Harrington G.I. Evan Cooperative interaction between c-myc and bac-2 proto-oncogenes Nature 359 1992 554-556
    • (1992) Nature , vol.359 , pp. 554-556
    • Fanidi, A.1    Harrington, E.A.2    Evan, G.I.3
  • 137
    • 0029808466 scopus 로고    scopus 로고
    • Cell cycle checkpoints: Preventing an identity crisis
    • Elledge SJ. Cell cycle checkpoints: Preventing an identity crisis. Science 1996;274:1664-72.
    • (1996) Science , vol.274 , pp. 1664-1672
    • Elledge, S.J.1
  • 139
    • 0026454763 scopus 로고
    • Prevention of programmed cell death of sympathetic neurons by the bcl-2 proto-oncogene
    • I. Garcia I. Martinou Y. Tsujimoto J.C. Martinou Prevention of programmed cell death of sympathetic neurons by the bcl-2 proto-oncogene Science 258 1992 302-304
    • (1992) Science , vol.258 , pp. 302-304
    • Garcia, I.1    Martinou, I.2    Tsujimoto, Y.3    Martinou, J.C.4
  • 141
    • 0036499892 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase: Killer or consipirator? The 'suicide hypothesis' revisited
    • A. Chiarugi Poly(ADP-ribose) polymerase: Killer or consipirator? The 'suicide hypothesis' revisited Trends Pharmacol Sci 23 2002 122-129
    • (2002) Trends Pharmacol Sci , vol.23 , pp. 122-129
    • Chiarugi, A.1
  • 142
  • 143
    • 0035796025 scopus 로고    scopus 로고
    • Functions of poly(ADP-ribose) polymerase (PARP) in DNA repair, genomic integrity and cell death
    • Z. Herceg Z.-Q. Wang Functions of poly(ADP-ribose) polymerase (PARP) in DNA repair, genomic integrity and cell death Mutat Res 477 2001 97-110
    • (2001) Mutat Res , vol.477 , pp. 97-110
    • Herceg, Z.1    Wang, Z.-Q.2
  • 144
    • 0040226769 scopus 로고    scopus 로고
    • Cellular responses to DNA damage in the absence of poly(ADP-ribose) polymerase
    • Y.L. Rhun J.B. Kirkland G.M. Shah Cellular responses to DNA damage in the absence of poly(ADP-ribose) polymerase Biochem Biophys Res Commun 245 1998 1-10
    • (1998) Biochem Biophys Res Commun , vol.245 , pp. 1-10
    • Rhun, Y.L.1    Kirkland, J.B.2    Shah, G.M.3
  • 146
    • 12444276626 scopus 로고    scopus 로고
    • PARP-3 localizes preferentially to the daughter centriole and interferes with the G1/S cell cycle progression
    • A. Augustin C. Spenlehauer H. Dumond J. Ménissier-de Murcia M. Piel A. Schmit et al. PARP-3 localizes preferentially to the daughter centriole and interferes with the G1/S cell cycle progression J Cell Sci 116 2003 1551-1562
    • (2003) J Cell Sci , vol.116 , pp. 1551-1562
    • Augustin, A.1    Spenlehauer, C.2    Dumond, H.3    Ménissier-de Murcia, J.4    Piel, M.5    Schmit, A.6
  • 147
    • 0035976732 scopus 로고    scopus 로고
    • TCDD-inducible poly(ADP-ribose) polymerase: A novel response to 2,3,7,8-tetrachlorodibenzo-p-dioxin
    • Q. Ma K.T. Baldwin A.J. Renzelli A. McDaniel L. Dong TCDD-inducible poly(ADP-ribose) polymerase: A novel response to 2,3,7,8-tetrachlorodibenzo-p-dioxin Biochem Biophys Res Commun 289 2001 499-506
    • (2001) Biochem Biophys Res Commun , vol.289 , pp. 499-506
    • Ma, Q.1    Baldwin, K.T.2    Renzelli, A.J.3    McDaniel, A.4    Dong, L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.