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Volumn 10, Issue 4, 2012, Pages 354-369

Redox signaling pathways involved in neuronal ischemic preconditioning

Author keywords

Epsilon PKC; HIF; Ischemic preconditioning; Nrf2; Reactive oxygen species; Reperfusion; SIRT1; Sirtuin

Indexed keywords

ANTIOXIDANT; CARBON MONOXIDE; DIAZOXIDE; HYDROGEN SULFIDE; HYPOXIA INDUCIBLE FACTOR 1; MITOCHONDRIAL PROTEIN; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE 1; NITRIC OXIDE; PROCOLLAGEN PROLINE 2 OXOGLUTARATE 4 DIOXYGENASE; PROTEIN KINASE C EPSILON; REACTIVE NITROGEN SPECIES; REACTIVE OXYGEN METABOLITE; SIRTUIN 1; SUPEROXIDE DISMUTASE; TRANSCRIPTION FACTOR NRF2; UBIDECARENONE;

EID: 84874864664     PISSN: 1570159X     EISSN: 18756190     Source Type: Journal    
DOI: 10.2174/1570159x11209040354     Document Type: Review
Times cited : (67)

References (188)
  • 2
    • 0037307212 scopus 로고    scopus 로고
    • To die or not to die for neurons in ischemia, traumatic brain injury and epilepsy: A review on the stress-activated signaling pathways and apoptotic pathways
    • Liou, A.K.; Clark, R.S.; Henshall, D.C.; Yin, X.M.; Chen, J. To die or not to die for neurons in ischemia, traumatic brain injury and epilepsy: a review on the stress-activated signaling pathways and apoptotic pathways. Prog. Neurobiol., 2003, 69(2), 103-142.
    • (2003) Prog. Neurobiol. , vol.69 , Issue.2 , pp. 103-142
    • Liou, A.K.1    Clark, R.S.2    Henshall, D.C.3    Yin, X.M.4    Chen, J.5
  • 3
    • 0033386202 scopus 로고    scopus 로고
    • Mitochondria in neurodegeneration: Bioenergetic function in cell life and death
    • Murphy, A.N.; Fiskum, G.; Beal, M.F. Mitochondria in neurodegeneration: bioenergetic function in cell life and death. J. Cereb. Blood Flow Metab., 1999, 19(3), 231-245.
    • (1999) J. Cereb. Blood Flow Metab. , vol.19 , Issue.3 , pp. 231-245
    • Murphy, A.N.1    Fiskum, G.2    Beal, M.F.3
  • 4
    • 0343247698 scopus 로고    scopus 로고
    • Antioxidants, mitochondrial hyperoxidation and electrical recovery after anoxia in hippocampal slices
    • Perez-Pinzon, M.A.; Mumford, P.L.; Rosenthal, M.; Sick, T.J. Antioxidants, mitochondrial hyperoxidation and electrical recovery after anoxia in hippocampal slices. Brain Res., 1997, 754(1-2), 163-170.
    • (1997) Brain Res. , vol.754 , Issue.1-2 , pp. 163-170
    • Perez-Pinzon, M.A.1    Mumford, P.L.2    Rosenthal, M.3    Sick, T.J.4
  • 5
    • 0343907202 scopus 로고    scopus 로고
    • Rapid preconditioning protects rats against ischemic neuronal damage after 3 but not 7 days of reperfusion following global cerebral ischemia
    • Perez-Pinzon, M.A.; Xu, G.P.; Dietrich, W.D.; Rosenthal, M.; Sick, T.J. Rapid preconditioning protects rats against ischemic neuronal damage after 3 but not 7 days of reperfusion following global cerebral ischemia. J. Cereb. Blood. Flow. Metab., 1997, 17(2), 175-182.
    • (1997) J. Cereb. Blood. Flow. Metab. , vol.17 , Issue.2 , pp. 175-182
    • Perez-Pinzon, M.A.1    Xu, G.P.2    Dietrich, W.D.3    Rosenthal, M.4    Sick, T.J.5
  • 6
    • 0029073811 scopus 로고
    • Mitochondrial hyperoxidation signals residual intracellular dysfunction after global ischemia in rat neocortex
    • Rosenthal, M.; Feng, Z.C.; Raffin, C.N.; Harrison, M.; Sick, T.J. Mitochondrial hyperoxidation signals residual intracellular dysfunction after global ischemia in rat neocortex. J. Cereb. Blood Flow Metab., 1995, 15(4), 655-665.
    • (1995) J. Cereb. Blood Flow Metab. , vol.15 , Issue.4 , pp. 655-665
    • Rosenthal, M.1    Feng, Z.C.2    Raffin, C.N.3    Harrison, M.4    Sick, T.J.5
  • 7
    • 0031405688 scopus 로고    scopus 로고
    • Mitochondrial hyperoxidation after cerebral anoxia/ischemia. Epiphenomenon or precursor to residual damage?
    • Rosenthal, M.; Mumford, P.L.; Sick, T.J.; Perez-Pinzon, M.A. Mitochondrial hyperoxidation after cerebral anoxia/ischemia. Epiphenomenon or precursor to residual damage? Adv. Exp. Med. Biol., 1997, 428, 189-195.
    • (1997) Adv. Exp. Med. Biol. , vol.428 , pp. 189-195
    • Rosenthal, M.1    Mumford, P.L.2    Sick, T.J.3    Perez-Pinzon, M.A.4
  • 8
    • 0025755787 scopus 로고
    • NADH fluorescence and regional energy metabolites during focal ischemia and reperfusion of rat brain
    • Welsh, F.A.; Marcy, V.R.; Sims, R.E. NADH fluorescence and regional energy metabolites during focal ischemia and reperfusion of rat brain. J. Cereb. Blood Flow Metab., 1991, 11(3), 459-465.
    • (1991) J. Cereb. Blood Flow Metab. , vol.11 , Issue.3 , pp. 459-465
    • Welsh, F.A.1    Marcy, V.R.2    Sims, R.E.3
  • 9
    • 0020326533 scopus 로고
    • Columnar alterations of NADH fluorescence during hypoxia-ischemia in immature rat brain
    • Welsh, F.A.; Vannucci, R.C.; Brierley, J.B. Columnar alterations of NADH fluorescence during hypoxia-ischemia in immature rat brain. J. Cereb. Blood. Flow Metab., 1982, 2(2), 221-228.
    • (1982) J. Cereb. Blood. Flow Metab. , vol.2 , Issue.2 , pp. 221-228
    • Welsh, F.A.1    Vannucci, R.C.2    Brierley, J.B.3
  • 12
    • 0018625858 scopus 로고
    • Hypoxia and oxygen toxicity
    • Fridovich, I. Hypoxia and oxygen toxicity. Adv. Neurol., 1979, 26, 255-259.
    • (1979) Adv. Neurol. , vol.26 , pp. 255-259
    • Fridovich, I.1
  • 13
    • 0024785709 scopus 로고
    • Oxygen radicals in CNS damage
    • Kontos, H.A. Oxygen radicals in CNS damage. Chem. Biol. Interact., 1989, 72(3), 229-255.
    • (1989) Chem. Biol. Interact. , vol.72 , Issue.3 , pp. 229-255
    • Kontos, H.A.1
  • 14
    • 0025347378 scopus 로고
    • Effect of peroxide, sodium, and calcium on brain mitochondrial respiration in vitro: Potential role in cerebral ischemia and reperfusion
    • Vlessis, A.A.; Widener, L.L.; Bartos, D. Effect of peroxide, sodium, and calcium on brain mitochondrial respiration in vitro: potential role in cerebral ischemia and reperfusion. J. Neurochem., 1990, 54(4), 1412-1418.
    • (1990) J. Neurochem. , vol.54 , Issue.4 , pp. 1412-1418
    • Vlessis, A.A.1    Widener, L.L.2    Bartos, D.3
  • 15
    • 0030551050 scopus 로고    scopus 로고
    • Endothelial cell injury in cardiovascular surgery: Ischemiareperfusion
    • Boyle, E. M, Jr.; Pohlman, T.H.; Cornejo, C.J.; Verrier, E.D. Endothelial cell injury in cardiovascular surgery: ischemiareperfusion. Ann. Thorac. Surg., 1996, 62(6), 1868-1875.
    • (1996) Ann. Thorac. Surg. , vol.62 , Issue.6 , pp. 1868-1875
    • Boyle Jr., E.M.1    Pohlman, T.H.2    Cornejo, C.J.3    Verrier, E.D.4
  • 16
    • 0021918432 scopus 로고
    • Effect of reperfusion late in the phase of reversible ischemic injury. Changes in cell volume, electrolytes, metabolites, and ultrastructure
    • Jennings, R.B.; Schaper, J.; Hill, M.L.; Steenbergen, C., Jr.; Reimer, K.A. Effect of reperfusion late in the phase of reversible ischemic injury. Changes in cell volume, electrolytes, metabolites, and ultrastructure. Circ. Res., 1985, 56(2), 262-278.
    • (1985) Circ. Res. , vol.56 , Issue.2 , pp. 262-278
    • Jennings, R.B.1    Schaper, J.2    Hill, M.L.3    Steenbergen Jr., C.4    Reimer, K.A.5
  • 18
    • 0026782517 scopus 로고
    • Pathophysiology and treatment of focal cerebral ischemia. Part II: Mechanisms of damage and treatment
    • Siesjo, B.K. Pathophysiology and treatment of focal cerebral ischemia. Part II: Mechanisms of damage and treatment. J. Neurosurg., 1992, 77(3), 337-354.
    • (1992) J. Neurosurg. , vol.77 , Issue.3 , pp. 337-354
    • Siesjo, B.K.1
  • 19
    • 84863849519 scopus 로고    scopus 로고
    • Studies of isolated global brain ischaemia: II. Controlled reperfusion provides complete neurologic recovery following 30 min of warm ischaemia-the importance of perfusion pressure
    • Allen, B.S.; Ko, Y.; Buckberg, G.D.; Tan, Z. Studies of isolated global brain ischaemia: II. Controlled reperfusion provides complete neurologic recovery following 30 min of warm ischaemia-the importance of perfusion pressure. Eur. J. Cardiothorac. Surg., 2012.
    • (2012) Eur. J. Cardiothorac. Surg.
    • Allen, B.S.1    Ko, Y.2    Buckberg, G.D.3    Tan, Z.4
  • 20
    • 0030561569 scopus 로고    scopus 로고
    • Anoxic preconditioning in hippocampal slices: Role of adenosine
    • Perez-Pinzon, M.A.; Mumford, P.L.; Rosenthal, M.; Sick, T.J. Anoxic preconditioning in hippocampal slices: role of adenosine. Neuroscience, 1996, 75(3), 687-694.
    • (1996) Neuroscience , vol.75 , Issue.3 , pp. 687-694
    • Perez-Pinzon, M.A.1    Mumford, P.L.2    Rosenthal, M.3    Sick, T.J.4
  • 21
    • 0029974018 scopus 로고    scopus 로고
    • Interleukin-1 mediates induction of tolerance to global ischemia in gerbil hippocampal CA1 neurons
    • Ohtsuki, T.; Ruetzler, C.A.; Tasaki, K.; Hallenbeck, J.M. Interleukin-1 mediates induction of tolerance to global ischemia in gerbil hippocampal CA1 neurons. J. Cereb. Blood. Flow. Metab., 1996, 16(6), 1137-1142.
    • (1996) J. Cereb. Blood. Flow. Metab. , vol.16 , Issue.6 , pp. 1137-1142
    • Ohtsuki, T.1    Ruetzler, C.A.2    Tasaki, K.3    Hallenbeck, J.M.4
  • 22
    • 0031578934 scopus 로고    scopus 로고
    • Neuroprotective effects of TNF binding protein in focal cerebral ischemia
    • Nawashiro, H.; Martin, D.; Hallenbeck, J.M. Neuroprotective effects of TNF binding protein in focal cerebral ischemia. Brain Res., 1997, 778(2), 265-271.
    • (1997) Brain Res. , vol.778 , Issue.2 , pp. 265-271
    • Nawashiro, H.1    Martin, D.2    Hallenbeck, J.M.3
  • 23
    • 0141992197 scopus 로고    scopus 로고
    • Brief, repeated, oxygen-glucose deprivation episodes protect neurotransmission from a longer ischemic episode in the in vitro hippocampus: Role of adenosine receptors
    • Pugliese, A.M.; Latini, S.; Corradetti, R.; Pedata, F. Brief, repeated, oxygen-glucose deprivation episodes protect neurotransmission from a longer ischemic episode in the in vitro hippocampus: role of adenosine receptors. Br. J. Pharmacol., 2003, 140(2), 305-314.
    • (2003) Br. J. Pharmacol. , vol.140 , Issue.2 , pp. 305-314
    • Pugliese, A.M.1    Latini, S.2    Corradetti, R.3    Pedata, F.4
  • 24
    • 0026547286 scopus 로고
    • Blockade of ATP-sensitive potassium channels prevents myocardial preconditioning in dogs
    • Gross, G.J.; Auchampach, J.A. Blockade of ATP-sensitive potassium channels prevents myocardial preconditioning in dogs. Circ. Res., 1992, 70(2), 223-233.
    • (1992) Circ. Res. , vol.70 , Issue.2 , pp. 223-233
    • Gross, G.J.1    Auchampach, J.A.2
  • 25
    • 0027297849 scopus 로고
    • Adenosine A1 receptors, KATP channels, and ischemic preconditioning in dogs
    • Auchampach, J.A.; Gross, G.J. Adenosine A1 receptors, KATP channels, and ischemic preconditioning in dogs. Am. J. Physiol., 1993, 264(5 Pt 2), H1327-1336.
    • (1993) Am. J. Physiol. , vol.264 , Issue.5 PART 2
    • Auchampach, J.A.1    Gross, G.J.2
  • 26
    • 0026346285 scopus 로고
    • The new K+ channel opener Aprikalim (RP 52891) reduces experimental infarct size in dogs in the absence of hemodynamic changes
    • Auchampach, J.A.; Maruyama, M.; Cavero, I.; Gross, G.J. The new K+ channel opener Aprikalim (RP 52891) reduces experimental infarct size in dogs in the absence of hemodynamic changes. J. Pharmacol. Exp. Ther., 1991, 259(3), 961-967.
    • (1991) J. Pharmacol. Exp. Ther. , vol.259 , Issue.3 , pp. 961-967
    • Auchampach, J.A.1    Maruyama, M.2    Cavero, I.3    Gross, G.J.4
  • 27
    • 0034721572 scopus 로고    scopus 로고
    • K(ATP) channel openers, adenosine agonists and epileptic preconditioning are stress signals inducing hippocampal neuroprotection
    • Blondeau, N.; Plamondon, H.; Richelme, C.; Heurteaux, C.; Lazdunski, M. K(ATP) channel openers, adenosine agonists and epileptic preconditioning are stress signals inducing hippocampal neuroprotection. Neuroscience, 2000, 100(3), 465-474.
    • (2000) Neuroscience , vol.100 , Issue.3 , pp. 465-474
    • Blondeau, N.1    Plamondon, H.2    Richelme, C.3    Heurteaux, C.4    Lazdunski, M.5
  • 28
    • 0033103144 scopus 로고    scopus 로고
    • Rapid preconditioning neuroprotection following anoxia in hippocampal slices: Role of the K+ ATP channel and protein kinase C
    • Perez-Pinzon, M.A.; Born, J.G. Rapid preconditioning neuroprotection following anoxia in hippocampal slices: role of the K+ ATP channel and protein kinase C. Neuroscience, 1999, 89(2), 453-459.
    • (1999) Neuroscience , vol.89 , Issue.2 , pp. 453-459
    • Perez-Pinzon, M.A.1    Born, J.G.2
  • 29
    • 0027081398 scopus 로고
    • Influence of oxidative stress on induced tolerance to ischemia in gerbil hippocampal neurons
    • Ohtsuki, T.; Matsumoto, M.; Kuwabara, K.; Kitagawa, K.; Suzuki, K.; Taniguchi, N.; Kamada, T. Influence of oxidative stress on induced tolerance to ischemia in gerbil hippocampal neurons. Brain Res., 1992, 599(2), 246-252.
    • (1992) Brain Res. , vol.599 , Issue.2 , pp. 246-252
    • Ohtsuki, T.1    Matsumoto, M.2    Kuwabara, K.3    Kitagawa, K.4    Suzuki, K.5    Taniguchi, N.6    Kamada, T.7
  • 30
    • 79957937727 scopus 로고    scopus 로고
    • Protective effect of natural antioxidants on heart against ischemia-reperfusion damage
    • Zhao, Y.; Zhao, B. Protective effect of natural antioxidants on heart against ischemia-reperfusion damage. Curr. Pharm. Biotechnol., 2010, 11(8), 868-874.
    • (2010) Curr. Pharm. Biotechnol. , vol.11 , Issue.8 , pp. 868-874
    • Zhao, Y.1    Zhao, B.2
  • 32
    • 0022321324 scopus 로고
    • The effects of medroxyprogesterone acetate on enzyme activities in human endometrial carcinoma
    • Philipson, K.A.; Elder, M.G.; White, J.O. The effects of medroxyprogesterone acetate on enzyme activities in human endometrial carcinoma. J. Steroid. Biochem., 1985, 23(6A), 1059-1064.
    • (1985) J. Steroid. Biochem. , vol.23 , Issue.6 A , pp. 1059-1064
    • Philipson, K.A.1    Elder, M.G.2    White, J.O.3
  • 33
    • 0030060186 scopus 로고    scopus 로고
    • Mitochondrial generation of reactive oxygen species after brain ischemia in the rat
    • discussion 332
    • Piantadosi, C.A.; Zhang, J. Mitochondrial generation of reactive oxygen species after brain ischemia in the rat. Stroke, 1996, 27(2), 327-331; discussion 332.
    • (1996) Stroke , vol.27 , Issue.2 , pp. 327-331
    • Piantadosi, C.A.1    Zhang, J.2
  • 34
    • 0025309904 scopus 로고
    • Oxidative damage to brain proteins, loss of glutamine synthetase activity, and production of free radicals during ischemia/reperfusion-induced injury to gerbil brain
    • Oliver, C.N.; Starke-Reed, P.E.; Stadtman, E.R.; Liu, G.J.; Carney, J.M.; Floyd, R.A. Oxidative damage to brain proteins, loss of glutamine synthetase activity, and production of free radicals during ischemia/reperfusion-induced injury to gerbil brain. Proc. Natl. Acad. Sci., U S A, 1990, 87(13), 5144-5147.
    • (1990) Proc. Natl. Acad. Sci., U S A , vol.87 , Issue.13 , pp. 5144-5147
    • Oliver, C.N.1    Starke-Reed, P.E.2    Stadtman, E.R.3    Liu, G.J.4    Carney, J.M.5    Floyd, R.A.6
  • 35
    • 0029019921 scopus 로고
    • The role of oxygen free radicals in preconditioning
    • Ambrosio, G.; Tritto, I.; Chiariello, M. The role of oxygen free radicals in preconditioning. J. Mol. Cell. Cardiol., 1995, 27(4), 1035-1039.
    • (1995) J. Mol. Cell. Cardiol. , vol.27 , Issue.4 , pp. 1035-1039
    • Ambrosio, G.1    Tritto, I.2    Chiariello, M.3
  • 36
    • 0030890196 scopus 로고    scopus 로고
    • Oxygen radicals released during ischemic preconditioning contribute to cardioprotection in the rabbit myocardium
    • Baines, C.P.; Goto, M.; Downey, J.M. Oxygen radicals released during ischemic preconditioning contribute to cardioprotection in the rabbit myocardium. J. Mol. Cell. Cardiol., 1997, 29(1), 207-216.
    • (1997) J. Mol. Cell. Cardiol. , vol.29 , Issue.1 , pp. 207-216
    • Baines, C.P.1    Goto, M.2    Downey, J.M.3
  • 37
    • 0029160860 scopus 로고
    • A redox-based mechanism for cardioprotection induced by ischemic preconditioning in perfused rat heart
    • Chen, W.; Gabel, S.; Steenbergen, C.; Murphy, E. A redox-based mechanism for cardioprotection induced by ischemic preconditioning in perfused rat heart. Circ. Res., 1995, 77(2), 424-429.
    • (1995) Circ. Res. , vol.77 , Issue.2 , pp. 424-429
    • Chen, W.1    Gabel, S.2    Steenbergen, C.3    Murphy, E.4
  • 38
    • 0035895321 scopus 로고    scopus 로고
    • Morphine mimics preconditioning via free radical signals and mitochondrial K(ATP) channels in myocytes
    • McPherson, B.C.; Yao, Z. Morphine mimics preconditioning via free radical signals and mitochondrial K(ATP) channels in myocytes. Circulation, 2001, 103(2), 290-295.
    • (2001) Circulation , vol.103 , Issue.2 , pp. 290-295
    • McPherson, B.C.1    Yao, Z.2
  • 40
    • 0344925103 scopus 로고    scopus 로고
    • Preconditioning potentiates redox signaling and converts death signal into survival signal
    • Das, D.K.; Maulik, N. Preconditioning potentiates redox signaling and converts death signal into survival signal. Arch. Biochem. Biophys., 2003, 420(2), 305-311.
    • (2003) Arch. Biochem. Biophys. , vol.420 , Issue.2 , pp. 305-311
    • Das, D.K.1    Maulik, N.2
  • 42
    • 5644241361 scopus 로고    scopus 로고
    • Brain ischemic preconditioning is abolished by antioxidant drugs but does not upregulate superoxide dismutase and glutathion peroxidase
    • Puisieux, F.; Deplanque, D.; Bulckaen, H.; Maboudou, P.; Gele, P.; Lhermitte, M.; Lebuffe, G.; Bordet, R. Brain ischemic preconditioning is abolished by antioxidant drugs but does not upregulate superoxide dismutase and glutathion peroxidase. Brain Res., 2004, 1027(1-2), 30-37.
    • (2004) Brain Res. , vol.1027 , Issue.1-2 , pp. 30-37
    • Puisieux, F.1    Deplanque, D.2    Bulckaen, H.3    Maboudou, P.4    Gele, P.5    Lhermitte, M.6    Lebuffe, G.7    Bordet, R.8
  • 43
    • 20444430402 scopus 로고    scopus 로고
    • Neuroprotection by hypoxic preconditioning involves oxidative stress-mediated expression of hypoxia-inducible factor and erythropoietin
    • Liu, J.; Narasimhan, P.; Yu, F.; Chan, P.H. Neuroprotection by hypoxic preconditioning involves oxidative stress-mediated expression of hypoxia-inducible factor and erythropoietin. Stroke, 2005, 36(6), 1264-1269.
    • (2005) Stroke , vol.36 , Issue.6 , pp. 1264-1269
    • Liu, J.1    Narasimhan, P.2    Yu, F.3    Chan, P.H.4
  • 44
    • 36348935147 scopus 로고    scopus 로고
    • EpsilonPKC phosphorylates the mitochondrial K(+) (ATP) channel during induction of ischemic preconditioning in the rat hippocampus
    • Raval, A.P.; Dave, K.R.; DeFazio, R.A.; Perez-Pinzon, M.A. epsilonPKC phosphorylates the mitochondrial K(+) (ATP) channel during induction of ischemic preconditioning in the rat hippocampus. Brain Res., 2007, 1184, 345-353.
    • (2007) Brain Res. , vol.1184 , pp. 345-353
    • Raval, A.P.1    Dave, K.R.2    DeFazio, R.A.3    Perez-Pinzon, M.A.4
  • 45
    • 0034660664 scopus 로고    scopus 로고
    • Block of cardiac ATP-sensitive K(+) channels reduces hydroxyl radicals in the rat myocardium
    • Obata, T.; Yamanaka, Y. Block of cardiac ATP-sensitive K(+) channels reduces hydroxyl radicals in the rat myocardium. Arch. Biochem. Biophys., 2000, 378(2), 195-200.
    • (2000) Arch. Biochem. Biophys. , vol.378 , Issue.2 , pp. 195-200
    • Obata, T.1    Yamanaka, Y.2
  • 46
    • 0031088154 scopus 로고    scopus 로고
    • The ischemiaselective KATP channel antagonist, 5-hydroxydecanoate, blocks ischemic preconditioning in the rat heart
    • Schultz, J.E.; Qian, Y.Z.; Gross, G.J.; Kukreja, R.C. The ischemiaselective KATP channel antagonist, 5-hydroxydecanoate, blocks ischemic preconditioning in the rat heart. J. Mol. Cell. Cardiol., 1997, 29(3), 1055-1060.
    • (1997) J. Mol. Cell. Cardiol. , vol.29 , Issue.3 , pp. 1055-1060
    • Schultz, J.E.1    Qian, Y.Z.2    Gross, G.J.3    Kukreja, R.C.4
  • 47
    • 0035957635 scopus 로고    scopus 로고
    • Diazoxide-induced cardioprotection requires signaling through a redox-sensitive mechanism
    • Forbes, R.A.; Steenbergen, C.; Murphy, E. Diazoxide-induced cardioprotection requires signaling through a redox-sensitive mechanism. Circ. Res., 2001, 88(8), 802-809.
    • (2001) Circ. Res. , vol.88 , Issue.8 , pp. 802-809
    • Forbes, R.A.1    Steenbergen, C.2    Murphy, E.3
  • 48
    • 0034860570 scopus 로고    scopus 로고
    • Mitochondrial K(ATP) channel opening protects a human atrial-derived cell line by a mechanism involving free radical generation
    • Carroll, R.; Gant, V.A.; Yellon, D.M. Mitochondrial K(ATP) channel opening protects a human atrial-derived cell line by a mechanism involving free radical generation. Cardiovasc. Res., 2001, 51(4), 691-700.
    • (2001) Cardiovasc. Res. , vol.51 , Issue.4 , pp. 691-700
    • Carroll, R.1    Gant, V.A.2    Yellon, D.M.3
  • 49
    • 17844398259 scopus 로고    scopus 로고
    • Reactive oxygen species mediate the neuroprotection conferred by a mitochondrial ATP-sensitive potassium channel opener during ischemia in the rat hippocampal slice
    • Liang, H.W.; Xia, Q.; Bruce, I.C. Reactive oxygen species mediate the neuroprotection conferred by a mitochondrial ATP-sensitive potassium channel opener during ischemia in the rat hippocampal slice. Brain Res., 2005, 1042(2), 169-175.
    • (2005) Brain Res. , vol.1042 , Issue.2 , pp. 169-175
    • Liang, H.W.1    Xia, Q.2    Bruce, I.C.3
  • 50
    • 80255132664 scopus 로고    scopus 로고
    • Involvement of neuronal nitric oxide synthase in ongoing fetal brain injury following near-term rabbit hypoxia-ischemia
    • Rao, S.; Lin, Z.; Drobyshevsky, A.; Chen, L.; Ji, X.; Ji, H.; Yang, Y.; Yu, L.; Derrick, M.; Silverman, R.B.; Tan, S. Involvement of neuronal nitric oxide synthase in ongoing fetal brain injury following near-term rabbit hypoxia-ischemia. Dev. Neurosci., 2011, 33(3-4), 288-298.
    • (2011) Dev. Neurosci. , vol.33 , Issue.3-4 , pp. 288-298
    • Rao, S.1    Lin, Z.2    Drobyshevsky, A.3    Chen, L.4    Ji, X.5    Ji, H.6    Yang, Y.7    Yu, L.8    Derrick, M.9    Silverman, R.B.10    Tan, S.11
  • 52
    • 23644455005 scopus 로고    scopus 로고
    • Surveillance of antimicrobial resistance of bacteria isolated from bloodstream infections: Data of the French National Observatory for Epidemiology of Bacterial Resistance to Antibiotics (ONERBA), 1998-2003
    • Bertrand, X.; Costa, Y.; Pina, P. Surveillance of antimicrobial resistance of bacteria isolated from bloodstream infections: data of the French National Observatory for Epidemiology of Bacterial Resistance to Antibiotics (ONERBA), 1998-2003. Med. Mal. Infect., 2005, 35(6), 329-334.
    • (2005) Med. Mal. Infect. , vol.35 , Issue.6 , pp. 329-334
    • Bertrand, X.1    Costa, Y.2    Pina, P.3
  • 53
    • 0029998238 scopus 로고    scopus 로고
    • Differential inhibitory action of nitric oxide and peroxynitrite on mitochondrial electron transport
    • Cassina, A.; Radi, R. Differential inhibitory action of nitric oxide and peroxynitrite on mitochondrial electron transport. Arch. Biochem. Biophys., 1996, 328(2), 309-316.
    • (1996) Arch. Biochem. Biophys. , vol.328 , Issue.2 , pp. 309-316
    • Cassina, A.1    Radi, R.2
  • 54
    • 34047142614 scopus 로고    scopus 로고
    • Cardioprotection and mitochondrial S-nitrosation: Effects of S-nitroso-2-mercaptopropionyl glycine (SNO-MPG) in cardiac ischemiareperfusion injury
    • Nadtochiy, S.M.; Burwell, L.S.; Brookes, P.S. Cardioprotection and mitochondrial S-nitrosation: effects of S-nitroso-2-mercaptopropionyl glycine (SNO-MPG) in cardiac ischemiareperfusion injury. J. Mol. Cell. Cardiol., 2007, 42(4), 812-825.
    • (2007) J. Mol. Cell. Cardiol. , vol.42 , Issue.4 , pp. 812-825
    • Nadtochiy, S.M.1    Burwell, L.S.2    Brookes, P.S.3
  • 56
    • 2442664117 scopus 로고    scopus 로고
    • Endogenous NO regulates superoxide production at low oxygen concentrations by modifying the redox state of cytochrome c oxidase
    • Palacios-Callender, M.; Quintero, M.; Hollis, V.S.; Springett, R.J.; Moncada, S. Endogenous NO regulates superoxide production at low oxygen concentrations by modifying the redox state of cytochrome c oxidase. Proc. Natl. Acad. Sci. U. S. A., 2004, 101(20), 7630-7635.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , Issue.20 , pp. 7630-7635
    • Palacios-Callender, M.1    Quintero, M.2    Hollis, V.S.3    Springett, R.J.4    Moncada, S.5
  • 57
    • 15444372431 scopus 로고    scopus 로고
    • Nitric oxideinduced persistent inhibition and nitrosylation of active site cysteine residues of mitochondrial cytochrome-c oxidase in lung endothelial cells
    • Zhang, J.; Jin, B.; Li, L.; Block, E.R.; Patel, J.M. Nitric oxideinduced persistent inhibition and nitrosylation of active site cysteine residues of mitochondrial cytochrome-c oxidase in lung endothelial cells. Am. J. Physiol. Cell. Physiol., 2005, 288(4), C840-849.
    • (2005) Am. J. Physiol. Cell. Physiol. , vol.288 , Issue.4
    • Zhang, J.1    Jin, B.2    Li, L.3    Block, E.R.4    Patel, J.M.5
  • 58
    • 64249133725 scopus 로고    scopus 로고
    • S-nitrosylation of Drp1 mediates beta-amyloid-related mitochondrial fission and neuronal injury
    • Cho, D.H.; Nakamura, T.; Fang, J.; Cieplak, P.; Godzik, A.; Gu, Z.; Lipton, S.A. S-nitrosylation of Drp1 mediates beta-amyloid-related mitochondrial fission and neuronal injury. Science, 2009, 324(5923), 102-105.
    • (2009) Science , vol.324 , Issue.5923 , pp. 102-105
    • Cho, D.H.1    Nakamura, T.2    Fang, J.3    Cieplak, P.4    Godzik, A.5    Gu, Z.6    Lipton, S.A.7
  • 59
    • 34247186472 scopus 로고    scopus 로고
    • Reactive oxygen species are essential for autophagy and specifically regulate the activity of Atg4
    • Scherz-Shouval, R.; Shvets, E.; Fass, E.; Shorer, H.; Gil, L.; Elazar, Z. Reactive oxygen species are essential for autophagy and specifically regulate the activity of Atg4. EMBO. J., 2007, 26(7), 1749-1760.
    • (2007) EMBO.J. , vol.26 , Issue.7 , pp. 1749-1760
    • Scherz-Shouval, R.1    Shvets, E.2    Fass, E.3    Shorer, H.4    Gil, L.5    Elazar, Z.6
  • 60
    • 0031045544 scopus 로고    scopus 로고
    • Pathways of peroxynitrite oxidation of thiol groups
    • Quijano, C.; Alvarez, B.; Gatti, R.M.; Augusto, O.; Radi, R. Pathways of peroxynitrite oxidation of thiol groups. Biochem. J., 1997, 322 (Pt 1), 167-173.
    • (1997) Biochem. J. , vol.322 , Issue.PART 1 , pp. 167-173
    • Quijano, C.1    Alvarez, B.2    Gatti, R.M.3    Augusto, O.4    Radi, R.5
  • 61
    • 0028275459 scopus 로고
    • Inhibition of mitochondrial electron transport by peroxynitrite
    • Radi, R.; Rodriguez, M.; Castro, L.; Telleri, R. Inhibition of mitochondrial electron transport by peroxynitrite. Arch. Biochem. Biophys., 1994, 308(1), 89-95.
    • (1994) Arch. Biochem. Biophys. , vol.308 , Issue.1 , pp. 89-95
    • Radi, R.1    Rodriguez, M.2    Castro, L.3    Telleri, R.4
  • 62
    • 79951951928 scopus 로고    scopus 로고
    • Exploring the molecular basis of human manganese superoxide dismutase inactivation mediated by tyrosine 34 nitration
    • Moreno, D.M.; Marti, M.A.; De Biase, P.M.; Estrin, D.A.; Demicheli, V.; Radi, R.; Boechi, L. Exploring the molecular basis of human manganese superoxide dismutase inactivation mediated by tyrosine 34 nitration. Arch. Biochem. Biophys., 2011, 507(2), 304-309.
    • (2011) Arch. Biochem. Biophys. , vol.507 , Issue.2 , pp. 304-309
    • Moreno, D.M.1    Marti, M.A.2    De Biase, P.M.3    Estrin, D.A.4    Demicheli, V.5    Radi, R.6    Boechi, L.7
  • 63
    • 0033150608 scopus 로고    scopus 로고
    • Tyrosine modifications and inactivation of active site manganese superoxide dismutase mutant (Y34F) by peroxynitrite
    • MacMillan-Crow, L.A.; Thompson, J.A. Tyrosine modifications and inactivation of active site manganese superoxide dismutase mutant (Y34F) by peroxynitrite. Arch. Biochem. Biophys., 1999, 366(1), 82-88.
    • (1999) Arch. Biochem. Biophys. , vol.366 , Issue.1 , pp. 82-88
    • McMillan-Crow, L.A.1    Thompson, J.A.2
  • 64
    • 0038305949 scopus 로고    scopus 로고
    • Specific nitration at tyrosine 430 revealed by high resolution mass spectrometry as basis for redox regulation of bovine prostacyclin synthase
    • Schmidt, P.; Youhnovski, N.; Daiber, A.; Balan, A.; Arsic, M.; Bachschmid, M.; Przybylski, M.; Ullrich, V. Specific nitration at tyrosine 430 revealed by high resolution mass spectrometry as basis for redox regulation of bovine prostacyclin synthase. J. Biol. Chem., 2003, 278(15), 12813-12819.
    • (2003) J. Biol. Chem. , vol.278 , Issue.15 , pp. 12813-12819
    • Schmidt, P.1    Youhnovski, N.2    Daiber, A.3    Balan, A.4    Arsic, M.5    Bachschmid, M.6    Przybylski, M.7    Ullrich, V.8
  • 65
    • 0037646955 scopus 로고    scopus 로고
    • Endothelial cell activation by endotoxin involves superoxide/NO-mediated nitration of prostacyclin synthase and thromboxane receptor stimulation
    • Bachschmid, M.; Thurau, S.; Zou, M.H.; Ullrich, V. Endothelial cell activation by endotoxin involves superoxide/NO-mediated nitration of prostacyclin synthase and thromboxane receptor stimulation. FASEB. J., 2003, 17(8), 914-916.
    • (2003) FASEB.J. , vol.17 , Issue.8 , pp. 914-916
    • Bachschmid, M.1    Thurau, S.2    Zou, M.H.3    Ullrich, V.4
  • 67
    • 0942290539 scopus 로고    scopus 로고
    • Peroxynitritemediated protein nitration and lipid peroxidation in a mouse model of traumatic brain injury
    • Hall, E.D.; Detloff, M.R.; Johnson, K.; Kupina, N.C. Peroxynitritemediated protein nitration and lipid peroxidation in a mouse model of traumatic brain injury. J. Neurotrauma, 2004, 21(1), 9-20.
    • (2004) J. Neurotrauma , vol.21 , Issue.1 , pp. 9-20
    • Hall, E.D.1    Detloff, M.R.2    Johnson, K.3    Kupina, N.C.4
  • 68
    • 0033103663 scopus 로고    scopus 로고
    • Contrasting roles for nitric oxide and peroxynitrite in the peroxidation of myelin lipids
    • van der Veen, R.C.; Roberts, L.J. Contrasting roles for nitric oxide and peroxynitrite in the peroxidation of myelin lipids. J. Neuroimmunol., 1999, 95(1-2), 1-7.
    • (1999) J. Neuroimmunol. , vol.95 , Issue.1-2 , pp. 1-7
    • van der Veen, R.C.1    Roberts, L.J.2
  • 69
    • 0142139286 scopus 로고    scopus 로고
    • Inhibition of peroxynitrite-mediated LDL oxidation by prenylated flavonoids: The alpha, beta-unsaturated keto functionality of 2'-hydroxychalcones as a novel antioxidant pharmacophore
    • Stevens, J.F.; Miranda, C.L.; Frei, B.; Buhler, D.R. Inhibition of peroxynitrite-mediated LDL oxidation by prenylated flavonoids: the alpha, beta-unsaturated keto functionality of 2'-hydroxychalcones as a novel antioxidant pharmacophore. Chem. Res. Toxicol., 2003, 16(10), 1277-1286.
    • (2003) Chem. Res. Toxicol. , vol.16 , Issue.10 , pp. 1277-1286
    • Stevens, J.F.1    Miranda, C.L.2    Frei, B.3    Buhler, D.R.4
  • 70
    • 0034938095 scopus 로고    scopus 로고
    • Peroxynitrite production, DNA breakage, and poly(ADP-ribose) polymerase activation in a mouse model of oxazolone-induced contact hypersensitivity
    • Szabo, E.; Virag, L.; Bakondi, E.; Gyure, L.; Hasko, G.; Bai, P.; Hunyadi, J.; Gergely, P.; Szabo, C. Peroxynitrite production, DNA breakage, and poly(ADP-ribose) polymerase activation in a mouse model of oxazolone-induced contact hypersensitivity. J. Invest. Dermatol., 2001, 117(1), 74-80.
    • (2001) J. Invest. Dermatol. , vol.117 , Issue.1 , pp. 74-80
    • Szabo, E.1    Virag, L.2    Bakondi, E.3    Gyure, L.4    Hasko, G.5    Bai, P.6    Hunyadi, J.7    Gergely, P.8    Szabo, C.9
  • 71
    • 79960844404 scopus 로고    scopus 로고
    • Myricetin affords protection against peroxynitrite-mediated DNA damage and hydroxyl radical formation
    • Chen, W.; Li, Y.; Li, J.; Han, Q.; Ye, L.; Li, A. Myricetin affords protection against peroxynitrite-mediated DNA damage and hydroxyl radical formation. Food. Chem. Toxicol., 2011, 49(9), 2439-2444.
    • (2011) Food. Chem. Toxicol. , vol.49 , Issue.9 , pp. 2439-2444
    • Chen, W.1    Li, Y.2    Li, J.3    Han, Q.4    Ye, L.5    Li, A.6
  • 72
    • 67349163258 scopus 로고    scopus 로고
    • Protein nitration, PARP activation and NAD+ depletion may play a critical role in the pathogenesis of cyclophosphamide-induced hemorrhagic cystitis in the rat
    • Abraham, P.; Rabi, S. Protein nitration, PARP activation and NAD+ depletion may play a critical role in the pathogenesis of cyclophosphamide-induced hemorrhagic cystitis in the rat. Cancer Chemother. Pharmacol., 2009, 64(2), 279-285.
    • (2009) Cancer Chemother. Pharmacol. , vol.64 , Issue.2 , pp. 279-285
    • Abraham, P.1    Rabi, S.2
  • 73
    • 0035896264 scopus 로고    scopus 로고
    • Contribution of peroxynitrite to the beneficial effects of preconditioning on ischaemia-induced arrhythmias in rat isolated hearts
    • Altup, S.; Demiryurek, A.T.; Ak, D.; Tungel, M.; Kanzik, I. Contribution of peroxynitrite to the beneficial effects of preconditioning on ischaemia-induced arrhythmias in rat isolated hearts. Eur. J. Pharmacol., 2001, 415(2-3), 239-246.
    • (2001) Eur. J. Pharmacol. , vol.415 , Issue.2-3 , pp. 239-246
    • Altup, S.1    Demiryurek, A.T.2    Ak, D.3    Tungel, M.4    Kanzik, I.5
  • 74
    • 0034801582 scopus 로고    scopus 로고
    • Preconditioning decreases ischemia/reperfusion-induced peroxynitrite formation
    • Csonka, C.; Csont, T.; Onody, A.; Ferdinandy, P. Preconditioning decreases ischemia/reperfusion-induced peroxynitrite formation. Biochem. Biophys. Res. Commun., 2001, 285(5), 1217-1219.
    • (2001) Biochem. Biophys. Res. Commun. , vol.285 , Issue.5 , pp. 1217-1219
    • Csonka, C.1    Csont, T.2    Onody, A.3    Ferdinandy, P.4
  • 77
    • 84864707133 scopus 로고    scopus 로고
    • The contribution of thioredoxin-2 reductase and glutathione peroxidase to H(2)O(2) detoxification of rat brain mitochondria
    • [Epub ahead of print]
    • Kudin, A.P.; Augustynek, B.; Lehmann, A.K.; Kovacs, R.; Kunz, W.S. The contribution of thioredoxin-2 reductase and glutathione peroxidase to H(2)O(2) detoxification of rat brain mitochondria. Biochim. Biophys. Acta., 2012. [Epub ahead of print].
    • (2012) Biochim. Biophys. Acta.
    • Kudin, A.P.1    Augustynek, B.2    Lehmann, A.K.3    Kovacs, R.4    Kunz, W.S.5
  • 78
    • 84863115387 scopus 로고    scopus 로고
    • Catalase deficiency accelerates diabetic renal injury through peroxisomal dysfunction
    • Hwang, I.; Lee, J.; Huh, J.Y.; Park, J.; Lee, H.B.; Ho, Y.S.; Ha, H. Catalase deficiency accelerates diabetic renal injury through peroxisomal dysfunction. Diabetes, 2012, 61(3), 728-738.
    • (2012) Diabetes , vol.61 , Issue.3 , pp. 728-738
    • Hwang, I.1    Lee, J.2    Huh, J.Y.3    Park, J.4    Lee, H.B.5    Ho, Y.S.6    Ha, H.7
  • 79
    • 35348835948 scopus 로고    scopus 로고
    • The highly expressed and inducible endogenous NAD(P)H:Quinone oxidoreductase 1 in cardiovascular cells acts as a potential superoxide scavenger
    • Zhu, H.; Jia, Z.; Mahaney, J.E.; Ross, D.; Misra, H.P.; Trush, M.A.; Li, Y. The highly expressed and inducible endogenous NAD(P)H:quinone oxidoreductase 1 in cardiovascular cells acts as a potential superoxide scavenger. Cardiovasc. Toxicol., 2007, 7(3), 202-211.
    • (2007) Cardiovasc. Toxicol. , vol.7 , Issue.3 , pp. 202-211
    • Zhu, H.1    Jia, Z.2    Mahaney, J.E.3    Ross, D.4    Misra, H.P.5    Trush, M.A.6    Li, Y.7
  • 80
    • 0030739681 scopus 로고    scopus 로고
    • The reduction of alpha-tocopherolquinone by human NAD(P)H: Quinone oxidoreductase: The role of alpha-tocopherolhydroquinone as a cellular antioxidant
    • Siegel, D.; Bolton, E.M.; Burr, J.A.; Liebler, D.C.; Ross, D. The reduction of alpha-tocopherolquinone by human NAD(P)H: quinone oxidoreductase: the role of alpha-tocopherolhydroquinone as a cellular antioxidant. Mol. Pharmacol., 1997, 52(2), 300-305.
    • (1997) Mol. Pharmacol. , vol.52 , Issue.2 , pp. 300-305
    • Siegel, D.1    Bolton, E.M.2    Burr, J.A.3    Liebler, D.C.4    Ross, D.5
  • 82
    • 0031594295 scopus 로고    scopus 로고
    • Coenzyme Q10 attenuates the 1-methyl-4-phenyl-1,2,3, tetrahydropyridine (MPTP) induced loss of striatal dopamine and dopaminergic axons in aged mice
    • Beal, M.F.; Matthews, R.T.; Tieleman, A.; Shults, C.W. Coenzyme Q10 attenuates the 1-methyl-4-phenyl-1,2,3, tetrahydropyridine (MPTP) induced loss of striatal dopamine and dopaminergic axons in aged mice. Brain Res., 1998, 783(1), 109-114.
    • (1998) Brain Res. , vol.783 , Issue.1 , pp. 109-114
    • Beal, M.F.1    Matthews, R.T.2    Tieleman, A.3    Shults, C.W.4
  • 83
    • 84860470497 scopus 로고    scopus 로고
    • Living with stress: Regulation of antioxidant defense genes in the subterranean, hypoxia-tolerant mole rat, Spalax
    • Schulke, S.; Dreidax, D.; Malik, A.; Burmester, T.; Nevo, E.; Band, M.; Avivi, A.; Hankeln, T. Living with stress: Regulation of antioxidant defense genes in the subterranean, hypoxia-tolerant mole rat, Spalax. Gene, 2012, 500(2), 199-206.
    • (2012) Gene , vol.500 , Issue.2 , pp. 199-206
    • Schulke, S.1    Dreidax, D.2    Malik, A.3    Burmester, T.4    Nevo, E.5    Band, M.6    Avivi, A.7    Hankeln, T.8
  • 84
    • 84861204399 scopus 로고    scopus 로고
    • Antioxidant-induced INrf2 (Keap1) tyrosine 85 phosphorylation controls the nuclear export and degradation of the INrf2-Cul3-Rbx1 complex to allow normal Nrf2 activation and repression
    • Kaspar, J.W.; Niture, S.K.; Jaiswal, A.K. Antioxidant-induced INrf2 (Keap1) tyrosine 85 phosphorylation controls the nuclear export and degradation of the INrf2-Cul3-Rbx1 complex to allow normal Nrf2 activation and repression. J. Cell. Sci., 2012, 125(Pt 4), 1027-1038.
    • (2012) J. Cell. Sci. , vol.125 , Issue.PART 4 , pp. 1027-1038
    • Kaspar, J.W.1    Niture, S.K.2    Jaiswal, A.K.3
  • 85
    • 0031589557 scopus 로고    scopus 로고
    • The possible role of hydrogen sulfide as an endogenous smooth muscle relaxant in synergy with nitric oxide
    • Hosoki, R.; Matsuki, N.; Kimura, H. The possible role of hydrogen sulfide as an endogenous smooth muscle relaxant in synergy with nitric oxide. Biochem. Biophys. Res. Commun., 1997, 237(3), 527-531.
    • (1997) Biochem. Biophys. Res. Commun. , vol.237 , Issue.3 , pp. 527-531
    • Hosoki, R.1    Matsuki, N.2    Kimura, H.3
  • 86
    • 0029876402 scopus 로고    scopus 로고
    • The possible role of hydrogen sulfide as an endogenous neuromodulator
    • Abe, K.; Kimura, H. The possible role of hydrogen sulfide as an endogenous neuromodulator. J. Neurosci., 1996, 16(3), 1066-1071.
    • (1996) J. Neurosci. , vol.16 , Issue.3 , pp. 1066-1071
    • Abe, K.1    Kimura, H.2
  • 87
    • 69249100078 scopus 로고    scopus 로고
    • Relative contributions of cystathionine beta-synthase and gammacystathionase to H2S biogenesis via alternative trans-sulfuration reactions
    • Singh, S.; Padovani, D.; Leslie, R.A.; Chiku, T.; Banerjee, R. Relative contributions of cystathionine beta-synthase and gammacystathionase to H2S biogenesis via alternative trans-sulfuration reactions. J. Biol. Chem., 2009, 284(33), 22457-22466.
    • (2009) J. Biol. Chem. , vol.284 , Issue.33 , pp. 22457-22466
    • Singh, S.1    Padovani, D.2    Leslie, R.A.3    Chiku, T.4    Banerjee, R.5
  • 88
    • 27744461725 scopus 로고    scopus 로고
    • Cystathionine beta-synthase, a key enzyme for homocysteine metabolism, is preferentially expressed in the radial glia/astrocyte lineage of developing mouse CNS
    • Enokido, Y.; Suzuki, E.; Iwasawa, K.; Namekata, K.; Okazawa, H.; Kimura, H. Cystathionine beta-synthase, a key enzyme for homocysteine metabolism, is preferentially expressed in the radial glia/astrocyte lineage of developing mouse CNS. FASEB J., 2005, 19(13), 1854-1856.
    • (2005) FASEB J. , vol.19 , Issue.13 , pp. 1854-1856
    • Enokido, Y.1    Suzuki, E.2    Iwasawa, K.3    Namekata, K.4    Okazawa, H.5    Kimura, H.6
  • 89
    • 0037369968 scopus 로고    scopus 로고
    • Expression of the cystathionine beta synthase (CBS) gene during mouse development and immunolocalization in adult brain
    • Robert, K.; Vialard, F.; Thiery, E.; Toyama, K.; Sinet, P.M.; Janel, N.; London, J. Expression of the cystathionine beta synthase (CBS) gene during mouse development and immunolocalization in adult brain. J. Histochem. Cytochem., 2003, 51(3), 363-371.
    • (2003) J. Histochem. Cytochem. , vol.51 , Issue.3 , pp. 363-371
    • Robert, K.1    Vialard, F.2    Thiery, E.3    Toyama, K.4    Sinet, P.M.5    Janel, N.6    London, J.7
  • 90
    • 33646680757 scopus 로고    scopus 로고
    • Hydrogen sulfide protects HT22 neuronal cells from oxidative stress
    • Kimura, Y.; Dargusch, R.; Schubert, D.; Kimura, H. Hydrogen sulfide protects HT22 neuronal cells from oxidative stress. Antioxid. Redox. Signal., 2006, 8(3-4), 661-670.
    • (2006) Antioxid. Redox. Signal. , vol.8 , Issue.3-4 , pp. 661-670
    • Kimura, Y.1    Dargusch, R.2    Schubert, D.3    Kimura, H.4
  • 91
    • 9444263079 scopus 로고    scopus 로고
    • Hydrogen sulfide protects neurons from oxidative stress
    • Kimura, Y.; Kimura, H. Hydrogen sulfide protects neurons from oxidative stress. FASEB. J., 2004, 18(10), 1165-1167.
    • (2004) FASEB.J. , vol.18 , Issue.10 , pp. 1165-1167
    • Kimura, Y.1    Kimura, H.2
  • 94
    • 0014670945 scopus 로고
    • Microsomal heme oxygenase. Characterization of the enzyme
    • Tenhunen, R.; Marver, H.S.; Schmid, R. Microsomal heme oxygenase. Characterization of the enzyme. J. Biol. Chem., 1969, 244(23), 6388-6394.
    • (1969) J. Biol. Chem. , vol.244 , Issue.23 , pp. 6388-6394
    • Tenhunen, R.1    Marver, H.S.2    Schmid, R.3
  • 95
    • 28844432578 scopus 로고    scopus 로고
    • The heme oxygenase system: Update 2005
    • Maines, M.D. The heme oxygenase system: update 2005. Antioxid. Redox. Signal., 2005, 7(11-12), 1761-1766.
    • (2005) Antioxid. Redox. Signal. , vol.7 , Issue.11-12 , pp. 1761-1766
    • Maines, M.D.1
  • 96
    • 19544370917 scopus 로고    scopus 로고
    • Heme oxygenase and the cardiovascular-renal system
    • Abraham, N.G.; Kappas, A. Heme oxygenase and the cardiovascular-renal system. Free Radic. Biol. Med., 2005, 39(1), 1-25.
    • (2005) Free Radic. Biol. Med. , vol.39 , Issue.1 , pp. 1-25
    • Abraham, N.G.1    Kappas, A.2
  • 97
    • 12544253089 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress stimulates heme oxygenase-1 gene expression in vascular smooth muscle role in cell survival
    • Liu, X.M.; Peyton, K.J.; Ensenat, D.; Wang, H.; Schafer, A.I.; Alam, J.; Durante, W. Endoplasmic reticulum stress stimulates heme oxygenase-1 gene expression in vascular smooth muscle role in cell survival. J. Biol. Chem., 2005, 280(2), 872-877.
    • (2005) J. Biol. Chem. , vol.280 , Issue.2 , pp. 872-877
    • Liu, X.M.1    Peyton, K.J.2    Ensenat, D.3    Wang, H.4    Schafer, A.I.5    Alam, J.6    Durante, W.7
  • 98
  • 99
    • 80052420822 scopus 로고    scopus 로고
    • Carbon monoxideactivated Nrf2 pathway leads to protection against permanent focal cerebral ischemia
    • Wang, B.; Cao, W.; Biswal, S.; Dore, S. Carbon monoxideactivated Nrf2 pathway leads to protection against permanent focal cerebral ischemia. Stroke., 2011, 42(9), 2605-2610.
    • (2011) Stroke. , vol.42 , Issue.9 , pp. 2605-2610
    • Wang, B.1    Cao, W.2    Biswal, S.3    Dore, S.4
  • 100
    • 33846993042 scopus 로고    scopus 로고
    • A new activating role for CO in cardiac mitochondrial biogenesis
    • Suliman, H.B.; Carraway, M.S.; Tatro, L.G.; Piantadosi, C.A. A new activating role for CO in cardiac mitochondrial biogenesis. J. Cell Sci., 2007, 120(Pt 2), 299-308.
    • (2007) J. Cell Sci. , vol.120 , Issue.PART 2 , pp. 299-308
    • Suliman, H.B.1    Carraway, M.S.2    Tatro, L.G.3    Piantadosi, C.A.4
  • 101
    • 33947628672 scopus 로고    scopus 로고
    • Carbon monoxide signals via inhibition of cytochrome c oxidase and generation of mitochondrial reactive oxygen species
    • Zuckerbraun, B.S.; Chin, B.Y.; Bilban, M.; d'Avila, J.C.; Rao, J.; Billiar, T.R.; Otterbein, L.E. Carbon monoxide signals via inhibition of cytochrome c oxidase and generation of mitochondrial reactive oxygen species. FASEB J., 2007, 21(4), 1099-1106.
    • (2007) FASEB J. , vol.21 , Issue.4 , pp. 1099-1106
    • Zuckerbraun, B.S.1    Chin, B.Y.2    Bilban, M.3    d'Avila, J.C.4    Rao, J.5    Billiar, T.R.6    Otterbein, L.E.7
  • 102
    • 0023262745 scopus 로고
    • Differences in brain cytochrome responses to carbon monoxide and cyanide in vivo
    • Piantadosi, C.A.; Sylvia, A.L.; Jobsis-Vandervliet, F.F. Differences in brain cytochrome responses to carbon monoxide and cyanide in vivo. J. Appl. Physiol., 1987, 62(3), 1277-1284.
    • (1987) J. Appl. Physiol. , vol.62 , Issue.3 , pp. 1277-1284
    • Piantadosi, C.A.1    Sylvia, A.L.2    Jobsis-Vandervliet, F.F.3
  • 103
    • 2642545057 scopus 로고    scopus 로고
    • Epsilon protein kinase C mediated ischemic tolerance requires activation of the extracellular regulated kinase pathway in the organotypic hippocampal slice
    • Lange-Asschenfeldt, C.; Raval, A.P.; Dave, K.R.; Mochly-Rosen, D.; Sick, T.J.; Perez-Pinzon, M.A. Epsilon protein kinase C mediated ischemic tolerance requires activation of the extracellular regulated kinase pathway in the organotypic hippocampal slice. J. Cereb. Blood. Flow. Metab., 2004, 24(6), 636-645.
    • (2004) J. Cereb. Blood. Flow. Metab. , vol.24 , Issue.6 , pp. 636-645
    • Lange-Asschenfeldt, C.1    Raval, A.P.2    Dave, K.R.3    Mochly-Rosen, D.4    Sick, T.J.5    Perez-Pinzon, M.A.6
  • 104
    • 0037437356 scopus 로고    scopus 로고
    • Epsilon PKC is required for the induction of tolerance by ischemic and NMDA-mediated preconditioning in the organotypic hippocampal slice
    • Raval, A.P.; Dave, K.R.; Mochly-Rosen, D.; Sick, T.J.; Perez-Pinzon, M.A. Epsilon PKC is required for the induction of tolerance by ischemic and NMDA-mediated preconditioning in the organotypic hippocampal slice. J. Neurosci., 2003, 23(2), 384-391.
    • (2003) J. Neurosci. , vol.23 , Issue.2 , pp. 384-391
    • Raval, A.P.1    Dave, K.R.2    Mochly-Rosen, D.3    Sick, T.J.4    Perez-Pinzon, M.A.5
  • 105
    • 34548033950 scopus 로고    scopus 로고
    • Ischemic preconditioning targets the reperfusion phase
    • Hausenloy, D.J.; Wynne, A.M.; Yellon, D.M. Ischemic preconditioning targets the reperfusion phase. Basic Res. Cardiol., 2007, 102(5), 445-452.
    • (2007) Basic Res. Cardiol. , vol.102 , Issue.5 , pp. 445-452
    • Hausenloy, D.J.1    Wynne, A.M.2    Yellon, D.M.3
  • 106
    • 37549058041 scopus 로고    scopus 로고
    • Redox signaling at reperfusion is required for protection from ischemic preconditioning but not from a direct PKC activator
    • Liu, Y.; Yang, X.M.; Iliodromitis, E.K.; Kremastinos, D.T.; Dost, T.; Cohen, M.V.; Downey, J.M. Redox signaling at reperfusion is required for protection from ischemic preconditioning but not from a direct PKC activator. Basic Res. Cardiol., 2008, 103(1), 54-59.
    • (2008) Basic Res. Cardiol. , vol.103 , Issue.1 , pp. 54-59
    • Liu, Y.1    Yang, X.M.2    Iliodromitis, E.K.3    Kremastinos, D.T.4    Dost, T.5    Cohen, M.V.6    Downey, J.M.7
  • 107
    • 0024724936 scopus 로고
    • Ca2+-and phospholipidindependent activation of protein kinase C by selective oxidative modification of the regulatory domain
    • Gopalakrishna, R.; Anderson, W.B. Ca2+-and phospholipidindependent activation of protein kinase C by selective oxidative modification of the regulatory domain. Proc. Natl. Acad. Sci. U. S. A., 1989, 86(17), 6758-6762.
    • (1989) Proc. Natl. Acad. Sci. U.S.A. , vol.86 , Issue.17 , pp. 6758-6762
    • Gopalakrishna, R.1    Anderson, W.B.2
  • 108
    • 0025779841 scopus 로고
    • Reversible oxidative activation and inactivation of protein kinase C by the mitogen/tumor promoter periodate
    • Gopalakrishna, R.; Anderson, W.B. Reversible oxidative activation and inactivation of protein kinase C by the mitogen/tumor promoter periodate. Arch. Biochem. Biophys., 1991, 285(2), 382-387.
    • (1991) Arch. Biochem. Biophys. , vol.285 , Issue.2 , pp. 382-387
    • Gopalakrishna, R.1    Anderson, W.B.2
  • 109
    • 0034190297 scopus 로고    scopus 로고
    • Protein kinase C signaling and oxidative stress
    • Gopalakrishna, R.; Jaken, S. Protein kinase C signaling and oxidative stress. Free Radic. Biol. Med., 2000, 28(9), 1349-1361.
    • (2000) Free Radic. Biol. Med. , vol.28 , Issue.9 , pp. 1349-1361
    • Gopalakrishna, R.1    Jaken, S.2
  • 110
    • 0001515988 scopus 로고    scopus 로고
    • Involvement of tyrosine phosphorylation and protein kinase C in the activation of phospholipase D by H2O2 in Swiss 3T3 fibroblasts
    • Min, D.S.; Kim, E.G.; Exton, J.H. Involvement of tyrosine phosphorylation and protein kinase C in the activation of phospholipase D by H2O2 in Swiss 3T3 fibroblasts. J. Biol. Chem., 1998, 273(45), 29986-29994.
    • (1998) J. Biol. Chem. , vol.273 , Issue.45 , pp. 29986-29994
    • Min, D.S.1    Kim, E.G.2    Exton, J.H.3
  • 111
    • 0027459024 scopus 로고
    • Activation of endothelial cell phospholipase D by hydrogen peroxide and fatty acid hydroperoxide
    • Natarajan, V.; Taher, M.M.; Roehm, B.; Parinandi, N.L.; Schmid, H.H.; Kiss, Z.; Garcia, J.G. Activation of endothelial cell phospholipase D by hydrogen peroxide and fatty acid hydroperoxide. J. Biol. Chem., 1993, 268(2), 930-937.
    • (1993) J. Biol. Chem. , vol.268 , Issue.2 , pp. 930-937
    • Natarajan, V.1    Taher, M.M.2    Roehm, B.3    Parinandi, N.L.4    Schmid, H.H.5    Kiss, Z.6    Garcia, J.G.7
  • 112
    • 67949102053 scopus 로고    scopus 로고
    • Recent progress in the biology and physiology of sirtuins
    • Finkel, T.; Deng, C.X.; Mostoslavsky, R. Recent progress in the biology and physiology of sirtuins. Nature, 2009, 460(7255), 587-591.
    • (2009) Nature , vol.460 , Issue.7255 , pp. 587-591
    • Finkel, T.1    Deng, C.X.2    Mostoslavsky, R.3
  • 114
    • 62249110887 scopus 로고    scopus 로고
    • Resveratrol pretreatment protects rat brain from cerebral ischemic damage via a sirtuin 1-uncoupling protein 2 pathway
    • Della-Morte, D.; Dave, K.R.; DeFazio, R.A.; Bao, Y.C.; Raval, A.P.; Perez-Pinzon, M.A. Resveratrol pretreatment protects rat brain from cerebral ischemic damage via a sirtuin 1-uncoupling protein 2 pathway. Neuroscience, 2009, 159(3), 993-1002.
    • (2009) Neuroscience , vol.159 , Issue.3 , pp. 993-1002
    • Della-Morte, D.1    Dave, K.R.2    DeFazio, R.A.3    Bao, Y.C.4    Raval, A.P.5    Perez-Pinzon, M.A.6
  • 116
    • 79551470041 scopus 로고    scopus 로고
    • Lysine deacetylation in ischaemic preconditioning: The role of SIRT1
    • Nadtochiy, S.M.; Redman, E.; Rahman, I.; Brookes, P.S. Lysine deacetylation in ischaemic preconditioning: the role of SIRT1. Cardiovasc. Res., 2011, 89(3), 643-649.
    • (2011) Cardiovasc. Res. , vol.89 , Issue.3 , pp. 643-649
    • Nadtochiy, S.M.1    Redman, E.2    Rahman, I.3    Brookes, P.S.4
  • 119
    • 79954609893 scopus 로고    scopus 로고
    • Hypoxia increases sirtuin 1 expression in a hypoxia-inducible factor-dependent manner
    • Chen, R.; Dioum, E.M.; Hogg, R.T.; Gerard, R.D.; Garcia, J.A. Hypoxia increases sirtuin 1 expression in a hypoxia-inducible factor-dependent manner. J. Biol. Chem., 2011, 286(16), 13869-13878.
    • (2011) J. Biol. Chem. , vol.286 , Issue.16 , pp. 13869-13878
    • Chen, R.1    Dioum, E.M.2    Hogg, R.T.3    Gerard, R.D.4    Garcia, J.A.5
  • 120
    • 77956180402 scopus 로고    scopus 로고
    • SIRT1 is a redoxsensitive deacetylase that is post-translationally modified by oxidants and carbonyl stress
    • Caito, S.; Rajendrasozhan, S.; Cook, S.; Chung, S.; Yao, H.; Friedman, A.E.; Brookes, P.S.; Rahman, I. SIRT1 is a redoxsensitive deacetylase that is post-translationally modified by oxidants and carbonyl stress. FASEB J., 2010, 24(9), 3145-3159.
    • (2010) FASEB J. , vol.24 , Issue.9 , pp. 3145-3159
    • Caito, S.1    Rajendrasozhan, S.2    Cook, S.3    Chung, S.4    Yao, H.5    Friedman, A.E.6    Brookes, P.S.7    Rahman, I.8
  • 121
    • 48149096759 scopus 로고    scopus 로고
    • Aneurysm repair in vitro and renal revascularization and renal autogenous transplantation for complex renal artery aneurysm in solitary kidney
    • Zhang, J.; Feng, R.; Feng, X.; Sun, Y.H.; Wang, L.H.; Zhao, Z.Q.; Guo, M.J.; Yang, B.; Li, W.X.; Jing, Z.P. Aneurysm repair in vitro and renal revascularization and renal autogenous transplantation for complex renal artery aneurysm in solitary kidney. Zhonghua Wai Ke Za Zhi, 2007, 45(18), 1253-1256.
    • (2007) Zhonghua Wai Ke Za Zhi , vol.45 , Issue.18 , pp. 1253-1256
    • Zhang, J.1    Feng, R.2    Feng, X.3    Sun, Y.H.4    Wang, L.H.5    Zhao, Z.Q.6    Guo, M.J.7    Yang, B.8    Li, W.X.9    Jing, Z.P.10
  • 124
    • 0035913911 scopus 로고    scopus 로고
    • Negative control of p53 by Sir2alpha promotes cell survival under stress
    • Luo, J.; Nikolaev, A.Y.; Imai, S.; Chen, D.; Su, F.; Shiloh, A.; Guarente, L.; Gu, W. Negative control of p53 by Sir2alpha promotes cell survival under stress. Cell, 2001, 107(2), 137-148.
    • (2001) Cell , vol.107 , Issue.2 , pp. 137-148
    • Luo, J.1    Nikolaev, A.Y.2    Imai, S.3    Chen, D.4    Su, F.5    Shiloh, A.6    Guarente, L.7    Gu, W.8
  • 126
    • 34447626095 scopus 로고    scopus 로고
    • SIRT2 deacetylates FOXO3a in response to oxidative stress and caloric restriction
    • Wang, F.; Nguyen, M.; Qin, F.X.; Tong, Q. SIRT2 deacetylates FOXO3a in response to oxidative stress and caloric restriction. Aging Cell., 2007, 6(4), 505-514.
    • (2007) Aging Cell. , vol.6 , Issue.4 , pp. 505-514
    • Wang, F.1    Nguyen, M.2    Qin, F.X.3    Tong, Q.4
  • 130
    • 84856739946 scopus 로고    scopus 로고
    • Hypoxia-inducible factors in physiology and medicine
    • Semenza, G.L. Hypoxia-inducible factors in physiology and medicine. Cell, 2012, 148(3), 399-408.
    • (2012) Cell , vol.148 , Issue.3 , pp. 399-408
    • Semenza, G.L.1
  • 132
    • 81155137317 scopus 로고    scopus 로고
    • Differential effects of HIF-1 inhibition by YC-1 on the overall outcome and blood-brain barrier damage in a rat model of ischemic stroke
    • Yan, J.; Zhou, B.; Taheri, S.; Shi, H. Differential effects of HIF-1 inhibition by YC-1 on the overall outcome and blood-brain barrier damage in a rat model of ischemic stroke. PLoS One, 2011, 6(11), e27798.
    • (2011) PLoS One , vol.6 , Issue.11
    • Yan, J.1    Zhou, B.2    Taheri, S.3    Shi, H.4
  • 134
    • 0034840276 scopus 로고    scopus 로고
    • Hypoxic preconditioning induces changes in HIF-1 target genes in neonatal rat brain
    • Jones, N.M.; Bergeron, M. Hypoxic preconditioning induces changes in HIF-1 target genes in neonatal rat brain. J. Cereb. Blood Flow. Metab., 2001, 21(9), 1105-1114.
    • (2001) J. Cereb. Blood Flow. Metab. , vol.21 , Issue.9 , pp. 1105-1114
    • Jones, N.M.1    Bergeron, M.2
  • 137
    • 18844408840 scopus 로고    scopus 로고
    • Regulation of the prolyl hydroxylase domain protein 2 (phd2/egln-1) gene: Identification of a functional hypoxia-responsive element
    • Metzen, E.; Stiehl, D.P.; Doege, K.; Marxsen, J.H.; Hellwig-Burgel, T.; Jelkmann, W. Regulation of the prolyl hydroxylase domain protein 2 (phd2/egln-1) gene: identification of a functional hypoxia-responsive element. Biochem. J., 2005, 387(Pt 3), 711-717.
    • (2005) Biochem. J. , vol.387 , Issue.PART 3 , pp. 711-717
    • Metzen, E.1    Stiehl, D.P.2    Doege, K.3    Marxsen, J.H.4    Hellwig-Burgel, T.5    Jelkmann, W.6
  • 141
    • 33947724515 scopus 로고    scopus 로고
    • HIF-1 regulates cytochrome oxidase subunits to optimize efficiency of respiration in hypoxic cells
    • Fukuda, R.; Zhang, H.; Kim, J.W.; Shimoda, L.; Dang, C.V.; Semenza, G.L. HIF-1 regulates cytochrome oxidase subunits to optimize efficiency of respiration in hypoxic cells. Cell., 2007, 129(1), 111-122.
    • (2007) Cell. , vol.129 , Issue.1 , pp. 111-122
    • Fukuda, R.1    Zhang, H.2    Kim, J.W.3    Shimoda, L.4    Dang, C.V.5    Semenza, G.L.6
  • 142
    • 0034682786 scopus 로고    scopus 로고
    • Reactive oxygen species generated at mitochondrial complex III stabilize hypoxia-inducible factor-1alpha during hypoxia: A mechanism of O2 sensing
    • Chandel, N.S.; McClintock, D.S.; Feliciano, C.E.; Wood, T.M.; Melendez, J.A.; Rodriguez, A.M.; Schumacker, P.T. Reactive oxygen species generated at mitochondrial complex III stabilize hypoxia-inducible factor-1alpha during hypoxia: a mechanism of O2 sensing. J. Biol. Chem., 2000, 275(33), 25130-25138.
    • (2000) J. Biol. Chem. , vol.275 , Issue.33 , pp. 25130-25138
    • Chandel, N.S.1    McClintock, D.S.2    Feliciano, C.E.3    Wood, T.M.4    Melendez, J.A.5    Rodriguez, A.M.6    Schumacker, P.T.7
  • 143
    • 84859843476 scopus 로고    scopus 로고
    • Nitric oxide produced by cytochrome c oxidase helps stabilize HIF-1alpha in hypoxic mammalian cells
    • Ball, K.A.; Nelson, A.W.; Foster, D.G.; Poyton, R.O. Nitric oxide produced by cytochrome c oxidase helps stabilize HIF-1alpha in hypoxic mammalian cells. Biochem. Biophys. Res. Commun., 2012, 420(4), 727-732.
    • (2012) Biochem. Biophys. Res. Commun. , vol.420 , Issue.4 , pp. 727-732
    • Ball, K.A.1    Nelson, A.W.2    Foster, D.G.3    Poyton, R.O.4
  • 144
    • 84862801103 scopus 로고    scopus 로고
    • Induction of inducible nitric oxide synthase by isoflurane post-conditioning via hypoxia inducible factor-1alpha during tolerance against ischemic neuronal injury
    • Li, Q.F.; Xu, H.; Sun, Y.; Hu, R.; Jiang, H. Induction of inducible nitric oxide synthase by isoflurane post-conditioning via hypoxia inducible factor-1alpha during tolerance against ischemic neuronal injury. Brain Res., 2012, 1451, 1-9.
    • (2012) Brain Res. , vol.1451 , pp. 1-9
    • Li, Q.F.1    Xu, H.2    Sun, Y.3    Hu, R.4    Jiang, H.5
  • 145
    • 0035864361 scopus 로고    scopus 로고
    • Accumulation of HIF-1alpha under the influence of nitric oxide
    • Sandau, K.B.; Fandrey, J.; Brune, B. Accumulation of HIF-1alpha under the influence of nitric oxide. Blood, 2001, 97(4), 1009-1015.
    • (2001) Blood , vol.97 , Issue.4 , pp. 1009-1015
    • Sandau, K.B.1    Fandrey, J.2    Brune, B.3
  • 146
    • 0033673457 scopus 로고    scopus 로고
    • Normoxic stabilization of hypoxia-inducible factor-1 expression and activity: Redoxdependent effect of nitrogen oxides
    • Palmer, L.A.; Gaston, B.; Johns, R.A. Normoxic stabilization of hypoxia-inducible factor-1 expression and activity: redoxdependent effect of nitrogen oxides. Mol. Pharmacol., 2000, 58(6), 1197-1203.
    • (2000) Mol. Pharmacol. , vol.58 , Issue.6 , pp. 1197-1203
    • Palmer, L.A.1    Gaston, B.2    Johns, R.A.3
  • 147
    • 0033975850 scopus 로고    scopus 로고
    • Hypoxia response element of the human vascular endothelial growth factor gene mediates transcriptional regulation by nitric oxide: Control of hypoxia-inducible factor-1 activity by nitric oxide
    • Kimura, H.; Weisz, A.; Kurashima, Y.; Hashimoto, K.; Ogura, T.; D'Acquisto, F.; Addeo, R.; Makuuchi, M.; Esumi, H. Hypoxia response element of the human vascular endothelial growth factor gene mediates transcriptional regulation by nitric oxide: control of hypoxia-inducible factor-1 activity by nitric oxide. Blood, 2000, 95(1), 189-197.
    • (2000) Blood , vol.95 , Issue.1 , pp. 189-197
    • Kimura, H.1    Weisz, A.2    Kurashima, Y.3    Hashimoto, K.4    Ogura, T.5    D'Acquisto, F.6    Addeo, R.7    Makuuchi, M.8    Esumi, H.9
  • 148
    • 0032511014 scopus 로고    scopus 로고
    • Carbon monoxide and nitric oxide suppress the hypoxic induction of vascular endothelial growth factor gene via the 5' enhancer
    • Liu, Y.; Christou, H.; Morita, T.; Laughner, E.; Semenza, G.L.; Kourembanas, S. Carbon monoxide and nitric oxide suppress the hypoxic induction of vascular endothelial growth factor gene via the 5' enhancer. J. Biol. Chem., 1998, 273(24), 15257-15262.
    • (1998) J. Biol. Chem. , vol.273 , Issue.24 , pp. 15257-15262
    • Liu, Y.1    Christou, H.2    Morita, T.3    Laughner, E.4    Semenza, G.L.5    Kourembanas, S.6
  • 149
    • 0042564792 scopus 로고    scopus 로고
    • S-nitrosation of Cys-800 of HIF-1alpha protein activates its interaction with p300 and stimulates its transcriptional activity
    • Yasinska, I.M.; Sumbayev, V.V. S-nitrosation of Cys-800 of HIF-1alpha protein activates its interaction with p300 and stimulates its transcriptional activity. FEBS Lett., 2003, 549(1-3), 105-109.
    • (2003) FEBS Lett. , vol.549 , Issue.1-3 , pp. 105-109
    • Yasinska, I.M.1    Sumbayev, V.V.2
  • 150
    • 0037472651 scopus 로고    scopus 로고
    • HIF-1 alpha protein as a target for S-nitrosation
    • Sumbayev, V.V.; Budde, A.; Zhou, J.; Brune, B. HIF-1 alpha protein as a target for S-nitrosation. FEBS. Lett., 2003, 535(1-3), 106-112.
    • (2003) FEBS. Lett. , vol.535 , Issue.1-3 , pp. 106-112
    • Sumbayev, V.V.1    Budde, A.2    Zhou, J.3    Brune, B.4
  • 151
    • 0346027211 scopus 로고    scopus 로고
    • Regulation of hypoxia-inducible factor-1alpha by nitric oxide through mitochondria-dependent and-independent pathways
    • Mateo, J.; Garcia-Lecea, M.; Cadenas, S.; Hernandez, C.; Moncada, S. Regulation of hypoxia-inducible factor-1alpha by nitric oxide through mitochondria-dependent and-independent pathways. Biochem. J., 2003, 376(Pt 2), 537-544.
    • (2003) Biochem. J. , vol.376 , Issue.PART 2 , pp. 537-544
    • Mateo, J.1    Garcia-Lecea, M.2    Cadenas, S.3    Hernandez, C.4    Moncada, S.5
  • 152
    • 0348134741 scopus 로고    scopus 로고
    • Redistribution of intracellular oxygen in hypoxia by nitric oxide: Effect on HIF1alpha
    • Hagen, T.; Taylor, C.T.; Lam, F.; Moncada, S. Redistribution of intracellular oxygen in hypoxia by nitric oxide: effect on HIF1alpha. Science, 2003, 302(5652), 1975-1978.
    • (2003) Science , vol.302 , Issue.5652 , pp. 1975-1978
    • Hagen, T.1    Taylor, C.T.2    Lam, F.3    Moncada, S.4
  • 153
    • 79958196739 scopus 로고    scopus 로고
    • Hypoxic-preconditioning induces neuroprotection against hypoxia-ischemia in newborn piglet brain
    • Ara, J.; Fekete, S.; Frank, M.; Golden, J.A.; Pleasure, D.; Valencia, I. Hypoxic-preconditioning induces neuroprotection against hypoxia-ischemia in newborn piglet brain. Neurobiol. Dis., 2011, 43(2), 473-485.
    • (2011) Neurobiol. Dis. , vol.43 , Issue.2 , pp. 473-485
    • Ara, J.1    Fekete, S.2    Frank, M.3    Golden, J.A.4    Pleasure, D.5    Valencia, I.6
  • 154
    • 0033839757 scopus 로고    scopus 로고
    • Role of hypoxia-inducible factor-1 in hypoxiainduced ischemic tolerance in neonatal rat brain
    • Bergeron, M.; Gidday, J.M.; Yu, A.Y.; Semenza, G.L.; Ferriero, D.M.; Sharp, F.R. Role of hypoxia-inducible factor-1 in hypoxiainduced ischemic tolerance in neonatal rat brain. Ann. Neurol., 2000, 48(3), 285-296.
    • (2000) Ann. Neurol. , vol.48 , Issue.3 , pp. 285-296
    • Bergeron, M.1    Gidday, J.M.2    Yu, A.Y.3    Semenza, G.L.4    Ferriero, D.M.5    Sharp, F.R.6
  • 155
    • 0029906134 scopus 로고    scopus 로고
    • Nrf1 and Nrf2 positively and c-Fos and Fra1 negatively regulate the human antioxidant response element-mediated expression of NAD(P)H:Quinone oxidoreductase1 gene
    • Venugopal, R.; Jaiswal, A.K. Nrf1 and Nrf2 positively and c-Fos and Fra1 negatively regulate the human antioxidant response element-mediated expression of NAD(P)H:quinone oxidoreductase1 gene. Proc. Natl. Acad. Sci., U. S. A., 1996, 93(25), 14960-14965.
    • (1996) Proc. Natl. Acad. Sci., U.S.A. , vol.93 , Issue.25 , pp. 14960-14965
    • Venugopal, R.1    Jaiswal, A.K.2
  • 156
    • 0032953192 scopus 로고    scopus 로고
    • Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain
    • Itoh, K.; Wakabayashi, N.; Katoh, Y.; Ishii, T.; Igarashi, K.; Engel, J.D.; Yamamoto, M. Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain. Genes. Dev., 1999, 13(1), 76-86.
    • (1999) Genes. Dev. , vol.13 , Issue.1 , pp. 76-86
    • Itoh, K.1    Wakabayashi, N.2    Katoh, Y.3    Ishii, T.4    Igarashi, K.5    Engel, J.D.6    Yamamoto, M.7
  • 157
    • 0037044791 scopus 로고    scopus 로고
    • Phosphorylation of Nrf2 at Ser-40 by protein kinase C regulates antioxidant response elementmediated transcription
    • Huang, H.C.; Nguyen, T.; Pickett, C.B. Phosphorylation of Nrf2 at Ser-40 by protein kinase C regulates antioxidant response elementmediated transcription. J. Biol. Chem., 2002, 277(45), 42769-42774.
    • (2002) J. Biol. Chem. , vol.277 , Issue.45 , pp. 42769-42774
    • Huang, H.C.1    Nguyen, T.2    Pickett, C.B.3
  • 158
    • 79953225194 scopus 로고    scopus 로고
    • Acetylation-deacetylation of the transcription factor Nrf2 (nuclear factor erythroid 2-related factor 2) regulates its transcriptional activity and nucleocytoplasmic localization
    • Kawai, Y.; Garduno, L.; Theodore, M.; Yang, J.; Arinze, I.J. Acetylation-deacetylation of the transcription factor Nrf2 (nuclear factor erythroid 2-related factor 2) regulates its transcriptional activity and nucleocytoplasmic localization. J. Biol. Chem., 2011, 286(9), 7629-7640.
    • (2011) J. Biol. Chem. , vol.286 , Issue.9 , pp. 7629-7640
    • Kawai, Y.1    Garduno, L.2    Theodore, M.3    Yang, J.4    Arinze, I.J.5
  • 159
    • 0035836698 scopus 로고    scopus 로고
    • An important function of Nrf2 in combating oxidative stress: Detoxification of acetaminophen
    • Chan, K.; Han, X.D.; Kan, Y.W. An important function of Nrf2 in combating oxidative stress: detoxification of acetaminophen. Proc. Natl. Acad. Sci. U. S. A., 2001, 98(8), 4611-4616.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , Issue.8 , pp. 4611-4616
    • Chan, K.1    Han, X.D.2    Kan, Y.W.3
  • 160
    • 37549050907 scopus 로고    scopus 로고
    • Heme oxygenase-1 induction by NRF2 requires inactivation of the transcriptional repressor BACH1
    • Reichard, J.F.; Motz, G.T.; Puga, A. Heme oxygenase-1 induction by NRF2 requires inactivation of the transcriptional repressor BACH1. Nucleic. Acids. Res., 2007, 35(21), 7074-7086.
    • (2007) Nucleic. Acids. Res. , vol.35 , Issue.21 , pp. 7074-7086
    • Reichard, J.F.1    Motz, G.T.2    Puga, A.3
  • 161
    • 67650229881 scopus 로고    scopus 로고
    • Nrf2-dependent upregulation of antioxidative enzymes: A novel pathway for proteasome inhibitormediated cardioprotection
    • Dreger, H.; Westphal, K.; Weller, A.; Baumann, G.; Stangl, V.; Meiners, S.; Stangl, K. Nrf2-dependent upregulation of antioxidative enzymes: a novel pathway for proteasome inhibitormediated cardioprotection. Cardiovasc. Res., 2009, 83(2), 354-361.
    • (2009) Cardiovasc. Res. , vol.83 , Issue.2 , pp. 354-361
    • Dreger, H.1    Westphal, K.2    Weller, A.3    Baumann, G.4    Stangl, V.5    Meiners, S.6    Stangl, K.7
  • 162
    • 52949139764 scopus 로고    scopus 로고
    • Nrf2-mediated transcriptional induction of antioxidant response in mouse embryos exposed to ethanol in vivo: Implications for the prevention of fetal alcohol spectrum disorders
    • Dong, J.; Sulik, K.K.; Chen, S.Y. Nrf2-mediated transcriptional induction of antioxidant response in mouse embryos exposed to ethanol in vivo: implications for the prevention of fetal alcohol spectrum disorders. Antioxid. Redox. Signal., 2008, 10(12), 2023-2033.
    • (2008) Antioxid. Redox. Signal. , vol.10 , Issue.12 , pp. 2023-2033
    • Dong, J.1    Sulik, K.K.2    Chen, S.Y.3
  • 163
    • 33644649422 scopus 로고    scopus 로고
    • Hyperoxia stimulates an Nrf2-ARE transcriptional response via ROS-EGFR-PI3K-Akt/ERK MAP kinase signaling in pulmonary epithelial cells
    • Papaiahgari, S.; Zhang, Q.; Kleeberger, S.R.; Cho, H.Y.; Reddy, S.P. Hyperoxia stimulates an Nrf2-ARE transcriptional response via ROS-EGFR-PI3K-Akt/ERK MAP kinase signaling in pulmonary epithelial cells. Antioxid. Redox. Signal., 2006, 8(1-2), 43-52.
    • (2006) Antioxid. Redox. Signal. , vol.8 , Issue.1-2 , pp. 43-52
    • Papaiahgari, S.1    Zhang, Q.2    Kleeberger, S.R.3    Cho, H.Y.4    Reddy, S.P.5
  • 166
    • 84862824580 scopus 로고    scopus 로고
    • Histone deacetylase inhibition activates transcription factor Nrf2 and protects against cerebral ischemic damage
    • Wang, B.; Zhu, X.; Kim, Y.; Li, J.; Huang, S.; Saleem, S.; Li, R.C.; Xu, Y.; Dore, S.; Cao, W. Histone deacetylase inhibition activates transcription factor Nrf2 and protects against cerebral ischemic damage. Free Radic. Biol. Med., 2012, 52(5), 928-936.
    • (2012) Free Radic. Biol. Med. , vol.52 , Issue.5 , pp. 928-936
    • Wang, B.1    Zhu, X.2    Kim, Y.3    Li, J.4    Huang, S.5    Saleem, S.6    Li, R.C.7    Xu, Y.8    Dore, S.9    Cao, W.10
  • 168
    • 80051548161 scopus 로고    scopus 로고
    • Nitric oxide activates Nrf2 through S-nitrosylation of Keap1 in PC12 cells
    • Um, H.C.; Jang, J.H.; Kim, D.H.; Lee, C.; Surh, Y.J. Nitric oxide activates Nrf2 through S-nitrosylation of Keap1 in PC12 cells. Nitric. Oxide., 2011, 25(2), 161-168.
    • (2011) Nitric. Oxide. , vol.25 , Issue.2 , pp. 161-168
    • Um, H.C.1    Jang, J.H.2    Kim, D.H.3    Lee, C.4    Surh, Y.J.5
  • 169
    • 80051973172 scopus 로고    scopus 로고
    • Resveratrol restores Nrf2 level and prevents ethanol-induced toxic effects in the cerebellum of a rodent model of fetal alcohol spectrum disorders
    • Kumar, A.; Singh, C.K.; Lavoie, H.A.; Dipette, D.J.; Singh, U.S. Resveratrol restores Nrf2 level and prevents ethanol-induced toxic effects in the cerebellum of a rodent model of fetal alcohol spectrum disorders. Mol. Pharmacol., 2011, 80(3), 446-457.
    • (2011) Mol. Pharmacol. , vol.80 , Issue.3 , pp. 446-457
    • Kumar, A.1    Singh, C.K.2    Lavoie, H.A.3    Dipette, D.J.4    Singh, U.S.5
  • 172
    • 0027301398 scopus 로고
    • Preconditioning the human myocardium
    • Yellon, D.M.; Alkhulaifi, A.M.; Pugsley, W.B. Preconditioning the human myocardium. Lancet., 1993, 342(8866), 276-277.
    • (1993) Lancet. , vol.342 , Issue.8866 , pp. 276-277
    • Yellon, D.M.1    Alkhulaifi, A.M.2    Pugsley, W.B.3
  • 173
    • 54949112815 scopus 로고    scopus 로고
    • Ischaemic preconditioning during cardiac surgery: Systematic review and meta-analysis of perioperative outcomes in randomised clinical trials
    • Walsh, S.R.; Tang, T.Y.; Kullar, P.; Jenkins, D.P.; Dutka, D.P.; Gaunt, M.E. Ischaemic preconditioning during cardiac surgery: systematic review and meta-analysis of perioperative outcomes in randomised clinical trials. Eur. J. Cardiothorac. Surg., 2008, 34(5), 985-994.
    • (2008) Eur. J. Cardiothorac. Surg. , vol.34 , Issue.5 , pp. 985-994
    • Walsh, S.R.1    Tang, T.Y.2    Kullar, P.3    Jenkins, D.P.4    Dutka, D.P.5    Gaunt, M.E.6
  • 174
    • 0037390281 scopus 로고    scopus 로고
    • Intravenous nicorandil in conjunction with coronary reperfusion therapy is associated with better clinical and functional outcomes in patients with acute myocardial infarction
    • Sugimoto, K.; Ito, H.; Iwakura, K.; Ikushima, M.; Kato, A.; Kimura, R.; Tanaka, K.; Masuyama, T.; Ogihara, T.; Kawano, S.; Fujii, K. Intravenous nicorandil in conjunction with coronary reperfusion therapy is associated with better clinical and functional outcomes in patients with acute myocardial infarction. Circ. J., 2003, 67(4), 295-300.
    • (2003) Circ. J. , vol.67 , Issue.4 , pp. 295-300
    • Sugimoto, K.1    Ito, H.2    Iwakura, K.3    Ikushima, M.4    Kato, A.5    Kimura, R.6    Tanaka, K.7    Masuyama, T.8    Ogihara, T.9    Kawano, S.10    Fujii, K.11
  • 175
    • 80055033089 scopus 로고    scopus 로고
    • The therapeutic potential of ischemic conditioning: An update
    • Hausenloy, D.J.; Yellon, D.M. The therapeutic potential of ischemic conditioning: an update. Nat. Rev. Cardiol., 2011, 8(11), 619-629.
    • (2011) Nat. Rev. Cardiol. , vol.8 , Issue.11 , pp. 619-629
    • Hausenloy, D.J.1    Yellon, D.M.2
  • 176
    • 84867029736 scopus 로고    scopus 로고
    • Resveratrol prevents CA1 neurons against ischemic injury by parallel modulation of both GSK-3beta and CREB through PI3-K/Akt pathways
    • [Epub ahead of print]
    • Simao, F.; Matte, A.; Pagnussat, A.S.; Netto, C.A.; Salbego, C.G. Resveratrol prevents CA1 neurons against ischemic injury by parallel modulation of both GSK-3beta and CREB through PI3-K/Akt pathways. Eur. J. Neurosci., 2012. [Epub ahead of print].
    • (2012) Eur. J. Neurosci.
    • Simao, F.1    Matte, A.2    Pagnussat, A.S.3    Netto, C.A.4    Salbego, C.G.5
  • 177
    • 84866490646 scopus 로고    scopus 로고
    • Resveratrol preconditioning modulates inflammatory response in the rat hippocampus following global cerebral ischemia
    • [Epub ahead of print]
    • Simao, F.; Matte, A.; Pagnussat, A.S.; Netto, C.A.; Salbego, C.G. Resveratrol preconditioning modulates inflammatory response in the rat hippocampus following global cerebral ischemia. Neurochem. Int., 2012. [Epub ahead of print].
    • (2012) Neurochem. Int.
    • Simao, F.1    Matte, A.2    Pagnussat, A.S.3    Netto, C.A.4    Salbego, C.G.5
  • 179
    • 84855689149 scopus 로고    scopus 로고
    • Repeated resveratrol administration confers lasting protection against neuronal damage but induces dose-related alterations of behavioral impairments after global ischemia
    • Girbovan, C.; Morin, L.; Plamondon, H. Repeated resveratrol administration confers lasting protection against neuronal damage but induces dose-related alterations of behavioral impairments after global ischemia. Behav. Pharmacol., 2012, 23(1), 1-13.
    • (2012) Behav. Pharmacol. , vol.23 , Issue.1 , pp. 1-13
    • Girbovan, C.1    Morin, L.2    Plamondon, H.3
  • 180
    • 80755129036 scopus 로고    scopus 로고
    • Resveratrol pretreatment attenuates cerebral ischemic injury by upregulating expression of transcription factor Nrf2 and HO-1 in rats
    • Ren, J.; Fan, C.; Chen, N.; Huang, J.; Yang, Q. Resveratrol pretreatment attenuates cerebral ischemic injury by upregulating expression of transcription factor Nrf2 and HO-1 in rats. Neurochem. Res., 2011, 36(12), 2352-2362.
    • (2011) Neurochem. Res. , vol.36 , Issue.12 , pp. 2352-2362
    • Ren, J.1    Fan, C.2    Chen, N.3    Huang, J.4    Yang, Q.5
  • 181
    • 79960995848 scopus 로고    scopus 로고
    • Resveratrol suppresses apoptosis in intact human cardiac tissue-in vitro model simulating extracorporeal circulation
    • Usta, E.; Mustafi, M.; Walker, T.; Ziemer, G. Resveratrol suppresses apoptosis in intact human cardiac tissue-in vitro model simulating extracorporeal circulation. J. Cardiovasc. Surg. (Torino)., 2011, 52(3), 399-409.
    • (2011) J. Cardiovasc. Surg. (Torino). , vol.52 , Issue.3 , pp. 399-409
    • Usta, E.1    Mustafi, M.2    Walker, T.3    Ziemer, G.4
  • 182
    • 84859589503 scopus 로고    scopus 로고
    • Deferoxamine attenuates lipid peroxidation, blocks interleukin-6 production, ameliorates sepsis inflammatory response syndrome, and confers renoprotection after acute hepatic ischemia in pigs
    • Vlahakos, D.; Arkadopoulos, N.; Kostopanagiotou, G.; Siasiakou, S.; Kaklamanis, L.; Degiannis, D.; Demonakou, M.; Smyrniotis, V. Deferoxamine attenuates lipid peroxidation, blocks interleukin-6 production, ameliorates sepsis inflammatory response syndrome, and confers renoprotection after acute hepatic ischemia in pigs. Artif. Organs, 2012, 36(4), 400-408.
    • (2012) Artif. Organs , vol.36 , Issue.4 , pp. 400-408
    • Vlahakos, D.1    Arkadopoulos, N.2    Kostopanagiotou, G.3    Siasiakou, S.4    Kaklamanis, L.5    Degiannis, D.6    Demonakou, M.7    Smyrniotis, V.8
  • 183
    • 69249240342 scopus 로고    scopus 로고
    • Effects of deferoxamine on brain injury after transient focal cerebral ischemia in rats with hyperglycemia
    • Xing, Y.; Hua, Y.; Keep, R.F.; Xi, G. Effects of deferoxamine on brain injury after transient focal cerebral ischemia in rats with hyperglycemia. Brain Res., 2009, 1291, 113-121.
    • (2009) Brain Res. , vol.1291 , pp. 113-121
    • Xing, Y.1    Hua, Y.2    Keep, R.F.3    Xi, G.4
  • 184
    • 58549109827 scopus 로고    scopus 로고
    • Combination of deferoxamine and erythropoietin: Therapy for hypoxia-ischemia-induced brain injury in the neonatal rat?
    • van der Kooij, M.A.; Groenendaal, F.; Kavelaars, A.; Heijnen, C.J.; van Bel, F. Combination of deferoxamine and erythropoietin: therapy for hypoxia-ischemia-induced brain injury in the neonatal rat? Neurosci. Lett., 2009, 451(2), 109-113.
    • (2009) Neurosci. Lett. , vol.451 , Issue.2 , pp. 109-113
    • van der Kooij, M.A.1    Groenendaal, F.2    Kavelaars, A.3    Heijnen, C.J.4    van Bel, F.5
  • 185
    • 42949089902 scopus 로고    scopus 로고
    • Hypoxia inducible factor-1 improves the actions of nitric oxide and natriuretic peptides after simulated ischemia-reperfusion
    • Luciano, J.A.; Tan, T.; Zhang, Q.; Huang, E.; Scholz, P.; Weiss, H.R. Hypoxia inducible factor-1 improves the actions of nitric oxide and natriuretic peptides after simulated ischemia-reperfusion. Cell. Physiol. Biochem., 2008, 21(5-6), 421-428.
    • (2008) Cell. Physiol. Biochem. , vol.21 , Issue.5-6 , pp. 421-428
    • Luciano, J.A.1    Tan, T.2    Zhang, Q.3    Huang, E.4    Scholz, P.5    Weiss, H.R.6
  • 187
    • 78650214094 scopus 로고    scopus 로고
    • Post-ischemic activation of protein kinase C epsilon protects the hippocampus from cerebral ischemic injury via alterations in cerebral blood flow
    • Della-Morte, D.; Raval, A.P.; Dave, K.R.; Lin, H.W.; Perez-Pinzon, M.A. Post-ischemic activation of protein kinase C epsilon protects the hippocampus from cerebral ischemic injury via alterations in cerebral blood flow. Neurosci. Lett., 2011, 487(2), 158-162.
    • (2011) Neurosci. Lett. , vol.487 , Issue.2 , pp. 158-162
    • Della-Morte, D.1    Raval, A.P.2    Dave, K.R.3    Lin, H.W.4    Perez-Pinzon, M.A.5
  • 188
    • 46149126358 scopus 로고    scopus 로고
    • EpsilonPKC confers acute tolerance to cerebral ischemic reperfusion injury
    • Bright, R.; Sun, G.H.; Yenari, M.A.; Steinberg, G.K.; Mochly-Rosen, D. epsilonPKC confers acute tolerance to cerebral ischemic reperfusion injury. Neurosci. Lett., 2008, 441(1), 120-124.
    • (2008) Neurosci. Lett. , vol.441 , Issue.1 , pp. 120-124
    • Bright, R.1    Sun, G.H.2    Yenari, M.A.3    Steinberg, G.K.4    Mochly-Rosen, D.5


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