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Volumn 14, Issue 9, 2014, Pages 1103-1125

Reactive oxygen Species: Physiological Roles in the Regulation of Vascular Cells

Author keywords

Cardiovascular system; Endothelial; Hydrogen peroxide; Platelet; Reactive oxygen species; Redox; Smooth muscle; Superoxide anion

Indexed keywords

ALPHA TOCOPHEROL; ENDOTHELIAL NITRIC OXIDE SYNTHASE; FOCAL ADHESION KINASE; GLUTATHIONE DISULFIDE; GLUTATHIONE PEROXIDASE; HEMOGLOBIN; HYDROGEN PEROXIDE; HYDROXYL RADICAL; HYPOCHLOROUS ACID; LIPOXYGENASE; MITOGEN ACTIVATED PROTEIN KINASE PHOSPHATASE; MYELOPEROXIDASE; NITRIC OXIDE; NITROGEN DIOXIDE; NUCLEIC ACID; PEROXIREDOXIN; PEROXYNITRITE; PHOSPHOPROTEIN PHOSPHATASE; PROSTAGLANDIN SYNTHASE; PROTEIN KINASE C; PROTEIN TYROSINE PHOSPHATASE; REACTIVE NITROGEN SPECIES; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; SINGLET OXYGEN; SUPEROXIDE; UNINDEXED DRUG; XANTHINE OXIDASE;

EID: 84924911735     PISSN: 15665240     EISSN: 18755666     Source Type: Journal    
DOI: 10.2174/1566524014666140603114010     Document Type: Article
Times cited : (101)

References (335)
  • 1
    • 0020397137 scopus 로고
    • The effect of hyperoxia on superoxide production by lung submitochondrial particles
    • Turrens JF, Freeman BA, Levitt JG, Crapo JD. The effect of hyperoxia on superoxide production by lung submitochondrial particles. Arch Biochem Biophys 1982; 217(2): 401-10.
    • (1982) Arch Biochem Biophys , vol.217 , Issue.2 , pp. 401-410
    • Turrens, J.F.1    Freeman, B.A.2    Levitt, J.G.3    Crapo, J.D.4
  • 2
    • 79952026736 scopus 로고    scopus 로고
    • NADPH oxidase-mediated redox signaling: Roles in cellular stress response, stress tolerance, and tissue repair
    • Jiang F, Zhang Y, Dusting GJ. NADPH oxidase-mediated redox signaling: roles in cellular stress response, stress tolerance, and tissue repair. Pharmacol Rev 2011; 63(1): 218-42.
    • (2011) Pharmacol Rev , vol.63 , Issue.1 , pp. 218-242
    • Jiang, F.1    Zhang, Y.2    Dusting, G.J.3
  • 3
    • 1642484244 scopus 로고    scopus 로고
    • Xanthine oxidoreductase and cardiovascular disease: Molecular mechanisms and pathophysiological implications
    • Berry CE, Hare JM. Xanthine oxidoreductase and cardiovascular disease: molecular mechanisms and pathophysiological implications. J Physiol 2004; 555(Pt 3): 589-606.
    • (2004) J Physiol , vol.555 , pp. 589-606
    • Berry, C.E.1    Hare, J.M.2
  • 4
    • 50949128741 scopus 로고    scopus 로고
    • Cytosolic phospholipase A(2), lipoxygenase metabolites, and reactive oxygen species
    • Kim C, Kim JY, Kim JH. Cytosolic phospholipase A(2), lipoxygenase metabolites, and reactive oxygen species. BMB Rep 2008; 41(8): 555-9.
    • (2008) BMB Rep , vol.41 , Issue.8 , pp. 555-559
    • Kim, C.1    Kim, J.Y.2    Kim, J.H.3
  • 5
    • 0023688174 scopus 로고
    • Postischemic generation of superoxide anion by newborn pig brain
    • Armstead WM, Mirro R, Busija DW, Leffler CW. Postischemic generation of superoxide anion by newborn pig brain. Am J Physiol 1988; 255(2 Pt 2): H401-3.
    • (1988) Am J Physiol , vol.255 , Issue.2 , pp. H401-H403
    • Armstead, W.M.1    Mirro, R.2    Busija, D.W.3    Leffler, C.W.4
  • 6
    • 0027076652 scopus 로고
    • Nitric oxide synthase-catalyzed activation of oxygen and reduction of cytochromes: Reaction mechanisms and possible physiological implications
    • Mayer B, Heinzel B, Klatt P, John M, Schmidt K, Bohme E. Nitric oxide synthase-catalyzed activation of oxygen and reduction of cytochromes: reaction mechanisms and possible physiological implications. J Cardiovasc Pharmacol 1992; 20 Suppl 12: S54-6.
    • (1992) J Cardiovasc Pharmacol , vol.20 , pp. S54-S56
    • Mayer, B.1    Heinzel, B.2    Klatt, P.3    John, M.4    Schmidt, K.5    Bohme, E.6
  • 7
    • 0020644952 scopus 로고
    • Superoxide radical: An endogenous toxicant
    • Fridovich I. Superoxide radical: an endogenous toxicant. Annu Rev Pharmacol Toxicol 1983; 23: 239-57.
    • (1983) Annu Rev Pharmacol Toxicol , vol.23 , pp. 239-257
    • Fridovich, I.1
  • 8
    • 0014962945 scopus 로고
    • Superoxide dismutase from escherichia coli B. A new manganese-containing enzyme
    • Keele BB, Jr., McCord JM, Fridovich I. Superoxide dismutase from escherichia coli B. A new manganese-containing enzyme. J Biol Chem 1970; 245(22): 6176-81.
    • (1970) J Biol Chem , vol.245 , Issue.22 , pp. 6176-6181
    • Keele, B.B.1    McCord, J.M.2    Fridovich, I.3
  • 9
    • 0034648298 scopus 로고    scopus 로고
    • The Haber-Weiss reaction and mechanisms of toxicity
    • Kehrer JP. The Haber-Weiss reaction and mechanisms of toxicity. Toxicology 2000; 149(1): 43-50.
    • (2000) Toxicology , vol.149 , Issue.1 , pp. 43-50
    • Kehrer, J.P.1
  • 10
    • 0032732998 scopus 로고    scopus 로고
    • Superoxide and iron: Partners in crime
    • Liochev SI, Fridovich I. Superoxide and iron: partners in crime. IUBMB Life 1999; 48(2): 157-61.
    • (1999) IUBMB Life , vol.48 , Issue.2 , pp. 157-161
    • Liochev, S.I.1    Fridovich, I.2
  • 11
    • 0029055476 scopus 로고
    • Chlorination of tyrosyl residues in peptides by myeloperoxidase and human neutrophils
    • Domigan NM, Charlton TS, Duncan MW, Winterbourn CC, Kettle AJ. Chlorination of tyrosyl residues in peptides by myeloperoxidase and human neutrophils. J Biol Chem 1995; 270(28): 16542-8.
    • (1995) J Biol Chem , vol.270 , Issue.28 , pp. 16542-16548
    • Domigan, N.M.1    Charlton, T.S.2    Duncan, M.W.3    Winterbourn, C.C.4    Kettle, A.J.5
  • 12
    • 0038322621 scopus 로고    scopus 로고
    • Physical mechanisms of generation and deactivation of singlet oxygen
    • Schweitzer C, Schmidt R. Physical mechanisms of generation and deactivation of singlet oxygen. Chem Rev 2003; 103(5): 1685-757.
    • (2003) Chem Rev , vol.103 , Issue.5 , pp. 1685-1757
    • Schweitzer, C.1    Schmidt, R.2
  • 13
    • 77954915684 scopus 로고    scopus 로고
    • Singlet oxygen: There is indeed something new under the sun
    • Ogilby PR. Singlet oxygen: there is indeed something new under the sun. Chem Soc Rev 2010; 39(8): 3181-209.
    • (2010) Chem Soc Rev , vol.39 , Issue.8 , pp. 3181-3209
    • Ogilby, P.R.1
  • 14
    • 0035425503 scopus 로고    scopus 로고
    • Nitric oxide synthases: Structure, function and inhibition
    • Alderton WK, Cooper CE, Knowles RG. Nitric oxide synthases: structure, function and inhibition. Biochem J 2001; 357(Pt 3): 593-615.
    • (2001) Biochem J , vol.357 , pp. 593-615
    • Alderton, W.K.1    Cooper, C.E.2    Knowles, R.G.3
  • 15
    • 0023198721 scopus 로고
    • Nitric oxide release accounts for the biological activity of endothelium-derived relaxing factor
    • Palmer RM, Ferrige AG, Moncada S. Nitric oxide release accounts for the biological activity of endothelium-derived relaxing factor. Nature 1987; 327(6122): 524-6.
    • (1987) Nature , vol.327 , Issue.6122 , pp. 524-526
    • Palmer, R.M.1    Ferrige, A.G.2    Moncada, S.3
  • 16
    • 34848894877 scopus 로고    scopus 로고
    • Platelet-derived nitric oxide signaling and regulation
    • Gkaliagkousi E, Ritter J, Ferro A. Platelet-derived nitric oxide signaling and regulation. Circ Res 2007; 101(7): 654-62.
    • (2007) Circ Res , vol.101 , Issue.7 , pp. 654-662
    • Gkaliagkousi, E.1    Ritter, J.2    Ferro, A.3
  • 17
    • 0001599370 scopus 로고
    • Role of endotheliumderived nitric oxide in the regulation of blood pressure
    • Rees DD, Palmer RM, Moncada S. Role of endotheliumderived nitric oxide in the regulation of blood pressure. Proc Natl Acad Sci USA 1989; 86(9): 3375-8.
    • (1989) Proc Natl Acad Sci USA , vol.86 , Issue.9 , pp. 3375-3378
    • Rees, D.D.1    Palmer, R.M.2    Moncada, S.3
  • 18
    • 0023200487 scopus 로고
    • Endogenous nitric oxide inhibits human platelet adhesion to vascular endothelium
    • Radomski MW, Palmer RM, Moncada S. Endogenous nitric oxide inhibits human platelet adhesion to vascular endothelium. Lancet 1987; 2(8567): 1057-8.
    • (1987) Lancet , vol.2 , Issue.8567 , pp. 1057-1058
    • Radomski, M.W.1    Palmer, R.M.2    Moncada, S.3
  • 19
    • 0034769118 scopus 로고    scopus 로고
    • Nitric oxide and the immune response
    • Bogdan C. Nitric oxide and the immune response. Nat Immunol 2001; 2(10): 907-16.
    • (2001) Nat Immunol , vol.2 , Issue.10 , pp. 907-916
    • Bogdan, C.1
  • 20
    • 0029805172 scopus 로고    scopus 로고
    • Nitric oxide, superoxide, and peroxynitrite: The good, the bad, and ugly
    • Beckman JS, Koppenol WH. Nitric oxide, superoxide, and peroxynitrite: the good, the bad, and ugly. Am J Physiol 1996; 271(5 Pt 1): C1424-37.
    • (1996) Am J Physiol , vol.271 , Issue.5 , pp. C1424-C1437
    • Beckman, J.S.1    Koppenol, W.H.2
  • 21
    • 0029834589 scopus 로고    scopus 로고
    • Syntheses of peroxynitrite: To go with the flow or on solid grounds?
    • Koppenol WH, Kissner R, Beckman JS. Syntheses of peroxynitrite: to go with the flow or on solid grounds? Methods Enzymol 1996; 269: 296-302.
    • (1996) Methods Enzymol , vol.269 , pp. 296-302
    • Koppenol, W.H.1    Kissner, R.2    Beckman, J.S.3
  • 22
    • 64749101531 scopus 로고    scopus 로고
    • Chemical biology of peroxynitrite: Kinetics, diffusion, and radicals
    • Ferrer-Sueta G, Radi R. Chemical biology of peroxynitrite: kinetics, diffusion, and radicals. ACS Chem Biol 2009; 4(3): 161-77.
    • (2009) ACS Chem Biol , vol.4 , Issue.3 , pp. 161-177
    • Ferrer-Sueta, G.1    Radi, R.2
  • 23
    • 3342976149 scopus 로고    scopus 로고
    • Human peroxiredoxin 5 is a peroxynitrite reductase
    • Dubuisson M, Vander Stricht D, Clippe A, et al. Human peroxiredoxin 5 is a peroxynitrite reductase. FEBS Lett 2004; 571(1-3): 161-5.
    • (2004) FEBS Lett , vol.571 , Issue.1-3 , pp. 161-165
    • Dubuisson, M.1    Vander Stricht, D.2    Clippe, A.3
  • 24
    • 33846863589 scopus 로고    scopus 로고
    • Nitric oxide and peroxynitrite in health and disease
    • Pacher P, Beckman JS, Liaudet L. Nitric oxide and peroxynitrite in health and disease. Physiol Rev 2007; 87(1): 315-424.
    • (2007) Physiol Rev , vol.87 , Issue.1 , pp. 315-424
    • Pacher, P.1    Beckman, J.S.2    Liaudet, L.3
  • 25
    • 0842309140 scopus 로고    scopus 로고
    • Diversity of structures and properties among catalases
    • Chelikani P, Fita I, Loewen PC. Diversity of structures and properties among catalases. Cell Mol Life Sci 2004; 61(2): 192-208.
    • (2004) Cell Mol Life Sci , vol.61 , Issue.2 , pp. 192-208
    • Chelikani, P.1    Fita, I.2    Loewen, P.C.3
  • 26
    • 77957960743 scopus 로고    scopus 로고
    • Search for new particles in two-jet final states in 7 TeV proton-proton collisions with the ATLAS detector at the LHC
    • Aad G, Abbott B, Abdallah J, et al. Search for new particles in two-jet final states in 7 TeV proton-proton collisions with the ATLAS detector at the LHC. Phys Rev Lett 2010; 105(16): 161801.
    • (2010) Phys Rev Lett , vol.105 , Issue.16
    • Aad, G.1    Abbott, B.2    Abdallah, J.3
  • 27
    • 0037505644 scopus 로고    scopus 로고
    • Analysis of glutathione: Implication in redox and detoxification
    • Pastore A, Federici G, Bertini E, Piemonte F. Analysis of glutathione: implication in redox and detoxification. Clin Chim Acta 2003; 333(1): 19-39.
    • (2003) Clin Chim Acta , vol.333 , Issue.1 , pp. 19-39
    • Pastore, A.1    Federici, G.2    Bertini, E.3    Piemonte, F.4
  • 28
    • 77952311188 scopus 로고    scopus 로고
    • Thioredoxin and thioredoxin reductase: Current research with special reference to human disease
    • Holmgren A, Lu J. Thioredoxin and thioredoxin reductase: current research with special reference to human disease. Biochem Biophys Res Commun 2010; 396(1): 120-4.
    • (2010) Biochem Biophys Res Commun , vol.396 , Issue.1 , pp. 120-124
    • Holmgren, A.1    Lu, J.2
  • 29
    • 84872687926 scopus 로고    scopus 로고
    • Multiple glutathione disulfide removal pathways mediate cytosolic redox homeostasis
    • Morgan B, Ezerina D, Amoako TN, Riemer J, Seedorf M, Dick TP. Multiple glutathione disulfide removal pathways mediate cytosolic redox homeostasis. Nat Chem Biol 2013; 9(2): 119-25.
    • (2013) Nat Chem Biol , vol.9 , Issue.2 , pp. 119-125
    • Morgan, B.1    Ezerina, D.2    Amoako, T.N.3    Riemer, J.4    Seedorf, M.5    Dick, T.P.6
  • 30
    • 82755166890 scopus 로고    scopus 로고
    • Inhibition of pyruvate kinase M2 by reactive oxygen species contributes to cellular antioxidant responses
    • Anastasiou D, Poulogiannis G, Asara JM, et al. Inhibition of pyruvate kinase M2 by reactive oxygen species contributes to cellular antioxidant responses. Science 2011; 334(6060): 1278-83.
    • (2011) Science , vol.334 , Issue.6060 , pp. 1278-1283
    • Anastasiou, D.1    Poulogiannis, G.2    Asara, J.M.3
  • 31
    • 0030956826 scopus 로고    scopus 로고
    • Formation of advanced glycation end (AGE) products in diabetes: Prevention by pyruvate and alpha-keto glutarate
    • Varma SD, Devamanoharan PS, Ali AH. Formation of advanced glycation end (AGE) products in diabetes: prevention by pyruvate and alpha-keto glutarate. Mol Cell Biochem 1997; 171(1-2): 23-8.
    • (1997) Mol Cell Biochem , vol.171 , Issue.1-2 , pp. 23-28
    • Varma, S.D.1    Devamanoharan, P.S.2    Ali, A.H.3
  • 32
    • 0029091686 scopus 로고
    • Prevention of oxidative damage to rat lens by pyruvate in vitro: Possible attenuation in vivo
    • Varma SD, Ramachandran S, Devamanoharan PS, Morris SM, Ali AH. Prevention of oxidative damage to rat lens by pyruvate in vitro: possible attenuation in vivo. Curr Eye Res 1995; 14(8): 643-9.
    • (1995) Curr Eye Res , vol.14 , Issue.8 , pp. 643-649
    • Varma, S.D.1    Ramachandran, S.2    Devamanoharan, P.S.3    Morris, S.M.4    Ali, A.H.5
  • 33
    • 77953954538 scopus 로고    scopus 로고
    • Chemical and molecular mechanisms of antioxidants: Experimental approaches and model systems
    • Lu JM, Lin PH, Yao Q, Chen C. Chemical and molecular mechanisms of antioxidants: experimental approaches and model systems. J Cell Mol Med 2010; 14(4): 840-60.
    • (2010) J Cell Mol Med , vol.14 , Issue.4 , pp. 840-860
    • Lu, J.M.1    Lin, P.H.2    Yao, Q.3    Chen, C.4
  • 34
    • 25844468618 scopus 로고    scopus 로고
    • Redox homeostasis and antioxidant signaling: A metabolic interface between stress perception and physiological responses
    • Foyer CH, Noctor G. Redox homeostasis and antioxidant signaling: a metabolic interface between stress perception and physiological responses. Plant Cell 2005; 17(7): 1866-75.
    • (2005) Plant Cell , vol.17 , Issue.7 , pp. 1866-1875
    • Foyer, C.H.1    Noctor, G.2
  • 35
    • 0034283054 scopus 로고    scopus 로고
    • Potential antiatherogenic mechanisms of ascorbate (Vitamin C) and alpha-tocopherol (vitamin E)
    • Carr AC, Zhu BZ, Frei B. Potential antiatherogenic mechanisms of ascorbate (vitamin C) and alpha-tocopherol (vitamin E). Circ Res 2000; 87(5): 349-54.
    • (2000) Circ Res , vol.87 , Issue.5 , pp. 349-354
    • Carr, A.C.1    Zhu, B.Z.2    Frei, B.3
  • 37
    • 0019787519 scopus 로고
    • Uric acid provides an antioxidant defense in humans against oxidantand radical-caused aging and cancer: A hypothesis
    • Ames BN, Cathcart R, Schwiers E, Hochstein P. Uric acid provides an antioxidant defense in humans against oxidantand radical-caused aging and cancer: a hypothesis. Proc Natl Acad Sci USA 1981; 78(11): 6858-62.
    • (1981) Proc Natl Acad Sci USA , vol.78 , Issue.11 , pp. 6858-6862
    • Ames, B.N.1    Cathcart, R.2    Schwiers, E.3    Hochstein, P.4
  • 38
    • 0038119701 scopus 로고    scopus 로고
    • Is there a pathogenetic role for uric acid in hypertension and cardiovascular and renal disease?
    • Johnson RJ, Kang DH, Feig D, et al. Is there a pathogenetic role for uric acid in hypertension and cardiovascular and renal disease? Hypertension 2003; 41(6): 1183-90.
    • (2003) Hypertension , vol.41 , Issue.6 , pp. 1183-1190
    • Johnson, R.J.1    Kang, D.H.2    Feig, D.3
  • 39
    • 0037733975 scopus 로고    scopus 로고
    • The importance of glutathione in human disease
    • Townsend DM, Tew KD, Tapiero H. The importance of glutathione in human disease. Biomed Pharmacother 2003; 57(3-4): 145-55.
    • (2003) Biomed Pharmacother , vol.57 , Issue.3-4 , pp. 145-155
    • Townsend, D.M.1    Tew, K.D.2    Tapiero, H.3
  • 40
    • 0042169046 scopus 로고    scopus 로고
    • Ginkgo biloba extracts and cancer: A research area in its infancy
    • DeFeudis FV, Papadopoulos V, Drieu K. Ginkgo biloba extracts and cancer: a research area in its infancy. Fundam Clin Pharmacol 2003; 17(4): 405-17.
    • (2003) Fundam Clin Pharmacol , vol.17 , Issue.4 , pp. 405-417
    • Defeudis, F.V.1    Papadopoulos, V.2    Drieu, K.3
  • 41
    • 3843095141 scopus 로고    scopus 로고
    • Total phenolics and antioxidant activities of fenugreek, green tea, black tea, grape seed, ginger, rosemary, gotu kola, and ginkgo extracts, vitamin E, and tert-butylhydroquinone
    • Rababah TM, Hettiarachchy NS, Horax R. Total phenolics and antioxidant activities of fenugreek, green tea, black tea, grape seed, ginger, rosemary, gotu kola, and ginkgo extracts, vitamin E, and tert-butylhydroquinone. J Agric Food Chem 2004; 52(16): 5183-6.
    • (2004) J Agric Food Chem , vol.52 , Issue.16 , pp. 5183-5186
    • Rababah, T.M.1    Hettiarachchy, N.S.2    Horax, R.3
  • 42
    • 33750455858 scopus 로고    scopus 로고
    • Consumption of flavonoid-rich foods and increased plasma antioxidant capacity in humans: Cause, consequence, or epiphenomenon?
    • Lotito SB, Frei B. Consumption of flavonoid-rich foods and increased plasma antioxidant capacity in humans: cause, consequence, or epiphenomenon? Free Radic Biol Med 2006; 41(12): 1727-46.
    • (2006) Free Radic Biol Med , vol.41 , Issue.12 , pp. 1727-1746
    • Lotito, S.B.1    Frei, B.2
  • 43
    • 69149110615 scopus 로고    scopus 로고
    • Ginseng compounds: An update on their molecular mechanisms and medical applications
    • Lu JM, Yao Q, Chen C. Ginseng compounds: an update on their molecular mechanisms and medical applications. Curr Vasc Pharmacol 2009; 7(3): 293-302.
    • (2009) Curr Vasc Pharmacol , vol.7 , Issue.3 , pp. 293-302
    • Lu, J.M.1    Yao, Q.2    Chen, C.3
  • 44
    • 13844271387 scopus 로고    scopus 로고
    • Bioavailability and bioefficacy of polyphenols in humans. II. Review of 93 intervention studies
    • Williamson G, Manach C. Bioavailability and bioefficacy of polyphenols in humans. II. Review of 93 intervention studies. Am J Clin Nutr 2005; 81(1 Suppl): 243S-55S.
    • (2005) Am J Clin Nutr , vol.81 , Issue.1 , pp. 243S-255S
    • Williamson, G.1    Manach, C.2
  • 45
    • 79960478547 scopus 로고    scopus 로고
    • Chemistry and biology of reactive oxygen species in signaling or stress responses
    • Dickinson BC, Chang CJ. Chemistry and biology of reactive oxygen species in signaling or stress responses. Nat Chem Biol 2011; 7(8): 504-11.
    • (2011) Nat Chem Biol , vol.7 , Issue.8 , pp. 504-511
    • Dickinson, B.C.1    Chang, C.J.2
  • 46
    • 80052753079 scopus 로고    scopus 로고
    • Localized cysteine sulfenic acid formation by vascular endothelial growth factor: Role in endothelial cell migration and angiogenesis
    • Kaplan N, Urao N, Furuta E, et al. Localized cysteine sulfenic acid formation by vascular endothelial growth factor: role in endothelial cell migration and angiogenesis. Free Radic Res 2011; 45(10): 1124-35.
    • (2011) Free Radic Res , vol.45 , Issue.10 , pp. 1124-1135
    • Kaplan, N.1    Urao, N.2    Furuta, E.3
  • 47
    • 65249134122 scopus 로고    scopus 로고
    • Role of the sulfur atom on the reactivity of methionine toward OH radicals: Comparison with norleucine
    • Francisco-Marquez M, Galano A. Role of the sulfur atom on the reactivity of methionine toward OH radicals: comparison with norleucine. J Phys Chem B 2009; 113(14): 4947-52.
    • (2009) J Phys Chem B , vol.113 , Issue.14 , pp. 4947-4952
    • Francisco-Marquez, M.1    Galano, A.2
  • 48
    • 0037082129 scopus 로고    scopus 로고
    • Peptide methionine sulfoxide reductase: Structure, mechanism of action, and biological function
    • Weissbach H, Etienne F, Hoshi T, et al. Peptide methionine sulfoxide reductase: structure, mechanism of action, and biological function. Arch Biochem Biophys 2002; 397(2): 172-8.
    • (2002) Arch Biochem Biophys , vol.397 , Issue.2 , pp. 172-178
    • Weissbach, H.1    Etienne, F.2    Hoshi, T.3
  • 49
    • 84861130344 scopus 로고    scopus 로고
    • Proposed role of primary protein carbonylation in cell signaling
    • Wong CM, Bansal G, Marcocci L, Suzuki YJ. Proposed role of primary protein carbonylation in cell signaling. Redox Rep 2012; 17(2): 90-4.
    • (2012) Redox Rep , vol.17 , Issue.2 , pp. 90-94
    • Wong, C.M.1    Bansal, G.2    Marcocci, L.3    Suzuki, Y.J.4
  • 50
    • 21144440053 scopus 로고    scopus 로고
    • A cysteine-sulfinic acid in peroxiredoxin regulates H2O2-sensing by the antioxidant Pap1 pathway
    • Vivancos AP, Castillo EA, Biteau B, et al. A cysteine-sulfinic acid in peroxiredoxin regulates H2O2-sensing by the antioxidant Pap1 pathway. Proc Natl Acad Sci USA 2005; 102(25): 8875-80.
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.25 , pp. 8875-8880
    • Vivancos, A.P.1    Castillo, E.A.2    Biteau, B.3
  • 51
    • 57749093093 scopus 로고    scopus 로고
    • Structural and functional characterization of 2-oxo-histidine in oxidized PerR protein
    • Traore DA, El Ghazouani A, Jacquamet L, et al. Structural and functional characterization of 2-oxo-histidine in oxidized PerR protein. Nat Chem Biol 2009; 5(1): 53-9.
    • (2009) Nat Chem Biol , vol.5 , Issue.1 , pp. 53-59
    • Traore, D.A.1    El Ghazouani, A.2    Jacquamet, L.3
  • 52
    • 0026586147 scopus 로고
    • S-nitrosylation of proteins with nitric oxide: Synthesis and characterization of biologically active compounds
    • Stamler JS, Simon DI, Osborne JA, et al. S-nitrosylation of proteins with nitric oxide: synthesis and characterization of biologically active compounds. Proc Natl Acad Sci USA 1992; 89(1): 444-8.
    • (1992) Proc Natl Acad Sci USA , vol.89 , Issue.1 , pp. 444-448
    • Stamler, J.S.1    Simon, D.I.2    Osborne, J.A.3
  • 54
    • 70049083635 scopus 로고    scopus 로고
    • Protein S-nitrosylation in health and disease: A current perspective
    • Foster MW, Hess DT, Stamler JS. Protein S-nitrosylation in health and disease: a current perspective. Trends Mol Med 2009; 15(9): 391-404.
    • (2009) Trends Mol Med , vol.15 , Issue.9 , pp. 391-404
    • Foster, M.W.1    Hess, D.T.2    Stamler, J.S.3
  • 55
    • 1642570319 scopus 로고    scopus 로고
    • Nitric oxide, oxidants, and protein tyrosine nitration
    • Radi R. Nitric oxide, oxidants, and protein tyrosine nitration. Proc Natl Acad Sci USA 2004; 101(12): 4003-8.
    • (2004) Proc Natl Acad Sci USA , vol.101 , Issue.12 , pp. 4003-4008
    • Radi, R.1
  • 56
    • 0034693229 scopus 로고    scopus 로고
    • Tyrosine nitration by peroxynitrite formed from nitric oxide and superoxide generated by xanthine oxidase
    • Sawa T, Akaike T, Maeda H. Tyrosine nitration by peroxynitrite formed from nitric oxide and superoxide generated by xanthine oxidase. J Biol Chem 2000; 275(42): 32467-74.
    • (2000) J Biol Chem , vol.275 , Issue.42 , pp. 32467-32474
    • Sawa, T.1    Akaike, T.2    Maeda, H.3
  • 57
    • 0035929149 scopus 로고    scopus 로고
    • Nitrosylation. The prototypic redox-based signaling mechanism
    • Stamler JS, Lamas S, Fang FC. Nitrosylation. the prototypic redox-based signaling mechanism. Cell 2001; 106(6): 675-83.
    • (2001) Cell , vol.106 , Issue.6 , pp. 675-683
    • Stamler, J.S.1    Lamas, S.2    Fang, F.C.3
  • 58
    • 69949102851 scopus 로고    scopus 로고
    • Role of protein tyrosine nitration in neurodegenerative diseases and atherosclerosis
    • Lee JR, Kim JK, Lee SJ, Kim KP. Role of protein tyrosine nitration in neurodegenerative diseases and atherosclerosis. Arch Pharm Res 2009; 32(8): 1109-18.
    • (2009) Arch Pharm Res , vol.32 , Issue.8 , pp. 1109-1118
    • Lee, J.R.1    Kim, J.K.2    Lee, S.J.3    Kim, K.P.4
  • 59
    • 84866867477 scopus 로고    scopus 로고
    • Tyrosine modifications in aging
    • Feeney MB, Schoneich C. Tyrosine modifications in aging. Antioxid Redox Signal 2012; 17(11): 1571-9.
    • (2012) Antioxid Redox Signal , vol.17 , Issue.11 , pp. 1571-1579
    • Feeney, M.B.1    Schoneich, C.2
  • 60
    • 84857116578 scopus 로고    scopus 로고
    • Reactive oxygen species (ROS) homeostasis and redox regulation in cellular signaling
    • Ray PD, Huang BW, Tsuji Y. Reactive oxygen species (ROS) homeostasis and redox regulation in cellular signaling. Cell Signal 2012; 24(5): 981-90.
    • (2012) Cell Signal , vol.24 , Issue.5 , pp. 981-990
    • Ray, P.D.1    Huang, B.W.2    Tsuji, Y.3
  • 61
    • 0038749600 scopus 로고    scopus 로고
    • Oxidation state of the active-site cysteine in protein tyrosine phosphatase 1B
    • van Montfort RL, Congreve M, Tisi D, Carr R, Jhoti H. Oxidation state of the active-site cysteine in protein tyrosine phosphatase 1B. Nature 2003; 423(6941): 773-7.
    • (2003) Nature , vol.423 , Issue.6941 , pp. 773-777
    • Van Montfort, R.L.1    Congreve, M.2    Tisi, D.3    Carr, R.4    Jhoti, H.5
  • 62
    • 0025945823 scopus 로고
    • Evidence for protein-tyrosinephosphatase catalysis proceeding via a cysteine-phosphate intermediate
    • Guan KL, Dixon JE. Evidence for protein-tyrosinephosphatase catalysis proceeding via a cysteine-phosphate intermediate. J Biol Chem 1991; 266(26): 17026-30.
    • (1991) J Biol Chem , vol.266 , Issue.26 , pp. 17026-17030
    • Guan, K.L.1    Dixon, J.E.2
  • 63
    • 80052290597 scopus 로고    scopus 로고
    • Global proteomic assessment of the classical protein-tyrosine phosphatome and "Redoxome"
    • Karisch R, Fernandez M, Taylor P, et al. Global proteomic assessment of the classical protein-tyrosine phosphatome and "Redoxome". Cell 2011; 146(5): 826-40.
    • (2011) Cell , vol.146 , Issue.5 , pp. 826-840
    • Karisch, R.1    Fernandez, M.2    Taylor, P.3
  • 64
    • 0038411479 scopus 로고    scopus 로고
    • Redox regulation of protein tyrosine phosphatase 1B involves a sulphenylamide intermediate
    • Salmeen A, Andersen JN, Myers MP, et al. Redox regulation of protein tyrosine phosphatase 1B involves a sulphenylamide intermediate. Nature 2003; 423(6941): 769-73.
    • (2003) Nature , vol.423 , Issue.6941 , pp. 769-773
    • Salmeen, A.1    Ersen, J.N.2    Myers, M.P.3
  • 65
    • 60349084974 scopus 로고    scopus 로고
    • Hydrogen peroxideinduced neuronal apoptosis is associated with inhibition of protein phosphatase 2A and 5, leading to activation of MAPK pathway
    • Chen L, Liu L, Yin J, Luo Y, Huang S. Hydrogen peroxideinduced neuronal apoptosis is associated with inhibition of protein phosphatase 2A and 5, leading to activation of MAPK pathway. Int J Biochem Cell Biol 2009; 41(6): 1284-95.
    • (2009) Int J Biochem Cell Biol , vol.41 , Issue.6 , pp. 1284-1295
    • Chen, L.1    Liu, L.2    Yin, J.3    Luo, Y.4    Huang, S.5
  • 66
    • 14844327760 scopus 로고    scopus 로고
    • Reactive oxygen species promote TNFalpha-induced death and sustained JNK activation by inhibiting MAP kinase phosphatases
    • Kamata H, Honda S, Maeda S, Chang L, Hirata H, Karin M. Reactive oxygen species promote TNFalpha-induced death and sustained JNK activation by inhibiting MAP kinase phosphatases. Cell 2005; 120(5): 649-61.
    • (2005) Cell , vol.120 , Issue.5 , pp. 649-661
    • Kamata, H.1    Honda, S.2    Maeda, S.3    Chang, L.4    Hirata, H.5    Karin, M.6
  • 67
    • 0037780966 scopus 로고    scopus 로고
    • Reactive oxygen species as essential mediators of cell adhesion: The oxidative inhibition of a FAK tyrosine phosphatase is required for cell adhesion
    • Chiarugi P, Pani G, Giannoni E, et al. Reactive oxygen species as essential mediators of cell adhesion: the oxidative inhibition of a FAK tyrosine phosphatase is required for cell adhesion. J Cell Biol 2003; 161(5): 933-44.
    • (2003) J Cell Biol , vol.161 , Issue.5 , pp. 933-944
    • Chiarugi, P.1    Pani, G.2    Giannoni, E.3
  • 68
    • 58049200135 scopus 로고    scopus 로고
    • Cysteine S-nitrosylation protects protein-tyrosine phosphatase 1B against oxidationinduced permanent inactivation
    • Chen YY, Chu HM, Pan KT, et al. Cysteine S-nitrosylation protects protein-tyrosine phosphatase 1B against oxidationinduced permanent inactivation. J Biol Chem 2008; 283(50): 35265-72.
    • (2008) J Biol Chem , vol.283 , Issue.50 , pp. 35265-35272
    • Chen, Y.Y.1    Chu, H.M.2    Pan, K.T.3
  • 69
    • 79961191673 scopus 로고    scopus 로고
    • Redox regulation of protein kinases as a modulator of vascular function
    • Knock GA, Ward JP. Redox regulation of protein kinases as a modulator of vascular function. Antioxid Redox Signal 2011; 15(6): 1531-47.
    • (2011) Antioxid Redox Signal , vol.15 , Issue.6 , pp. 1531-1547
    • Knock, G.A.1    Ward, J.P.2
  • 70
    • 34948845017 scopus 로고    scopus 로고
    • Disulfide Bond-mediated multimerization of Ask1 and its reduction by thioredoxin-1 regulate H(2)O(2)-induced c-Jun NH(2)-terminal kinase activation and apoptosis
    • Nadeau PJ, Charette SJ, Toledano MB, Landry J. Disulfide Bond-mediated multimerization of Ask1 and its reduction by thioredoxin-1 regulate H(2)O(2)-induced c-Jun NH(2)-terminal kinase activation and apoptosis. Mol Biol Cell 2007; 18(10): 3903-13.
    • (2007) Mol Biol Cell , vol.18 , Issue.10 , pp. 3903-3913
    • Nadeau, P.J.1    Charette, S.J.2    Toledano, M.B.3    Landry, J.4
  • 71
    • 0032080283 scopus 로고    scopus 로고
    • Mammalian thioredoxin is a direct inhibitor of apoptosis signal-regulating kinase (ASK) 1
    • Saitoh M, Nishitoh H, Fujii M, et al. Mammalian thioredoxin is a direct inhibitor of apoptosis signal-regulating kinase (ASK) 1. EMBO J 1998; 17(9): 2596-606.
    • (1998) EMBO J , vol.17 , Issue.9 , pp. 2596-2606
    • Saitoh, M.1    Nishitoh, H.2    Fujii, M.3
  • 72
    • 36849043546 scopus 로고    scopus 로고
    • Thioredoxin and TRAF family proteins regulate reactive oxygen speciesdependent activation of ASK1 through reciprocal modulation of the N-terminal homophilic interaction of ASK1
    • Fujino G, Noguchi T, Matsuzawa A, et al. Thioredoxin and TRAF family proteins regulate reactive oxygen speciesdependent activation of ASK1 through reciprocal modulation of the N-terminal homophilic interaction of ASK1. Mol Cell Biol 2007; 27(23): 8152-63.
    • (2007) Mol Cell Biol , vol.27 , Issue.23 , pp. 8152-8163
    • Fujino, G.1    Noguchi, T.2    Matsuzawa, A.3
  • 73
    • 0033520310 scopus 로고    scopus 로고
    • Nitric oxide controls src kinase activity through a sulfhydryl group modificationmediated Tyr-527-independent and Tyr-416-linked mechanism
    • Akhand AA, Pu M, Senga T, et al. Nitric oxide controls src kinase activity through a sulfhydryl group modificationmediated Tyr-527-independent and Tyr-416-linked mechanism. J Biol Chem 1999; 274(36): 25821-6.
    • (1999) J Biol Chem , vol.274 , Issue.36 , pp. 25821-25826
    • Akhand, A.A.1    Pu, M.2    Senga, T.3
  • 74
    • 22544453858 scopus 로고    scopus 로고
    • Intracellular reactive oxygen species activate Src tyrosine kinase during cell adhesion and anchorage-dependent cell growth
    • Giannoni E, Buricchi F, Raugei G, Ramponi G, Chiarugi P. Intracellular reactive oxygen species activate Src tyrosine kinase during cell adhesion and anchorage-dependent cell growth. Mol Cell Biol 2005; 25(15): 6391-403.
    • (2005) Mol Cell Biol , vol.25 , Issue.15 , pp. 6391-6403
    • Giannoni, E.1    Buricchi, F.2    Raugei, G.3    Ramponi, G.4    Chiarugi, P.5
  • 75
    • 21244471166 scopus 로고    scopus 로고
    • Inactivation of SRC family tyrosine kinases by reactive oxygen species in vivo
    • Tang H, Hao Q, Rutherford SA, Low B, Zhao ZJ. Inactivation of SRC family tyrosine kinases by reactive oxygen species in vivo. J Biol Chem 2005; 280(25): 23918-25.
    • (2005) J Biol Chem , vol.280 , Issue.25 , pp. 23918-23925
    • Tang, H.1    Hao, Q.2    Rutherford, S.A.3    Low, B.4    Zhao, Z.J.5
  • 76
    • 0034604723 scopus 로고    scopus 로고
    • Superoxide-induced stimulation of protein kinase C via thiol modification and modulation of zinc content
    • Knapp LT, Klann E. Superoxide-induced stimulation of protein kinase C via thiol modification and modulation of zinc content. J Biol Chem 2000; 275(31): 24136-45.
    • (2000) J Biol Chem , vol.275 , Issue.31 , pp. 24136-24145
    • Knapp, L.T.1    Klann, E.2
  • 77
    • 0029174009 scopus 로고
    • Modifications of cysteine-rich regions in protein kinase C induced by oxidant tumor promoters and enzyme-specific inhibitors
    • Gopalakrishna R, Chen ZH, Gundimeda U. Modifications of cysteine-rich regions in protein kinase C induced by oxidant tumor promoters and enzyme-specific inhibitors. Methods Enzymol 1995; 252: 132-46.
    • (1995) Methods Enzymol , vol.252 , pp. 132-146
    • Gopalakrishna, R.1    Chen, Z.H.2    Gundimeda, U.3
  • 78
    • 47249122974 scopus 로고    scopus 로고
    • A direct redox regulation of protein kinase C isoenzymes mediates oxidant-induced neuritogenesis in PC12 cells
    • Gopalakrishna R, Gundimeda U, Schiffman JE, McNeill TH. A direct redox regulation of protein kinase C isoenzymes mediates oxidant-induced neuritogenesis in PC12 cells. J Biol Chem 2008; 283(21): 14430-44.
    • (2008) J Biol Chem , vol.283 , Issue.21 , pp. 14430-14444
    • Gopalakrishna, R.1    Gundimeda, U.2    Schiffman, J.E.3    McNeill, T.H.4
  • 79
    • 14044252389 scopus 로고    scopus 로고
    • Cellular protein kinase C isozyme regulation by exogenously delivered physiological disulfides--implications of oxidative protein kinase C regulation to cancer prevention
    • Chu F, Chen LH, O'Brian CA. Cellular protein kinase C isozyme regulation by exogenously delivered physiological disulfides--implications of oxidative protein kinase C regulation to cancer prevention. Carcinogenesis 2004; 25(4): 585-96.
    • (2004) Carcinogenesis , vol.25 , Issue.4 , pp. 585-596
    • Chu, F.1    Chen, L.H.2    O'brian, C.A.3
  • 80
    • 0034903753 scopus 로고    scopus 로고
    • Potent inactivation of representative members of each PKC isozyme subfamily and PKD via S-thiolation by the tumor-promotion/progression antagonist glutathione but not by its precursor cysteine
    • Chu F, Ward NE, O'Brian CA. Potent inactivation of representative members of each PKC isozyme subfamily and PKD via S-thiolation by the tumor-promotion/progression antagonist glutathione but not by its precursor cysteine. Carcinogenesis 2001; 22(8): 1221-9.
    • (2001) Carcinogenesis , vol.22 , Issue.8 , pp. 1221-1229
    • Chu, F.1    Ward, N.E.2    O'brian, C.A.3
  • 81
    • 0028903322 scopus 로고
    • Down-regulation of protein kinase C attenuates the oxidant hydrogen peroxide-mediated activation of phospholipase A2 in pulmonary vascular smooth muscle cells
    • Chakraborti S, Chakraborti T. Down-regulation of protein kinase C attenuates the oxidant hydrogen peroxide-mediated activation of phospholipase A2 in pulmonary vascular smooth muscle cells. Cell Signal 1995; 7(1): 75-83.
    • (1995) Cell Signal , vol.7 , Issue.1 , pp. 75-83
    • Chakraborti, S.1    Chakraborti, T.2
  • 82
    • 0024547684 scopus 로고
    • Protein kinase inhibitor prevents pulmonary edema in response to H2O2
    • Johnson A, Phillips P, Hocking D, Tsan MF, Ferro T. Protein kinase inhibitor prevents pulmonary edema in response to H2O2. Am J Physiol 1989; 256(4 Pt 2): H1012-22.
    • (1989) Am J Physiol , vol.256 , Issue.4 , pp. H1012-H1022
    • Johnson, A.1    Phillips, P.2    Hocking, D.3    Tsan, M.F.4    Ferro, T.5
  • 83
    • 42949085382 scopus 로고    scopus 로고
    • A dynamic pathway for calcium-independent activation of CaMKII by methionine oxidation
    • Erickson JR, Joiner ML, Guan X, et al. A dynamic pathway for calcium-independent activation of CaMKII by methionine oxidation. Cell 2008; 133(3): 462-74.
    • (2008) Cell , vol.133 , Issue.3 , pp. 462-474
    • Erickson, J.R.1    Joiner, M.L.2    Guan, X.3
  • 84
    • 34548695863 scopus 로고    scopus 로고
    • Cysteine redox sensor in PKGIa enables oxidant-induced activation
    • Burgoyne JR, Madhani M, Cuello F, et al. Cysteine redox sensor in PKGIa enables oxidant-induced activation. Science 2007; 317(5843): 1393-7.
    • (2007) Science , vol.317 , Issue.5843 , pp. 1393-1397
    • Burgoyne, J.R.1    Madhani, M.2    Cuello, F.3
  • 85
    • 79960611172 scopus 로고    scopus 로고
    • Isoform-specific regulation of Akt by PDGF-induced reactive oxygen species
    • Wani R, Qian J, Yin L, et al. Isoform-specific regulation of Akt by PDGF-induced reactive oxygen species. Proc Natl Acad Sci USA 2011; 108(26): 10550-5.
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.26 , pp. 10550-10555
    • Wani, R.1    Qian, J.2    Yin, L.3
  • 86
    • 0346749513 scopus 로고    scopus 로고
    • Glutaredoxin exerts an antiapoptotic effect by regulating the redox state of Akt
    • Murata H, Ihara Y, Nakamura H, Yodoi J, Sumikawa K, Kondo T. Glutaredoxin exerts an antiapoptotic effect by regulating the redox state of Akt. J Biol Chem 2003; 278(50): 50226-33.
    • (2003) J Biol Chem , vol.278 , Issue.50 , pp. 50226-50233
    • Murata, H.1    Ihara, Y.2    Nakamura, H.3    Yodoi, J.4    Sumikawa, K.5    Kondo, T.6
  • 87
    • 79951887419 scopus 로고    scopus 로고
    • Forkhead box o as a sensor, mediator, and regulator of redox signaling
    • de Keizer PL, Burgering BM, Dansen TB. Forkhead box o as a sensor, mediator, and regulator of redox signaling. Antioxid Redox Signal 2011; 14(6): 1093-106.
    • (2011) Antioxid Redox Signal , vol.14 , Issue.6 , pp. 1093-1106
    • De Keizer, P.L.1    Burgering, B.M.2    Dansen, T.B.3
  • 88
    • 14044277556 scopus 로고    scopus 로고
    • Redox regulation of NF-kappaB activation: Distinct redox regulation between the cytoplasm and the nucleus
    • Kabe Y, Ando K, Hirao S, Yoshida M, Handa H. Redox regulation of NF-kappaB activation: distinct redox regulation between the cytoplasm and the nucleus. Antioxid Redox Signal 2005; 7(3-4): 395-403.
    • (2005) Antioxid Redox Signal , vol.7 , Issue.3-4 , pp. 395-403
    • Kabe, Y.1    Osu, K.2    Hirao, S.3    Yoshida, M.4    Handa, H.5
  • 89
    • 78650894319 scopus 로고    scopus 로고
    • Crosstalk of reactive oxygen species and NF-kappaB signaling
    • Morgan MJ, Liu ZG. Crosstalk of reactive oxygen species and NF-kappaB signaling. Cell Res 2011; 21(1): 103-15.
    • (2011) Cell Res , vol.21 , Issue.1 , pp. 103-115
    • Morgan, M.J.1    Liu, Z.G.2
  • 90
    • 33747596652 scopus 로고    scopus 로고
    • Oxygen sensing by mitochondria at complex III: The paradox of increased reactive oxygen species during hypoxia
    • Guzy RD, Schumacker PT. Oxygen sensing by mitochondria at complex III: the paradox of increased reactive oxygen species during hypoxia. Exp Physiol 2006; 91(5): 807-19.
    • (2006) Exp Physiol , vol.91 , Issue.5 , pp. 807-819
    • Guzy, R.D.1    Schumacker, P.T.2
  • 91
    • 24144493814 scopus 로고    scopus 로고
    • Mitochondrial complex III is required for hypoxia-induced ROS production and cellular oxygen sensing
    • Guzy RD, Hoyos B, Robin E, et al. Mitochondrial complex III is required for hypoxia-induced ROS production and cellular oxygen sensing. Cell Metab 2005; 1(6): 401-8.
    • (2005) Cell Metab , vol.1 , Issue.6 , pp. 401-408
    • Guzy, R.D.1    Hoyos, B.2    Robin, E.3
  • 92
    • 84857535891 scopus 로고    scopus 로고
    • Tarnawski AS. Critical role of hypoxia sensor--HIF-1alpha in VEGF gene activation. Implications for angiogenesis and tissue injury healing
    • Ahluwalia A, Tarnawski AS. Critical role of hypoxia sensor--HIF-1alpha in VEGF gene activation. Implications for angiogenesis and tissue injury healing. Curr Med Chem 2012; 19(1): 90-7.
    • (2012) Curr Med Chem , vol.19 , Issue.1 , pp. 90-97
    • Ahluwalia, A.1
  • 93
    • 84870587105 scopus 로고    scopus 로고
    • Reactive oxygen species regulate ERBB2 and ERBB3 expression via miR-199a/125b and DNA methylation
    • He J, Xu Q, Jing Y, et al. Reactive oxygen species regulate ERBB2 and ERBB3 expression via miR-199a/125b and DNA methylation. EMBO Rep 2012; 13(12): 1116-22.
    • (2012) EMBO Rep , vol.13 , Issue.12 , pp. 1116-1122
    • He, J.1    Xu, Q.2    Jing, Y.3
  • 94
    • 84878660136 scopus 로고    scopus 로고
    • Oxidative stress causes epigenetic alteration of CDX1 expression in colorectal cancer cells
    • Zhang R, Kang KA, Kim KC, et al. Oxidative stress causes epigenetic alteration of CDX1 expression in colorectal cancer cells. Gene 2013; 524(2): 214-9.
    • (2013) Gene , vol.524 , Issue.2 , pp. 214-219
    • Zhang, R.1    Kang, K.A.2    Kim, K.C.3
  • 95
    • 84860269756 scopus 로고    scopus 로고
    • Epigenetic changes induced by oxidative stress in colorectal cancer cells: Methylation of tumor suppressor RUNX3
    • Kang KA, Zhang R, Kim GY, Bae SC, Hyun JW. Epigenetic changes induced by oxidative stress in colorectal cancer cells: methylation of tumor suppressor RUNX3. Tumour Biol 2012; 33(2): 403-12.
    • (2012) Tumour Biol , vol.33 , Issue.2 , pp. 403-412
    • Kang, K.A.1    Zhang, R.2    Kim, G.Y.3    Bae, S.C.4    Hyun, J.W.5
  • 96
    • 0034329425 scopus 로고    scopus 로고
    • Unprecedented proximal binding of nitric oxide to heme: Implications for guanylate cyclase
    • Lawson DM, Stevenson CE, Andrew CR, Eady RR. Unprecedented proximal binding of nitric oxide to heme: implications for guanylate cyclase. EMBO J 2000; 19(21): 5661-71.
    • (2000) EMBO J , vol.19 , Issue.21 , pp. 5661-5671
    • Lawson, D.M.1    Stevenson, C.E.2    Rew, C.R.3    Eady, R.R.4
  • 97
    • 0037013155 scopus 로고    scopus 로고
    • OxyR: A molecular code for redox-related signaling
    • Kim SO, Merchant K, Nudelman R, et al. OxyR: a molecular code for redox-related signaling. Cell 2002; 109(3): 383-96.
    • (2002) Cell , vol.109 , Issue.3 , pp. 383-396
    • Kim, S.O.1    Merchant, K.2    Nudelman, R.3
  • 98
    • 0035283587 scopus 로고    scopus 로고
    • Redox-operated genetic switches: The SoxR and OxyR transcription factors
    • Pomposiello PJ, Demple B. Redox-operated genetic switches: the SoxR and OxyR transcription factors. Trends Biotechnol 2001; 19(3): 109-14.
    • (2001) Trends Biotechnol , vol.19 , Issue.3 , pp. 109-114
    • Pomposiello, P.J.1    Demple, B.2
  • 99
    • 0024460992 scopus 로고
    • Endogenous oxidative DNA damage, aging, and cancer
    • Ames BN. Endogenous oxidative DNA damage, aging, and cancer. Free Radic Res Commun 1989; 7(3-6): 121-8.
    • (1989) Free Radic Res Commun , vol.7 , Issue.3-6 , pp. 121-128
    • Ames, B.N.1
  • 100
    • 84864326787 scopus 로고    scopus 로고
    • Damage by reactive species: Mechanisms, mutation and repair
    • Jena NR. DNA damage by reactive species: Mechanisms, mutation and repair. J Biosci 2012; 37(3): 503-17.
    • (2012) J Biosci , vol.37 , Issue.3 , pp. 503-517
    • Jena, N.1
  • 101
    • 0031782930 scopus 로고    scopus 로고
    • Formation of 8-oxoguanine in cellular DNA of Escherichia coli strains defective in different antioxidant defences
    • Alhama J, Ruiz-Laguna J, Rodriguez-Ariza A, Toribio F, Lopez-Barea J, Pueyo C. Formation of 8-oxoguanine in cellular DNA of Escherichia coli strains defective in different antioxidant defences. Mutagenesis 1998; 13(6): 589-94.
    • (1998) Mutagenesis , vol.13 , Issue.6 , pp. 589-594
    • Alhama, J.1    Ruiz-Laguna, J.2    Rodriguez-Ariza, A.3    Toribio, F.4    Lopez-Barea, J.5    Pueyo, C.6
  • 102
    • 0037867770 scopus 로고    scopus 로고
    • Imidazole ring-opened DNA purines and their biological significance
    • Tudek B. Imidazole ring-opened DNA purines and their biological significance. J Biochem Mol Biol 2003; 36(1): 12-9.
    • (2003) J Biochem Mol Biol , vol.36 , Issue.1 , pp. 12-19
    • Tudek, B.1
  • 103
    • 0025972738 scopus 로고
    • DNA damage by oxygen-derived species. Its mechanism and measurement in mammalian systems
    • Halliwell B, Aruoma OI. DNA damage by oxygen-derived species. Its mechanism and measurement in mammalian systems. FEBS Lett 1991; 281(1-2): 9-19.
    • (1991) FEBS Lett , vol.281 , Issue.1-2 , pp. 9-19
    • Halliwell, B.1    Aruoma, O.I.2
  • 104
    • 0022259419 scopus 로고
    • Mammalian cells are not killed by DNA single-strand breaks caused by hydroxyl radicals from hydrogen peroxide
    • Ward JF, Blakely WF, Joner EI. Mammalian cells are not killed by DNA single-strand breaks caused by hydroxyl radicals from hydrogen peroxide. Radiat Res 1985; 103(3): 383-92.
    • (1985) Radiat Res , vol.103 , Issue.3 , pp. 383-392
    • Ward, J.F.1    Blakely, W.F.2    Joner, E.I.3
  • 105
    • 79956191022 scopus 로고    scopus 로고
    • Role of oxidative stress and DNA damage in human carcinogenesis
    • Kryston TB, Georgiev AB, Pissis P, Georgakilas AG. Role of oxidative stress and DNA damage in human carcinogenesis. Mutat Res 2011; 711(1-2): 193-201.
    • (2011) Mutat Res , vol.711 , Issue.1-2 , pp. 193-201
    • Kryston, T.B.1    Georgiev, A.B.2    Pissis, P.3    Georgakilas, A.G.4
  • 106
    • 33745853157 scopus 로고    scopus 로고
    • 8-nitroguanine, a product of nitrative DNA damage caused by reactive nitrogen species: Formation, occurrence, and implications in inflammation and carcinogenesis
    • Ohshima H, Sawa T, Akaike T. 8-nitroguanine, a product of nitrative DNA damage caused by reactive nitrogen species: formation, occurrence, and implications in inflammation and carcinogenesis. Antioxid Redox Signal 2006; 8(5-6): 1033-45.
    • (2006) Antioxid Redox Signal , vol.8 , Issue.5-6 , pp. 1033-1045
    • Ohshima, H.1    Sawa, T.2    Akaike, T.3
  • 107
    • 31544432817 scopus 로고    scopus 로고
    • Peroxynitriteinduced oxidation and nitration products of guanine and 8-oxoguanine: Structures and mechanisms of product formation
    • Niles JC, Wishnok JS, Tannenbaum SR. Peroxynitriteinduced oxidation and nitration products of guanine and 8-oxoguanine: structures and mechanisms of product formation. Nitric Oxide 2006; 14(2): 109-21.
    • (2006) Nitric Oxide , vol.14 , Issue.2 , pp. 109-121
    • Niles, J.C.1    Wishnok, J.S.2    Tannenbaum, S.R.3
  • 108
    • 34248330315 scopus 로고    scopus 로고
    • Formation of 8-nitroguanine and 8-oxoguanine due to reactions of peroxynitrite with guanine
    • Jena NR, Mishra PC. Formation of 8-nitroguanine and 8-oxoguanine due to reactions of peroxynitrite with guanine. J Comput Chem 2007; 28(8): 1321-35.
    • (2007) J Comput Chem , vol.28 , Issue.8 , pp. 1321-1335
    • Jena, N.R.1    Mishra, P.C.2
  • 109
    • 84861633363 scopus 로고    scopus 로고
    • Formation of ring-opened and rearranged products of guanine: Mechanisms and biological significance
    • Jena NR, Mishra PC. Formation of ring-opened and rearranged products of guanine: mechanisms and biological significance. Free Radic Biol Med 2012; 53(1): 81-94.
    • (2012) Free Radic Biol Med , vol.53 , Issue.1 , pp. 81-94
    • Jena, N.R.1    Mishra, P.C.2
  • 111
    • 4043112183 scopus 로고    scopus 로고
    • Oxidative damage to methyl-CpG sequences inhibits the binding of the methyl-CpG binding domain (MBD) of methyl-CpG binding protein 2 (MeCP2)
    • Valinluck V, Tsai HH, Rogstad DK, Burdzy A, Bird A, Sowers LC. Oxidative damage to methyl-CpG sequences inhibits the binding of the methyl-CpG binding domain (MBD) of methyl-CpG binding protein 2 (MeCP2). Nucleic Acids Res 2004; 32(14): 4100-8.
    • (2004) Nucleic Acids Res , vol.32 , Issue.14 , pp. 4100-4108
    • Valinluck, V.1    Tsai, H.H.2    Rogstad, D.K.3    Burdzy, A.4    Bird, A.5    Sowers, L.C.6
  • 112
    • 58149094898 scopus 로고    scopus 로고
    • Hypoxiainduced oxidative base modifications in the VEGF hypoxiaresponse element are associated with transcriptionally active nucleosomes
    • Ruchko MV, Gorodnya OM, Pastukh VM, et al. Hypoxiainduced oxidative base modifications in the VEGF hypoxiaresponse element are associated with transcriptionally active nucleosomes. Free Radic Biol Med 2009; 46(3): 352-9.
    • (2009) Free Radic Biol Med , vol.46 , Issue.3 , pp. 352-359
    • Ruchko, M.V.1    Gorodnya, O.M.2    Pastukh, V.M.3
  • 113
    • 84863664040 scopus 로고    scopus 로고
    • Perinuclear mitochondrial clustering creates an oxidant-rich nuclear domain required for hypoxia-induced transcription
    • Al-Mehdi AB, Pastukh VM, Swiger BM, et al. Perinuclear mitochondrial clustering creates an oxidant-rich nuclear domain required for hypoxia-induced transcription. Sci Signal 2012; 5(231): ra47.
    • (2012) Sci Signal , vol.5 , Issue.231
    • Al-Mehdi, A.B.1    Pastukh, V.M.2    Swiger, B.M.3
  • 114
    • 33745255099 scopus 로고    scopus 로고
    • A topoisomerase IIbetamediated dsDNA break required for regulated transcription
    • Ju BG, Lunyak VV, Perissi V, et al. A topoisomerase IIbetamediated dsDNA break required for regulated transcription. Science 2006; 312(5781): 1798-802.
    • (2006) Science , vol.312 , Issue.5781 , pp. 1798-1802
    • Ju, B.G.1    Lunyak, V.V.2    Perissi, V.3
  • 115
    • 38149045693 scopus 로고    scopus 로고
    • DNA oxidation as triggered by H3K9me2 demethylation drives estrogeninduced gene expression
    • Perillo B, Ombra MN, Bertoni A, et al. DNA oxidation as triggered by H3K9me2 demethylation drives estrogeninduced gene expression. Science 2008; 319(5860): 202-6.
    • (2008) Science , vol.319 , Issue.5860 , pp. 202-206
    • Perillo, B.1    Ombra, M.N.2    Bertoni, A.3
  • 116
    • 3042527868 scopus 로고    scopus 로고
    • The NADPH oxidase of professional phagocytes--prototype of the NOX electron transport chain systems
    • Cross AR, Segal AW. The NADPH oxidase of professional phagocytes--prototype of the NOX electron transport chain systems. Biochim Biophys Acta 2004; 1657(1): 1-22.
    • (2004) Biochim Biophys Acta , vol.1657 , Issue.1 , pp. 1-22
    • Cross, A.R.1    Segal, A.W.2
  • 117
    • 45549085141 scopus 로고    scopus 로고
    • Disorders of neutrophil function: An overview
    • Dinauer MC. Disorders of neutrophil function: an overview. Methods Mol Biol 2007; 412: 489-504.
    • (2007) Methods Mol Biol , vol.412 , pp. 489-504
    • Dinauer, M.C.1
  • 118
    • 79957890939 scopus 로고    scopus 로고
    • Combating oxidative stress in vascular disease: NADPH oxidases as therapeutic targets
    • Drummond GR, Selemidis S, Griendling KK, Sobey CG. Combating oxidative stress in vascular disease: NADPH oxidases as therapeutic targets. Nat Rev Drug Discov 2011; 10(6): 453-71.
    • (2011) Nat Rev Drug Discov , vol.10 , Issue.6 , pp. 453-471
    • Drummond, G.R.1    Selemidis, S.2    Griendling, K.K.3    Sobey, C.G.4
  • 120
    • 79953881843 scopus 로고    scopus 로고
    • The E-loop is involved in hydrogen peroxide formation by the NADPH oxidase Nox4
    • Takac I, Schroder K, Zhang L, et al. The E-loop is involved in hydrogen peroxide formation by the NADPH oxidase Nox4. J Biol Chem 2011; 286(15): 13304-13.
    • (2011) J Biol Chem , vol.286 , Issue.15 , pp. 13304-13313
    • Takac, I.1    Schroder, K.2    Zhang, L.3
  • 121
    • 0035921417 scopus 로고    scopus 로고
    • Tyrosine cross-linking of extracellular matrix is catalyzed by Duox, a multidomain oxidase/peroxidase with homology to the phagocyte oxidase subunit gp91phox
    • Edens WA, Sharling L, Cheng G, et al. Tyrosine cross-linking of extracellular matrix is catalyzed by Duox, a multidomain oxidase/peroxidase with homology to the phagocyte oxidase subunit gp91phox. J Cell Biol 2001; 154(4): 879-91.
    • (2001) J Cell Biol , vol.154 , Issue.4 , pp. 879-891
    • Edens, W.A.1    Sharling, L.2    Cheng, G.3
  • 122
    • 77949593677 scopus 로고    scopus 로고
    • Targeting and regulation of reactive oxygen species generation by Nox family NADPH oxidases
    • Leto TL, Morand S, Hurt D, Ueyama T. Targeting and regulation of reactive oxygen species generation by Nox family NADPH oxidases. Antioxid Redox Signal 2009; 11(10): 2607-19.
    • (2009) Antioxid Redox Signal , vol.11 , Issue.10 , pp. 2607-2619
    • Leto, T.L.1    Morand, S.2    Hurt, D.3    Ueyama, T.4
  • 123
    • 65349172964 scopus 로고    scopus 로고
    • Duox maturation factors form cell surface complexes with Duox affecting the specificity of reactive oxygen species generation
    • Morand S, Ueyama T, Tsujibe S, Saito N, Korzeniowska A, Leto TL. Duox maturation factors form cell surface complexes with Duox affecting the specificity of reactive oxygen species generation. FASEB J 2009; 23(4): 1205-18.
    • (2009) FASEB J , vol.23 , Issue.4 , pp. 1205-1218
    • Morand, S.1    Ueyama, T.2    Tsujibe, S.3    Saito, N.4    Korzeniowska, A.5    Leto, T.L.6
  • 124
    • 33645285957 scopus 로고    scopus 로고
    • Regulation of NADPH oxidases: The role of Rac proteins
    • Hordijk PL. Regulation of NADPH oxidases: the role of Rac proteins. Circ Res 2006; 98(4): 453-62.
    • (2006) Circ Res , vol.98 , Issue.4 , pp. 453-462
    • Hordijk, P.L.1
  • 125
    • 42549085269 scopus 로고    scopus 로고
    • NADPH oxidasederived reactive oxygen species in the regulation of endothelial phenotype
    • Dworakowski R, Alom-Ruiz SP, Shah AM. NADPH oxidasederived reactive oxygen species in the regulation of endothelial phenotype. Pharmacol Rep 2008; 60(1): 21-8.
    • (2008) Pharmacol Rep , vol.60 , Issue.1 , pp. 21-28
    • Dworakowski, R.1    Alom-Ruiz, S.P.2    Shah, A.M.3
  • 126
    • 77950896739 scopus 로고    scopus 로고
    • NADPH oxidases: Functions and pathologies in the vasculature
    • Lassegue B, Griendling KK. NADPH oxidases: functions and pathologies in the vasculature. Arterioscler Thromb Vasc Biol 2010; 30(4): 653-61.
    • (2010) Arterioscler Thromb Vasc Biol , vol.30 , Issue.4 , pp. 653-661
    • Lassegue, B.1    Griendling, K.K.2
  • 127
    • 34547791794 scopus 로고    scopus 로고
    • Adventitial fibroblast reactive oxygen species as autacrine and paracrine mediators of remodeling: Bellwether for vascular disease?
    • Haurani MJ, Pagano PJ. Adventitial fibroblast reactive oxygen species as autacrine and paracrine mediators of remodeling: bellwether for vascular disease? Cardiovasc Res 2007; 75(4): 679-89.
    • (2007) Cardiovasc Res , vol.75 , Issue.4 , pp. 679-689
    • Haurani, M.J.1    Pagano, P.J.2
  • 128
    • 56149093044 scopus 로고    scopus 로고
    • NADPH oxidases in the vasculature: Molecular features, roles in disease and pharmacological inhibition
    • Selemidis S, Sobey CG, Wingler K, Schmidt HH, Drummond GR. NADPH oxidases in the vasculature: molecular features, roles in disease and pharmacological inhibition. Pharmacol Ther 2008; 120(3): 254-91.
    • (2008) Pharmacol Ther , vol.120 , Issue.3 , pp. 254-291
    • Selemidis, S.1    Sobey, C.G.2    Wingler, K.3    Schmidt, H.H.4    Drummond, G.R.5
  • 130
    • 0035980160 scopus 로고    scopus 로고
    • Novel competitive inhibitor of NAD(P)H oxidase assembly attenuates vascular O(2)(-) and systolic blood pressure in mice
    • Rey FE, Cifuentes ME, Kiarash A, Quinn MT, Pagano PJ. Novel competitive inhibitor of NAD(P)H oxidase assembly attenuates vascular O(2)(-) and systolic blood pressure in mice. Cirs Res 2001; 89(5): 408-14.
    • (2001) Cirs Res , vol.89 , Issue.5 , pp. 408-414
    • Rey, F.E.1    Cifuentes, M.E.2    Kiarash, A.3    Quinn, M.T.4    Pagano, P.J.5
  • 131
    • 27444447834 scopus 로고    scopus 로고
    • Nox1 overexpression potentiates angiotensin II-induced hypertension and vascular smooth muscle hypertrophy in transgenic mice
    • Dikalova A, Clempus R, Lassegue B, et al. Nox1 overexpression potentiates angiotensin II-induced hypertension and vascular smooth muscle hypertrophy in transgenic mice. Circulation 2005; 112(17): 2668-76.
    • (2005) Circulation , vol.112 , Issue.17 , pp. 2668-2676
    • Dikalova, A.1    Clempus, R.2    Lassegue, B.3
  • 132
    • 77956671191 scopus 로고    scopus 로고
    • Upregulation of Nox1 in vascular smooth muscle leads to impaired endothelium-dependent relaxation via eNOS uncoupling
    • Dikalova AE, Gongora MC, Harrison DG, Lambeth JD, Dikalov S, Griendling KK. Upregulation of Nox1 in vascular smooth muscle leads to impaired endothelium-dependent relaxation via eNOS uncoupling. Am J Physiol 2010; 299(3): H673-9.
    • (2010) Am J Physiol , vol.299 , Issue.3 , pp. H673-H679
    • Dikalova, A.E.1    Gongora, M.C.2    Harrison, D.G.3    Lambeth, J.D.4    Dikalov, S.5    Griendling, K.K.6
  • 133
    • 30644458693 scopus 로고    scopus 로고
    • Decreased blood pressure in NOX1-deficient mice
    • Gavazzi G, Banfi B, Deffert C, et al. Decreased blood pressure in NOX1-deficient mice. FEBS Lett 2006; 580(2): 497-504.
    • (2006) FEBS Lett , vol.580 , Issue.2 , pp. 497-504
    • Gavazzi, G.1    Banfi, B.2    Deffert, C.3
  • 134
    • 27444441677 scopus 로고    scopus 로고
    • Nox1 is involved in angiotensin II-mediated hypertension: A study in Nox1-deficient mice
    • Matsuno K, Yamada H, Iwata K, et al. Nox1 is involved in angiotensin II-mediated hypertension: a study in Nox1-deficient mice. Circulation 2005; 112(17): 2677-85.
    • (2005) Circulation , vol.112 , Issue.17 , pp. 2677-2685
    • Matsuno, K.1    Yamada, H.2    Iwata, K.3
  • 135
    • 33750926794 scopus 로고    scopus 로고
    • Role of Nox family NADPH oxidases in host defense
    • Leto TL, Geiszt M. Role of Nox family NADPH oxidases in host defense. Antioxid Redox Signal 2006; 8(9-10): 1549-61.
    • (2006) Antioxid Redox Signal , vol.8 , Issue.9-10 , pp. 1549-1561
    • Leto, T.L.1    Geiszt, M.2
  • 136
    • 84865818831 scopus 로고    scopus 로고
    • Erythrocytes, leukocytes and platelets as a source of oxidative stress in chronic vascular diseases: Detoxifying mechanisms and potential therapeutic options
    • Martin-Ventura JL, Madrigal-Matute J, Martinez-Pinna R, et al. Erythrocytes, leukocytes and platelets as a source of oxidative stress in chronic vascular diseases: detoxifying mechanisms and potential therapeutic options. Thromb Haemost 2012; 108(3): 435-42.
    • (2012) Thromb Haemost , vol.108 , Issue.3 , pp. 435-442
    • Martin-Ventura, J.L.1    Madrigal-Matute, J.2    Martinez-Pinna, R.3
  • 137
    • 84877589196 scopus 로고    scopus 로고
    • Erythrocyte NADPH oxidase activity modulated by Rac GTPases, PKC, and plasma cytokines contributes to oxidative stress in sickle cell disease
    • George A, Pushkaran S, Konstantinidis DG, et al. Erythrocyte NADPH oxidase activity modulated by Rac GTPases, PKC, and plasma cytokines contributes to oxidative stress in sickle cell disease. Blood 2013; 121(11): 2099-107.
    • (2013) Blood , vol.121 , Issue.11 , pp. 2099-2107
    • George, A.1    Pushkaran, S.2    Konstantinidis, D.G.3
  • 139
    • 17944369584 scopus 로고    scopus 로고
    • Involvement of NADH/NADPH oxidase in human platelet ROS production
    • Seno T, Inoue N, Gao D, et al. Involvement of NADH/NADPH oxidase in human platelet ROS production. Thromb Res 2001; 103(5): 399-409.
    • (2001) Thromb Res , vol.103 , Issue.5 , pp. 399-409
    • Seno, T.1    Inoue, N.2    Gao, D.3
  • 140
    • 77957596612 scopus 로고    scopus 로고
    • The anti-platelet effects of apocynin in mice are not mediated by inhibition of NADPH oxidase activity
    • Dharmarajah J, Arthur JF, Sobey CG, Drummond GR. The anti-platelet effects of apocynin in mice are not mediated by inhibition of NADPH oxidase activity. Naunyn Schmiedebergs Arch Pharmacol 2010; 382(4): 377-84.
    • (2010) Naunyn Schmiedebergs Arch Pharmacol , vol.382 , Issue.4 , pp. 377-384
    • Dharmarajah, J.1    Arthur, J.F.2    Sobey, C.G.3    Drummond, G.R.4
  • 141
    • 4444294006 scopus 로고    scopus 로고
    • Gp91phox-dependent expression of platelet CD40 ligand
    • Pignatelli P, Sanguigni V, Lenti L, et al. gp91phox-dependent expression of platelet CD40 ligand. Circulation 2004; 110(10): 1326-9.
    • (2004) Circulation , vol.110 , Issue.10 , pp. 1326-1329
    • Pignatelli, P.1    Sanguigni, V.2    Lenti, L.3
  • 142
    • 84872869398 scopus 로고    scopus 로고
    • The novel NOX inhibitor 2-acetylphenothiazine impairs collagen-dependent thrombus formation in a GPVI-dependent manner
    • Vara D, Campanella M, Pula G. The novel NOX inhibitor 2-acetylphenothiazine impairs collagen-dependent thrombus formation in a GPVI-dependent manner. Br J Pharmacol 2013; 168(1): 212-24.
    • (2013) Br J Pharmacol , vol.168 , Issue.1 , pp. 212-224
    • Vara, D.1    Campanella, M.2    Pula, G.3
  • 143
    • 33750200993 scopus 로고    scopus 로고
    • Tetrahydrobiopterin and cardiovascular disease
    • Moens AL, Kass DA. Tetrahydrobiopterin and cardiovascular disease. Arterioscler Thromb Vasc Biol 2006; 26(11): 2439-44.
    • (2006) Arterioscler Thromb Vasc Biol , vol.26 , Issue.11 , pp. 2439-2444
    • Moens, A.L.1    Kass, D.A.2
  • 144
    • 47649122637 scopus 로고    scopus 로고
    • Reversal of cardiac hypertrophy and fibrosis from pressure overload by tetrahydrobiopterin: Efficacy of recoupling nitric oxide synthase as a therapeutic strategy
    • Moens AL, Takimoto E, Tocchetti CG, et al. Reversal of cardiac hypertrophy and fibrosis from pressure overload by tetrahydrobiopterin: efficacy of recoupling nitric oxide synthase as a therapeutic strategy. Circulation 2008; 117(20): 2626-36.
    • (2008) Circulation , vol.117 , Issue.20 , pp. 2626-2636
    • Moens, A.L.1    Takimoto, E.2    Tocchetti, C.G.3
  • 145
    • 67449085150 scopus 로고    scopus 로고
    • Role of urate, xanthine oxidase and the effects of allopurinol in vascular oxidative stress
    • George J, Struthers AD. Role of urate, xanthine oxidase and the effects of allopurinol in vascular oxidative stress. Vasc Health Risk Manag 2009; 5(1): 265-72.
    • (2009) Vasc Health Risk Manag , vol.5 , Issue.1 , pp. 265-272
    • George, J.1    Struthers, A.D.2
  • 146
    • 79957951218 scopus 로고    scopus 로고
    • Febuxostat inhibition of endothelial-bound XO: Implications for targeting vascular ROS production
    • Malik UZ, Hundley NJ, Romero G, et al. Febuxostat inhibition of endothelial-bound XO: implications for targeting vascular ROS production. Free Radic Biol Med 2011; 51(1): 179-84.
    • (2011) Free Radic Biol Med , vol.51 , Issue.1 , pp. 179-184
    • Malik, U.Z.1    Hundley, N.J.2    Romero, G.3
  • 148
    • 44949262935 scopus 로고    scopus 로고
    • Mammalian xanthine oxidoreductase-mechanism of transition from xanthine dehydrogenase to xanthine oxidase
    • Nishino T, Okamoto K, Eger BT, Pai EF, Nishino T. Mammalian xanthine oxidoreductase-mechanism of transition from xanthine dehydrogenase to xanthine oxidase. FEBS J 2008; 275(13): 3278-89.
    • (2008) FEBS J , vol.275 , Issue.13 , pp. 3278-3289
    • Nishino, T.1    Okamoto, K.2    Eger, B.T.3    Pai, E.F.4    Nishino, T.5
  • 149
    • 33751200338 scopus 로고    scopus 로고
    • Acute effects of febuxostat, a nonpurine selective inhibitor of xanthine oxidase, in pacing induced heart failure
    • Hou M, Hu Q, Chen Y, Zhao L, Zhang J, Bache RJ. Acute effects of febuxostat, a nonpurine selective inhibitor of xanthine oxidase, in pacing induced heart failure. J Cardiovasc Pharmacol 2006; 48(5): 255-63.
    • (2006) J Cardiovasc Pharmacol , vol.48 , Issue.5 , pp. 255-263
    • Hou, M.1    Hu, Q.2    Chen, Y.3    Zhao, L.4    Zhang, J.5    Bache, R.J.6
  • 150
    • 33749819577 scopus 로고    scopus 로고
    • Oxidative stressassociated vascular aging is xanthine oxidase-dependent but not NAD(P)H oxidase-dependent
    • Newaz MA, Yousefipour Z, Oyekan A. Oxidative stressassociated vascular aging is xanthine oxidase-dependent but not NAD(P)H oxidase-dependent. J Cardiovasc Pharmacol 2006; 48(3): 88-94.
    • (2006) J Cardiovasc Pharmacol , vol.48 , Issue.3 , pp. 88-94
    • Newaz, M.A.1    Yousefipour, Z.2    Oyekan, A.3
  • 151
    • 0037469205 scopus 로고    scopus 로고
    • Xanthine oxidase inhibition reverses endothelial dysfunction in heavy smokers
    • Guthikonda S, Sinkey C, Barenz T, Haynes WG. Xanthine oxidase inhibition reverses endothelial dysfunction in heavy smokers. Circulation 2003; 107(3): 416-21.
    • (2003) Circulation , vol.107 , Issue.3 , pp. 416-421
    • Guthikonda, S.1    Sinkey, C.2    Barenz, T.3    Haynes, W.G.4
  • 152
    • 44649122196 scopus 로고    scopus 로고
    • Impact of oxypurinol in patients with symptomatic heart failure. Results of the OPTCHF study
    • Hare JM, Mangal B, Brown J, et al. Impact of oxypurinol in patients with symptomatic heart failure. Results of the OPTCHF study. J Am Coll Cardiol 2008; 51(24): 2301-9.
    • (2008) J am Coll Cardiol , vol.51 , Issue.24 , pp. 2301-2309
    • Hare, J.M.1    Mangal, B.2    Brown, J.3
  • 154
    • 55149124723 scopus 로고    scopus 로고
    • Xanthine oxidase inhibition with febuxostat attenuates systolic overload-induced left ventricular hypertrophy and dysfunction in mice
    • Xu X, Hu X, Lu Z, et al. Xanthine oxidase inhibition with febuxostat attenuates systolic overload-induced left ventricular hypertrophy and dysfunction in mice. J Card Fail 2008; 14(9): 746-53.
    • (2008) J Card Fail , vol.14 , Issue.9 , pp. 746-753
    • Xu, X.1    Hu, X.2    Lu, Z.3
  • 155
    • 0142150051 scopus 로고    scopus 로고
    • Mitochondrial formation of reactive oxygen species
    • Turrens JF. Mitochondrial formation of reactive oxygen species. J Physiol 2003; 552(Pt 2): 335-44.
    • (2003) J Physiol , vol.552 , Issue.2 , pp. 335-344
    • Turrens, J.F.1
  • 156
    • 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 NS, McClintock DS, Feliciano CE, et al. 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): 25130-8.
    • (2000) J Biol Chem , vol.275 , Issue.33 , pp. 25130-25138
    • Chandel, N.S.1    McClintock, D.S.2    Feliciano, C.E.3
  • 157
    • 10344221083 scopus 로고    scopus 로고
    • Releases superoxide to both sides of the inner mitochondrial membrane
    • Muller FL, Liu Y, Van Remmen H. Complex III releases superoxide to both sides of the inner mitochondrial membrane. J Biol Chem 2004; 279(47): 49064-73.
    • (2004) J Biol Chem , vol.279 , Issue.47 , pp. 49064-49073
    • Muller, F.L.1    Liu, Y.2    Van Remmen, H.3    Complex, I.4
  • 158
    • 0021996572 scopus 로고
    • Ubisemiquinone is the electron donor for superoxide formation by complex III of heart mitochondria
    • Turrens JF, Alexandre A, Lehninger AL. Ubisemiquinone is the electron donor for superoxide formation by complex III of heart mitochondria. Arch Biochem Biophys 1985; 237(2): 408-14.
    • (1985) Arch Biochem Biophys , vol.237 , Issue.2 , pp. 408-414
    • Turrens, J.F.1    Alexandre, A.2    Lehninger, A.L.3
  • 159
    • 0025358947 scopus 로고
    • The protonmotive Q cycle. Energy transduction by coupling of proton translocation to electron transfer by the cytochrome bc1 complex
    • Trumpower BL. The protonmotive Q cycle. Energy transduction by coupling of proton translocation to electron transfer by the cytochrome bc1 complex. J Biol Chem 1990; 265(20): 11409-12.
    • (1990) J Biol Chem , vol.265 , Issue.20 , pp. 11409-11412
    • Trumpower, B.L.1
  • 160
    • 0029053451 scopus 로고
    • Superoxide radical and superoxide dismutases
    • Fridovich I. Superoxide radical and superoxide dismutases. Annu Rev Biochem 1995; 64: 97-112.
    • (1995) Annu Rev Biochem , vol.64 , pp. 97-112
    • Fridovich, I.1
  • 161
    • 0035914342 scopus 로고    scopus 로고
    • Subcellular distribution of superoxide dismutases (SOD) in rat liver: Cu,Zn-SOD in mitochondria
    • Okado-Matsumoto A, Fridovich I. Subcellular distribution of superoxide dismutases (SOD) in rat liver: Cu,Zn-SOD in mitochondria. J Biol Chem 2001; 276(42): 38388-93.
    • (2001) J Biol Chem , vol.276 , Issue.42 , pp. 38388-38393
    • Okado-Matsumoto, A.1    Fridovich, I.2
  • 163
    • 33847180453 scopus 로고    scopus 로고
    • Cyclooxygenase-2 does not contribute to postischemic production of reactive oxygen species
    • Kunz A, Anrather J, Zhou P, Orio M, Iadecola C. Cyclooxygenase-2 does not contribute to postischemic production of reactive oxygen species. J Cereb Blood Flow Metab 2007; 27(3): 545-51.
    • (2007) J Cereb Blood Flow Metab , vol.27 , Issue.3 , pp. 545-551
    • Kunz, A.1    Anrather, J.2    Zhou, P.3    Orio, M.4    Iadecola, C.5
  • 164
    • 4444356653 scopus 로고    scopus 로고
    • Arachidonic acidinduced carbon-centered radicals and phospholipid peroxidation in cyclo-oxygenase-2-transfected PC12 cells
    • Jiang J, Borisenko GG, Osipov A, et al. Arachidonic acidinduced carbon-centered radicals and phospholipid peroxidation in cyclo-oxygenase-2-transfected PC12 cells. J Neurochem 2004; 90(5): 1036-49.
    • (2004) J Neurochem , vol.90 , Issue.5 , pp. 1036-1049
    • Jiang, J.1    Borisenko, G.G.2    Osipov, A.3
  • 165
    • 80053616414 scopus 로고    scopus 로고
    • Reciprocal regulation of NADPH oxidases and the cyclooxygenase-2 pathway
    • Sancho P, Martin-Sanz P, Fabregat I. Reciprocal regulation of NADPH oxidases and the cyclooxygenase-2 pathway. Free Radic Biol Med 2011; 51(9): 1789-98.
    • (2011) Free Radic Biol Med , vol.51 , Issue.9 , pp. 1789-1798
    • Sancho, P.1    Martin-Sanz, P.2    Fabregat, I.3
  • 166
    • 34247608691 scopus 로고    scopus 로고
    • Calcium and reactive oxygen species increase in endothelial cells in response to releasers of endothelium-derived contracting factor
    • Tang EH, Leung FP, Huang Y, et al. Calcium and reactive oxygen species increase in endothelial cells in response to releasers of endothelium-derived contracting factor. Br J Pharmacol 2007; 151(1): 15-23.
    • (2007) Br J Pharmacol , vol.151 , Issue.1 , pp. 15-23
    • Tang, E.H.1    Leung, F.P.2    Huang, Y.3
  • 167
    • 0036264483 scopus 로고    scopus 로고
    • Oxygen-derived free radicals mediate endothelium-dependent contractions to acetylcholine in aortas from spontaneously hypertensive rats
    • Yang D, Feletou M, Boulanger CM, et al. Oxygen-derived free radicals mediate endothelium-dependent contractions to acetylcholine in aortas from spontaneously hypertensive rats. Br J Pharmacol 2002; 136(1): 104-10.
    • (2002) Br J Pharmacol , vol.136 , Issue.1 , pp. 104-110
    • Yang, D.1    Feletou, M.2    Boulanger, C.M.3
  • 168
    • 0037219457 scopus 로고    scopus 로고
    • A diffusible substance(S) mediates endothelium-dependent contractions in the aorta of SHR
    • Yang D, Feletou M, Levens N, Zhang JN, Vanhoutte PM. A diffusible substance(s) mediates endothelium-dependent contractions in the aorta of SHR. Hypertension 2003; 41(1): 143-8.
    • (2003) Hypertension , vol.41 , Issue.1 , pp. 143-148
    • Yang, D.1    Feletou, M.2    Levens, N.3    Zhang, J.N.4    Vanhoutte, P.M.5
  • 169
    • 0345479153 scopus 로고    scopus 로고
    • Reactive oxygen species mediate arachidonic acid-induced dilation in porcine coronary microvessels
    • Oltman CL, Kane NL, Miller FJ, Jr., Spector AA, Weintraub NL, Dellsperger KC. Reactive oxygen species mediate arachidonic acid-induced dilation in porcine coronary microvessels. Am J Physiol 2003; 285(6): H2309-15.
    • (2003) Am J Physiol , vol.285 , Issue.6 , pp. H2309-H2315
    • Oltman, C.L.1    Kane, N.L.2    Miller, F.J.3    Spector, A.A.4    Weintraub, N.L.5    Dellsperger, K.C.6
  • 170
    • 84870519907 scopus 로고    scopus 로고
    • Reciprocal relationship between reactive oxygen species and cyclooxygenase-2 and vascular dysfunction in hypertension
    • Martinez-Revelles S, Avendano MS, Garcia-Redondo AB, et al. Reciprocal relationship between reactive oxygen species and cyclooxygenase-2 and vascular dysfunction in hypertension. Antioxid Redox Signal 2013; 18(1): 51-65.
    • (2013) Antioxid Redox Signal , vol.18 , Issue.1 , pp. 51-65
    • Martinez-Revelles, S.1    Avendano, M.S.2    Garcia-Redondo, A.B.3
  • 171
    • 79952695168 scopus 로고    scopus 로고
    • Bioactive lipoxygenase metabolites stimulation of NADPH oxidases and reactive oxygen species
    • Cho KJ, Seo JM, Kim JH. Bioactive lipoxygenase metabolites stimulation of NADPH oxidases and reactive oxygen species. Mol Cells 2011; 32(1): 1-5.
    • (2011) Mol Cells , vol.32 , Issue.1 , pp. 1-5
    • Cho, K.J.1    Seo, J.M.2    Kim, J.H.3
  • 172
    • 77953334791 scopus 로고    scopus 로고
    • 5-Lipoxygenase plays an essential role in 4-HNE-enhanced ROS production in murine macrophages via activation of NADPH oxidase
    • Yun MR, Park HM, Seo KW, Lee SJ, Im DS, Kim CD. 5-Lipoxygenase plays an essential role in 4-HNE-enhanced ROS production in murine macrophages via activation of NADPH oxidase. Free Rad Res 2010; 44(7): 742-50.
    • (2010) Free Rad Res , vol.44 , Issue.7 , pp. 742-750
    • Yun, M.R.1    Park, H.M.2    Seo, K.W.3    Lee, S.J.4    Im, D.S.5    Kim, C.D.6
  • 173
    • 78650535640 scopus 로고    scopus 로고
    • Metabolites and analogs induce lipoxygenase mRNA expression and activity as well as reactive oxygen species (ROS) production in human bone cell line
    • Somjen D, Katzburg S, Grafi-Cohen M, Knoll E, Sharon O, Posner GH. Vitamin D metabolites and analogs induce lipoxygenase mRNA expression and activity as well as reactive oxygen species (ROS) production in human bone cell line. J Steroid Biochem Mol Biol 2011; 123(1-2): 85-9.
    • (2011) J Steroid Biochem Mol Biol , vol.123 , Issue.1-2 , pp. 85-89
    • Somjen, D.1    Katzburg, S.2    Grafi-Cohen, M.3    Knoll, E.4    Sharon, O.5    Posner, G.H.6    Vitamin, D.7
  • 174
    • 84874282084 scopus 로고    scopus 로고
    • 12/15-Lipoxygenasederived lipid metabolites induce retinal endothelial cell barrier dysfunction: Contribution of NADPH oxidase
    • Othman A, Ahmad S, Megyerdi S, et al. 12/15-Lipoxygenasederived lipid metabolites induce retinal endothelial cell barrier dysfunction: contribution of NADPH oxidase. PLoS One 2013; 8(2): e57254.
    • (2013) Plos One , vol.8 , Issue.2
    • Othman, A.1    Ahmad, S.2    Megyerdi, S.3
  • 175
    • 62149118589 scopus 로고    scopus 로고
    • Lysophosphatidylcholine enhances oxidative stress via the 5-lipoxygenase pathway in rat aorta during aging
    • Zou Y, Kim DH, Jung KJ, et al. Lysophosphatidylcholine enhances oxidative stress via the 5-lipoxygenase pathway in rat aorta during aging. Rejuvenation Res 2009; 12(1): 15-24.
    • (2009) Rejuvenation Res , vol.12 , Issue.1 , pp. 15-24
    • Zou, Y.1    Kim, D.H.2    Jung, K.J.3
  • 176
    • 84894448724 scopus 로고    scopus 로고
    • Inhibition of 12-lipoxygenase reduces platelet activation and prevents their mitogenic function
    • Svensson Holm AC, Grenegard M, Ollinger K, Lindstrom EG. Inhibition of 12-lipoxygenase reduces platelet activation and prevents their mitogenic function. Platelets 2014; 25(2): 111-7.
    • (2014) Platelets , vol.25 , Issue.2 , pp. 111-117
    • Svensson Holm, A.C.1    Grenegard, M.2    Ollinger, K.3    Lindstrom, E.G.4
  • 177
    • 65249151456 scopus 로고    scopus 로고
    • Structural analysis of fish versus mammalian hemoglobins: Effect of the heme pocket environment on autooxidation and hemin loss
    • Aranda Rt, Cai H, Worley CE, et al. Structural analysis of fish versus mammalian hemoglobins: effect of the heme pocket environment on autooxidation and hemin loss. Proteins 2009; 75(1): 217-30.
    • (2009) Proteins , vol.75 , Issue.1 , pp. 217-230
    • Rt, A.1    Cai, H.2    Worley, C.E.3
  • 178
    • 77953961138 scopus 로고    scopus 로고
    • Red cells, hemoglobin, heme, iron, and atherogenesis
    • Nagy E, Eaton JW, Jeney V, et al. Red cells, hemoglobin, heme, iron, and atherogenesis. Arterioscler Thromb Vasc Biol 2010; 30(7): 1347-53.
    • (2010) Arterioscler Thromb Vasc Biol , vol.30 , Issue.7 , pp. 1347-1353
    • Nagy, E.1    Eaton, J.W.2    Jeney, V.3
  • 179
    • 34648860530 scopus 로고    scopus 로고
    • Free hemoglobin: A dangerous signal for the immune system in patients with carotid atherosclerosis?
    • Buttari B, Profumo E, Petrone L, et al. Free hemoglobin: a dangerous signal for the immune system in patients with carotid atherosclerosis? Ann N Y Acad Sci 2007; 1107: 42-50.
    • (2007) Ann N Y Acad Sci , vol.1107 , pp. 42-50
    • Buttari, B.1    Profumo, E.2    Petrone, L.3
  • 180
    • 76049083966 scopus 로고    scopus 로고
    • Reactive oxygen species, cellular redox systems, and apoptosis
    • Circu ML, Aw TY. Reactive oxygen species, cellular redox systems, and apoptosis. Free Radic Biol Med 2010; 48(6): 749-62.
    • (2010) Free Radic Biol Med , vol.48 , Issue.6 , pp. 749-762
    • Circu, M.L.1    Aw, T.Y.2
  • 181
    • 0036478970 scopus 로고    scopus 로고
    • Mitochondrial reactive oxygen species in cell death signaling
    • Fleury C, Mignotte B, Vayssiere JL. Mitochondrial reactive oxygen species in cell death signaling. Biochimie 2002; 84(2-3): 131-41.
    • (2002) Biochimie , vol.84 , Issue.2-3 , pp. 131-141
    • Fleury, C.1    Mignotte, B.2    Vayssiere, J.L.3
  • 182
    • 0344304669 scopus 로고    scopus 로고
    • Redox-dependent signalling by angiotensin II and vascular remodelling in hypertension
    • Touyz RM, Tabet F, Schiffrin EL. Redox-dependent signalling by angiotensin II and vascular remodelling in hypertension. Clin Exp Pharmacol Physiol 2003; 30(11): 860-6.
    • (2003) Clin Exp Pharmacol Physiol , vol.30 , Issue.11 , pp. 860-866
    • Touyz, R.M.1    Tabet, F.2    Schiffrin, E.L.3
  • 183
    • 83455185433 scopus 로고    scopus 로고
    • Reactive oxygen species and endothelial function--role of nitric oxide synthase uncoupling and Nox family nicotinamide adenine dinucleotide phosphate oxidases
    • Montezano AC, Touyz RM. Reactive oxygen species and endothelial function--role of nitric oxide synthase uncoupling and Nox family nicotinamide adenine dinucleotide phosphate oxidases. Basic Clin Pharm Tox 2012; 110(1): 87-94.
    • (2012) Basic Clin Pharm Tox , vol.110 , Issue.1 , pp. 87-94
    • Montezano, A.C.1    Touyz, R.M.2
  • 184
    • 33750475625 scopus 로고    scopus 로고
    • Free radicals, mitochondria, and oxidized lipids: The emerging role in signal transduction in vascular cells
    • Gutierrez J, Ballinger SW, Darley-Usmar VM, Landar A. Free radicals, mitochondria, and oxidized lipids: the emerging role in signal transduction in vascular cells. Circ Res 2006; 99(9): 924-32.
    • (2006) Circ Res , vol.99 , Issue.9 , pp. 924-932
    • Gutierrez, J.1    Ballinger, S.W.2    Darley-Usmar, V.M.3    Landar, A.4
  • 185
    • 77952480033 scopus 로고    scopus 로고
    • Role of reactive oxygen species in the progression of type 2 diabetes and atherosclerosis
    • Kaneto H, Katakami N, Matsuhisa M, Matsuoka TA. Role of reactive oxygen species in the progression of type 2 diabetes and atherosclerosis. Mediators Inflamm 2010; 2010: 453892.
    • (2010) Mediators Inflamm , pp. 2010
    • Kaneto, H.1    Katakami, N.2    Matsuhisa, M.3    Matsuoka, T.A.4
  • 186
    • 84861234894 scopus 로고    scopus 로고
    • Mitochondrial reactive oxygen species and risk of atherosclerosis
    • Hulsmans M, Van Dooren E, Holvoet P. Mitochondrial reactive oxygen species and risk of atherosclerosis. Curr Atheroscler Rep 2012; 14(3): 264-76.
    • (2012) Curr Atheroscler Rep , vol.14 , Issue.3 , pp. 264-276
    • Hulsmans, M.1    Van Dooren, E.2    Holvoet, P.3
  • 187
    • 80051666038 scopus 로고    scopus 로고
    • Reactive oxygen species in cardiovascular disease
    • Sugamura K, Keaney JF, Jr. Reactive oxygen species in cardiovascular disease. Free Radic Biol Med 2011; 51(5): 978-92.
    • (2011) Free Radic Biol Med , vol.51 , Issue.5 , pp. 978-992
    • Sugamura, K.1    Keaney, J.F.2
  • 188
    • 0015596284 scopus 로고
    • Biological defense mechanisms. The production by leukocytes of superoxide, a potential bactericidal agent
    • Babior BM, Kipnes RS, Curnutte JT. Biological defense mechanisms. The production by leukocytes of superoxide, a potential bactericidal agent. J Clin Invest 1973; 52(3): 741-4.
    • (1973) J Clin Invest , vol.52 , Issue.3 , pp. 741-744
    • Babior, B.M.1    Kipnes, R.S.2    Curnutte, J.T.3
  • 189
    • 0016391727 scopus 로고
    • Defective superoxide production by granulocytes from patients with chronic granulomatous disease
    • Curnutte JT, Whitten DM, Babior BM. Defective superoxide production by granulocytes from patients with chronic granulomatous disease. N Engl J Med 1974; 290(11): 593-7.
    • (1974) N Engl J Med , vol.290 , Issue.11 , pp. 593-597
    • Curnutte, J.T.1    Whitten, D.M.2    Babior, B.M.3
  • 191
    • 1542406446 scopus 로고    scopus 로고
    • NOX enzymes and the biology of reactive oxygen
    • Lambeth JD. NOX enzymes and the biology of reactive oxygen. Nat Rev Immunol 2004; 4(3): 181-9.
    • (2004) Nat Rev Immunol , vol.4 , Issue.3 , pp. 181-189
    • Lambeth, J.D.1
  • 192
    • 9144257277 scopus 로고    scopus 로고
    • Tissue distribution and putative physiological function of NOX family NADPH oxidases
    • Krause KH. Tissue distribution and putative physiological function of NOX family NADPH oxidases. Jpn J Infect Dis 2004; 57(5): S28-9.
    • (2004) Jpn J Infect Dis , vol.57 , Issue.5 , pp. S28-S29
    • Krause, K.H.1
  • 193
    • 0038205912 scopus 로고    scopus 로고
    • NAD(P)H oxidase 1, a product of differentiated colon epithelial cells, can partially replace glycoprotein 91phox in the regulated production of superoxide by phagocytes
    • Geiszt M, Lekstrom K, Brenner S, et al. NAD(P)H oxidase 1, a product of differentiated colon epithelial cells, can partially replace glycoprotein 91phox in the regulated production of superoxide by phagocytes. J Immunol 2003; 171(1): 299-306.
    • (2003) J Immunol , vol.171 , Issue.1 , pp. 299-306
    • Geiszt, M.1    Lekstrom, K.2    Brenner, S.3
  • 194
    • 0034977290 scopus 로고    scopus 로고
    • Type I Helicobacter pylori lipopolysaccharide stimulates toll-like receptor 4 and activates mitogen oxidase 1 in gastric pit cells
    • Kawahara T, Teshima S, Oka A, Sugiyama T, Kishi K, Rokutan K. Type I Helicobacter pylori lipopolysaccharide stimulates toll-like receptor 4 and activates mitogen oxidase 1 in gastric pit cells. Infect Immun 2001; 69(7): 4382-9.
    • (2001) Infect Immun , vol.69 , Issue.7 , pp. 4382-4389
    • Kawahara, T.1    Teshima, S.2    Oka, A.3    Sugiyama, T.4    Kishi, K.5    Rokutan, K.6
  • 195
    • 0042203535 scopus 로고    scopus 로고
    • Dual oxidases represent novel hydrogen peroxide sources supporting mucosal surface host defense
    • Geiszt M, Witta J, Baffi J, Lekstrom K, Leto TL. Dual oxidases represent novel hydrogen peroxide sources supporting mucosal surface host defense. FASEB J 2003; 17(11): 1502-4.
    • (2003) FASEB J , vol.17 , Issue.11 , pp. 1502-1504
    • Geiszt, M.1    Witta, J.2    Baffi, J.3    Lekstrom, K.4    Leto, T.L.5
  • 196
    • 4844227764 scopus 로고    scopus 로고
    • Antimicrobial reactive oxygen and nitrogen species: Concepts and controversies
    • Fang FC. Antimicrobial reactive oxygen and nitrogen species: concepts and controversies. Nat Rev Microbiol 2004; 2(10): 820-32.
    • (2004) Nat Rev Microbiol , vol.2 , Issue.10 , pp. 820-832
    • Fang, F.C.1
  • 197
    • 84876931396 scopus 로고    scopus 로고
    • Beyond oxidative stress: An immunologist's guide to reactive oxygen species
    • Nathan C, Cunningham-Bussel A. Beyond oxidative stress: an immunologist's guide to reactive oxygen species. Nat Rev Immunol 2013; 13(5): 349-61.
    • (2013) Nat Rev Immunol , vol.13 , Issue.5 , pp. 349-361
    • Nathan, C.1    Cunningham-Bussel, A.2
  • 198
    • 67649255876 scopus 로고    scopus 로고
    • A tissuescale gradient of hydrogen peroxide mediates rapid wound detection in zebrafish
    • Niethammer P, Grabher C, Look AT, Mitchison TJ. A tissuescale gradient of hydrogen peroxide mediates rapid wound detection in zebrafish. Nature 2009; 459(7249): 996-9.
    • (2009) Nature , vol.459 , Issue.7249 , pp. 996-999
    • Niethammer, P.1    Grabher, C.2    Look, A.T.3    Mitchison, T.J.4
  • 199
    • 82555168190 scopus 로고    scopus 로고
    • Lyn is a redox sensor that mediates leukocyte wound attraction in vivo
    • Yoo SK, Starnes TW, Deng Q, Huttenlocher A. Lyn is a redox sensor that mediates leukocyte wound attraction in vivo. Nature 2011; 480(7375): 109-12.
    • (2011) Nature , vol.480 , Issue.7375 , pp. 109-112
    • Yoo, S.K.1    Starnes, T.W.2    Deng, Q.3    Huttenlocher, A.4
  • 200
    • 83055161506 scopus 로고    scopus 로고
    • Rac regulates PtdInsP(3) signaling and the chemotactic compass through a redox-mediated feedback loop
    • Kuiper JW, Sun C, Magalhaes MA, Glogauer M. Rac regulates PtdInsP(3) signaling and the chemotactic compass through a redox-mediated feedback loop. Blood 2011; 118(23): 6164-71.
    • (2011) Blood , vol.118 , Issue.23 , pp. 6164-6171
    • Kuiper, J.W.1    Sun, C.2    Magalhaes, M.A.3    Glogauer, M.4
  • 201
    • 80052835209 scopus 로고    scopus 로고
    • Remodeling of actin cytoskeleton in mouse periosteal cells under mechanical loading induces periosteal cell proliferation during bone formation
    • Sakai D, Kii I, Nakagawa K, et al. Remodeling of actin cytoskeleton in mouse periosteal cells under mechanical loading induces periosteal cell proliferation during bone formation. PLoS One 2011; 6(9): e24847.
    • (2011) Plos One , vol.6 , Issue.9
    • Sakai, D.1    Kii, I.2    Nakagawa, K.3
  • 202
    • 0041915623 scopus 로고    scopus 로고
    • High pressure induces superoxide production in isolated arteries via protein kinase C-dependent activation of NAD(P)H oxidase
    • Ungvari Z, Csiszar A, Huang A, Kaminski PM, Wolin MS, Koller A. High pressure induces superoxide production in isolated arteries via protein kinase C-dependent activation of NAD(P)H oxidase. Circulation 2003; 108(10): 1253-8.
    • (2003) Circulation , vol.108 , Issue.10 , pp. 1253-1258
    • Ungvari, Z.1    Csiszar, A.2    Huang, A.3    Kaminski, P.M.4    Wolin, M.S.5    Koller, A.6
  • 203
    • 0028902704 scopus 로고
    • Potentiation of the hypoxic contraction of guinea-pig isolated pulmonary arteries by two inhibitors of superoxide dismutase
    • Abdalla S, Will JA. Potentiation of the hypoxic contraction of guinea-pig isolated pulmonary arteries by two inhibitors of superoxide dismutase. Gen Pharmacol 1995; 26(4): 785-92.
    • (1995) Gen Pharmacol , vol.26 , Issue.4 , pp. 785-792
    • Abdalla, S.1    Will, J.A.2
  • 204
    • 35548967033 scopus 로고    scopus 로고
    • Comparison of H2O2-induced vasoconstriction in the abdominal aorta and mesenteric artery of the mouse
    • Ardanaz N, Beierwaltes WH, Pagano PJ. Comparison of H2O2-induced vasoconstriction in the abdominal aorta and mesenteric artery of the mouse. Vascul Pharmacol 2007; 47(5-6): 288-94.
    • (2007) Vascul Pharmacol , vol.47 , Issue.5-6 , pp. 288-294
    • Ardanaz, N.1    Beierwaltes, W.H.2    Pagano, P.J.3
  • 205
    • 54349129263 scopus 로고    scopus 로고
    • Constriction of pulmonary artery by peroxide: Role of Ca2+ release and PKC
    • Pourmahram GE, Snetkov VA, Shaifta Y, et al. Constriction of pulmonary artery by peroxide: role of Ca2+ release and PKC. Free Radic Biol Med 2008; 45(10): 1468-76.
    • (2008) Free Radic Biol Med , vol.45 , Issue.10 , pp. 1468-1476
    • Pourmahram, G.E.1    Snetkov, V.A.2    Shaifta, Y.3
  • 206
    • 33845892562 scopus 로고    scopus 로고
    • Cyclooxygenase, p38 mitogen-activated protein kinase (MAPK), extracellular signal-regulated kinase MAPK, Rho kinase, and Src mediate hydrogen peroxide-induced contraction of rat thoracic aorta and vena cava
    • Thakali K, Davenport L, Fink GD, Watts SW. Cyclooxygenase, p38 mitogen-activated protein kinase (MAPK), extracellular signal-regulated kinase MAPK, Rho kinase, and Src mediate hydrogen peroxide-induced contraction of rat thoracic aorta and vena cava. J Pharmacol Exp Ther 2007; 320(1): 236-43.
    • (2007) J Pharmacol Exp Ther , vol.320 , Issue.1 , pp. 236-243
    • Thakali, K.1    Davenport, L.2    Fink, G.D.3    Watts, S.W.4
  • 207
    • 59249090538 scopus 로고    scopus 로고
    • Superoxide constricts rat pulmonary arteries via Rho-kinase-mediated Ca(2+) sensitization
    • Knock GA, Snetkov VA, Shaifta Y, et al. Superoxide constricts rat pulmonary arteries via Rho-kinase-mediated Ca(2+) sensitization. Free Radic Biol Med 2009; 46(5): 633-42.
    • (2009) Free Radic Biol Med , vol.46 , Issue.5 , pp. 633-642
    • Knock, G.A.1    Snetkov, V.A.2    Shaifta, Y.3
  • 208
    • 39149088964 scopus 로고    scopus 로고
    • Regulation of contractility by Hsp27 and Hic-5 in rat mesenteric small arteries
    • Srinivasan R, Forman S, Quinlan RA, Ohanian J, Ohanian V. Regulation of contractility by Hsp27 and Hic-5 in rat mesenteric small arteries. Am J Physiol 2008; 294(2): H961-9.
    • (2008) Am J Physiol , vol.294 , Issue.2 , pp. H961-H969
    • Srinivasan, R.1    Forman, S.2    Quinlan, R.A.3    Ohanian, J.4    Ohanian, V.5
  • 209
    • 0032554630 scopus 로고    scopus 로고
    • Electrostatic evaluation of the signature motif (H/V)CX5R(S/T) in protein-tyrosine phosphatases
    • Peters GH, Frimurer TM, Olsen OH. Electrostatic evaluation of the signature motif (H/V)CX5R(S/T) in protein-tyrosine phosphatases. Biochemistry 1998; 37(16): 5383-93.
    • (1998) Biochemistry , vol.37 , Issue.16 , pp. 5383-5393
    • Peters, G.H.1    Frimurer, T.M.2    Olsen, O.H.3
  • 210
    • 20444400257 scopus 로고    scopus 로고
    • Redox redux: Revisiting PTPs and the control of cell signaling
    • Tonks NK. Redox redux: revisiting PTPs and the control of cell signaling. Cell 2005; 121(5): 667-70.
    • (2005) Cell , vol.121 , Issue.5 , pp. 667-670
    • Tonks, N.K.1
  • 211
    • 45049085873 scopus 로고    scopus 로고
    • Redox-based regulation of signal transduction: Principles, pitfalls, and promises
    • Janssen-Heininger YM, Mossman BT, Heintz NH, et al. Redox-based regulation of signal transduction: principles, pitfalls, and promises. Free Radic Biol Med 2008; 45(1): 1-17.
    • (2008) Free Radic Biol Med , vol.45 , Issue.1 , pp. 1-17
    • Janssen-Heininger, Y.M.1    Mossman, B.T.2    Heintz, N.H.3
  • 212
    • 63849103058 scopus 로고    scopus 로고
    • Role of peroxynitrite in the redox regulation of cell signal transduction pathways
    • Liaudet L, Vassalli G, Pacher P. Role of peroxynitrite in the redox regulation of cell signal transduction pathways. Front Biosci 2009; 14: 4809-14.
    • (2009) Front Biosci , vol.14 , pp. 4809-4814
    • Liaudet, L.1    Vassalli, G.2    Pacher, P.3
  • 213
    • 42149107390 scopus 로고    scopus 로고
    • U-shaped dose response in vasomotor tone: A mixed result of heterogenic response of multiple cells to xenobiotics
    • Bae ON, Lim KM, Han JY, et al. U-shaped dose response in vasomotor tone: a mixed result of heterogenic response of multiple cells to xenobiotics. Toxicol Sci 2008; 103(1): 181-90.
    • (2008) Toxicol Sci , vol.103 , Issue.1 , pp. 181-190
    • Bae, O.N.1    Lim, K.M.2    Han, J.Y.3
  • 214
    • 0344125376 scopus 로고    scopus 로고
    • Mechanisms of hydrogen-peroxide-induced biphasic response in rat mesenteric artery
    • Gao YJ, Hirota S, Zhang DW, Janssen LJ, Lee RM. Mechanisms of hydrogen-peroxide-induced biphasic response in rat mesenteric artery. Br J Pharmacol 2003; 138(6): 1085-92.
    • (2003) Br J Pharmacol , vol.138 , Issue.6 , pp. 1085-1092
    • Gao, Y.J.1    Hirota, S.2    Zhang, D.W.3    Janssen, L.J.4    Lee, R.M.5
  • 215
    • 0037428064 scopus 로고    scopus 로고
    • Stretch enhances contraction of bovine coronary arteries via an NAD(P)H oxidase-mediated activation of the extracellular signalregulated kinase mitogen-activated protein kinase cascade
    • Oeckler RA, Kaminski PM, Wolin MS. Stretch enhances contraction of bovine coronary arteries via an NAD(P)H oxidase-mediated activation of the extracellular signalregulated kinase mitogen-activated protein kinase cascade. Circ Res 2003; 92(1): 23-31.
    • (2003) Circ Res , vol.92 , Issue.1 , pp. 23-31
    • Oeckler, R.A.1    Kaminski, P.M.2    Wolin, M.S.3
  • 216
    • 0030820714 scopus 로고    scopus 로고
    • Activation of tyrosine kinases in H2O2-induced contraction in pulmonary artery
    • Jin N, Rhoades RA. Activation of tyrosine kinases in H2O2-induced contraction in pulmonary artery. Am J Physiol 1997; 272(6 Pt 2): H2686-92.
    • (1997) Am J Physiol , vol.272 , Issue.6 , pp. H2686-H2692
    • Jin, N.1    Rhoades, R.A.2
  • 217
    • 0033396236 scopus 로고    scopus 로고
    • Hydrogen peroxide induces contraction and raises [Ca2+]i in canine cerebral arterial smooth muscle: Participation of cellular signaling pathways
    • Yang ZW, Zheng T, Wang J, Zhang A, Altura BT, Altura BM. Hydrogen peroxide induces contraction and raises [Ca2+]i in canine cerebral arterial smooth muscle: participation of cellular signaling pathways. Naunyn Schmiedebergs Arch Pharmacol 1999; 360(6): 646-53.
    • (1999) Naunyn Schmiedebergs Arch Pharmacol , vol.360 , Issue.6 , pp. 646-653
    • Yang, Z.W.1    Zheng, T.2    Wang, J.3    Zhang, A.4    Altura, B.T.5    Altura, B.M.6
  • 218
    • 0034521371 scopus 로고    scopus 로고
    • Hydrogen peroxide is an endothelium-derived hyperpolarizing factor in mice
    • Matoba T, Shimokawa H, Nakashima M, et al. Hydrogen peroxide is an endothelium-derived hyperpolarizing factor in mice. J Clin Invest 2000; 106(12): 1521-30.
    • (2000) J Clin Invest , vol.106 , Issue.12 , pp. 1521-1530
    • Matoba, T.1    Shimokawa, H.2    Nakashima, M.3
  • 219
    • 18844397807 scopus 로고    scopus 로고
    • Hydrogen peroxide acts as both vasodilator and vasoconstrictor in the control of perfused mouse mesenteric resistance arteries
    • Lucchesi PA, Belmadani S, Matrougui K. Hydrogen peroxide acts as both vasodilator and vasoconstrictor in the control of perfused mouse mesenteric resistance arteries. J Hypertens 2005; 23(3): 571-9.
    • (2005) J Hypertens , vol.23 , Issue.3 , pp. 571-579
    • Lucchesi, P.A.1    Belmadani, S.2    Matrougui, K.3
  • 220
    • 33847720297 scopus 로고    scopus 로고
    • H2O2 activates redox-and 4-aminopyridine-sensitive Kv channels in coronary vascular smooth muscle
    • Rogers PA, Chilian WM, Bratz IN, Bryan RM, Jr., Dick GM. H2O2 activates redox-and 4-aminopyridine-sensitive Kv channels in coronary vascular smooth muscle. Am J Physiol 2007; 292(3): H1404-11.
    • (2007) Am J Physiol , vol.292 , Issue.3 , pp. H1404-H1411
    • Rogers, P.A.1    Chilian, W.M.2    Bratz, I.N.3    Bryan, R.M.4    Dick, G.M.5
  • 221
    • 22144494977 scopus 로고    scopus 로고
    • Characterization of four different effects elicited by H2O2 in rat aorta
    • Gil-Longo J, Gonzalez-Vazquez C. Characterization of four different effects elicited by H2O2 in rat aorta. Vascul Pharmacol 2005; 43(2): 128-38.
    • (2005) Vascul Pharmacol , vol.43 , Issue.2 , pp. 128-138
    • Gil-Longo, J.1    Gonzalez-Vazquez, C.2
  • 222
    • 0024402398 scopus 로고
    • Contractions to oxygen-derived free radicals are augmented in aorta of the spontaneously hypertensive rat
    • Auch-Schwelk W, Katusic ZS, Vanhoutte PM. Contractions to oxygen-derived free radicals are augmented in aorta of the spontaneously hypertensive rat. Hypertension 1989; 13(6 Pt 2): 859-64.
    • (1989) Hypertension , vol.13 , Issue.6 , pp. 859-864
    • Auch-Schwelk, W.1    Katusic, Z.S.2    Vanhoutte, P.M.3
  • 223
    • 0025322514 scopus 로고
    • Superoxide radical-mediated endothelial injury and vasoconstriction of rat thoracic aortic rings
    • Lawson DL, Mehta JL, Nichols WW, Mehta P, Donnelly WH. Superoxide radical-mediated endothelial injury and vasoconstriction of rat thoracic aortic rings. J Lab Clin Med 1990; 115(5): 541-8.
    • (1990) J Lab Clin Med , vol.115 , Issue.5 , pp. 541-548
    • Lawson, D.L.1    Mehta, J.L.2    Nichols, W.W.3    Mehta, P.4    Donnelly, W.H.5
  • 224
    • 19344376164 scopus 로고    scopus 로고
    • Mechanisms of hydroxyl radical-induced contraction of rat aorta
    • Li J, Li W, Liu W, Altura BT, Altura BM. Mechanisms of hydroxyl radical-induced contraction of rat aorta. Eur J Pharmacol 2004; 499(1-2): 171-8.
    • (2004) Eur J Pharmacol , vol.499 , Issue.1-2 , pp. 171-178
    • Li, J.1    Li, W.2    Liu, W.3    Altura, B.T.4    Altura, B.M.5
  • 225
    • 0025883342 scopus 로고
    • Nitric oxide: Physiology, pathophysiology, and pharmacology
    • Moncada S, Palmer RM, Higgs EA. Nitric oxide: physiology, pathophysiology, and pharmacology. Pharmacol Rev 1991; 43(2): 109-42.
    • (1991) Pharmacol Rev , vol.43 , Issue.2 , pp. 109-142
    • Moncada, S.1    Palmer, R.M.2    Higgs, E.A.3
  • 226
    • 0027752805 scopus 로고
    • The L-arginine-nitric oxide pathway
    • Moncada S, Higgs A. The L-arginine-nitric oxide pathway. N Engl J Med 1993; 329(27): 2002-12.
    • (1993) N Engl J Med , vol.329 , Issue.27 , pp. 2002-2012
    • Moncada, S.1    Higgs, A.2
  • 227
    • 4444248457 scopus 로고    scopus 로고
    • Transduction of NO-bioactivity by the red blood cell in sepsis: Novel mechanisms of vasodilation during acute inflammatory disease
    • Crawford JH, Chacko BK, Pruitt HM, Piknova B, Hogg N, Patel RP. Transduction of NO-bioactivity by the red blood cell in sepsis: novel mechanisms of vasodilation during acute inflammatory disease. Blood 2004; 104(5): 1375-82.
    • (2004) Blood , vol.104 , Issue.5 , pp. 1375-1382
    • Crawford, J.H.1    Chacko, B.K.2    Pruitt, H.M.3    Piknova, B.4    Hogg, N.5    Patel, R.P.6
  • 228
    • 0027935877 scopus 로고
    • Nitric oxide and cGMP cause vasorelaxation by activation of a charybdotoxin-sensitive K channel by cGMPdependent protein kinase
    • Archer SL, Huang JM, Hampl V, Nelson DP, Shultz PJ, Weir EK. Nitric oxide and cGMP cause vasorelaxation by activation of a charybdotoxin-sensitive K channel by cGMPdependent protein kinase. Proc Natl Acad Sci USA 1994; 91(16): 7583-7.
    • (1994) Proc Natl Acad Sci USA , vol.91 , Issue.16 , pp. 7583-7587
    • Archer, S.L.1    Huang, J.M.2    Hampl, V.3    Nelson, D.P.4    Shultz, P.J.5    Weir, E.K.6
  • 229
    • 0034721608 scopus 로고    scopus 로고
    • Mechanisms of NO/cGMP-dependent vasorelaxation
    • Sausbier M, Schubert R, Voigt V, et al. Mechanisms of NO/cGMP-dependent vasorelaxation. Circ Res 2000; 87(9): 825-30.
    • (2000) Circ Res , vol.87 , Issue.9 , pp. 825-830
    • Sausbier, M.1    Schubert, R.2    Voigt, V.3
  • 230
    • 38849162730 scopus 로고    scopus 로고
    • The nitrate-nitritenitric oxide pathway in physiology and therapeutics
    • Lundberg JO, Weitzberg E, Gladwin MT. The nitrate-nitritenitric oxide pathway in physiology and therapeutics. Nat Rev Drug Discov 2008; 7(2): 156-67.
    • (2008) Nat Rev Drug Discov , vol.7 , Issue.2 , pp. 156-167
    • Lundberg, J.O.1    Weitzberg, E.2    Gladwin, M.T.3
  • 231
    • 70350005373 scopus 로고    scopus 로고
    • Hemoglobin, nitric oxide and molecular mechanisms of hypoxic vasodilation
    • Allen BW, Stamler JS, Piantadosi CA. Hemoglobin, nitric oxide and molecular mechanisms of hypoxic vasodilation. Trends Mol Med 2009; 15(10): 452-60.
    • (2009) Trends Mol Med , vol.15 , Issue.10 , pp. 452-460
    • Allen, B.W.1    Stamler, J.S.2    Piantadosi, C.A.3
  • 232
    • 52649097054 scopus 로고    scopus 로고
    • Gap junction inhibitors reduce endothelium-dependent contractions in the aorta of spontaneously hypertensive rats
    • Tang EH, Vanhoutte PM. Gap junction inhibitors reduce endothelium-dependent contractions in the aorta of spontaneously hypertensive rats. J Pharmacol Exp Ther 2008; 327(1): 148-53.
    • (2008) J Pharmacol Exp Ther , vol.327 , Issue.1 , pp. 148-153
    • Tang, E.H.1    Vanhoutte, P.M.2
  • 233
    • 0032934950 scopus 로고    scopus 로고
    • Oxygen-derived free radical-induced vasoconstriction by thromboxane A2 in aorta of the spontaneously hypertensive rat
    • Hibino M, Okumura K, Iwama Y, et al. Oxygen-derived free radical-induced vasoconstriction by thromboxane A2 in aorta of the spontaneously hypertensive rat. J Cardiovasc Pharmacol 1999; 33(4): 605-10.
    • (1999) J Cardiovasc Pharmacol , vol.33 , Issue.4 , pp. 605-610
    • Hibino, M.1    Okumura, K.2    Iwama, Y.3
  • 234
    • 0017397321 scopus 로고
    • Enhancement of platelet function by superoxide anion
    • Handin RI, Karabin R, Boxer GJ. Enhancement of platelet function by superoxide anion. J Clin Invest 1977; 59(5): 959-65.
    • (1977) J Clin Invest , vol.59 , Issue.5 , pp. 959-965
    • Handin, R.I.1    Karabin, R.2    Boxer, G.J.3
  • 235
    • 0031048297 scopus 로고    scopus 로고
    • Platelet activation by superoxide anion and hydroxyl radicals intrinsically generated by platelets that had undergone anoxia and then reoxygenated
    • Leo R, Pratico D, Iuliano L, et al. Platelet activation by superoxide anion and hydroxyl radicals intrinsically generated by platelets that had undergone anoxia and then reoxygenated. Circulation 1997; 95(4): 885-91.
    • (1997) Circulation , vol.95 , Issue.4 , pp. 885-891
    • Leo, R.1    Pratico, D.2    Iuliano, L.3
  • 236
    • 34249893093 scopus 로고    scopus 로고
    • Platelet-associated NAD(P)H oxidase contributes to the thrombogenic phenotype induced by hypercholesterolemia
    • Stokes KY, Russell JM, Jennings MH, Alexander JS, Granger DN. Platelet-associated NAD(P)H oxidase contributes to the thrombogenic phenotype induced by hypercholesterolemia. Free Radic Biol Med 2007; 43(1): 22-30.
    • (2007) Free Radic Biol Med , vol.43 , Issue.1 , pp. 22-30
    • Stokes, K.Y.1    Russell, J.M.2    Jennings, M.H.3    Alexander, J.S.4    Granger, D.N.5
  • 237
    • 79951669903 scopus 로고    scopus 로고
    • Platelet receptor signaling in thrombus formation
    • Stegner D, Nieswandt B. Platelet receptor signaling in thrombus formation. J Mol Med (Berl) 2011; 89(2): 109-21.
    • (2011) J Mol Med (Berl) , vol.89 , Issue.2 , pp. 109-121
    • Stegner, D.1    Nieswandt, B.2
  • 238
    • 77949279691 scopus 로고    scopus 로고
    • Diverse functions of protein kinase C isoforms in platelet activation and thrombus formation
    • Harper MT, Poole AW. Diverse functions of protein kinase C isoforms in platelet activation and thrombus formation. J Thromb Haemost 2010; 8(3): 454-62.
    • (2010) J Thromb Haemost , vol.8 , Issue.3 , pp. 454-462
    • Harper, M.T.1    Poole, A.W.2
  • 239
    • 40749132588 scopus 로고    scopus 로고
    • Oxidative stress and platelets
    • Freedman JE. Oxidative stress and platelets. Arterioscler Thromb Vasc Biol 2008; 28(3): s11-6.
    • (2008) Arterioscler Thromb Vasc Biol , vol.28 , Issue.3 , pp. s11-s16
    • Freedman, J.E.1
  • 241
    • 8344283475 scopus 로고    scopus 로고
    • Reactive oxygen species: Players in the platelet game
    • Krotz F, Sohn HY, Pohl U. Reactive oxygen species: players in the platelet game. Arterioscler Thromb Vasc Biol 2004; 24(11): 1988-96.
    • (2004) Arterioscler Thromb Vasc Biol , vol.24 , Issue.11 , pp. 1988-1996
    • Krotz, F.1    Sohn, H.Y.2    Pohl, U.3
  • 242
    • 27144548487 scopus 로고    scopus 로고
    • Platelet NAD(P)H-oxidase-generated ROS production regulates alphaIIbbeta3-integrin activation independent of the NO/cGMP pathway
    • Begonja AJ, Gambaryan S, Geiger J, et al. Platelet NAD(P)H-oxidase-generated ROS production regulates alphaIIbbeta3-integrin activation independent of the NO/cGMP pathway. Blood 2005; 106(8): 2757-60.
    • (2005) Blood , vol.106 , Issue.8 , pp. 2757-2760
    • Begonja, A.J.1    Gambaryan, S.2    Geiger, J.3
  • 243
    • 0036682478 scopus 로고    scopus 로고
    • NAD(P)H oxidasedependent platelet superoxide anion release increases platelet recruitment
    • Krotz F, Sohn HY, Gloe T, et al. NAD(P)H oxidasedependent platelet superoxide anion release increases platelet recruitment. Blood 2002; 100(3): 917-24.
    • (2002) Blood , vol.100 , Issue.3 , pp. 917-924
    • Krotz, F.1    Sohn, H.Y.2    Gloe, T.3
  • 244
    • 33746010873 scopus 로고    scopus 로고
    • Polyphenols enhance platelet nitric oxide by inhibiting protein kinase C-dependent NADPH oxidase activation: Effect on platelet recruitment
    • Pignatelli P, Di Santo S, Buchetti B, Sanguigni V, Brunelli A, Violi F. Polyphenols enhance platelet nitric oxide by inhibiting protein kinase C-dependent NADPH oxidase activation: effect on platelet recruitment. FASEB J 2006; 20(8): 1082-9.
    • (2006) FASEB J , vol.20 , Issue.8 , pp. 1082-1089
    • Pignatelli, P.1    Di Santo, S.2    Buchetti, B.3    Sanguigni, V.4    Brunelli, A.5    Violi, F.6
  • 245
    • 0346492587 scopus 로고    scopus 로고
    • Regulation of endogenous reactive oxygen species in platelets can reverse aggregation
    • Clutton P, Miermont A, Freedman JE. Regulation of endogenous reactive oxygen species in platelets can reverse aggregation. Arterioscler Thromb Vasc Biol 2004; 24(1): 187-92.
    • (2004) Arterioscler Thromb Vasc Biol , vol.24 , Issue.1 , pp. 187-192
    • Clutton, P.1    Miermont, A.2    Freedman, J.E.3
  • 247
    • 36549018143 scopus 로고    scopus 로고
    • Reactive oxygen species and human platelet GP IIb/IIIa receptor activation
    • Sill JC, Proper JA, Johnson ME, Uhl CB, Katusic ZS. Reactive oxygen species and human platelet GP IIb/IIIa receptor activation. Platelets 2007; 18(8): 613-9.
    • (2007) Platelets , vol.18 , Issue.8 , pp. 613-619
    • Sill, J.C.1    Proper, J.A.2    Johnson, M.E.3    Uhl, C.B.4    Katusic, Z.S.5
  • 249
    • 35649019167 scopus 로고    scopus 로고
    • Ligand binding rapidly induces disulfidedependent dimerization of glycoprotein VI on the platelet plasma membrane
    • Arthur JF, Shen Y, Kahn ML, Berndt MC, Andrews RK, Gardiner EE. Ligand binding rapidly induces disulfidedependent dimerization of glycoprotein VI on the platelet plasma membrane. J Biol Chem 2007; 282(42): 30434-41.
    • (2007) J Biol Chem , vol.282 , Issue.42 , pp. 30434-30441
    • Arthur, J.F.1    Shen, Y.2    Kahn, M.L.3    Berndt, M.C.4    Rews, R.K.5    Gardiner, E.E.6
  • 250
    • 0141567629 scopus 로고    scopus 로고
    • Enzymatically catalyzed disulfide exchange is required for platelet adhesion to collagen via integrin alpha2beta1
    • Lahav J, Wijnen EM, Hess O, et al. Enzymatically catalyzed disulfide exchange is required for platelet adhesion to collagen via integrin alpha2beta1. Blood 2003; 102(6): 2085-92.
    • (2003) Blood , vol.102 , Issue.6 , pp. 2085-2092
    • Lahav, J.1    Wijnen, E.M.2    Hess, O.3
  • 251
    • 84875465881 scopus 로고    scopus 로고
    • Hydrogen peroxide promotes aging-related platelet hyperactivation and thrombosis
    • Dayal S, Wilson KM, Motto DG, Miller FJ, Jr., Chauhan AK, Lentz SR. Hydrogen peroxide promotes aging-related platelet hyperactivation and thrombosis. Circulation 2013; 127(12): 1308-16.
    • (2013) Circulation , vol.127 , Issue.12 , pp. 1308-1316
    • Dayal, S.1    Wilson, K.M.2    Motto, D.G.3    Miller, F.J.4    Chauhan, A.K.5    Lentz, S.R.6
  • 252
    • 33745635938 scopus 로고    scopus 로고
    • The use of hydrogen peroxide for achieving dermal hemostasis after burn excision in a patient with platelet dysfunction
    • Potyondy L, Lottenberg L, Anderson J, Mozingo DW. The use of hydrogen peroxide for achieving dermal hemostasis after burn excision in a patient with platelet dysfunction. J Burn Care Res 2006; 27(1): 99-101.
    • (2006) J Burn Care Res , vol.27 , Issue.1 , pp. 99-101
    • Potyondy, L.1    Lottenberg, L.2    Erson, J.3    Mozingo, D.W.4
  • 253
    • 0025735394 scopus 로고
    • Hydrogen peroxide is an intermediate in the platelet activation cascade triggered by collagen, but not by thrombin
    • Del Principe D, Menichelli A, De Matteis W, et al. Hydrogen peroxide is an intermediate in the platelet activation cascade triggered by collagen, but not by thrombin. Thromb Res 1991; 62(5): 365-75.
    • (1991) Thromb Res , vol.62 , Issue.5 , pp. 365-375
    • Del Principe, D.1    Menichelli, A.2    De Matteis, W.3
  • 254
    • 0031962580 scopus 로고    scopus 로고
    • Hydrogen peroxide is involved in collagen-induced platelet activation
    • Pignatelli P, Pulcinelli FM, Lenti L, Gazzaniga PP, Violi F. Hydrogen peroxide is involved in collagen-induced platelet activation. Blood 1998; 91(2): 484-90.
    • (1998) Blood , vol.91 , Issue.2 , pp. 484-490
    • Pignatelli, P.1    Pulcinelli, F.M.2    Lenti, L.3    Gazzaniga, P.P.4    Violi, F.5
  • 255
    • 84878627332 scopus 로고    scopus 로고
    • Autocrine amplification of integrin alphaIIbbeta3 activation and platelet adhesive responses by deoxyribose-1-phosphate
    • Vara DS, Campanella M, Canobbio I, et al. Autocrine amplification of integrin alphaIIbbeta3 activation and platelet adhesive responses by deoxyribose-1-phosphate. Thromb Haemost 2013; 109(6): 1108-19.
    • (2013) Thromb Haemost , vol.109 , Issue.6 , pp. 1108-1119
    • Vara, D.S.1    Campanella, M.2    Canobbio, I.3
  • 256
    • 84883247945 scopus 로고    scopus 로고
    • 12-lipoxygenase activity plays an important role in PAR4 and GPVI-mediated platelet reactivity
    • Yeung J, Apopa PL, Vesci J, et al. 12-lipoxygenase activity plays an important role in PAR4 and GPVI-mediated platelet reactivity. Thromb Haemost 2013; 110(3): 569-81.
    • (2013) Thromb Haemost , vol.110 , Issue.3 , pp. 569-581
    • Yeung, J.1    Apopa, P.L.2    Vesci, J.3
  • 257
    • 57049117316 scopus 로고    scopus 로고
    • Circulating white blood cells and platelets amplify oxidative stress in heart failure
    • Ijsselmuiden AJ, Musters RJ, de Ruiter G, et al. Circulating white blood cells and platelets amplify oxidative stress in heart failure. Nat Clin Pract Cardiovasc Med 2008; 5(12): 811-20.
    • (2008) Nat Clin Pract Cardiovasc Med , vol.5 , Issue.12 , pp. 811-820
    • Ijsselmuiden, A.J.1    Musters, R.J.2    De Ruiter, G.3
  • 258
    • 44649152906 scopus 로고    scopus 로고
    • Spatially distinct production of reactive oxygen species regulates platelet activation
    • Bakdash N, Williams MS. Spatially distinct production of reactive oxygen species regulates platelet activation. Free Radic Biol Med 2008; 45(2): 158-66.
    • (2008) Free Radic Biol Med , vol.45 , Issue.2 , pp. 158-166
    • Bakdash, N.1    Williams, M.S.2
  • 259
    • 64549119138 scopus 로고    scopus 로고
    • Redox control of platelet function
    • Essex DW. Redox control of platelet function. Antioxid Redox Signal 2009; 11(5): 1191-225.
    • (2009) Antioxid Redox Signal , vol.11 , Issue.5 , pp. 1191-1225
    • Essex, D.W.1
  • 260
    • 33846425317 scopus 로고    scopus 로고
    • Identification of redox sensitive thiols of protein disulfide isomerase using isotope coded affinity technology and mass spectrometry
    • Kozarova A, Sliskovic I, Mutus B, Simon ES, Andrews PC, Vacratsis PO. Identification of redox sensitive thiols of protein disulfide isomerase using isotope coded affinity technology and mass spectrometry. J Am Soc Mass Spectrom 2007; 18(2): 260-9.
    • (2007) J am Soc Mass Spectrom , vol.18 , Issue.2 , pp. 260-269
    • Kozarova, A.1    Sliskovic, I.2    Mutus, B.3    Simon, E.S.4    Rews, P.C.5    Vacratsis, P.O.6
  • 261
    • 77449149046 scopus 로고    scopus 로고
    • Redox-dependent domain rearrangement of protein disulfide isomerase coupled with exposure of its substrate-binding hydrophobic surface
    • Serve O, Kamiya Y, Maeno A, et al. Redox-dependent domain rearrangement of protein disulfide isomerase coupled with exposure of its substrate-binding hydrophobic surface. J Mol Biol 2010; 396(2): 361-74.
    • (2010) J Mol Biol , vol.396 , Issue.2 , pp. 361-374
    • Serve, O.1    Kamiya, Y.2    Maeno, A.3
  • 262
    • 75149147568 scopus 로고    scopus 로고
    • Platelets release novel thiol isomerase enzymes which are recruited to the cell surface following activation
    • Holbrook LM, Watkins NA, Simmonds AD, Jones CI, Ouwehand WH, Gibbins JM. Platelets release novel thiol isomerase enzymes which are recruited to the cell surface following activation. Br J Haematol 2010; 148(4): 627-37.
    • (2010) Br J Haematol , vol.148 , Issue.4 , pp. 627-637
    • Holbrook, L.M.1    Watkins, N.A.2    Simmonds, A.D.3    Jones, C.I.4    Ouwehand, W.H.5    Gibbins, J.M.6
  • 263
    • 33646698875 scopus 로고    scopus 로고
    • Extracellular disulfide exchange and the regulation of cellular function
    • Jordan PA, Gibbins JM. Extracellular disulfide exchange and the regulation of cellular function. Antioxid Redox Signal 2006; 8(3-4): 312-24.
    • (2006) Antioxid Redox Signal , vol.8 , Issue.3-4 , pp. 312-324
    • Jordan, P.A.1    Gibbins, J.M.2
  • 264
    • 0034711264 scopus 로고    scopus 로고
    • The platelet integrin alpha IIbbeta 3 has an endogenous thiol isomerase activity
    • O'Neill S, Robinson A, Deering A, Ryan M, Fitzgerald DJ, Moran N. The platelet integrin alpha IIbbeta 3 has an endogenous thiol isomerase activity. J Biol Chem 2000; 275(47): 36984-90.
    • (2000) J Biol Chem , vol.275 , Issue.47 , pp. 36984-36990
    • O'neill, S.1    Robinson, A.2    Deering, A.3    Ryan, M.4    Fitzgerald, D.J.5    Moran, N.6
  • 265
    • 68449103573 scopus 로고    scopus 로고
    • Flavonoids as anti-inflammatory agents: Implications in cancer and cardiovascular disease
    • Garcia-Lafuente A, Guillamon E, Villares A, Rostagno MA, Martinez JA. Flavonoids as anti-inflammatory agents: implications in cancer and cardiovascular disease. Inflamm Res 2009; 58(9): 537-52.
    • (2009) Inflamm Res , vol.58 , Issue.9 , pp. 537-552
    • Garcia-Lafuente, A.1    Guillamon, E.2    Villares, A.3    Rostagno, M.A.4    Martinez, J.A.5
  • 266
    • 67650735222 scopus 로고    scopus 로고
    • Oxidative stress and cardiovascular disease: Novel tools give (free) radical insight
    • Fearon IM, Faux SP. Oxidative stress and cardiovascular disease: novel tools give (free) radical insight. J Mol Cell Cardiol 2009; 47(3): 372-81.
    • (2009) J Mol Cell Cardiol , vol.47 , Issue.3 , pp. 372-381
    • Fearon, I.M.1    Faux, S.P.2
  • 267
    • 84873344743 scopus 로고    scopus 로고
    • Efficacy of vitamin and antioxidant supplements in prevention of cardiovascular disease: Systematic review and metaanalysis of randomised controlled trials
    • Myung SK, Ju W, Cho B, Oh SW, Park SM, Koo BK, et al. Efficacy of vitamin and antioxidant supplements in prevention of cardiovascular disease: systematic review and metaanalysis of randomised controlled trials. BMJ 2013; 346: f10.
    • (2013) BMJ , pp. 346
    • Myung, S.K.1    Ju, W.2    Cho, B.3    Oh, S.W.4    Park, S.M.5    Koo, B.K.6
  • 268
    • 0023912670 scopus 로고
    • Vascular endothelial cells synthesize nitric oxide from L-arginine
    • Palmer RM, Ashton DS, Moncada S. Vascular endothelial cells synthesize nitric oxide from L-arginine. Nature 1988; 333(6174): 664-6.
    • (1988) Nature , vol.333 , Issue.6174 , pp. 664-666
    • Palmer, R.M.1    Ashton, D.S.2    Moncada, S.3
  • 269
    • 79751507132 scopus 로고    scopus 로고
    • Nitric oxide at a glance
    • Naseem KM, Roberts W. Nitric oxide at a glance. Platelets 2011; 22(2): 148-52.
    • (2011) Platelets , vol.22 , Issue.2 , pp. 148-152
    • Naseem, K.M.1    Roberts, W.2
  • 270
    • 0033583481 scopus 로고    scopus 로고
    • Increased adhesion and aggregation of platelets lacking cyclic guanosine 3',5'-monophosphate kinase I
    • Massberg S, Sausbier M, Klatt P, et al. Increased adhesion and aggregation of platelets lacking cyclic guanosine 3',5'-monophosphate kinase I. J Exp Med 1999; 189(8): 1255-64.
    • (1999) J Exp Med , vol.189 , Issue.8 , pp. 1255-1264
    • Massberg, S.1    Sausbier, M.2    Klatt, P.3
  • 271
    • 0032725027 scopus 로고    scopus 로고
    • Cyclic nucleotides and phosphodiesterases in platelets
    • Haslam RJ, Dickinson NT, Jang EK. Cyclic nucleotides and phosphodiesterases in platelets. Thromb Haemost 1999; 82(2): 412-23.
    • (1999) Thromb Haemost , vol.82 , Issue.2 , pp. 412-423
    • Haslam, R.J.1    Dickinson, N.T.2    Jang, E.K.3
  • 272
    • 0029911717 scopus 로고    scopus 로고
    • Prostacyclin and sodium nitroprusside inhibit the activity of the platelet inositol 1,4,5-trisphosphate receptor and promote its phosphorylation
    • Cavallini L, Coassin M, Borean A, Alexandre A. Prostacyclin and sodium nitroprusside inhibit the activity of the platelet inositol 1,4,5-trisphosphate receptor and promote its phosphorylation. J Biol Chem 1996; 271(10): 5545-51.
    • (1996) J Biol Chem , vol.271 , Issue.10 , pp. 5545-5551
    • Cavallini, L.1    Coassin, M.2    Borean, A.3    Alexandre, A.4
  • 273
    • 33846187547 scopus 로고    scopus 로고
    • IRAG mediates NO/cGMP-dependent inhibition of platelet aggregation and thrombus formation
    • Antl M, von Bruhl ML, Eiglsperger C, et al. IRAG mediates NO/cGMP-dependent inhibition of platelet aggregation and thrombus formation. Blood 2007; 109(2): 552-9.
    • (2007) Blood , vol.109 , Issue.2 , pp. 552-559
    • Antl, M.1    Von Bruhl, M.L.2    Eiglsperger, C.3
  • 274
    • 0033529302 scopus 로고    scopus 로고
    • Megakaryocyte hyperplasia and enhanced agonist-induced platelet activation in vasodilator-stimulated phosphoprotein knockout mice
    • Hauser W, Knobeloch KP, Eigenthaler M, et al. Megakaryocyte hyperplasia and enhanced agonist-induced platelet activation in vasodilator-stimulated phosphoprotein knockout mice. Proc Natl Acad Sci USA 1999; 96(14): 8120-5.
    • (1999) Proc Natl Acad Sci USA , vol.96 , Issue.14 , pp. 8120-8125
    • Hauser, W.1    Knobeloch, K.P.2    Eigenthaler, M.3
  • 275
    • 56749158772 scopus 로고    scopus 로고
    • Nitric oxide specifically inhibits integrinmediated platelet adhesion and spreading on collagen
    • Roberts W, Riba R, Homer-Vanniasinkam S, Farndale RW, Naseem KM. Nitric oxide specifically inhibits integrinmediated platelet adhesion and spreading on collagen. J Thromb Haemost 2008; 6(12): 2175-85.
    • (2008) J Thromb Haemost , vol.6 , Issue.12 , pp. 2175-2185
    • Roberts, W.1    Riba, R.2    Homer-Vanniasinkam, S.3    Farndale, R.W.4    Naseem, K.M.5
  • 277
    • 0034680825 scopus 로고    scopus 로고
    • The role of mitochondria in the regulation of hypoxia-inducible factor 1 expression during hypoxia
    • Agani FH, Pichiule P, Chavez JC, LaManna JC. The role of mitochondria in the regulation of hypoxia-inducible factor 1 expression during hypoxia. J Biol Chem 2000; 275(46): 35863-7.
    • (2000) J Biol Chem , vol.275 , Issue.46 , pp. 35863-35867
    • Agani, F.H.1    Pichiule, P.2    Chavez, J.C.3    Lamanna, J.C.4
  • 278
    • 13644267272 scopus 로고    scopus 로고
    • Mutation in mitochondrial complex I ND6 subunit is associated with defective response to hypoxia in human glioma cells
    • DeHaan C, Habibi-Nazhad B, Yan E, Salloum N, Parliament M, Allalunis-Turner J. Mutation in mitochondrial complex I ND6 subunit is associated with defective response to hypoxia in human glioma cells. Mol Cancer 2004; 3: 19.
    • (2004) Mol Cancer , vol.3 , pp. 19
    • Dehaan, C.1    Habibi-Nazhad, B.2    Yan, E.3    Salloum, N.4    Parliament, M.5    Allalunis-Turner, J.6
  • 279
    • 79951539813 scopus 로고    scopus 로고
    • Targeting vascular NADPH oxidase 1 blocks tumor angiogenesis through a PPARalpha mediated mechanism
    • Garrido-Urbani S, Jemelin S, Deffert C, et al. Targeting vascular NADPH oxidase 1 blocks tumor angiogenesis through a PPARalpha mediated mechanism. PLoS One 2011; 6(2): e14665.
    • (2011) Plos One , vol.6 , Issue.2
    • Garrido-Urbani, S.1    Jemelin, S.2    Deffert, C.3
  • 280
    • 0037154250 scopus 로고    scopus 로고
    • Reactive oxygen generated by Nox1 triggers the angiogenic switch
    • Arbiser JL, Petros J, Klafter R, et al. Reactive oxygen generated by Nox1 triggers the angiogenic switch. Proc Natl Acad Sci USA 2002; 99(2): 715-20.
    • (2002) Proc Natl Acad Sci USA , vol.99 , Issue.2 , pp. 715-720
    • Arbiser, J.L.1    Petros, J.2    Klafter, R.3
  • 281
    • 36348938884 scopus 로고    scopus 로고
    • Reactive oxygen species regulate angiogenesis and tumor growth through vascular endothelial growth factor
    • Xia C, Meng Q, Liu LZ, Rojanasakul Y, Wang XR, Jiang BH. Reactive oxygen species regulate angiogenesis and tumor growth through vascular endothelial growth factor. Cancer Res 2007; 67(22): 10823-30.
    • (2007) Cancer Res , vol.67 , Issue.22 , pp. 10823-10830
    • Xia, C.1    Meng, Q.2    Liu, L.Z.3    Rojanasakul, Y.4    Wang, X.R.5    Jiang, B.H.6
  • 282
    • 33846495553 scopus 로고    scopus 로고
    • NOX5 variants are functionally active in endothelial cells
    • BelAiba RS, Djordjevic T, Petry A, et al. NOX5 variants are functionally active in endothelial cells. Free Radic Biol Med 2007; 42(4): 446-59.
    • (2007) Free Radic Biol Med , vol.42 , Issue.4 , pp. 446-459
    • Belaiba, R.S.1    Djordjevic, T.2    Petry, A.3
  • 283
    • 33748429741 scopus 로고    scopus 로고
    • Mechanisms of endothelial response to oxidative aggression: Protective role of autologous VEGF and induction of VEGFR2 by H2O2
    • Gonzalez-Pacheco FR, Deudero JJ, Castellanos MC, et al. Mechanisms of endothelial response to oxidative aggression: protective role of autologous VEGF and induction of VEGFR2 by H2O2. Am J Physiol 2006; 291(3): H1395-401.
    • (2006) Am J Physiol , vol.291 , Issue.3 , pp. H1395-H1401
    • Gonzalez-Pacheco, F.R.1    Deudero, J.J.2    Castellanos, M.C.3
  • 284
    • 33947389882 scopus 로고    scopus 로고
    • Activation of vascular endothelial growth factor through reactive oxygen species mediates 20-hydroxyeicosatetraenoic acid-induced endothelial cell proliferation
    • Guo AM, Arbab AS, Falck JR, et al. Activation of vascular endothelial growth factor through reactive oxygen species mediates 20-hydroxyeicosatetraenoic acid-induced endothelial cell proliferation. J Pharmacol Exp Ther 2007; 321(1): 18-27.
    • (2007) J Pharmacol Exp Ther , vol.321 , Issue.1 , pp. 18-27
    • Guo, A.M.1    Arbab, A.S.2    Falck, J.R.3
  • 285
    • 14844357720 scopus 로고    scopus 로고
    • Novel role of ARF6 in vascular endothelial growth factor-induced signaling and angiogenesis
    • Ikeda S, Ushio-Fukai M, Zuo L, et al. Novel role of ARF6 in vascular endothelial growth factor-induced signaling and angiogenesis. Circ Res 2005; 96(4): 467-75.
    • (2005) Circ Res , vol.96 , Issue.4 , pp. 467-475
    • Ikeda, S.1    Ushio-Fukai, M.2    Zuo, L.3
  • 286
    • 0036954803 scopus 로고    scopus 로고
    • Novel role of gp91(Phox)-containing NAD(P)H oxidase in vascular endothelial growth factor-induced signaling and angiogenesis
    • Ushio-Fukai M, Tang Y, Fukai T, et al. Novel role of gp91(phox)-containing NAD(P)H oxidase in vascular endothelial growth factor-induced signaling and angiogenesis. Circ Res 2002; 91(12): 1160-7.
    • (2002) Circ Res , vol.91 , Issue.12 , pp. 1160-1167
    • Ushio-Fukai, M.1    Tang, Y.2    Fukai, T.3
  • 287
    • 4043148481 scopus 로고    scopus 로고
    • IQGAP1, a novel vascular endothelial growth factor receptor binding protein, is involved in reactive oxygen species--dependent endothelial migration and proliferation
    • Yamaoka-Tojo M, Ushio-Fukai M, Hilenski L, et al. IQGAP1, a novel vascular endothelial growth factor receptor binding protein, is involved in reactive oxygen species--dependent endothelial migration and proliferation. Circ Res 2004; 95(3): 276-83.
    • (2004) Circ Res , vol.95 , Issue.3 , pp. 276-283
    • Yamaoka-Tojo, M.1    Ushio-Fukai, M.2    Hilenski, L.3
  • 288
    • 26444449537 scopus 로고    scopus 로고
    • Roles of reactive oxygen species in angiopoietin-1/tie-2 receptor signaling
    • Harfouche R, Malak NA, Brandes RP, Karsan A, Irani K, Hussain SN. Roles of reactive oxygen species in angiopoietin-1/tie-2 receptor signaling. FASEB J 2005; 19(12): 1728-30.
    • (2005) FASEB J , vol.19 , Issue.12 , pp. 1728-1730
    • Harfouche, R.1    Malak, N.A.2    Brandes, R.P.3    Karsan, A.4    Irani, K.5    Hussain, S.N.6
  • 289
    • 0037404757 scopus 로고    scopus 로고
    • Pigment epithelium-derived factor inhibits leptininduced angiogenesis by suppressing vascular endothelial growth factor gene expression through anti-oxidative properties
    • Yamagishi S, Amano S, Inagaki Y, Okamoto T, Takeuchi M, Inoue H. Pigment epithelium-derived factor inhibits leptininduced angiogenesis by suppressing vascular endothelial growth factor gene expression through anti-oxidative properties. Microvasc Res 2003; 65(3): 186-90.
    • (2003) Microvasc Res , vol.65 , Issue.3 , pp. 186-190
    • Yamagishi, S.1    Amano, S.2    Inagaki, Y.3    Okamoto, T.4    Takeuchi, M.5    Inoue, H.6
  • 291
    • 0036479214 scopus 로고    scopus 로고
    • Reactive oxygen species as downstream mediators of angiogenic signaling by vascular endothelial growth factor receptor-2/KDR
    • Colavitti R, Pani G, Bedogni B, et al. Reactive oxygen species as downstream mediators of angiogenic signaling by vascular endothelial growth factor receptor-2/KDR. J Biol Chem 2002; 277(5): 3101-8.
    • (2002) J Biol Chem , vol.277 , Issue.5 , pp. 3101-3108
    • Colavitti, R.1    Pani, G.2    Bedogni, B.3
  • 292
    • 34547788817 scopus 로고    scopus 로고
    • Peroxynitrite mediates VEGF's angiogenic signal and function via a nitration-independent mechanism in endothelial cells
    • El-Remessy AB, Al-Shabrawey M, Platt DH, et al. Peroxynitrite mediates VEGF's angiogenic signal and function via a nitration-independent mechanism in endothelial cells. FASEB J 2007; 21(10): 2528-39.
    • (2007) FASEB J , vol.21 , Issue.10 , pp. 2528-2539
    • El-Remessy, A.B.1    Al-Shabrawey, M.2    Platt, D.H.3
  • 293
    • 0035514402 scopus 로고    scopus 로고
    • Vascular endothelial growth factor induces manganesesuperoxide dismutase expression in endothelial cells by a Rac1-regulated NADPH oxidase-dependent mechanism
    • Abid MR, Tsai JC, Spokes KC, Deshpande SS, Irani K, Aird WC. Vascular endothelial growth factor induces manganesesuperoxide dismutase expression in endothelial cells by a Rac1-regulated NADPH oxidase-dependent mechanism. FASEB J 2001; 15(13): 2548-50.
    • (2001) FASEB J , vol.15 , Issue.13 , pp. 2548-2550
    • Abid, M.R.1    Tsai, J.C.2    Spokes, K.C.3    Deshpande, S.S.4    Irani, K.5    Aird, W.C.6
  • 294
    • 18444401175 scopus 로고    scopus 로고
    • Role of gp91phox (Nox2)-containing NAD(P)H oxidase in angiogenesis in response to hindlimb ischemia
    • Tojo T, Ushio-Fukai M, Yamaoka-Tojo M, Ikeda S, Patrushev N, Alexander RW. Role of gp91phox (Nox2)-containing NAD(P)H oxidase in angiogenesis in response to hindlimb ischemia. Circulation 2005; 111(18): 2347-55.
    • (2005) Circulation , vol.111 , Issue.18 , pp. 2347-2355
    • Tojo, T.1    Ushio-Fukai, M.2    Yamaoka-Tojo, M.3    Ikeda, S.4    Patrushev, N.5    Alexander, R.W.6
  • 295
    • 0036558283 scopus 로고    scopus 로고
    • Reactive oxygen species mediate Rac-induced loss of cell-cell adhesion in primary human endothelial cells
    • van Wetering S, van Buul JD, Quik S, et al. Reactive oxygen species mediate Rac-induced loss of cell-cell adhesion in primary human endothelial cells. J Cell Sci 2002; 115(Pt 9): 1837-46.
    • (2002) J Cell Sci , vol.115 , Issue.9 , pp. 1837-1846
    • Van Wetering, S.1    Van Buul, J.D.2    Quik, S.3
  • 296
    • 2942628119 scopus 로고    scopus 로고
    • Sequential activation of phosphatidylinositol 3-kinase, beta Pix, Rac1, and Nox1 in growth factor-induced production of H2O2
    • Park HS, Lee SH, Park D, et al. Sequential activation of phosphatidylinositol 3-kinase, beta Pix, Rac1, and Nox1 in growth factor-induced production of H2O2. Mol Cell Biol 2004; 24(10): 4384-94.
    • (2004) Mol Cell Biol , vol.24 , Issue.10 , pp. 4384-4394
    • Park, H.S.1    Lee, S.H.2    Park, D.3
  • 297
    • 33748466565 scopus 로고    scopus 로고
    • Specificity in reactive oxidant signaling: Think globally, act locally
    • Terada LS. Specificity in reactive oxidant signaling: think globally, act locally. J Cell Biol 2006; 174(5): 615-23.
    • (2006) J Cell Biol , vol.174 , Issue.5 , pp. 615-623
    • Terada, L.S.1
  • 298
    • 33749047437 scopus 로고    scopus 로고
    • Localizing NADPH oxidase-derived ROS
    • Ushio-Fukai M. Localizing NADPH oxidase-derived ROS. Sci STKE 2006; 2006(349): re8.
    • (2006) Sci STKE , vol.2006 , Issue.349
    • Ushio-Fukai, M.1
  • 299
    • 0141703529 scopus 로고    scopus 로고
    • Vascular endothelial growth factor causes translocation of p47phox to membrane ruffles through WAVE1
    • Wu RF, Gu Y, Xu YC, Nwariaku FE, Terada LS. Vascular endothelial growth factor causes translocation of p47phox to membrane ruffles through WAVE1. J Biol Chem 2003; 278(38): 36830-40.
    • (2003) J Biol Chem , vol.278 , Issue.38 , pp. 36830-36840
    • Wu, R.F.1    Gu, Y.2    Xu, Y.C.3    Nwariaku, F.E.4    Terada, L.S.5
  • 300
    • 27644585373 scopus 로고    scopus 로고
    • IQGAP1 regulates reactive oxygen species-dependent endothelial cell migration through interacting with Nox2
    • Ikeda S, Yamaoka-Tojo M, Hilenski L, et al. IQGAP1 regulates reactive oxygen species-dependent endothelial cell migration through interacting with Nox2. Arterioscler Thromb Vasc Biol 2005; 25(11): 2295-300.
    • (2005) Arterioscler Thromb Vasc Biol , vol.25 , Issue.11 , pp. 2295-2300
    • Ikeda, S.1    Yamaoka-Tojo, M.2    Hilenski, L.3
  • 301
    • 33747423658 scopus 로고    scopus 로고
    • IQGAP1 mediates VE-cadherin-based cell-cell contacts and VEGF signaling at adherence junctions linked to angiogenesis
    • Yamaoka-Tojo M, Tojo T, Kim HW, et al. IQGAP1 mediates VE-cadherin-based cell-cell contacts and VEGF signaling at adherence junctions linked to angiogenesis. Arterioscler Thromb Vasc Biol 2006; 26(9): 1991-7.
    • (2006) Arterioscler Thromb Vasc Biol , vol.26 , Issue.9 , pp. 1991-1997
    • Yamaoka-Tojo, M.1    Tojo, T.2    Kim, H.W.3
  • 302
    • 0033134604 scopus 로고    scopus 로고
    • Angiogenesis and vasculogenesis as therapeutic strategies for postnatal neovascularization
    • Isner JM, Asahara T. Angiogenesis and vasculogenesis as therapeutic strategies for postnatal neovascularization. J Clin Invest 1999; 103(9): 1231-6.
    • (1999) J Clin Invest , vol.103 , Issue.9 , pp. 1231-1236
    • Isner, J.M.1    Asahara, T.2
  • 303
    • 48849116997 scopus 로고    scopus 로고
    • Role of nox2-based NADPH oxidase in bone marrow and progenitor cell function involved in neovascularization induced by hindlimb ischemia
    • Urao N, Inomata H, Razvi M, et al. Role of nox2-based NADPH oxidase in bone marrow and progenitor cell function involved in neovascularization induced by hindlimb ischemia. Circ Res 2008; 103(2): 212-20.
    • (2008) Circ Res , vol.103 , Issue.2 , pp. 212-220
    • Urao, N.1    Inomata, H.2    Razvi, M.3
  • 304
    • 70349368518 scopus 로고    scopus 로고
    • Novel role of NADPH oxidase in angiogenesis and stem/progenitor cell function
    • Ushio-Fukai M, Urao N. Novel role of NADPH oxidase in angiogenesis and stem/progenitor cell function. Antioxid Redox Signal 2009; 11(10): 2517-33.
    • (2009) Antioxid Redox Signal , vol.11 , Issue.10 , pp. 2517-2533
    • Ushio-Fukai, M.1    Urao, N.2
  • 305
    • 5344229985 scopus 로고    scopus 로고
    • Antioxidative stress-associated genes in circulating progenitor cells: Evidence for enhanced resistance against oxidative stress
    • Dernbach E, Urbich C, Brandes RP, Hofmann WK, Zeiher AM, Dimmeler S. Antioxidative stress-associated genes in circulating progenitor cells: evidence for enhanced resistance against oxidative stress. Blood 2004; 104(12): 3591-7.
    • (2004) Blood , vol.104 , Issue.12 , pp. 3591-3597
    • Dernbach, E.1    Urbich, C.2    Brandes, R.P.3    Hofmann, W.K.4    Zeiher, A.M.5    Dimmeler, S.6
  • 306
    • 0035527489 scopus 로고    scopus 로고
    • Green tea catechins and vitamin E inhibit angiogenesis of human microvascular endothelial cells through suppression of IL-8 production
    • Tang FY, Meydani M. Green tea catechins and vitamin E inhibit angiogenesis of human microvascular endothelial cells through suppression of IL-8 production. Nutr Cancer 2001; 41(1-2): 119-25.
    • (2001) Nutr Cancer , vol.41 , Issue.1-2 , pp. 119-125
    • Tang, F.Y.1    Meydani, M.2
  • 307
    • 37349130190 scopus 로고    scopus 로고
    • Natural antioxidant pedicularioside G inhibits angiogenesis and tumourigenesis in vitro and in vivo
    • Mu P, Gao X, Jia ZJ, Zheng RL. Natural antioxidant pedicularioside G inhibits angiogenesis and tumourigenesis in vitro and in vivo. Basic Clin Pharmacol Toxicol 2008; 102(1): 30-4.
    • (2008) Basic Clin Pharmacol Toxicol , vol.102 , Issue.1 , pp. 30-34
    • Mu, P.1    Gao, X.2    Jia, Z.J.3    Zheng, R.L.4
  • 308
    • 84869150471 scopus 로고    scopus 로고
    • Antioxidant potential of all-trans retinoic acid (ATRA) and enhanced activity of liposome encapsulated ATRA against inflammation and tumor-directed angiogenesis
    • Siddikuzzaman, Grace VM. Antioxidant potential of all-trans retinoic acid (ATRA) and enhanced activity of liposome encapsulated ATRA against inflammation and tumor-directed angiogenesis. Immunopharmacol Immunotoxicol 2013; 35(1): 164-73.
    • (2013) Immunopharmacol Immunotoxicol , vol.35 , Issue.1 , pp. 164-173
    • Siddikuzzaman, G.V.1
  • 309
    • 0032761948 scopus 로고    scopus 로고
    • An antioxidant, probucol, induces anti-angiogenesis and apoptosis in athymic nude mouse xenografted human head and neck squamous carcinoma cells
    • Nishimura G, Yanoma S, Mizuno H, Kawakami K, Tsukuda M. An antioxidant, probucol, induces anti-angiogenesis and apoptosis in athymic nude mouse xenografted human head and neck squamous carcinoma cells. Jpn J Cancer Res 1999; 90(11): 1224-30.
    • (1999) Jpn J Cancer Res , vol.90 , Issue.11 , pp. 1224-1230
    • Nishimura, G.1    Yanoma, S.2    Mizuno, H.3    Kawakami, K.4    Tsukuda, M.5
  • 310
    • 0142210188 scopus 로고    scopus 로고
    • Inhibition of vascular endothelial growth factor-induced angiogenesis by resveratrol through interruption of Src-dependent vascular endothelial cadherin tyrosine phosphorylation
    • Lin MT, Yen ML, Lin CY, Kuo ML. Inhibition of vascular endothelial growth factor-induced angiogenesis by resveratrol through interruption of Src-dependent vascular endothelial cadherin tyrosine phosphorylation. Mol Pharmacol 2003; 64(5): 1029-36.
    • (2003) Mol Pharmacol , vol.64 , Issue.5 , pp. 1029-1036
    • Lin, M.T.1    Yen, M.L.2    Lin, C.Y.3    Kuo, M.L.4
  • 311
    • 34447542710 scopus 로고    scopus 로고
    • Optimal reactive oxygen species concentration and p38 MAP kinase are required for coronary collateral growth
    • Rocic P, Kolz C, Reed R, Potter B, Chilian WM. Optimal reactive oxygen species concentration and p38 MAP kinase are required for coronary collateral growth. Am J Physiol 2007; 292(6): H2729-36.
    • (2007) Am J Physiol , vol.292 , Issue.6 , pp. H2729-H2736
    • Rocic, P.1    Kolz, C.2    Reed, R.3    Potter, B.4    Chilian, W.M.5
  • 312
    • 33746641678 scopus 로고    scopus 로고
    • NADPH oxidasederived overproduction of reactive oxygen species impairs postischemic neovascularization in mice with type 1 diabetes
    • Ebrahimian TG, Heymes C, You D, et al. NADPH oxidasederived overproduction of reactive oxygen species impairs postischemic neovascularization in mice with type 1 diabetes. Am J Pathol 2006; 169(2): 719-28.
    • (2006) Am J Pathol , vol.169 , Issue.2 , pp. 719-728
    • Ebrahimian, T.G.1    Heymes, C.2    You, D.3
  • 313
    • 0019867381 scopus 로고
    • Increase in microvascular permeability induced by enzymatically generated free radicals. I. In vivo study
    • Del Maestro RF, Bjork J, Arfors KE. Increase in microvascular permeability induced by enzymatically generated free radicals. I. In vivo study. Microvasc Res 1981; 22(3): 239-54.
    • (1981) Microvasc Res , vol.22 , Issue.3 , pp. 239-254
    • Del Maestro, R.F.1    Bjork, J.2    Arfors, K.E.3
  • 314
    • 0019805197 scopus 로고
    • Increase in microvascular permeability induced by enzymatically generated free radicals. II. Role of superoxide anion radical, hydrogen peroxide, and hydroxyl radical
    • Del Maestro RF, Bjork J, Arfors KE. Increase in microvascular permeability induced by enzymatically generated free radicals. II. Role of superoxide anion radical, hydrogen peroxide, and hydroxyl radical. Microvasc Res 1981; 22(3): 255-70.
    • (1981) Microvasc Res , vol.22 , Issue.3 , pp. 255-270
    • Del Maestro, R.F.1    Bjork, J.2    Arfors, K.E.3
  • 315
    • 70350015332 scopus 로고    scopus 로고
    • The regulation of vascular endothelial growth factor-induced microvascular permeability requires Rac and reactive oxygen species
    • Monaghan-Benson E, Burridge K. The regulation of vascular endothelial growth factor-induced microvascular permeability requires Rac and reactive oxygen species. J Biol Chem 2009; 284(38): 25602-11.
    • (2009) J Biol Chem , vol.284 , Issue.38 , pp. 25602-25611
    • Monaghan-Benson, E.1    Burridge, K.2
  • 316
    • 0345258511 scopus 로고    scopus 로고
    • Redox regulation of reactive oxygen speciesinduced p38 MAP kinase activation and barrier dysfunction in lung microvascular endothelial cells
    • Usatyuk PV, Vepa S, Watkins T, He D, Parinandi NL, Natarajan V. Redox regulation of reactive oxygen speciesinduced p38 MAP kinase activation and barrier dysfunction in lung microvascular endothelial cells. Antioxid Redox Signal 2003; 5(6): 723-30.
    • (2003) Antioxid Redox Signal , vol.5 , Issue.6 , pp. 723-730
    • Usatyuk, P.V.1    Vepa, S.2    Watkins, T.3    He, D.4    Parinandi, N.L.5    Natarajan, V.6
  • 317
    • 61349202912 scopus 로고    scopus 로고
    • Iron oxide nanoparticles induce human microvascular endothelial cell permeability through reactive oxygen species production and microtubule remodeling
    • Apopa PL, Qian Y, Shao R, et al. Iron oxide nanoparticles induce human microvascular endothelial cell permeability through reactive oxygen species production and microtubule remodeling. Part Fibre Toxicol 2009; 6: 1.
    • (2009) Part Fibre Toxicol , vol.6 , pp. 1
    • Apopa, P.L.1    Qian, Y.2    Shao, R.3
  • 318
    • 35948971753 scopus 로고    scopus 로고
    • Reactive oxygen species alter brain endothelial tight junction dynamics via RhoA, PI3 kinase, and PKB signaling
    • Schreibelt G, Kooij G, Reijerkerk A, et al. Reactive oxygen species alter brain endothelial tight junction dynamics via RhoA, PI3 kinase, and PKB signaling. FASEB J 2007; 21(13): 3666-76.
    • (2007) FASEB J , vol.21 , Issue.13 , pp. 3666-3676
    • Schreibelt, G.1    Kooij, G.2    Reijerkerk, A.3
  • 319
    • 0032785562 scopus 로고    scopus 로고
    • Endothelial permeability and IL-6 production during hypoxia: Role of ROS in signal transduction
    • Ali MH, Schlidt SA, Chandel NS, Hynes KL, Schumacker PT, Gewertz BL. Endothelial permeability and IL-6 production during hypoxia: role of ROS in signal transduction. Am J Physiol 1999; 277(5 Pt 1): L1057-65.
    • (1999) Am J Physiol , vol.277 , Issue.5 , pp. L1057-L1065
    • Ali, M.H.1    Schlidt, S.A.2    Chandel, N.S.3    Hynes, K.L.4    Schumacker, P.T.5    Gewertz, B.L.6
  • 320
    • 61649085317 scopus 로고    scopus 로고
    • Amifostine reduces lung vascular permeability via suppression of inflammatory signalling
    • Fu P, Birukova AA, Xing J, et al. Amifostine reduces lung vascular permeability via suppression of inflammatory signalling. Eur Respir J 2009; 33(3): 612-24.
    • (2009) Eur Respir J , vol.33 , Issue.3 , pp. 612-624
    • Fu, P.1    Birukova, A.A.2    Xing, J.3
  • 321
    • 84884877254 scopus 로고    scopus 로고
    • Lipid peroxidation triggers neurodegeneration: A redox proteomics view into the Alzheimer disease brain
    • Sultana R, Perluigi M, Allan Butterfield D. Lipid peroxidation triggers neurodegeneration: a redox proteomics view into the Alzheimer disease brain. Free Radic Biol Med 2013; 62: 157-69.
    • (2013) Free Radic Biol Med , vol.62 , pp. 157-169
    • Sultana, R.1    Perluigi, M.2    Allan Butterfield, D.3
  • 322
    • 84899111176 scopus 로고    scopus 로고
    • Abeta, oxidative stress in Alzheimer disease: Evidence based on proteomics studies
    • Swomley AM, Forster S, Keeney JT, et al. Abeta, oxidative stress in Alzheimer disease: Evidence based on proteomics studies. Biochim Biophys Acta 2013; pii: S0925-4439(13)00297-4.
    • (2013) Biochim Biophys Acta , Issue.13
    • Swomley, A.M.1    Forster, S.2    Keeney, J.T.3
  • 323
    • 84881525560 scopus 로고    scopus 로고
    • Oxidative stress and the pathogenesis of Alzheimer's disease
    • Zhao Y, Zhao B. Oxidative stress and the pathogenesis of Alzheimer's disease. Oxid Med Cell Longev 2013; 2013: 316523.
    • (2013) Oxid Med Cell Longev , pp. 2013
    • Zhao, Y.1    Zhao, B.2
  • 324
    • 85027950089 scopus 로고    scopus 로고
    • Role of iron in ischemiainduced neurodegeneration: Mechanisms and insights
    • Minhas G, Modgil S, Anand A. Role of iron in ischemiainduced neurodegeneration: mechanisms and insights. Metab Brain Dis 2014; [Epub ahead of printing].
    • (2014) Metab Brain Dis
    • Minhas, G.1    Modgil, S.2    Anand, A.3
  • 325
    • 84874860528 scopus 로고    scopus 로고
    • Redox processes in neurodegenerative disease involving reactive oxygen species
    • Kovacic P, Somanathan R. Redox processes in neurodegenerative disease involving reactive oxygen species. Curr Neuropharmacol 2012; 10(4): 289-302.
    • (2012) Curr Neuropharmacol , vol.10 , Issue.4 , pp. 289-302
    • Kovacic, P.1    Somanathan, R.2
  • 326
    • 53049093018 scopus 로고    scopus 로고
    • Neurodegeneration in multiple sclerosis: The role of oxidative stress and excitotoxicity
    • Gonsette RE. Neurodegeneration in multiple sclerosis: the role of oxidative stress and excitotoxicity. J Neurol Sci 2008; 274(1-2): 48-53.
    • (2008) J Neurol Sci , vol.274 , Issue.1-2 , pp. 48-53
    • Gonsette, R.E.1
  • 327
    • 84855301917 scopus 로고    scopus 로고
    • Oxidative modification of patient's plasma proteins and its role in pathogenesis of multiple sclerosis
    • Miller E, Walczak A, Saluk J, Ponczek MB, Majsterek I. Oxidative modification of patient's plasma proteins and its role in pathogenesis of multiple sclerosis. Clin Biochem 2012; 45(1-2): 26-30.
    • (2012) Clin Biochem , vol.45 , Issue.1-2 , pp. 26-30
    • Miller, E.1    Walczak, A.2    Saluk, J.3    Ponczek, M.B.4    Majsterek, I.5
  • 328
    • 84875674753 scopus 로고    scopus 로고
    • The role of reactive oxygen species and proinflammatory cytokines in type 1 diabetes pathogenesis
    • Padgett LE, Broniowska KA, Hansen PA, Corbett JA, Tse HM. The role of reactive oxygen species and proinflammatory cytokines in type 1 diabetes pathogenesis. Ann N Y Acad Sci 2013; 1281: 16-35.
    • (2013) Ann N Y Acad Sci , vol.1281 , pp. 16-35
    • Padgett, L.E.1    Broniowska, K.A.2    Hansen, P.A.3    Corbett, J.A.4    Tse, H.M.5
  • 329
    • 84881230708 scopus 로고    scopus 로고
    • Reactive aldehydes--second messengers of free radicals in diabetes mellitus
    • Jaganjac M, Tirosh O, Cohen G, Sasson S, Zarkovic N. Reactive aldehydes--second messengers of free radicals in diabetes mellitus. Free Radic Res 2013; 47 Suppl 1: 39-48.
    • (2013) Free Radic Res , vol.47 , pp. 39-48
    • Jaganjac, M.1    Tirosh, O.2    Cohen, G.3    Sasson, S.4    Zarkovic, N.5
  • 330
    • 80051978779 scopus 로고    scopus 로고
    • Hydrogen sulfide replacement therapy protects the vascular endothelium in hyperglycemia by preserving mitochondrial function
    • Suzuki K, Olah G, Modis K, et al. Hydrogen sulfide replacement therapy protects the vascular endothelium in hyperglycemia by preserving mitochondrial function. Proc Natl Acad Sci USA 2011; 108(33): 13829-34.
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.33 , pp. 13829-13834
    • Suzuki, K.1    Olah, G.2    Modis, K.3
  • 331
    • 84884245354 scopus 로고    scopus 로고
    • Oxidative stress and nucleic acid oxidation in patients with chronic kidney disease
    • Sung CC, Hsu YC, Chen CC, Lin YF, Wu CC. Oxidative stress and nucleic acid oxidation in patients with chronic kidney disease. Oxid Med Cell Longev 2013; 2013: 301982.
    • (2013) Oxid Med Cell Longev , vol.2013
    • Sung, C.C.1    Hsu, Y.C.2    Chen, C.C.3    Lin, Y.F.4    Wu, C.C.5
  • 332
    • 84876135208 scopus 로고    scopus 로고
    • The role of redox signaling in epigenetics and cardiovascular disease
    • Kim GH, Ryan JJ, Archer SL. The role of redox signaling in epigenetics and cardiovascular disease. Antioxid Redox Signal 2013; 18(15): 1920-36.
    • (2013) Antioxid Redox Signal , vol.18 , Issue.15 , pp. 1920-1936
    • Kim, G.H.1    Ryan, J.J.2    Archer, S.L.3
  • 333
    • 0038673091 scopus 로고    scopus 로고
    • Antioxidant activities and oxidative stress byproducts in human hypertension
    • Redon J, Oliva MR, Tormos C, et al. Antioxidant activities and oxidative stress byproducts in human hypertension. Hypertension 2003; 41(5): 1096-101.
    • (2003) Hypertension , vol.41 , Issue.5 , pp. 1096-1101
    • Redon, J.1    Oliva, M.R.2    Tormos, C.3
  • 334
    • 77954083190 scopus 로고    scopus 로고
    • Epigenetic attenuation of mitochondrial superoxide dismutase 2 in pulmonary arterial hypertension: A basis for excessive cell proliferation and a new therapeutic target
    • Archer SL, Marsboom G, Kim GH, et al. Epigenetic attenuation of mitochondrial superoxide dismutase 2 in pulmonary arterial hypertension: a basis for excessive cell proliferation and a new therapeutic target. Circulation 2010; 121(24): 2661-71.
    • (2010) Circulation , vol.121 , Issue.24 , pp. 2661-2671
    • Archer, S.L.1    Marsboom, G.2    Kim, G.H.3
  • 335
    • 67549140385 scopus 로고    scopus 로고
    • Reactive oxidative metabolites are associated with atrial conduction disturbance in patients with atrial fibrillation
    • Shimano M, Shibata R, Inden Y, et al. Reactive oxidative metabolites are associated with atrial conduction disturbance in patients with atrial fibrillation. Heart Rhythm 2009; 6(7): 935-40.
    • (2009) Heart Rhythm , vol.6 , Issue.7 , pp. 935-940
    • Shimano, M.1    Shibata, R.2    Inden, Y.3


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