메뉴 건너뛰기




Volumn 1 E, Issue 1, 2009, Pages 179-188

Mechanisms of the suppression of free radical overproduction by antioxidants

Author keywords

Antioxidants; Catalase; Deferoxamine; Free radical overproduction; Glutathione peroxidases; Lipoxygenase; Myeloperoxidase; Nadph oxidase; Oxidative stress; Peroxides; Peroxyl radicals; Plants polyphenols; Prooxidant enzymes; Reactive oxygen species; Review; Superoxide dismutase; Transition metals; Vitamin C; Vitamin E; Xanthine oxidase

Indexed keywords

ANTIOXIDANT; CHELATING AGENT; ENZYME INHIBITOR; FREE RADICAL; OXIDOREDUCTASE; PERHYDROXYL RADICAL; PEROXIDE; SCAVENGER;

EID: 77649320307     PISSN: 19450494     EISSN: 19450508     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (17)

References (77)
  • 1
    • 0033281840 scopus 로고    scopus 로고
    • Food processing and lipid oxidation
    • J. German: Food processing and lipid oxidation. Adv Exp Med Biol 459, 23-50 (1999)
    • (1999) Adv Exp Med Biol , vol.459 , pp. 23-50
    • German, J.1
  • 2
    • 0029680559 scopus 로고
    • Three eitamin C discovery
    • R. Jacob: Three eitamin C discovery. Subcell Biochem 25, 1-16 (1966)
    • (1966) Subcell Biochem , vol.25 , pp. 1-16
    • Jacob, R.1
  • 3
    • 0031741551 scopus 로고    scopus 로고
    • Free radicals: Their history and current status in aging and disease
    • J. Knight: Free radicals: their history and current status in aging and disease. Ann Clin Lab Sci 28, 331-346 (1998) (Pubitemid 28541691)
    • (1998) Annals of Clinical and Laboratory Science , vol.28 , Issue.6 , pp. 331-346
    • Knight, J.A.1
  • 4
    • 0015523099 scopus 로고
    • The role of superoxide anion in the autoxidation of epinephrine and a simple assay for superoxide dismutase
    • H. P. Misra and I. Fridovich: The role of superoxide anion in the autoxidation of epinephrine and a simple assay for superoxide dismutase. J Biol Chem 247, 3170-3175 (1972)
    • (1972) J Biol Chem , vol.247 , pp. 3170-3175
    • Misra, H.P.1    Fridovich, I.2
  • 6
    • 0037296183 scopus 로고    scopus 로고
    • Superoxide as an obligatory, catalytic intermediate in photosynthetic reduction of oxygen by adrenaline and dopamine
    • J. F. Allen: Superoxide as an obligatory, catalytic intermediate in photosynthetic reduction of oxygen by adrenaline and dopamine antioxidants. Redox Signaling 5, 7-14 (2003) (Pubitemid 36337011)
    • (2003) Antioxidants and Redox Signaling , vol.5 , Issue.1 , pp. 7-14
    • Allen, J.F.1
  • 7
    • 0020966585 scopus 로고
    • Importance of oxygen free radicals in asbestos-induced injury to airway epithelial cells
    • B. T. Mossman and J. M. Landesman: Importance of oxygen-free radicals in asbestos-induced injury to airway epithelial cells. Chest 83, 50S-51S (1983) (Pubitemid 13084782)
    • (1983) Chest , vol.83 , Issue.5 SUPPL.
    • Mossman, B.T.1    Landesman, J.M.2
  • 10
    • 0032127729 scopus 로고    scopus 로고
    • Antiradical and chelating effects in flavonoid protection against silica-induced cell injury
    • DOI 10.1006/abbi.1998.0708
    • V. A. Kostyuk and A. I. Potapovich: Antiradical and chelating effects in flavonoids protection against silicainduced cells injury. Arch Biochem Biophys 355, 43-48 (1998) (Pubitemid 28371150)
    • (1998) Archives of Biochemistry and Biophysics , vol.355 , Issue.1 , pp. 43-48
    • Kostyuk, V.A.1    Potapovich, A.I.2
  • 11
    • 0034518915 scopus 로고    scopus 로고
    • Protective effects of green tea catechins against asbestos-induced cell injury
    • DOI 10.1055/s-2000-9567
    • V. A. Kostyuk, A. I. Potapovich, E. N. Vladykovskaya and M. Hiramatsu: Protective effects of green tea catechins against asbestos-induced cell injury. Planta Med 66, 762-764 (2000) (Pubitemid 32038937)
    • (2000) Planta Medica , vol.66 , Issue.8 , pp. 762-764
    • Kostyuk, V.A.1    Potapovich, A.I.2    Vladykovskaya, E.N.3    Hiramatsu, M.4
  • 12
    • 0038548415 scopus 로고    scopus 로고
    • Comparative study of antioxidant properties and cytoprotective activity of flavonoids
    • A. I. Potapovich and V. A. Kostyuk: Comparative study of antioxidant properties and cytoprotective activity of flavonoids. Biochemistry (Moscow) 68, 514-519 (2003)
    • (2003) Biochemistry (Moscow) , vol.68 , pp. 514-519
    • Potapovich, A.I.1    Kostyuk, V.A.2
  • 13
    • 73049136229 scopus 로고
    • Reduction of carbon tetrachloride in vivo and reduction of carbon tetrachloride and chloroform in vitro by tissues and tissue constituents
    • T. C. Butler: Reduction of carbon tetrachloride in vivo and reduction of carbon tetrachloride and chloroform in vitro by tissues and tissue constituents. J Pharmacol Exp Ther 134, 311-319 (1961)
    • (1961) J Pharmacol Exp Ther , vol.134 , pp. 311-319
    • Butler, T.C.1
  • 15
    • 0014012187 scopus 로고
    • Lipoperoxidation of rat liver microsomal lipids induced by carbon tetrachloride
    • R. O. Recknagel and A. K. Ghoshal: Lipoperoxidation of rat liver microsomal lipids induced by carbon tetrachloride. Nature 210, 1162-1163 (1966)
    • (1966) Nature , vol.210 , pp. 1162-1163
    • Recknagel, R.O.1    Ghoshal, A.K.2
  • 16
    • 0013872594 scopus 로고
    • Necrogenic action of carbon tetrachloride in the rat: A speculative mechanism based on activation
    • T. F. Slater: Necrogenic action of carbon tetrachloride in the rat: a speculative mechanism based on activation. Nature 209, 36-46 (1966)
    • (1966) Nature , vol.209 , pp. 36-46
    • Slater, T.F.1
  • 17
    • 0018084856 scopus 로고
    • .) with amino acids: Pulse radiolysis evidence
    • J. S. Packer, T. F. Slater and R. L. Willson: Reactions of the carbon tetrachloride-related peroxy free radical with amino acids: pulse radiolysis evidence. Life Sci 23, 2617-2620 (1978) (Pubitemid 9079236)
    • (1978) Life Sciences , vol.23 , Issue.26 , pp. 2617-2620
    • Packer, J.E.1    Slater, T.F.2    Willson, R.L.3
  • 18
    • 0003101832 scopus 로고
    • Biochemical aspects of fatty liver
    • Ed: R. G. Meeks., S. D. Harrison and R. J. Bull. London
    • M. U. Dianzani: Biochemical aspects of fatty liver. In: Hepatotoxicology. Ed: R. G. Meeks., S. D. Harrison and R. J. Bull. London, 327-399 (1991)
    • (1991) Hepatotoxicology , pp. 327-399
    • Dianzani, M.U.1
  • 19
    • 0026327953 scopus 로고
    • 4-(4-R-phenylamino)-5-methoxy-1, 2-benzoquinones are new selective inhibitors of carbon tetrachloride-initiated free radical reactions in liver
    • V. A. Kostyuk, A. I. Potapovich and S. M. Tereshchenko: 4-(4-R-phenylamino)-5-methoxy-1, 2-benzoquinones are new selective inhibitors of carbon tetrachloride-initiated free radical reactions in liver. Biochem Int 25, 167-172 (1991)
    • (1991) Biochem Int , vol.25 , pp. 167-172
    • Kostyuk, V.A.1    Potapovich, A.I.2    Tereshchenko, S.M.3
  • 20
    • 0026331392 scopus 로고
    • Damage of the liver microsomal mixed function oxidase system by carbon tetrachloride in vivo study with selective inhibitor of lipid peroxidation
    • V. A. Kostyuk and A. I. Potapovich: Damage of the liver microsomal mixed function oxidase system by carbon tetrachloride. in vivo study with selective inhibitor of lipid peroxidation. Biochem Int 25, 349-353 (1991)
    • (1991) Biochem Int , vol.25 , pp. 349-353
    • Kostyuk, V.A.1    Potapovich, A.I.2
  • 21
    • 0032810265 scopus 로고    scopus 로고
    • Nitrogen dioxide radical generated by the myeloperoxidase-hydrogen peroxide-nitrite system promotes lipid peroxidation of low density lipoprotein
    • DOI 10.1016/S0014-5793(99)00893-5, PII S0014579399008935
    • J. Byun, D. M. Mueller, J. S. Fabjan and J. W. Heinecke: Nitrogen dioxide radical generated by the myeloperoxidase-hydrogen peroxide-nitrite system promotes lipid peroxidation of low density lipoprotein. FEBS Lett 455, 243-246 (1999) (Pubitemid 29333044)
    • (1999) FEBS Letters , vol.455 , Issue.3 , pp. 243-246
    • Byun, J.1    Mueller, D.M.2    Fabjan, J.S.3    Heinecke, J.W.4
  • 22
    • 0030909465 scopus 로고    scopus 로고
    • Formation of reactive nitrogen species during peroxidase-catalyzed oxidation of nitrite: A potential additional mechanism of nitric oxide- dependent toxicity
    • DOI 10.1074/jbc.272.12.7617
    • A. Van der Vliet, J. P. Eiserich, B. Halliwell and C. E. Cross: Formation of reactive nitrogen species during peroxidase-catalyzed oxidation of nitrite. A potential additional mechanism of nitric oxide-dependent toxicity. J Biol Chem 272, 7617-7625 (1997) (Pubitemid 27137309)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.12 , pp. 7617-7625
    • Van Der Vliet, A.1    Eiserich, J.P.2    Halliwell, B.3    Cross, C.E.4
  • 23
    • 0037468521 scopus 로고    scopus 로고
    • Myeloperoxidase/nitrite-mediated lipid peroxidation of low-density lipoprotein as modulated by flavonoids
    • DOI 10.1016/S0014-5793(03)00113-3
    • V. A. Kostyuk, T. Kraemer, H. Sies and T. Schewe: Myeloperoxidase/ nitrate-mediated lipid peroxidation of low-density lipoprotein as modulated by flavonoids. FEBS Lett 537, 146-150 (2003) (Pubitemid 36246692)
    • (2003) FEBS Letters , vol.537 , Issue.1-3 , pp. 146-150
    • Kostyuk, V.A.1    Kraemer, T.2    Sies, H.3    Schewe, T.4
  • 24
    • 33845374568 scopus 로고
    • Vitamin E: Application of the principles of physical organic chemistry to exploration of its structure and function
    • G. W. Burton and K. U. Ingold: Vitamin E: Application of the principles of physical organic chemistry to exploration of its structure and function. Acc Chem Res 19, 194-201 (1986)
    • (1986) Acc Chem Res , vol.19 , pp. 194-201
    • Burton, G.W.1    Ingold, K.U.2
  • 25
    • 0034656850 scopus 로고    scopus 로고
    • Phenolic antioxidants: A rationale for design and evaluation of novel antioxidant drug for atherosclerosis
    • DOI 10.1016/S0891-5849(00)00256-2, PII S0891584900002562
    • N. Noguchi and E. Niki: Phenolic antioxidants: a rationale for design and evaluation of novel antioxidant drug for atherosclerosis. Free Radic Biol Med 28, 1538-1546 (2000) (Pubitemid 30604237)
    • (2000) Free Radical Biology and Medicine , vol.28 , Issue.10 , pp. 1538-1546
    • Noguchi, N.1    Niki, E.2
  • 26
    • 33845377128 scopus 로고
    • Autoxidation of biological molecules. 4. Maximizing the antioxidant activity of phenols
    • G. W. Burton, T. Doba, E. J. Gabe, L. Hughes, F. L. Lee, L. Prasa and K. U. Ingold: Autoxidation of biological molecules. 4. Maximizing the antioxidant activity of phenols. J Am Chem Soc 107, 7053-7065 (1985)
    • (1985) J Am Chem Soc , vol.107 , pp. 7053-7065
    • Burton, G.W.1    Doba, T.2    Gabe, E.J.3    Hughes, L.4    Lee, F.L.5    Prasa, L.6    Ingold, K.U.7
  • 27
    • 0022564974 scopus 로고
    • Nomenclature Policy: Generic descriptors and trivial names for vitamins and related compounds
    • Nomenclature Policy: Generic descriptors and trivial names for vitamins and related compounds. J Nutr 116, 8-16 (1986)
    • (1986) J Nutr , vol.116 , pp. 8-16
  • 28
    • 0020074850 scopus 로고
    • Autoxidation of biological molecules. 1. The antioxidant activity of vitamin E and related chain-breaking phenolic antioxidants in vitro
    • DOI 10.1021/ja00411a035
    • G. W. Burton and K. U. Ingold: Autoxidation of biological molecules. 1. The antioxidant activity of vitamin E and related chain-breaking phenolic antioxidants in vitro. J Am Chem Soc 103, 6472-6477 (1981) (Pubitemid 12145820)
    • (1982) Journal of the American Chemical Society , vol.103 , Issue.21 , pp. 6472-6477
    • Burton, G.W.1    Ingold, K.U.2
  • 29
    • 0019915241 scopus 로고
    • Oxidation of lipids. II. Rate of inhibition of oxidation by tocopherol and hindered phenols measured by chemiluminescence
    • DOI 10.1246/bcsj.55.1551
    • E. Niki, R. Tanimura and Y. Kamiya: Oxidation of lipids. II. Rate of inhibition of oxidation of α-tocopherol and hindered phenols measured by chemiluminescence. Bull Chem Soc Jpn 55, 1551-1555 (1982) (Pubitemid 12008357)
    • (1982) Bulletin of the Chemical Society of Japan , vol.55 , Issue.5 , pp. 1551-1555
    • Niki, E.1    Tanimura, R.2    Kamiya, Y.3
  • 30
    • 0027232771 scopus 로고
    • Syntex Award lecture. Model biomembranes: Quantitative studies of peroxidation, antioxidat action, partitioning, and oxidative stress
    • L. R. C. Burclay: Syntex Award lecture. Model biomembranes: quantitative studies of peroxidation, antioxidat action, partitioning, and oxidative stress. Can J Chem 71, 1-16 (1993)
    • (1993) Can J Chem , vol.71 , pp. 1-16
    • Burclay, L.R.C.1
  • 32
    • 0001896864 scopus 로고
    • Peroxy radicals
    • K. U. Ingold: Peroxy radicals. Acc Chem Res 2, 1-9 (1969)
    • (1969) Acc Chem Res , vol.2 , pp. 1-9
    • Ingold, K.U.1
  • 33
    • 2942534387 scopus 로고    scopus 로고
    • Formation of phosphatidic acid, ceramide, and diglyceride on radiolysis of lipids: Identification by MALDI-TOF mass spectrometry
    • DOI 10.1016/j.freeradbiomed.2004.03.013, PII S0891584904002746
    • O. Shadyro, I. Yurkova, M. Kisel, O. Brede and J. Arnhold: Formation of phosphatidic acid, ceramide, and diglyceride on radiolysis of lipids: identification by MALDI-TOF mass spectrometry. Free Radic Biol Med 36, 1612-1624 (2004) (Pubitemid 38746567)
    • (2004) Free Radical Biology and Medicine , vol.36 , Issue.12 , pp. 1612-1624
    • Shadyro, O.1    Yurkova, I.2    Kisel, M.3    Brede, O.4    Arnhold, J.5
  • 34
    • 0035910611 scopus 로고    scopus 로고
    • Interactions between nitric oxide and lipid oxidation pathways
    • V. B. O'Donnell and B. A. Freeman: Interactions between nitric oxide and lipid oxidation pathways. Circ Res 88, 12-21 (2001)
    • (2001) Circ Res , vol.88 , pp. 12-21
    • O'Donnell, V.B.1    Freeman, B.A.2
  • 35
    • 0022529172 scopus 로고
    • Oxygen free radicals and iron in relation to biology and medicine: Some problems and concepts
    • B. Halliwell and J. M. C. Gutteridge: Oxygen free radicals and iron in relation to biology and medicine: some problems and concepts. Arch Biochem Biophys 246, 501-514 (1986) (Pubitemid 16072574)
    • (1986) Archives of Biochemistry and Biophysics , vol.246 , Issue.2 , pp. 501-514
    • Halliwell, B.1    Gutteridge, J.M.C.2
  • 36
    • 0024407187 scopus 로고
    • Biochemistry of oxygen toxicity
    • E. Cadenas: Biochemistry of oxygen toxicity. Annu Rev Biochem 58, 79-110 (1989) (Pubitemid 19172965)
    • (1989) Annual Review of Biochemistry , vol.58 , pp. 79-110
    • Cadenas, E.1
  • 38
    • 0031934177 scopus 로고    scopus 로고
    • Low molecular weight iron in cerebral ischemic acidosis in vivo
    • D. C. Lipscomb, L. G. Gorman, R. J. Traystman and P. D. Hurn: Low molecular weight iron in cerebral ischemic acidosis in vivo. Stroke 29, 487-493 (1998) (Pubitemid 28086696)
    • (1998) Stroke , vol.29 , Issue.2 , pp. 487-493
    • Lipscomb, D.C.1    Gorman, L.G.2    Traystman, R.J.3    Hurn, P.D.4
  • 39
    • 0026692807 scopus 로고
    • Role of iron and iron chelation in dopaminergicinduced neurodegeneration: Implication for Parkinson's disease
    • D. Ben-Shachar, G. Eshel, P. Riedere and M. B. H. Youdim: Role of iron and iron chelation in dopaminergicinduced neurodegeneration: implication for Parkinson's disease. Ann Neurol 32, S105-S110 (1992)
    • (1992) Ann Neurol , vol.32
    • Ben-Shachar, D.1    Eshel, G.2    Riedere, P.3    Youdim, M.B.H.4
  • 40
    • 0026484388 scopus 로고
    • The oxidant stress hypothesis in Parkinson's disease: Evidence supporting it
    • S. Fahn and G. Cohen: The oxidant stress hypothesis in Parkinson's disease: evidence supporting it. Ann Neurol 32, 804-812 (1992)
    • (1992) Ann Neurol , vol.32 , pp. 804-812
    • Fahn, S.1    Cohen, G.2
  • 41
    • 0032971328 scopus 로고    scopus 로고
    • Increased iron in the dentate nucleus of patients with Friedreich's ataxia
    • DOI 10.1002/1531-8249 (199907)46:1<123::AID-ANA19>3.0.CO;2-H
    • D. Waldvogel, P. Van Gelderen and M. Hallett: Increased iron in the dentate nucleus of patients with Friedrich's ataxia. Ann Neurol 46; 123-125 (1999) (Pubitemid 29314392)
    • (1999) Annals of Neurology , vol.46 , Issue.1 , pp. 123-125
    • Waldvogel, D.1    Van Gelderen, P.2    Hallett, M.3
  • 42
    • 0033617578 scopus 로고    scopus 로고
    • Undetectable intracellular free copper: The requirement of a copper chaperone for superoxide dismutase
    • DOI 10.1126/science.284.5415.805
    • T. D. Rae, P. J. Schmidt, R. A. Pufahl, V. C. Culotta and T. V. O'Halloran: Undetectable intracellular free copper: the requirement of a copper chaperone for superoxide dismutase. Science 284, 805-808 (1999) (Pubitemid 29291346)
    • (1999) Science , vol.284 , Issue.5415 , pp. 805-808
    • Rae, T.D.1    Schmidt, P.J.2    Pufahl, R.A.3    Culotta, V.C.4    O'Halloran, T.V.5
  • 43
    • 0021111024 scopus 로고
    • Hydroxil free radical formation from hydrogen peroxide by ferrous ironnucleotide complexes
    • R. A. Floyd and C. A. Lewis: Hydroxil free radical formation from hydrogen peroxide by ferrous ironnucleotide complexes. Biochem 22, 2645-2649 (1983)
    • (1983) Biochem , vol.22 , pp. 2645-2649
    • Floyd, R.A.1    Lewis, C.A.2
  • 44
    • 0023338482 scopus 로고
    • Ferrous-salt-promoted damage to deoxyribose and benzoate. The increased effectiveness of hydroxyl-radical scavangers in the presence of EDTA
    • J. M. C. Gutteridge: Ferrous-salt-promoted damage to deoxyribose and benzoate. The increased effectiveness of hydroxyl-radical scavangers in the presence of EDTA. Biochem J 243, 709-714 (1987)
    • (1987) Biochem J , vol.243 , pp. 709-714
    • Gutteridge, J.M.C.1
  • 45
    • 0023547633 scopus 로고
    • Radical-driven Fenton reactions: Studies with paraquat, adriamycin, and anthraquinone 6-sulfonate and citrate, ATP, ADP, and pyrophosphate iron chelates
    • G. F. Vile, C. C. Winterbourn and H. C. Sutton: Radical-driven Fenton reactions: studies with paraquat, adriamycin, and anthraquinone 6-sulfonate and citrate, ATP, ADP, and pyrophosphate iron chelates. Arch Biochem Biophys 259, 616-626 (1987) (Pubitemid 18022772)
    • (1987) Archives of Biochemistry and Biophysics , vol.259 , Issue.2 , pp. 616-626
    • Vile, G.F.1    Winterbourn, C.C.2    Sutton, H.C.3
  • 46
    • 0024790459 scopus 로고
    • Protection against tissue damage in vivo by desferrioxamine: What is its mechanism of action?
    • B. Halliwell: Protection against tissue damage in vivo by desferrioxamine: what is its mechanism of action? Free Radic Biol Med 7, 645.651 (1989)
    • (1989) Free Radic Biol Med , vol.7 , pp. 645651
    • Halliwell, B.1
  • 48
    • 0023854331 scopus 로고
    • Evidence suggesting a role for hydroxyl radical in gentamicin-induced acute renal failure in rats
    • P. D. Walker and S. V. Shah: Evidence suggesting a role for hydroxyl radical in gentamicin-induced acute renal failure in rats. J Clin Invest 81, 334.341 (1988)
    • (1988) J Clin Invest , vol.81 , pp. 334341
    • Walker, P.D.1    Shah, S.V.2
  • 49
    • 0024364268 scopus 로고
    • Chelating and free radical scavenging mechanisms of inhibitory action of rutin and quercetin in lipid peroxidation
    • DOI 10.1016/0006-2952(89)90410-3
    • I. B. Afanas'ev, A. I. Dorozhko, A. V. Brodskii, V. A. Kostyuk and A. I. Potapovitch: Chelating and free radical scavenging mechanisms of inhibitory action of rutin and quercetin in lipid peroxidation. Biochem Pharmacol 38, 1763-1769 (1989) (Pubitemid 19138525)
    • (1989) Biochemical Pharmacology , vol.38 , Issue.11 , pp. 1763-1769
    • Afanas'ev, I.B.1    Dorozhko, A.I.2    Brodskii, A.V.3    Kostyuk, V.A.4    Potapovitch, A.I.5
  • 50
    • 0033859612 scopus 로고    scopus 로고
    • Flavonoids as antioxidants
    • P. G. Pietta: Flavonoids as antioxidants. J Nat Prod 63, 1035-1042 (2000)
    • (2000) J Nat Prod , vol.63 , pp. 1035-1042
    • Pietta, P.G.1
  • 52
    • 3042718120 scopus 로고    scopus 로고
    • Experimental evidence that flavonoid metal complexes may act as mimics of superoxide dismutase
    • DOI 10.1016/j.abb.2004.06.008, PII S0003986104003212
    • V. A. Kostyuk, A. I. Potapovich, E. N. Strigunova, T. V. Kostyuk and I. B. Afanas'ev: Experimental evidence that flavonoids metal complexes may act as mimics of superoxide dismutase. Arch Biochem Biophys 428, 204-208 (2004) (Pubitemid 38891564)
    • (2004) Archives of Biochemistry and Biophysics , vol.428 , Issue.2 , pp. 204-208
    • Kostyuk, V.A.1    Potapovich, A.I.2    Strigunova, E.N.3    Kostyuk, T.V.4    Afanas'ev, I.B.5
  • 53
    • 0348047624 scopus 로고    scopus 로고
    • Lipoxygenase Interactions with Natural Flavonoid, Quercetin, Reveal a Complex with Protocatechuic Acid in Its X-Ray Structure at 2.1 A Resolution
    • DOI 10.1002/prot.10579
    • O. Y. Borbulevych, J. Jankun, S. H. Selman and E. Skrzypczak-Jankun: Lipoxygenase interactions with natural flavonoid, quercetin, reveal a complex with protocatechuic acid in its X-ray structure at 2.1 A resolution. Proteins 54, 13-19 (2004) (Pubitemid 38036911)
    • (2004) Proteins: Structure, Function and Genetics , vol.54 , Issue.1 , pp. 13-19
    • Borbulevych, O.Y.1    Jankun, J.2    Selman, S.H.3    Skrzypczak-Jankun, E.4
  • 55
    • 0036299977 scopus 로고    scopus 로고
    • Flavonoids of cocoa inhibit recombinant human 5-lipoxygenase
    • T. Schewe, H. Kuhn and H. Sies: Flavonoids of cocoa inhibit recombinant human 5-lipoxygenase. J Nutr 132, 1825.1829 (2002)
    • (2002) J Nutr , vol.132 , pp. 18251829
    • Schewe, T.1    Kuhn, H.2    Sies, H.3
  • 56
    • 0026095778 scopus 로고
    • Inhibition of mammalian 5-lipoxygenase and cyclo-oxygenase by flavonoids and phenolic dietary additives. Relationship to antioxidant activity and to iron ion-reducing ability
    • M. J. Laughton, P. J. Evans, M. A. Moroney, J. R. Hoult and B. Halliwell: Inhibition of mammalian 5-lipoxygenase and cyclo-oxygenase by flavonoids and phenolic dietary additives. Relationship to antioxidant activity and to iron ion-reducing ability. Biochem Pharmacol 42, 1673-1681 (1991)
    • (1991) Biochem Pharmacol , vol.42 , pp. 1673-1681
    • Laughton, M.J.1    Evans, P.J.2    Moroney, M.A.3    Hoult, J.R.4    Halliwell, B.5
  • 57
  • 58
    • 0036249657 scopus 로고    scopus 로고
    • 15-Lipoxygenase-1: A prooxidant menzyme
    • T. Schewe: 15-Lipoxygenase-1: a prooxidant menzyme. Biol Chem 383, 365.374 (2002)
    • (2002) Biol Chem , vol.383 , pp. 365374
    • Schewe, T.1
  • 59
    • 0019440515 scopus 로고
    • Superoxide radicals in feline intestinal ischemia
    • D. N. Granger, G. Rutili and J. M. McCord: Superoxide radicals in feline intestinal ischemia. Gastroenterology 81, 22-29 (1981) (Pubitemid 11078477)
    • (1981) Gastroenterology , vol.81 , Issue.1 , pp. 22-29
    • Granger, D.N.1    Rutili, G.2    McCord, J.M.3
  • 60
    • 0021984681 scopus 로고
    • Oxygen-derived free radical in postischemic tissue injury
    • J. M. McCord: Oxygen-derived free radical in postischemic tissue injury. N Engl J Med 312, 159.163 (1985)
    • (1985) N Engl J Med , vol.312 , pp. 159163
    • McCord, J.M.1
  • 61
    • 0034028841 scopus 로고    scopus 로고
    • Exposure to cigarette smoke increases apoptosis in the rat gastric mucosa through a reactive oxygen species-mediated and p53-independent pathway
    • DOI 10.1016/S0891-5849(00)00207-0, PII S0891584900002070
    • H.-Y. Wang, L. Ma, Y. Li and C.-H. Cho: Exposure to cigarette smoke increases apoptosis in the rat gastric mucosa through a reactive oxygen species.mediated and p53-independent pathway. Free Radic Biol Med 28, 1125. 1131 (2000) (Pubitemid 30314711)
    • (2000) Free Radical Biology and Medicine , vol.28 , Issue.7 , pp. 1125-1131
    • Wang, H.-Y.1    Ma, L.2    Li, Y.3    Cho, C.-H.4
  • 62
    • 34250212563 scopus 로고    scopus 로고
    • Epicatechin elevates nitric oxide in endothelial cells via inhibition of NADPH oxidase
    • Y. Steffen, T. Schewe, H. Sies: (-)-Epicatechin elevates nitric oxide in endothelial cells via inhibition of NADPH oxidase. Biochem Biophys Res Commun 359, 828.833 (2007).
    • (2007) Biochem Biophys Res Commun , vol.359 , pp. 828833
    • Steffen, Y.1    Schewe, T.2    Sies, H.3
  • 63
    • 37549011857 scopus 로고    scopus 로고
    • Mono-Omethylated flavanols and other flavonoids as inhibitors of endothelial NADPH oxidase
    • doi:10.1016/j.abb.2007.10.012
    • Y. Steffen, C. Gruber, T. Schewe, H. Sies: Mono-Omethylated flavanols and other flavonoids as inhibitors of endothelial NADPH oxidase. Arch Biochem Biophys doi:10.1016/j.abb.2007.10.012 (2007)
    • (2007) Arch Biochem Biophys
    • Steffen, Y.1    Gruber, C.2    Schewe, T.3    Sies, H.4
  • 64
    • 0021351203 scopus 로고
    • Oxygen toxicity, oxygen radicals, transition metals and disease
    • B. Halliwell and J. M. C. Gutteridge: Oxygen toxicity, oxygen radicals, transition metals and disease. Biochem J 219, 1-14 (1984) (Pubitemid 14171443)
    • (1984) Biochemical Journal , vol.219 , Issue.1 , pp. 1-14
    • Halliwell, B.1    Gutteridge, J.M.C.2
  • 66
    • 0027931061 scopus 로고
    • Immunolocalization of antioxidant enzymes in adult hamster kidney
    • K. E. Muse, T. D. Oberley, J. M. Sempf and L. W. Oberley: Immunolocalization of antioxidant enzymes in adult hamster kidney. Histochem J 26, 734.753 (1994)
    • (1994) Histochem J , vol.26 , pp. 734753
    • Muse, K.E.1    Oberley, T.D.2    Sempf, J.M.3    Oberley, L.W.4
  • 67
    • 0023003551 scopus 로고
    • Antioxidant defense mechanisms of endothelial cells: Glutathione redox cycle versus catalase
    • N. Suttorp, W. Toepfer and L. Roka: Antioxidant defense mechanisms of endothelial cells: glutathione redox cycle versus catalase. Am J Physiol 251, 671-680 (1986)
    • (1986) Am J Physiol , vol.251 , pp. 671-680
    • Suttorp, N.1    Toepfer, W.2    Roka, L.3
  • 68
    • 0026353296 scopus 로고
    • Antioxidant defenses of cultured gastric cells against oxygen metabolites - Role of GSH redox cycle and endogenous catalase
    • H. Hiraishi, A. Terano, S. Ota, H. Mutoh, T. Sugimoto, M. Razandi and K. J. Ivey: Antioxidant defenses of cultured gastric cells against oxygen metabolites - role of GSH redox cycle and endogenous catalase. Am J Physiol 261, 921-928 (1991)
    • (1991) Am J Physiol , vol.261 , pp. 921-928
    • Hiraishi, H.1    Terano, A.2    Ota, S.3    Mutoh, H.4    Sugimoto, T.5    Razandi, M.6    Ivey, K.J.7
  • 69
    • 0023942502 scopus 로고
    • Significance of alterations in hepatic antioxidant enzymes. Primacy of glutathione peroxidase
    • T. W. Simmons and I. S. Jamall: Significance of alterations in hepatic antioxidant enzymes. Primacy of glutathione peroxidase. Biochem J 251, 913-917 (1988)
    • (1988) Biochem J , vol.251 , pp. 913-917
    • Simmons, T.W.1    Jamall, I.S.2
  • 70
    • 70449174079 scopus 로고
    • Hemoglobin catabolism. 1. Glutathione peroxidase, an erythrocyte enzyme which protects hemoglobin from oxidative breakdown
    • G. C. Mills: Hemoglobin catabolism. 1. Glutathione peroxidase, an erythrocyte enzyme which protects hemoglobin from oxidative breakdown. J Biol Chem 229, 189-197 (1957)
    • (1957) J Biol Chem , vol.229 , pp. 189-197
    • Mills, G.C.1
  • 71
    • 0001412723 scopus 로고
    • Glutathione peroxidase brought into focus
    • Ed: W. A. Pryor. New York
    • L. Flohe: Glutathione peroxidase brought into focus. In: Free radicals in biology. Ed: W. A. Pryor. New York, 223-275 (1982)
    • (1982) Free Radicals in Biology , pp. 223-275
    • Flohe, L.1
  • 73
    • 0001445231 scopus 로고    scopus 로고
    • Characterization of three isoforms of mammalian peroxiredoxin that reduce peroxides in the presence of thioredoxin
    • DOI 10.1016/S0168-8227(99)00037-6, PII S0168822799000376
    • H. Z. Chae, H. J. Kim, S. W. Kang and S. G. Rhee: Characterization of three isoforms of mammalian preoxiredoxin that reduce peroxides in the presence of thioredoxin. Diabetes Res Clin Pract 45, 101-112 (1999) (Pubitemid 29457756)
    • (1999) Diabetes Research and Clinical Practice , vol.45 , Issue.2-3 , pp. 101-112
    • Chae, H.Z.1    Kim, H.J.2    Kang, S.W.3    Rhee, S.G.4
  • 75
    • 0027432212 scopus 로고
    • Is copper pro- or anti-inflammatory? A reconciling view and a novel approach for the use of copper in the control of inflammation
    • DOI 10.1007/BF01998975
    • G. Berthon: Is copper pro-or anti-inflammatory? A reconciling view and a novel approach for the use of copper in the control of inflammation. Agents Actions 39, 210-217 (1993) (Pubitemid 23349831)
    • (1993) Agents and Actions , vol.39 , Issue.3-4 , pp. 210-217
    • Berthon, G.1
  • 76
    • 33244458002 scopus 로고    scopus 로고
    • .OH-inactivating ligand: A quantitative investigation of its copper handling role in vivo
    • DOI 10.1016/j.jinorgbio.2005.12.002, PII S016201340500351X
    • B. Halova-Lajoie, V. Brumas, M. M. Fiallo and G. Berthon: Copper (II) interactions with non-steroidal antiinflammatory agents. III-3- Methoxyanthranilic acid as a potential ·OH-inactivating ligand: a quantitative investigation of its copper handling role in vivo. J Inorg Biochem 100, 362-373 (2006) (Pubitemid 43276087)
    • (2006) Journal of Inorganic Biochemistry , vol.100 , Issue.3 , pp. 362-373
    • Halova-Lajoie, B.1    Brumas, V.2    Fiallo, M.M.L.3    Berthon, G.4
  • 77
    • 70450199883 scopus 로고    scopus 로고
    • Plant polyphenol-metal complexes: Effects on reactive oxygen species and cytoprotection against oxidative damage
    • October 10-13, 2007, Vilamoura, Algarve, Portugal, Medimond
    • V. Kostyuk, A. Potapovich and L. Korkina: Plant polyphenol-metal complexes: effects on reactive oxygen species and cytoprotection against oxidative damage. The Proceedings of European Meeting of the Society for Free Radical Research October 10-13, 2007, Vilamoura, Algarve, Portugal, Medimond 131-135 (2007)
    • (2007) The Proceedings of European Meeting of the Society for Free Radical Research , pp. 131-135
    • Kostyuk, V.1    Potapovich, A.2    Korkina, L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.