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Volumn 37, Issue 9-10, 1999, Pages 949-962

Intracellular antioxidants: From chemical to biochemical mechanisms

Author keywords

Antioxidants; Ascorbate; Ascorbate peroxidase; Catalase; Ergothioneine; Glutathione; Glutathione peroxidase; NADPH; Superoxide dismutase; Thioredoxin

Indexed keywords

ANTIOXIDANT; ASCORBATE OXIDASE; ASCORBIC ACID; CATALASE; FREE RADICAL; GLUTATHIONE; GLUTATHIONE PEROXIDASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; SCAVENGER; SUPEROXIDE DISMUTASE; THIOREDOXIN;

EID: 0043197852     PISSN: 02786915     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0278-6915(99)00090-3     Document Type: Review
Times cited : (557)

References (151)
  • 2
    • 0025358184 scopus 로고
    • The reduction of ferryl myoglobin by ergothioneine: Novel function of ergothioneine
    • Arduini A., Eddy L., Hochstein P. The reduction of ferryl myoglobin by ergothioneine: novel function of ergothioneine. Archives of Biochemistry and Biophysics. 281:1990;41-43.
    • (1990) Archives of Biochemistry and Biophysics , vol.281 , pp. 41-43
    • Arduini, A.1    Eddy, L.2    Hochstein, P.3
  • 3
    • 0001662170 scopus 로고
    • Ascorbate free radical reductase, a key enzyme of the ascorbic acid system
    • Arrigoni O., Dippierro S., Borraccino G. Ascorbate free radical reductase, a key enzyme of the ascorbic acid system. FEBS Letters. 125:1981;242-244.
    • (1981) FEBS Letters , vol.125 , pp. 242-244
    • Arrigoni, O.1    Dippierro, S.2    Borraccino, G.3
  • 4
    • 0023554040 scopus 로고
    • Action of hypochlorous acid on the antioxidant enzymes superoxide dismutase, catalase and glutathione peroxidase
    • Aruoma O. I., Halliwell B. Action of hypochlorous acid on the antioxidant enzymes superoxide dismutase, catalase and glutathione peroxidase. Biochemical Journal. 248:1987;973-976.
    • (1987) Biochemical Journal , vol.248 , pp. 973-976
    • Aruoma, O.I.1    Halliwell, B.2
  • 5
    • 0023144940 scopus 로고
    • Superoxide-dependent and ascorbate-dependent formation of hydroxyl radicals from hydrogen peroxide in the presence of iron
    • Aruoma O. I., Halliwell B. Superoxide-dependent and ascorbate-dependent formation of hydroxyl radicals from hydrogen peroxide in the presence of iron. Biochemical Journal. 241:1987;273-278.
    • (1987) Biochemical Journal , vol.241 , pp. 273-278
    • Aruoma, O.I.1    Halliwell, B.2
  • 7
    • 0001512204 scopus 로고
    • Production and scavenging of active oxygen species in chloroplasts
    • ed. J. G. Scandalios Cold Spring Harbor Laboratory Press, New York
    • Asada K. (1992) Production and scavenging of active oxygen species in chloroplasts. In Molecular Biology of Free Radical Scavenging Systems, ed. J. G. Scandalios, pp. 173-192. Cold Spring Harbor Laboratory Press, New York.
    • (1992) In Molecular Biology of Free Radical Scavenging Systems , pp. 173-192
    • Asada, K.1
  • 9
    • 0030695902 scopus 로고    scopus 로고
    • Redox potentials of glutaredoxins and other thiol-disulfide oxidoreductases of the thioredoxin superfamily determined by direct protein-protein redox equilibria
    • Aslund F., Berndt K. D., Holmgren A. Redox potentials of glutaredoxins and other thiol-disulfide oxidoreductases of the thioredoxin superfamily determined by direct protein-protein redox equilibria. Journal of Biological Chemistry. 272:1997;30780-30786.
    • (1997) Journal of Biological Chemistry , vol.272 , pp. 30780-30786
    • Aslund, F.1    Berndt, K.D.2    Holmgren, A.3
  • 10
    • 0029872542 scopus 로고    scopus 로고
    • One-electron oxidation of ergothioneine and analogues investigated by pulse radiolysis: Redox reaction involving ergothioneine and vitamin C
    • Asmus K. D., Bensasson R. V., Bernier J. L., Houssin R., Land E. J. One-electron oxidation of ergothioneine and analogues investigated by pulse radiolysis: redox reaction involving ergothioneine and vitamin C. Biochemical Journal. 315:1996;625-629.
    • (1996) Biochemical Journal , vol.315 , pp. 625-629
    • Asmus, K.D.1    Bensasson, R.V.2    Bernier, J.L.3    Houssin, R.4    Land, E.J.5
  • 11
    • 0028010677 scopus 로고
    • Regulation of NADP-dependent glyceraldehyde 3-phosphate dehydrogenase activity in spinach chloroplasts
    • Baalmann E., Backhausen J. E., Kitzmann C., Scheibe R. Regulation of NADP-dependent glyceraldehyde 3-phosphate dehydrogenase activity in spinach chloroplasts. Botanica Acta. 107:1994;313-320.
    • (1994) Botanica Acta , vol.107 , pp. 313-320
    • Baalmann, E.1    Backhausen, J.E.2    Kitzmann, C.3    Scheibe, R.4
  • 13
    • 0029063167 scopus 로고
    • A stress-associated citrus protein is a distinct plant phospholipid hydroperoxide glutathione peroxidase
    • Beeor-Tzahar T., Ben-Hayyim G., Holland D., Faltin Z., Eshdat Y. A stress-associated citrus protein is a distinct plant phospholipid hydroperoxide glutathione peroxidase. FEBS Letters. 366:1995;151-155.
    • (1995) FEBS Letters , vol.366 , pp. 151-155
    • Beeor-Tzahar, T.1    Ben-Hayyim, G.2    Holland, D.3    Faltin, Z.4    Eshdat, Y.5
  • 15
    • 0025286523 scopus 로고
    • The participation of coenzyme Q in free radical production and antioxidation
    • Beyer R. The participation of coenzyme Q in free radical production and antioxidation. Free Radical Biology and Medicine. 8:1990;545-565.
    • (1990) Free Radical Biology and Medicine , vol.8 , pp. 545-565
    • Beyer, R.1
  • 16
    • 0022259872 scopus 로고
    • Inactivation of glutathione peroxidase by superoxide radical
    • Blum J., Fridovich I. Inactivation of glutathione peroxidase by superoxide radical. Archives of Biochemistry and Biophysics. 240:1985;500-508.
    • (1985) Archives of Biochemistry and Biophysics , vol.240 , pp. 500-508
    • Blum, J.1    Fridovich, I.2
  • 17
    • 0029744560 scopus 로고    scopus 로고
    • Kinetic evidence for protein complexes between thioredoxin and NADP-malate dehydrogenase and presence of a thioredoxin binding site at the N-terminus of the enzyme
    • Braun H., Lichter A., Haberlein I. Kinetic evidence for protein complexes between thioredoxin and NADP-malate dehydrogenase and presence of a thioredoxin binding site at the N-terminus of the enzyme. European Journal of Biochemistry. 240:1996;781-788.
    • (1996) European Journal of Biochemistry , vol.240 , pp. 781-788
    • Braun, H.1    Lichter, A.2    Haberlein, I.3
  • 18
    • 0020805770 scopus 로고
    • Glutathione oxidation and activation of pentose phosphate cycle during hydroperoxide metabolism
    • Brigelius R. Glutathione oxidation and activation of pentose phosphate cycle during hydroperoxide metabolism. Hoppe-Seyler's Zeitschrift für Physikalische Chemie. 364:1983;989-996.
    • (1983) Hoppe-Seyler's Zeitschrift für Physikalische Chemie , vol.364 , pp. 989-996
    • Brigelius, R.1
  • 20
    • 0029598850 scopus 로고
    • Structure and properties of carotenoids in relation to function
    • Britton G. Structure and properties of carotenoids in relation to function. FASEB Journal. 9:1995;1551-1558.
    • (1995) FASEB Journal , vol.9 , pp. 1551-1558
    • Britton, G.1
  • 21
    • 0029132167 scopus 로고
    • Reversible binding and inhibition of catalase by nitric oxide
    • Brown G. C. Reversible binding and inhibition of catalase by nitric oxide. European Journal of Biochemistry. 232:1995;188-191.
    • (1995) European Journal of Biochemistry , vol.232 , pp. 188-191
    • Brown, G.C.1
  • 24
    • 0020074850 scopus 로고
    • Autoxidation of biological molecules. 1. The antioxidant activity of vitamin E and related chain-breaking phenolic antioxidants in vitro
    • Burton G. W., Ingold K. U. Autoxidation of biological molecules. 1. The antioxidant activity of vitamin E and related chain-breaking phenolic antioxidants in vitro. Journal of the American Chemical Society. 103:1981;6472-6477.
    • (1981) Journal of the American Chemical Society , vol.103 , pp. 6472-6477
    • Burton, G.W.1    Ingold, K.U.2
  • 25
    • 0021362463 scopus 로고
    • β-carotene: An unusual type of lipid antioxidant
    • Burton G. W., Ingold K. U. β-carotene: an unusual type of lipid antioxidant. Science. 224:1984;569-573.
    • (1984) Science , vol.224 , pp. 569-573
    • Burton, G.W.1    Ingold, K.U.2
  • 28
    • 0023833808 scopus 로고
    • Induction of selenium-glutathione peroxidase by stimulation of metabolic hydrogen peroxide production in vivo
    • Chaudière J., Gérard D., Clément M., Bourre J. M. Induction of selenium-glutathione peroxidase by stimulation of metabolic hydrogen peroxide production in vivo. Bioelectrochemistry and Bioenergetics. 18:1987;247-256.
    • (1987) Bioelectrochemistry and Bioenergetics , vol.18 , pp. 247-256
    • Chaudière, J.1    Gérard, D.2    Clément, M.3    Bourre, J.M.4
  • 29
    • 0344164366 scopus 로고
    • Pharmaco-toxicological effectors of glutathione peroxidase
    • ed. Ursini and E. Cadenas CLEUP University Press
    • Chaudière J. and Gérard-Monnier D. (1992) Pharmaco-toxicological effectors of glutathione peroxidase. In Biological Free Radical Oxidations and Antioxidants, ed. Ursini and E. Cadenas, pp. 143-145. CLEUP University Press.
    • (1992) In Biological Free Radical Oxidations and Antioxidants , pp. 143-145
    • Chaudière, J.1    Gérard-Monnier, D.2
  • 30
    • 0001891503 scopus 로고
    • Some chemical and biochemical constraints of oxidative stress in living cells
    • ed. C. Rice-Evans and R. H. Burdon New Comprehensive Biochemistry, Elsevier Science, Amsterdam
    • Chaudière J. (1994) Some chemical and biochemical constraints of oxidative stress in living cells. In Free Radical Damage and its Control, ed. C. Rice-Evans and R. H. Burdon, pp. 23-64. New Comprehensive Biochemistry, Elsevier Science, Amsterdam.
    • (1994) In Free Radical Damage and Its Control , pp. 23-64
    • Chaudière, J.1
  • 31
    • 0023202545 scopus 로고
    • Differential effect of cadmium on GSH peroxidase activity in the Leydig and the Sertoli cells of rat testis
    • Chung A. S., Maines M. D. Differential effect of cadmium on GSH peroxidase activity in the Leydig and the Sertoli cells of rat testis. Biochemical and Pharmacology. 36:1987;1367-1372.
    • (1987) Biochemical and Pharmacology , vol.36 , pp. 1367-1372
    • Chung, A.S.1    Maines, M.D.2
  • 32
    • 0024232411 scopus 로고
    • What is unique about superoxide toxicity as compared to other biological reductants? a hypothesis
    • Czapski G., Goldstein S., Meyerstein D. What is unique about superoxide toxicity as compared to other biological reductants? a hypothesis. Free Radical Research Communications. 4:1988;231-235.
    • (1988) Free Radical Research Communications , vol.4 , pp. 231-235
    • Czapski, G.1    Goldstein, S.2    Meyerstein, D.3
  • 34
    • 0013897667 scopus 로고
    • Peroxisomes (microbodies and related particles)
    • De Duve C., Baudhuin P. Peroxisomes (microbodies and related particles). Physiology Reviews. 46:1966;323-357.
    • (1966) Physiology Reviews , vol.46 , pp. 323-357
    • De Duve, C.1    Baudhuin, P.2
  • 35
    • 0030497826 scopus 로고    scopus 로고
    • Characterization of glutathione transferases and glutathione peroxidases in pea (Pisum sativum)
    • Edwards R. Characterization of glutathione transferases and glutathione peroxidases in pea (Pisum sativum). Physiologia Plantarum. 98:1996;594-604.
    • (1996) Physiologia Plantarum , vol.98 , pp. 594-604
    • Edwards, R.1
  • 36
    • 0020775636 scopus 로고
    • The refined structure of the selenoenzyme glutathione peroxidase at 0.2-nm resolution
    • Epp O., Ladenstein R., Wendel A. The refined structure of the selenoenzyme glutathione peroxidase at 0.2-nm resolution. European Journal of Biochemistry. 133:1983;51-69.
    • (1983) European Journal of Biochemistry , vol.133 , pp. 51-69
    • Epp, O.1    Ladenstein, R.2    Wendel, A.3
  • 38
  • 39
    • 0343673041 scopus 로고
    • Mécanismes naturels de protection des végétaux supérieurs contre les espèces oxygénées réactives
    • Ferrari-Iliou R., Pham Thi A.T., Mazliak P., Da Silva Vieira J. Mécanismes naturels de protection des végétaux supérieurs contre les espèces oxygénées réactives. L'Année Biologique. 31:1992;115-136.
    • (1992) l'Année Biologique , vol.31 , pp. 115-136
    • Ferrari-Iliou, R.1    Pham, T.A.T.2    Mazliak, P.3    Da Silva, V.J.4
  • 40
    • 0015982070 scopus 로고
    • The mechanism of action of superoxide dismutase from pulse radiolysis and electron paramagnetic resonance. Evidence that only half the active sites function in catalysis
    • Fielden E. M., Roberts P. B., Bray R. C., Lowe D. J., Mautner G. N., Rotilio G., Calabrese L. The mechanism of action of superoxide dismutase from pulse radiolysis and electron paramagnetic resonance. Evidence that only half the active sites function in catalysis. Biochemical Journal. 139:1974;49-60.
    • (1974) Biochemical Journal , vol.139 , pp. 49-60
    • Fielden, E.M.1    Roberts, P.B.2    Bray, R.C.3    Lowe, D.J.4    Mautner, G.N.5    Rotilio, G.6    Calabrese, L.7
  • 41
    • 0000704119 scopus 로고
    • The selenoprotein glutathione peroxidase
    • ed. D. Dolphin, O. Avramovic and R. Poulson John Wiley & Sons
    • FlohéL. (1989) The selenoprotein glutathione peroxidase. In Glutathione: Chemical, Biochemical and Medical Aspects, Part A, ed. D. Dolphin, O. Avramovic and R. Poulson, pp. 643-731. John Wiley & Sons.
    • (1989) In Glutathione: Chemical, Biochemical and Medical Aspects , Issue.PART A , pp. 643-731
    • Flohé, L.1
  • 42
    • 0015880169 scopus 로고
    • Glutathione peroxidase: A selenoenzyme
    • Flohé L., Gunzler W. A., Schock H. H. Glutathione peroxidase: a selenoenzyme. FEBS Letters. 32:1973;132-134.
    • (1973) FEBS Letters , vol.32 , pp. 132-134
    • Flohé, L.1    Gunzler, W.A.2    Schock, H.H.3
  • 47
    • 0030806863 scopus 로고    scopus 로고
    • Superoxide anion radical, superoxide dismutases and related matters
    • Fridovich I. Superoxide anion radical, superoxide dismutases and related matters. Journal of Biological Chemistry. 272:1997;18515-18517.
    • (1997) Journal of Biological Chemistry , vol.272 , pp. 18515-18517
    • Fridovich, I.1
  • 48
    • 0006444328 scopus 로고
    • The organic chemistry of superoxide anion radical
    • ed. L. W. Oberley CRC Press, Boca Raton, FL
    • Frimer A. A. (1982) The organic chemistry of superoxide anion radical. In Superoxide Dismutases, ed. L. W. Oberley, Vol. II, pp. 83-125. CRC Press, Boca Raton, FL.
    • (1982) In Superoxide Dismutases , vol.2 , pp. 83-125
    • Frimer, A.A.1
  • 49
    • 0029865602 scopus 로고    scopus 로고
    • Métabolisme et fonction antioxydante du glutathion
    • Gérard-Monnier D., Chaudière J. Métabolisme et fonction antioxydante du glutathion. Pathological Biology. 44:1996;77-85.
    • (1996) Pathological Biology , vol.44 , pp. 77-85
    • Gérard-Monnier, D.1    Chaudière, J.2
  • 50
    • 0030995292 scopus 로고    scopus 로고
    • Mechanistic aspects of xanthophyll cycle-dependent photoprotection in higher plant chloroplasts and leaves
    • Gilmore A. M. Mechanistic aspects of xanthophyll cycle-dependent photoprotection in higher plant chloroplasts and leaves. Physiologia Plantarum. 99:1997;197-209.
    • (1997) Physiologia Plantarum , vol.99 , pp. 197-209
    • Gilmore, A.M.1
  • 53
    • 0001024136 scopus 로고
    • Different aspects of protective activity of the xanthophyll cycle under stress conditions
    • Gruszecki W. I. Different aspects of protective activity of the xanthophyll cycle under stress conditions. Acta Physiologia Plantarum. 17:1995;145-152.
    • (1995) Acta Physiologia Plantarum , vol.17 , pp. 145-152
    • Gruszecki, W.I.1
  • 54
    • 0018145231 scopus 로고
    • Superoxide dependent formation of hydroxyl radicals in the presence of iron salts
    • Halliwell B. Superoxide dependent formation of hydroxyl radicals in the presence of iron salts. FEBS Letters. 92:1978;321-326.
    • (1978) FEBS Letters , vol.92 , pp. 321-326
    • Halliwell, B.1
  • 56
    • 0026634285 scopus 로고
    • Regulation of antioxidant enzymes
    • Harris E. D. Regulation of antioxidant enzymes. FASEB Journal. 6:1992;2675-2683.
    • (1992) FASEB Journal , vol.6 , pp. 2675-2683
    • Harris, E.D.1
  • 57
    • 0025040577 scopus 로고
    • Ergothioneine as antioxidant
    • Hartman P. E. Ergothioneine as antioxidant. Methods in Enzymology. 186:1990;310-318.
    • (1990) Methods in Enzymology , vol.186 , pp. 310-318
    • Hartman, P.E.1
  • 58
    • 0027399926 scopus 로고
    • Species difference in hydroperoxide-scavenging enzymes with special reference to glutathione peroxidase in guinea pigs
    • Himeno S., Takekawa A., Imura N. Species difference in hydroperoxide-scavenging enzymes with special reference to glutathione peroxidase in guinea pigs. Comparative Biochemistry and Physiology. 104B:1993;27-31.
    • (1993) Comparative Biochemistry and Physiology , vol.104 , pp. 27-31
    • Himeno, S.1    Takekawa, A.2    Imura, N.3
  • 61
    • 85006931658 scopus 로고
    • Glutaredoxin: Structure and function
    • ed. J. Vina CRC Press, Boca Raton, FL
    • Holmgren A. (1990) Glutaredoxin: Structure and function. In Glutathione: Metabolism and Physiological Functions, ed. J. Vina, pp. 145-154. CRC Press, Boca Raton, FL.
    • (1990) In Glutathione: Metabolism and Physiological Functions , pp. 145-154
    • Holmgren, A.1
  • 62
    • 0002458223 scopus 로고
    • Purification of dehydroascorbate reductase from spinach and its characterization as a thiol enzyme
    • Hossain M. A., Asada K. Purification of dehydroascorbate reductase from spinach and its characterization as a thiol enzyme. Plant and Cellular Physiology. 25:1984;85-92.
    • (1984) Plant and Cellular Physiology , vol.25 , pp. 85-92
    • Hossain, M.A.1    Asada, K.2
  • 63
    • 0022372087 scopus 로고
    • Monodehydroascorbate reductase from cucumber is a flavin adenine dinucleotide enzyme
    • Hossain M. A., Asada K. Monodehydroascorbate reductase from cucumber is a flavin adenine dinucleotide enzyme. Journal of Biological Chemistry. 260:1985;12920-12926.
    • (1985) Journal of Biological Chemistry , vol.260 , pp. 12920-12926
    • Hossain, M.A.1    Asada, K.2
  • 64
    • 37049092355 scopus 로고
    • Acid-base studies of glutathione (L-γ-glutamyl-L-cysteinyl-L-glycine) by one- And two-dimensional nuclear magnetic resonance spectroscopy
    • Huckerby T. N., Tudor A. J., Dawber J. G. Acid-base studies of glutathione (L-γ-glutamyl-L-cysteinyl-L-glycine) by one- and two-dimensional nuclear magnetic resonance spectroscopy. Journal of Chemical Society, Perkin Transactions. 2:1985;759-763.
    • (1985) Journal of Chemical Society, Perkin Transactions , vol.2 , pp. 759-763
    • Huckerby, T.N.1    Tudor, A.J.2    Dawber, J.G.3
  • 66
    • 1842295744 scopus 로고    scopus 로고
    • Regulatory role for a novel human thioredoxin peroxidase in NFκ-B activation
    • Jin D. Y., Zoon Chae H., Goo-Rhee S., Jeang K. T. Regulatory role for a novel human thioredoxin peroxidase in NFκ-B activation. Journal of Biological Chemistry. 272:1997;30952-30961.
    • (1997) Journal of Biological Chemistry , vol.272 , pp. 30952-30961
    • Jin, D.Y.1    Zoon, C.H.2    Goo-Rhee, S.3    Jeang, K.T.4
  • 70
  • 73
    • 0028176627 scopus 로고
    • Glucose-6-phosphate dehydrogenase: A "house-keeping" enzyme subject to tissue-specific regulation by hormones, nutrients and oxidant stress
    • Kletzien R. F., Harris P. K., Foellmi L. A. Glucose-6-phosphate dehydrogenase: a "house-keeping" enzyme subject to tissue-specific regulation by hormones, nutrients and oxidant stress. FASEB Journal. 8:1994;174-181.
    • (1994) FASEB Journal , vol.8 , pp. 174-181
    • Kletzien, R.F.1    Harris, P.K.2    Foellmi, L.A.3
  • 76
    • 0029999693 scopus 로고    scopus 로고
    • Inhibition of Iκ-B phosphorylation and degradation and subsequent NFκ-B activation by glutathione peroxidase overexpression
    • Kretz-Remy C., Mehlen P., Mirault M. E., Arrigo A. P. Inhibition of Iκ-B phosphorylation and degradation and subsequent NFκ-B activation by glutathione peroxidase overexpression. Journal of Cell Biology. 133:1996;1083-1093.
    • (1996) Journal of Cell Biology , vol.133 , pp. 1083-1093
    • Kretz-Remy, C.1    Mehlen, P.2    Mirault, M.E.3    Arrigo, A.P.4
  • 79
    • 0018248040 scopus 로고
    • Hepatic cytosolic non selenium-dependent glutathione peroxidase activity: Its nature and the effect of selenium deficiency
    • Lawrence R. A., Parkhill L. K., Burk R. F. Hepatic cytosolic non selenium-dependent glutathione peroxidase activity: its nature and the effect of selenium deficiency. Journal of Nutrition. 108:1978;981-987.
    • (1978) Journal of Nutrition , vol.108 , pp. 981-987
    • Lawrence, R.A.1    Parkhill, L.K.2    Burk, R.F.3
  • 81
    • 0024253976 scopus 로고
    • Plant senescence processes and free radicals
    • Leshem Y. Y. Plant senescence processes and free radicals. Free Radical Biology and Medicine. 5:1988;39-49.
    • (1988) Free Radical Biology and Medicine , vol.5 , pp. 39-49
    • Leshem, Y.Y.1
  • 82
    • 0028894508 scopus 로고
    • Regulation of NADP-malate dehydrogenase in C-4 plants: Activity and properties of maize thioredoxin m and the significance of non-active site thiol groups
    • Lunn J. E., Agostino A., Hatch M. D. Regulation of NADP-malate dehydrogenase in C-4 plants: Activity and properties of maize thioredoxin m and the significance of non-active site thiol groups. Australian Journal of Plant Physiology. 22:1995;577-584.
    • (1995) Australian Journal of Plant Physiology , vol.22 , pp. 577-584
    • Lunn, J.E.1    Agostino, A.2    Hatch, M.D.3
  • 84
    • 0030611083 scopus 로고    scopus 로고
    • Reduction of dehydroascorbate to ascorbate by the selenoenzyme thioredoxin reductase
    • May J. M., Mendiratta S., Hill K. E., Burk R. F. Reduction of dehydroascorbate to ascorbate by the selenoenzyme thioredoxin reductase. Journal of Biological Chemistry. 272:1997;22607-22610.
    • (1997) Journal of Biological Chemistry , vol.272 , pp. 22607-22610
    • May, J.M.1    Mendiratta, S.2    Hill, K.E.3    Burk, R.F.4
  • 85
    • 0021776272 scopus 로고
    • Vitamin E: Interactions with free radicals and ascorbate
    • McCay P. Vitamin E: Interactions with free radicals and ascorbate. Annual Review of Nutrition. 5:1985;323-340.
    • (1985) Annual Review of Nutrition , vol.5 , pp. 323-340
    • McCay, P.1
  • 86
    • 0014691242 scopus 로고
    • Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein)
    • McCord J., Fridovich I. Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). Journal of Biological Chemistry. 244:1969;6049-6055.
    • (1969) Journal of Biological Chemistry , vol.244 , pp. 6049-6055
    • McCord, J.1    Fridovich, I.2
  • 87
    • 0028263767 scopus 로고
    • Glutathione-ascorbic acid antioxidant system in animals
    • Meister A. Glutathione-ascorbic acid antioxidant system in animals. Journal of Biological Chemistry. 269:1994;9397-9400.
    • (1994) Journal of Biological Chemistry , vol.269 , pp. 9397-9400
    • Meister, A.1
  • 89
    • 0027269781 scopus 로고
    • 2 and antioxidants have opposite effects on activation of NFκ-B and AP-1 in intact cells: AP-1 as secondary antioxidant-responsive factor
    • 2 and antioxidants have opposite effects on activation of NFκ-B and AP-1 in intact cells: AP-1 as secondary antioxidant-responsive factor. EMBO Journal. 12:1993;2005-2015.
    • (1993) EMBO Journal , vol.12 , pp. 2005-2015
    • Meyer, M.1    Schreck, R.2    Bauerle, P.A.3
  • 90
    • 0031968714 scopus 로고    scopus 로고
    • Re-appraisal of the tocopheroxyl radical reaction with β-carotene: Evidence for oxidation of vitamin E by the β-carotene radical cation
    • Mortensen A., Skibsted L. H., Willnow A., Everett S. A. Re-appraisal of the tocopheroxyl radical reaction with β-carotene: evidence for oxidation of vitamin E by the β-carotene radical cation. Free Radical Biology and Medicine. 28:1998;69-80.
    • (1998) Free Radical Biology and Medicine , vol.28 , pp. 69-80
    • Mortensen, A.1    Skibsted, L.H.2    Willnow, A.3    Everett, S.A.4
  • 92
    • 0029886243 scopus 로고    scopus 로고
    • Removal of hydrogen peroxide by thiol-specific antioxidant enzyme (TSA) is involved with its antioxidant properties
    • Netto L. E., Chae H. Z., Kang S. W., Rhee S. G., Stadtman E. R. Removal of hydrogen peroxide by thiol-specific antioxidant enzyme (TSA) is involved with its antioxidant properties. Journal of Biological Chemistry. 271:1996;15315-15321.
    • (1996) Journal of Biological Chemistry , vol.271 , pp. 15315-15321
    • Netto, L.E.1    Chae, H.Z.2    Kang, S.W.3    Rhee, S.G.4    Stadtman, E.R.5
  • 93
    • 0015510722 scopus 로고
    • Contributions of catalase and glutathione peroxidase to red cell peroxide removal
    • Nicholls P. Contributions of catalase and glutathione peroxidase to red cell peroxide removal. Biochimica et Biophysica Acta. 279:1972;306-309.
    • (1972) Biochimica et Biophysica Acta , vol.279 , pp. 306-309
    • Nicholls, P.1
  • 94
    • 0019073929 scopus 로고
    • The metabolic fate of mitochondrial hydrogen peroxide
    • Nohl H., Jordan W. The metabolic fate of mitochondrial hydrogen peroxide. European Journal of Biochemistry. 111:1980;203-210.
    • (1980) European Journal of Biochemistry , vol.111 , pp. 203-210
    • Nohl, H.1    Jordan, W.2
  • 95
    • 0001644805 scopus 로고
    • Catalase activity at high concentration of hydrogen peroxide
    • Ogura Y. Catalase activity at high concentration of hydrogen peroxide. Archives of Biochemistry and Biophysics. 57:1955;288-300.
    • (1955) Archives of Biochemistry and Biophysics , vol.57 , pp. 288-300
    • Ogura, Y.1
  • 96
    • 0022260427 scopus 로고
    • Diffusion of extracellular hydrogen peroxide into intracellular compartments of human neutrophils: Studies utilizing the inactivation of myeloperoxidase by hydrogen peroxide and azide
    • Ohno Y., Gallin J. L. Diffusion of extracellular hydrogen peroxide into intracellular compartments of human neutrophils: Studies utilizing the inactivation of myeloperoxidase by hydrogen peroxide and azide. Journal of Biological Chemistry. 260:1985;8438-8446.
    • (1985) Journal of Biological Chemistry , vol.260 , pp. 8438-8446
    • Ohno, Y.1    Gallin, J.L.2
  • 97
    • 0018348794 scopus 로고
    • Direct observation of a free radical interaction between vitamin E and vitamin C
    • Packer J. E., Slater T. F., Willson R. L. Direct observation of a free radical interaction between vitamin E and vitamin C. Nature. 278:1979;737-738.
    • (1979) Nature , vol.278 , pp. 737-738
    • Packer, J.E.1    Slater, T.F.2    Willson, R.L.3
  • 99
    • 0026989766 scopus 로고
    • Astaxanthin and cantaxanthin are potent antioxidants in a membrane model
    • Palozza P., Krinsky N. I. Astaxanthin and cantaxanthin are potent antioxidants in a membrane model. Archives of Biochemistry and Biophysics. 297:1992;291-295.
    • (1992) Archives of Biochemistry and Biophysics , vol.297 , pp. 291-295
    • Palozza, P.1    Krinsky, N.I.2
  • 101
    • 0029872005 scopus 로고    scopus 로고
    • Purification, cloning and expression of dehydroascorbic acid-reducing activity from human neutrophils
    • Park J. B., Levine M. Purification, cloning and expression of dehydroascorbic acid-reducing activity from human neutrophils. Biochemical Journal. 315:1996;931-938.
    • (1996) Biochemical Journal , vol.315 , pp. 931-938
    • Park, J.B.1    Levine, M.2
  • 102
    • 0030238701 scopus 로고    scopus 로고
    • Nitric oxide-induced inhibition of lung endothelial cell nitric oxide synthase via interaction with allosteric thiols: Role of thioredoxin in regulation of catalytic activity
    • Patel J. M., Zhang J., Block E. R. Nitric oxide-induced inhibition of lung endothelial cell nitric oxide synthase via interaction with allosteric thiols: role of thioredoxin in regulation of catalytic activity. American Journal of Respiratory Cell and Molecular Biology. 15:1996;410-419.
    • (1996) American Journal of Respiratory Cell and Molecular Biology , vol.15 , pp. 410-419
    • Patel, J.M.1    Zhang, J.2    Block, E.R.3
  • 103
    • 0026030924 scopus 로고
    • Cellular and regional distribution of reduced glutathione in the nervous system of the rat: Histochemical localization by mercury orange and o-phtaldialdehyde-induced histofluorescence
    • Philbert M. A., Beiswanger C. M., Waters D. K., Reuhl K. L., Lowndes H. E. Cellular and regional distribution of reduced glutathione in the nervous system of the rat: histochemical localization by mercury orange and o-phtaldialdehyde-induced histofluorescence. Toxicology and Applied Pharmacology. 107:1991;215-227.
    • (1991) Toxicology and Applied Pharmacology , vol.107 , pp. 215-227
    • Philbert, M.A.1    Beiswanger, C.M.2    Waters, D.K.3    Reuhl, K.L.4    Lowndes, H.E.5
  • 105
    • 0030056515 scopus 로고    scopus 로고
    • Mitochondrial complex I deficiency leads to increased production of superoxide radicals and induction of superoxide dismutase
    • Pitkänen S., Robinson B. H. Mitochondrial complex I deficiency leads to increased production of superoxide radicals and induction of superoxide dismutase. Journal of Clinical Investigation. 98:1996;345-351.
    • (1996) Journal of Clinical Investigation , vol.98 , pp. 345-351
    • Pitkänen, S.1    Robinson, B.H.2
  • 106
    • 0029644240 scopus 로고
    • Solution structure of human thioredoxin in a mixed disulfide intermediate complex with its target peptide from the transcription factor NFκ-B
    • Qin J., Clore G. M., Kennedy W. M., Huth J. R., Gronenborn A. M. Solution structure of human thioredoxin in a mixed disulfide intermediate complex with its target peptide from the transcription factor NFκ-B. Structure. 3:1995;289-297.
    • (1995) Structure , vol.3 , pp. 289-297
    • Qin, J.1    Clore, G.M.2    Kennedy, W.M.3    Huth, J.R.4    Gronenborn, A.M.5
  • 109
    • 0026587399 scopus 로고
    • Purification and properties of a recombinant sulfur analog of murine selenium-glutathione peroxidase
    • Rocher C., Lalanne J. L., Chaudière J. Purification and properties of a recombinant sulfur analog of murine selenium-glutathione peroxidase. European Journal of Biochemistry. 205:1992;955-960.
    • (1992) European Journal of Biochemistry , vol.205 , pp. 955-960
    • Rocher, C.1    Lalanne, J.L.2    Chaudière, J.3
  • 110
    • 0024534983 scopus 로고
    • Selective enrichment and biochemical characterization of seven human skin fibroblast cell types in vitro
    • Rodemann H. P., Bayreuther K., Francz P. I., Dittmann K., Albiez M. Selective enrichment and biochemical characterization of seven human skin fibroblast cell types in vitro. Experimental Cell Research. 180:1989;84-93.
    • (1989) Experimental Cell Research , vol.180 , pp. 84-93
    • Rodemann, H.P.1    Bayreuther, K.2    Francz, P.I.3    Dittmann, K.4    Albiez, M.5
  • 112
    • 0023990311 scopus 로고
    • Deactivation of singlet molecular oxygen by thiols and related compounds, possible protectors against skin photosensitivity
    • Rougee M., Bensasson R. V., Land E. J., Pariente R. Deactivation of singlet molecular oxygen by thiols and related compounds, possible protectors against skin photosensitivity. Photochemistry and Photobiology. 47:1988;485-489.
    • (1988) Photochemistry and Photobiology , vol.47 , pp. 485-489
    • Rougee, M.1    Bensasson, R.V.2    Land, E.J.3    Pariente, R.4
  • 113
    • 0028291969 scopus 로고
    • Enzymatic and immunological measurements of soluble and membrane-bound phospholipid-hydroperoxide glutathione peroxidase
    • Roveri A., Maiorino M., Ursini F. Enzymatic and immunological measurements of soluble and membrane-bound phospholipid-hydroperoxide glutathione peroxidase. Methods in Enzymology. 233:1994;202-212.
    • (1994) Methods in Enzymology , vol.233 , pp. 202-212
    • Roveri, A.1    Maiorino, M.2    Ursini, F.3
  • 114
    • 0027155884 scopus 로고
    • Autocrine production of extracellular catalase prevents apoptosis of the human CEM T-cell line in serum-free medium
    • Sandstrom P. A., Buttke T. M. Autocrine production of extracellular catalase prevents apoptosis of the human CEM T-cell line in serum-free medium. Proceedings of the National Academy of Scienices of the U.S.A. 90:1993;4708-4712.
    • (1993) Proceedings of the National Academy of Scienices of the U.S.A. , vol.90 , pp. 4708-4712
    • Sandstrom, P.A.1    Buttke, T.M.2
  • 115
    • 0025733716 scopus 로고
    • Purification and characterization of α-tocopherol transfer protein from rat liver
    • Sato Y., Hagiwara K., Akai H., Inoue K. Purification and characterization of α-tocopherol transfer protein from rat liver. FEBS Letters. 288:1991;41-45.
    • (1991) FEBS Letters , vol.288 , pp. 41-45
    • Sato, Y.1    Hagiwara, K.2    Akai, H.3    Inoue, K.4
  • 117
    • 0024024922 scopus 로고
    • Fenton reactions in lipid phases
    • Schaich K. M., Borg D. C. Fenton reactions in lipid phases. Lipids. 23:1988;570-579.
    • (1988) Lipids , vol.23 , pp. 570-579
    • Schaich, K.M.1    Borg, D.C.2
  • 119
    • 77956932249 scopus 로고
    • Catalase
    • ed. P. D. Boyer, 2nd edn New York Academy
    • Schonbaum G. R. and Chance B. (1976) Catalase. In The Enzymes, ed. P. D. Boyer, 2nd edn, Vol. XIII, pp. 363-408. New York Academy.
    • (1976) In the Enzymes , vol.13 , pp. 363-408
    • Schonbaum, G.R.1    Chance, B.2
  • 120
    • 0029984062 scopus 로고    scopus 로고
    • Antioxidant and redox regulation of gene transcription
    • Sen C. K., Packer L. Antioxidant and redox regulation of gene transcription. FASEB Journal. 10:1996;709-720.
    • (1996) FASEB Journal , vol.10 , pp. 709-720
    • Sen, C.K.1    Packer, L.2
  • 121
    • 0027948428 scopus 로고
    • Antioxidant properties of α-tocopherol and (-tocotrienol
    • Serbinova E. A., Packer L. Antioxidant properties of α-tocopherol and (-tocotrienol. Methods in Enzymology. 234:1994;354-366.
    • (1994) Methods in Enzymology , vol.234 , pp. 354-366
    • Serbinova, E.A.1    Packer, L.2
  • 123
    • 0019811815 scopus 로고
    • Inactivation of the human copper-zinc superoxide dismutase during exposure to the superoxide radical and hydrogen peroxide
    • Sinet P. M., Garber P. Inactivation of the human copper-zinc superoxide dismutase during exposure to the superoxide radical and hydrogen peroxide. Archives of Biochemistry and Biophysics. 212:1981;411-416.
    • (1981) Archives of Biochemistry and Biophysics , vol.212 , pp. 411-416
    • Sinet, P.M.1    Garber, P.2
  • 125
    • 0023236818 scopus 로고
    • Histochemical evaluation of glutathione in brain
    • Slivka A., Mytilneau C., Cohen G. Histochemical evaluation of glutathione in brain. Brain Research. 409:1987;275-284.
    • (1987) Brain Research , vol.409 , pp. 275-284
    • Slivka, A.1    Mytilneau, C.2    Cohen, G.3
  • 126
    • 0030459907 scopus 로고    scopus 로고
    • The function and metabolism of ascorbic acid in plants
    • Smirnoff N. The function and metabolism of ascorbic acid in plants. Annals of Botany. 78:1996;661-669.
    • (1996) Annals of Botany , vol.78 , pp. 661-669
    • Smirnoff, N.1
  • 127
    • 0025953866 scopus 로고
    • Biosynthesis and function of selenocysteine-containing enzymes
    • Stadtman T. C. Biosynthesis and function of selenocysteine-containing enzymes. Journal of Biological Chemistry. 266:1991;16257-16260.
    • (1991) Journal of Biological Chemistry , vol.266 , pp. 16257-16260
    • Stadtman, T.C.1
  • 129
    • 0002877219 scopus 로고
    • Superoxide dismutases: Protein chemistry and structure-function relationships
    • ed. L. W. Oberley, CRC Press, Boca Raton, FL
    • Steinman H. M. (1982) Superoxide dismutases: Protein chemistry and structure-function relationships. In Superoxide Dismutase, ed. L. W. Oberley, Vol. I, pp. 11-68. CRC Press, Boca Raton, FL.
    • (1982) In Superoxide Dismutase , vol.1 , pp. 11-68
    • Steinman, H.M.1
  • 130
    • 0004155427 scopus 로고
    • W. H. Freeman & Co, New York
    • Stryer L. 1995. Biochemistry. 4th edn, pp. 559-580. W. H. Freeman & Co, New York.
    • (1995) Biochemistry. 4th Edn , pp. 559-580
    • Stryer, L.1
  • 133
    • 0019349080 scopus 로고
    • Metabolic pathways in peroxisomes and glyoxysomes
    • Tolbert N. E. Metabolic pathways in peroxisomes and glyoxysomes. Annual Review of Biochemistry. 50:1981;133-157.
    • (1981) Annual Review of Biochemistry , vol.50 , pp. 133-157
    • Tolbert, N.E.1
  • 134
    • 0028100040 scopus 로고
    • Antioxidant activity of α-tocopherol, β-carotene and ubiquinol in membranes: Cis-parinaric acid-incorporated liposomes
    • Tsuchiya M., Kagan V. E., Friesleben H. J., Manabe M., Packer L. Antioxidant activity of α-tocopherol, β-carotene and ubiquinol in membranes: cis-parinaric acid-incorporated liposomes. Methods in Enzymology. 234:1994;371-383.
    • (1994) Methods in Enzymology , vol.234 , pp. 371-383
    • Tsuchiya, M.1    Kagan, V.E.2    Friesleben, H.J.3    Manabe, M.4    Packer, L.5
  • 135
    • 0021803196 scopus 로고
    • The selenoenzyme phospholipid hydroperoxide glutathione peroxidase
    • Ursini F., Maiorino M., Gregolin C. The selenoenzyme phospholipid hydroperoxide glutathione peroxidase. Biochimica et Biophysica Acta. 839:1985;62-70.
    • (1985) Biochimica et Biophysica Acta , vol.839 , pp. 62-70
    • Ursini, F.1    Maiorino, M.2    Gregolin, C.3
  • 138
    • 84872846883 scopus 로고
    • Reduction potentials of one-electron couples involving free radicals in aqueous solution
    • Wardman P. Reduction potentials of one-electron couples involving free radicals in aqueous solution. Journal of Physical and Chemical Reference Data. 18:1989;1637-1755.
    • (1989) Journal of Physical and Chemical Reference Data , vol.18 , pp. 1637-1755
    • Wardman, P.1
  • 139
    • 0031878182 scopus 로고    scopus 로고
    • Evaluation of the "radical sink" hypothesis from a chemical-kinetic viewpoint
    • Wardman P. Evaluation of the "radical sink" hypothesis from a chemical-kinetic viewpoint. Journal of Radioanalytical and Nuclear Chemistry. 232:1998;23-27.
    • (1998) Journal of Radioanalytical and Nuclear Chemistry , vol.232 , pp. 23-27
    • Wardman, P.1
  • 140
    • 0029002385 scopus 로고
    • Kinetic factors that control the fate of thiyl radicals in cells
    • Wardman P., Von Sonntag C. Kinetic factors that control the fate of thiyl radicals in cells. Methods in Enzymology. 251:1995;31-45.
    • (1995) Methods in Enzymology , vol.251 , pp. 31-45
    • Wardman, P.1    Von Sonntag, C.2
  • 141
    • 0027419580 scopus 로고
    • Selenoenzymes regulate the activity of leukocyte 5-lipoxygenase via the peroxide tone
    • Weitzel F., Wendel A. Selenoenzymes regulate the activity of leukocyte 5-lipoxygenase via the peroxide tone. Journal of Biological Chemistry. 268:1994;6288-6292.
    • (1994) Journal of Biological Chemistry , vol.268 , pp. 6288-6292
    • Weitzel, F.1    Wendel, A.2
  • 142
    • 0025082330 scopus 로고
    • Mammalian thioltransferase (glutaredoxin) and protein disulfide isomerase have dehydroascorbate reductase activity
    • Wells W. W., Xu D. P., Yang Y., Rocque P. A. Mammalian thioltransferase (glutaredoxin) and protein disulfide isomerase have dehydroascorbate reductase activity. Journal of Biological Chemistry. 265:1990;15361-15364.
    • (1990) Journal of Biological Chemistry , vol.265 , pp. 15361-15364
    • Wells, W.W.1    Xu, D.P.2    Yang, Y.3    Rocque, P.A.4
  • 143
    • 0030822030 scopus 로고    scopus 로고
    • Identification of the cysteine residues involved in redox modification of plant plastidic glucose-6-phosphate dehydrogenase
    • Wenderoth I., Scheibe R., Von Schaewen A. Identification of the cysteine residues involved in redox modification of plant plastidic glucose-6-phosphate dehydrogenase. Journal of Biological Chemistry. 272:1997;26985-26990.
    • (1997) Journal of Biological Chemistry , vol.272 , pp. 26985-26990
    • Wenderoth, I.1    Scheibe, R.2    Von Schaewen, A.3
  • 144
    • 0029904762 scopus 로고    scopus 로고
    • Selenium-dependent peroxidases suppress 5-lipoxygenase activity in B-lymphocytes and immature myeloid cells: The presence of peroxidase-insensitive 5-lipoxygenase activity in differentiated myeloid cells
    • Werz O., Steinhilber D. Selenium-dependent peroxidases suppress 5-lipoxygenase activity in B-lymphocytes and immature myeloid cells: The presence of peroxidase-insensitive 5-lipoxygenase activity in differentiated myeloid cells. European Journal of Biochemistry. 242:1996;90-97.
    • (1996) European Journal of Biochemistry , vol.242 , pp. 90-97
    • Werz, O.1    Steinhilber, D.2
  • 145
    • 0027935268 scopus 로고
    • The redox couple between glutathione and ascorbic acid: A chemical and physiological perspective
    • Winkler B. S., Orselli S. M., Rex T. S. The redox couple between glutathione and ascorbic acid: a chemical and physiological perspective. Free Radical Biology and Medicine. 17:1994;333-349.
    • (1994) Free Radical Biology and Medicine , vol.17 , pp. 333-349
    • Winkler, B.S.1    Orselli, S.M.2    Rex, T.S.3
  • 147
    • 0024202127 scopus 로고
    • Induction of manganous superoxide dismutase by tumor necrosis factor: Possible protective mechanism
    • Wong G., Goeddel D. Induction of manganous superoxide dismutase by tumor necrosis factor: possible protective mechanism. Science. 242:1988;941-944.
    • (1988) Science , vol.242 , pp. 941-944
    • Wong, G.1    Goeddel, D.2
  • 148
    • 0024428198 scopus 로고
    • Manganous superoxide dismutase is essential for cellular resistance to tumor necrosis factor
    • Wong G., Elwell J. H., Oberley L. W., Goeddel D. Manganous superoxide dismutase is essential for cellular resistance to tumor necrosis factor. Cell. 58:1988;923-931.
    • (1988) Cell , vol.58 , pp. 923-931
    • Wong, G.1    Elwell, J.H.2    Oberley, L.W.3    Goeddel, D.4
  • 149
    • 0029928826 scopus 로고    scopus 로고
    • Purification and characterization of a glutathione dependent dehydroascorbate reductase from human erythrocytes
    • Xu D. P., Washburn M. P., Sun G. P., Wells W. W. Purification and characterization of a glutathione dependent dehydroascorbate reductase from human erythrocytes. Biochemical and Biophysical Research Communications. 221:1996;117-121.
    • (1996) Biochemical and Biophysical Research Communications , vol.221 , pp. 117-121
    • Xu, D.P.1    Washburn, M.P.2    Sun, G.P.3    Wells, W.W.4
  • 150
    • 0030692005 scopus 로고    scopus 로고
    • Thioredoxin peroxidase is a novel inhibitor of apoptosis with a mechanism distinct from that of Bcl-2
    • Zhang P., Liu B., Kang S. W., Seo M. S., Rhee S. G., Obeid L. M. Thioredoxin peroxidase is a novel inhibitor of apoptosis with a mechanism distinct from that of Bcl-2. Journal of Biological Chemistry. 272:1997;30615-30618.
    • (1997) Journal of Biological Chemistry , vol.272 , pp. 30615-30618
    • Zhang, P.1    Liu, B.2    Kang, S.W.3    Seo, M.S.4    Rhee, S.G.5    Obeid, L.M.6
  • 151
    • 0021891877 scopus 로고
    • Role of reversible oxidation-reduction of enzyme thiol-disulfides in metabolic regulation
    • Ziegler D. M. Role of reversible oxidation-reduction of enzyme thiol-disulfides in metabolic regulation. Annual Review of Biochemistry. 54:1985;305-329.
    • (1985) Annual Review of Biochemistry , vol.54 , pp. 305-329
    • Ziegler, D.M.1


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