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1
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0003440321
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Plainview: Cold Spring Harbor Laboratory Press; This book contains an excellent collection of review articles by several of the leaders in the field of biological oxidative stress research. It provides broad coverage of relevant topics and a welcome emphasis on plant systems
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Scandalios JG: Oxidative stress and the molecular biology of antioxidant defenses. Plainview: Cold Spring Harbor Laboratory Press; 1997. This book contains an excellent collection of review articles by several of the leaders in the field of biological oxidative stress research. It provides broad coverage of relevant topics and a welcome emphasis on plant systems.
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(1997)
Oxidative Stress and the Molecular Biology of Antioxidant Defenses
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Scandalios, J.G.1
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2
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0030965985
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Antioxidant activity of vitamin C in iron-overloaded human plasma
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Ascorbate is a biological antioxidant of major importance. Nevertheless, it can act as a reductant of metal ions (such as iron and copper) that promote Fenton reactions of hydrogen peroxide to produce dangerous oxidants, it has frequently been claimed that ascorbate can, under certain conditions, act as a pro-oxidant in vivo. This paper reports evidence to the contrary indicating that ascorbate is an antioxidant and not a pro-oxidant in human plasma in vivo, even under conditions of iron overload
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Berger TM, Polidori MC, Dabbagh A, Evans PJ, Halliwell B, Morrow JD, Roberts LJ, Frei B: Antioxidant activity of vitamin C in iron-overloaded human plasma. J Biol Chem 1997, 272:15656-15660. Ascorbate is a biological antioxidant of major importance. Nevertheless, it can act as a reductant of metal ions (such as iron and copper) that promote Fenton reactions of hydrogen peroxide to produce dangerous oxidants, it has frequently been claimed that ascorbate can, under certain conditions, act as a pro-oxidant in vivo. This paper reports evidence to the contrary indicating that ascorbate is an antioxidant and not a pro-oxidant in human plasma in vivo, even under conditions of iron overload.
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(1997)
J Biol Chem
, vol.272
, pp. 15656-15660
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Berger, T.M.1
Polidori, M.C.2
Dabbagh, A.3
Evans, P.J.4
Halliwell, B.5
Morrow, J.D.6
Roberts, L.J.7
Frei, B.8
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3
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0030611083
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Reduction of dehydroascorbate to ascorbate by the selenoenzyme thioredoxin reductase
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Stoichiometric antioxidants such as ascorbate and glutathione (GSH) are re-reduced and thus recycled many times in vivo. The reduction of oxidized GSH (GSSG) is catalyzed by GSH reductase. Less is known about mechanisms of reduction of dehydroascorbate to ascorbate in vivo, but it is widely believed that the biological reductant is GSH. This paper reports an alternative mechanism in which the selenoenzyme thioredoxin reductase catalyzes reduction of dehydroascorbate by reduced nicotinamide adenine dinucleotide phosphate (NADPH)
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May JM, Mendiratta S, Hill KE, Burk RF: Reduction of dehydroascorbate to ascorbate by the selenoenzyme thioredoxin reductase. J Biol Chem 1997, 272:22607-22610. Stoichiometric antioxidants such as ascorbate and glutathione (GSH) are re-reduced and thus recycled many times in vivo. The reduction of oxidized GSH (GSSG) is catalyzed by GSH reductase. Less is known about mechanisms of reduction of dehydroascorbate to ascorbate in vivo, but it is widely believed that the biological reductant is GSH. This paper reports an alternative mechanism in which the selenoenzyme thioredoxin reductase catalyzes reduction of dehydroascorbate by reduced nicotinamide adenine dinucleotide phosphate (NADPH).
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(1997)
J Biol Chem
, vol.272
, pp. 22607-22610
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May, J.M.1
Mendiratta, S.2
Hill, K.E.3
Burk, R.F.4
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4
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0030806863
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--), superoxide dismutases, and related matters
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This is a timely minireview of superoxide and superoxide dismutases
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--), superoxide dismutases, and related matters. J Biol Chem 1997, 272:18515-18517. This is a timely minireview of superoxide and superoxide dismutases.
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(1997)
J Biol Chem
, vol.272
, pp. 18515-18517
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Fridovich, I.1
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5
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0029799910
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Enhanced sensitivity of ubiquinone-deficient mutants of Saccharomyces cerevisiae to products of autoxidized polyunsaturated fatty acids
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Yeast lacking coenzyme Q were hypersensitive to polyunsaturated fatty acids and lipid hydroperoxides were elevated. The hypersensitivity was rescued by addition of antioxidants. The paper provides dramatic evidence for the antioxidant action of reduced ubiquinone in vivo and of the toxicity of the autoxidation products of unsaturated fatty acids
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Do TQ, Schultz JR, Clarke CF: Enhanced sensitivity of ubiquinone-deficient mutants of Saccharomyces cerevisiae to products of autoxidized polyunsaturated fatty acids. Proc Natl Acad Sci USA 1996, 93:7534-7539. Yeast lacking coenzyme Q were hypersensitive to polyunsaturated fatty acids and lipid hydroperoxides were elevated. The hypersensitivity was rescued by addition of antioxidants. The paper provides dramatic evidence for the antioxidant action of reduced ubiquinone in vivo and of the toxicity of the autoxidation products of unsaturated fatty acids.
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(1996)
Proc Natl Acad Sci USA
, vol.93
, pp. 7534-7539
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Do, T.Q.1
Schultz, J.R.2
Clarke, C.F.3
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6
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0031010333
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Reactive oxygen-mediated protein oxidation in aging and disease
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A comprehensive review of biochemical mechanisms of oxidative damage caused by reactive oxygen species, with emphasis on proteins as targets for such damage
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Stadtman ER, Berlett BS: Reactive oxygen-mediated protein oxidation in aging and disease. Chem Res Toxicol 1997, 10:485-494. A comprehensive review of biochemical mechanisms of oxidative damage caused by reactive oxygen species, with emphasis on proteins as targets for such damage.
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(1997)
Chem Res Toxicol
, vol.10
, pp. 485-494
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Stadtman, E.R.1
Berlett, B.S.2
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8
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0030988742
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Biochemistry and pathology of radical-mediated protein oxidation
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A review of radical-mediated protein oxidation with emphasis on the physiology and pathology of the resulting protein damage
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Dean RT, Fu S, Stocker R, Davies MJ: Biochemistry and pathology of radical-mediated protein oxidation. Biochem J 1997, 324:1-18. A review of radical-mediated protein oxidation with emphasis on the physiology and pathology of the resulting protein damage.
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(1997)
Biochem J
, vol.324
, pp. 1-18
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Dean, R.T.1
Fu, S.2
Stocker, R.3
Davies, M.J.4
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9
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0030799043
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Low density lipoprotein oxidation and its pathobiological significance
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A timely minireview of LDL oxidation
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Steinberg D: Low density lipoprotein oxidation and its pathobiological significance. J Biol Chem 1997, 272:20963-20966. A timely minireview of LDL oxidation.
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(1997)
J Biol Chem
, vol.272
, pp. 20963-20966
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Steinberg, D.1
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10
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0030797051
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Formation, prevention, and repair of DNA damage by iron/hydrogen peroxide
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A timely minireview of mechanisms of DNA oxidation catalyzed by iron
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Henle ES, Linn S: Formation, prevention, and repair of DNA damage by iron/hydrogen peroxide. J Biol Chem 1997, 272:19095-19098. A timely minireview of mechanisms of DNA oxidation catalyzed by iron.
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(1997)
J Biol Chem
, vol.272
, pp. 19095-19098
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Henle, E.S.1
Linn, S.2
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11
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0030839865
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Oxidative decay of DNA
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A timely minireview of biological DNA oxidation
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Beckman KB, Ames BN: Oxidative decay of DNA. J Biol Chem 1997, 272:19633-19636. A timely minireview of biological DNA oxidation.
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(1997)
J Biol Chem
, vol.272
, pp. 19633-19636
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Beckman, K.B.1
Ames, B.N.2
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12
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0030008268
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Fenton chemistry: An introduction
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Wardman P, Candeias LP: Fenton chemistry: an introduction. Radiat Res 1996, 145:523-531.
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(1996)
Radiat Res
, vol.145
, pp. 523-531
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Wardman, P.1
Candeias, L.P.2
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13
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0030851818
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Identification of the prooxidant site of human ceruloplasmin: A model for oxidative damage by copper bound to protein surfaces
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This paper reports the presence of a single histidine residue that is at or near the surface of the protein ceruloplasmin and that coordinates copper ions. The presence of the surface bound copper confers pro-oxidant properties on that protein. Mutagenesis of the surface histidine residue to an arginine results in the loss of this property. This study provides a precedent for surface binding of a redox-active metal by a protein that can enhance its ability to act as a catalyst of oxidative damage because of its accessibility to other components of the cell
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Mukhopadhyay CK, Mazumder B, Lindley PF, Fox PL: Identification of the prooxidant site of human ceruloplasmin: A model for oxidative damage by copper bound to protein surfaces. Proc Natl Acad Sci USA 1997, 94:11546-11551. This paper reports the presence of a single histidine residue that is at or near the surface of the protein ceruloplasmin and that coordinates copper ions. The presence of the surface bound copper confers pro-oxidant properties on that protein. Mutagenesis of the surface histidine residue to an arginine results in the loss of this property. This study provides a precedent for surface binding of a redox-active metal by a protein that can enhance its ability to act as a catalyst of oxidative damage because of its accessibility to other components of the cell.
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(1997)
Proc Natl Acad Sci USA
, vol.94
, pp. 11546-11551
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Mukhopadhyay, C.K.1
Mazumder, B.2
Lindley, P.F.3
Fox, P.L.4
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14
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0001531847
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Iron-sulfur proteins with non redox functions
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A comprehensive review of the properties of such proteins, including a detailed discussion of the sensitivity of some of them to oxidation by superoxide or other oxidants
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Flint DH, Allen RM: Iron-sulfur proteins with non redox functions. Chem Rev 1996, 96:2315-2334. A comprehensive review of the properties of such proteins, including a detailed discussion of the sensitivity of some of them to oxidation by superoxide or other oxidants.
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(1996)
Chem Rev
, vol.96
, pp. 2315-2334
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Flint, D.H.1
Allen, R.M.2
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15
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0030993117
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Superoxide-driven aconitase FE-S center cycling
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Gardner PR: Superoxide-driven aconitase FE-S center cycling. Biosci Rep 1997, 17:33-42.
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(1997)
Biosci Rep
, vol.17
, pp. 33-42
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Gardner, P.R.1
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16
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0030912902
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Redox signal transduction via iron-sulfur clusters in the SoxR transcription activator
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SoxR contains 2Fe-2S clusters and acts as a redox-sensitive transcriptional activator. This minireview of SoxR describes recent findings and includes a comparison of regulatory proteins containing 2Fe-2S and 4Fe-4S clusters as sensors for dioxygen, superoxide, nitric oxide or other oxidants or iron. The authors point out that a potential advantage of 2Fe-2S clusters as redox sensors may be the stability of the cluster in both oxidized and reduced redox states
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Hidalgo E, Ding H, Demple B: Redox signal transduction via iron-sulfur clusters in the SoxR transcription activator. Trends Biochem Sci 1997, 22:207-210. SoxR contains 2Fe-2S clusters and acts as a redox-sensitive transcriptional activator. This minireview of SoxR describes recent findings and includes a comparison of regulatory proteins containing 2Fe-2S and 4Fe-4S clusters as sensors for dioxygen, superoxide, nitric oxide or other oxidants or iron. The authors point out that a potential advantage of 2Fe-2S clusters as redox sensors may be the stability of the cluster in both oxidized and reduced redox states.
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(1997)
Trends Biochem Sci
, vol.22
, pp. 207-210
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Hidalgo, E.1
Ding, H.2
Demple, B.3
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17
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0030957824
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Study of redox-regulated transcription factors in prokaryotes
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Demple B: Study of redox-regulated transcription factors in prokaryotes. Methods 1997, 11:267-278.
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(1997)
Methods
, vol.11
, pp. 267-278
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Demple, B.1
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18
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0032513362
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Activation of the OxyR transcription factor by reversible disulfide bond formation
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Zheng M, Aslund F, Storz G: Activation of the OxyR transcription factor by reversible disulfide bond formation. Science 1998, 279:1718-1721.
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(1998)
Science
, vol.279
, pp. 1718-1721
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Zheng, M.1
Aslund, F.2
Storz, G.3
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19
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0030809576
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Reactive oxygen species, mitochondria, apoptosis and aging
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This interesting review points out that the best method to guard against reactive oxygen species formed in vivo is not antioxidants but reduction in the amount of superoxide formed at the mitochondria that subsequently reacts to give the reactive oxygen species. Topics discussed include mechanisms of superoxide formation in the cell, respiration as a tool to lower dioxygen concentrations, uncoupling as a mechanism to prevent superoxide formation, mitochondrial pores, and the link between the state of the mitochondrion and apoptosis
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Papa S, Skulachev VP: Reactive oxygen species, mitochondria, apoptosis and aging. Mol Cell Biochem 1997, 174:305-319. This interesting review points out that the best method to guard against reactive oxygen species formed in vivo is not antioxidants but reduction in the amount of superoxide formed at the mitochondria that subsequently reacts to give the reactive oxygen species. Topics discussed include mechanisms of superoxide formation in the cell, respiration as a tool to lower dioxygen concentrations, uncoupling as a mechanism to prevent superoxide formation, mitochondrial pores, and the link between the state of the mitochondrion and apoptosis.
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(1997)
Mol Cell Biochem
, vol.174
, pp. 305-319
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Papa, S.1
Skulachev, V.P.2
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21
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0002886891
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Superoxide dismutase: Studies in the yeast Saccharomyces cerevisiae
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Edited by Scandalios JG, Plainview: Cold Spring Harbor Laboratory Press.
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Gralla EB: Superoxide dismutase: studies in the yeast Saccharomyces cerevisiae. In Oxidative Stress and the Molecular Biology of Antioxidant Defenses. Edited by Scandalios JG, Plainview: Cold Spring Harbor Laboratory Press. 1997:495-525.
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(1997)
Oxidative Stress and the Molecular Biology of Antioxidant Defenses
, pp. 495-525
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Gralla, E.B.1
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23
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0030574273
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The oxidative burst protects plants against pathogen attack: Mechanism and role as an emergency signal for plant bio-defence - A review
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Plant cells respond rapidly to infection or wounding with an oxidative burst. This review describes the mechanism of this phenomenon and its function as an internal emergency signal for active defense by the plant
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Doke N, Miura Y, Sanchez LM, Park HJ, Noritake T, Yoshioka H, Kawakita K: The oxidative burst protects plants against pathogen attack: mechanism and role as an emergency signal for plant bio-defence - a review. Gene 1996, 179:45-51. Plant cells respond rapidly to infection or wounding with an oxidative burst. This review describes the mechanism of this phenomenon and its function as an internal emergency signal for active defense by the plant.
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(1996)
Gene
, vol.179
, pp. 45-51
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Doke, N.1
Miura, Y.2
Sanchez, L.M.3
Park, H.J.4
Noritake, T.5
Yoshioka, H.6
Kawakita, K.7
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24
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0030795788
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In vivo kinetics of a redox-regulated transcriptional switch
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This paper shows that the 2Fe-2S clusters of SoxR are reversibly oxidized in vivo in response to superoxide generation. This oxidation correlates with the transcriptional activity of soxS, the target of SoxR. Thus SoxR is the first transcription factor containing iron-sulfur clusters whose activity has been demonstrated to be a direct function of the redox state of the cluster
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Ding H, Demple B: In vivo kinetics of a redox-regulated transcriptional switch. Proc Natl Acad Sci USA 1997, 94:8445-8449. This paper shows that the 2Fe-2S clusters of SoxR are reversibly oxidized in vivo in response to superoxide generation. This oxidation correlates with the transcriptional activity of soxS, the target of SoxR. Thus SoxR is the first transcription factor containing iron-sulfur clusters whose activity has been demonstrated to be a direct function of the redox state of the cluster.
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(1997)
Proc Natl Acad Sci USA
, vol.94
, pp. 8445-8449
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Ding, H.1
Demple, B.2
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25
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0031000271
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2: [4Fe-4S] to [2Fe-2S] conversion with loss of biological activity
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2+ cluster upon exposure to air in vitro was observed using electronic, EPR (electron paramagnetic resonance) and Mossbauer spectroscopies. Little 3Fe-4S cluster was observed. Thus the 4Fe-4S cluster in FNR appears to be more susceptible to direct reaction with dioxygen than the 4Fe-4S cluster in aconitase, which is oxidized rapidly by superoxide but not by dioxygen. These results suggest that the degree of reactivity of 4Fe-4S clusters toward oxidants can be modulated by their individual protein environments
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2+ cluster upon exposure to air in vitro was observed using electronic, EPR (electron paramagnetic resonance) and Mossbauer spectroscopies. Little 3Fe-4S cluster was observed. Thus the 4Fe-4S cluster in FNR appears to be more susceptible to direct reaction with dioxygen than the 4Fe-4S cluster in aconitase, which is oxidized rapidly by superoxide but not by dioxygen. These results suggest that the degree of reactivity of 4Fe-4S clusters toward oxidants can be modulated by their individual protein environments.
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(1997)
Proc Natl Acad Sci USA
, vol.94
, pp. 6087-6092
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Khoroshilova, N.1
Popescu, C.2
Munck, E.3
Beinert, H.4
Kiley, P.J.5
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26
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15144343374
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Epidermal growth factor (EGF)-induced generation of hydrogen peroxide. Role in EGF receptor-mediated tyrosine phosphorylation
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Bae YS, Kang SW, Seo MS, Baines IC, Tekle E, Chock PB, Rhee SG: Epidermal growth factor (EGF)-induced generation of hydrogen peroxide. Role in EGF receptor-mediated tyrosine phosphorylation. J Biol Chem 1997, 272:217-221.
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(1997)
J Biol Chem
, vol.272
, pp. 217-221
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Bae, Y.S.1
Kang, S.W.2
Seo, M.S.3
Baines, I.C.4
Tekle, E.5
Chock, P.B.6
Rhee, S.G.7
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27
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0030980641
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Mitogenic signaling mediated by oxidants in Ras-transformed fibroblasts
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The GTP-binding protein Ras participates in a variety of normal cellular processes, but overexpression of Ras or mutations leading to constitutive activation of Ras can lead to tumor formation. This paper reports that fibroblasts with constitutively active Ras produced large quantities of superoxide and that addition of the antioxidant N-acetyl-L-cysteine to these cells inhibited DNA synthesis. These results imply that superoxide-derived reactive oxygen species induced by the presence of Ras act as signaling agents
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Irani K, Xia Y, Zweier JL, Sollott SJ, Der CJ, Fearon ER, Sundaresan M, Finkel T, Goldschmidt-Clermont PJ: Mitogenic signaling mediated by oxidants in Ras-transformed fibroblasts. Science 1997, 275:1649-1652. The GTP-binding protein Ras participates in a variety of normal cellular processes, but overexpression of Ras or mutations leading to constitutive activation of Ras can lead to tumor formation. This paper reports that fibroblasts with constitutively active Ras produced large quantities of superoxide and that addition of the antioxidant N-acetyl-L-cysteine to these cells inhibited DNA synthesis. These results imply that superoxide-derived reactive oxygen species induced by the presence of Ras act as signaling agents.
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(1997)
Science
, vol.275
, pp. 1649-1652
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Irani, K.1
Xia, Y.2
Zweier, J.L.3
Sollott, S.J.4
Der, C.J.5
Fearon, E.R.6
Sundaresan, M.7
Finkel, T.8
Goldschmidt-Clermont, P.J.9
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28
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0030911732
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Activation of transcription factor NF-KB and p38 mitogen-activated protein kinase is mediated by distinct and separate stress effector pathways
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Wesselborg S, Bauer MKA, Vogt M, Schmitz ML, Schulze-Osthoff K: Activation of transcription factor NF-KB and p38 mitogen-activated protein kinase is mediated by distinct and separate stress effector pathways. J Biol Chem 1997, 272:12422-12429.
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(1997)
J Biol Chem
, vol.272
, pp. 12422-12429
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Wesselborg, S.1
Bauer, M.K.A.2
Vogt, M.3
Schmitz, M.L.4
Schulze-Osthoff, K.5
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29
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0030930366
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A model for p53-induced apoptosis
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The tumor suppressor protein p53 can induce programmed cell death (apoptosis). This paper shows that p53 expression induces expression of many genes with redox-related activities, followed by increased levels of oxidative stress, which is in turn followed by mitochondrial lipid degradation. These results suggest that p53 mediates apoptosis by inducing oxidative damage to the mitochondria
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Polyak K, Xia Y, Zweier JL, Kinzler KW, Vogelstein B: A model for p53-induced apoptosis. Nature 1997, 389:300-305. The tumor suppressor protein p53 can induce programmed cell death (apoptosis). This paper shows that p53 expression induces expression of many genes with redox-related activities, followed by increased levels of oxidative stress, which is in turn followed by mitochondrial lipid degradation. These results suggest that p53 mediates apoptosis by inducing oxidative damage to the mitochondria.
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(1997)
Nature
, vol.389
, pp. 300-305
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Polyak, K.1
Xia, Y.2
Zweier, J.L.3
Kinzler, K.W.4
Vogelstein, B.5
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30
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0030782177
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Cytochrome c: Can't live with it - Can't live without it
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Reed JC: Cytochrome c: can't live with it - can't live without it Cell 1997, 91:559-562.
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(1997)
Cell
, vol.91
, pp. 559-562
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Reed, J.C.1
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31
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0030995428
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On the voltage dependence of the mitochondrial permeability transition pore. A critical appraisal
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Scorrano L, Petronilli V, Bernardi P: On the voltage dependence of the mitochondrial permeability transition pore. A critical appraisal. J Biol Chem 1997, 272:12295-12299.
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(1997)
J Biol Chem
, vol.272
, pp. 12295-12299
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Scorrano, L.1
Petronilli, V.2
Bernardi, P.3
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32
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15844393658
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Motor neurons in Cu/Zn superoxide dismutase-deficient mice develop normally but exhibit enhanced cell death after axonal injury
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Reaume AG, Elliott JL, Hoffman EK, Kowall NW, Ferrante RJ, Siwek DF, Wilcox HM, Flood DG, Beal MF, Brown RH Jr et al.: Motor neurons in Cu/Zn superoxide dismutase-deficient mice develop normally but exhibit enhanced cell death after axonal injury. Nat Genet 1996, 13:43-47.
-
(1996)
Nat Genet
, vol.13
, pp. 43-47
-
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Reaume, A.G.1
Elliott, J.L.2
Hoffman, E.K.3
Kowall, N.W.4
Ferrante, R.J.5
Siwek, D.F.6
Wilcox, H.M.7
Flood, D.G.8
Beal, M.F.9
Brown R.H., Jr.10
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33
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0030971057
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Mice deficient in cellular glutathione peroxidase develop normally and show no increased sensitivity to hyperoxia
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Ho Y-S, Magnenat J-L, Bronson RT, Cao J, Gargano M, Sugawara M, Funk CD: Mice deficient in cellular glutathione peroxidase develop normally and show no increased sensitivity to hyperoxia. J Biol Chem 1997, 272:16644-16651.
-
(1997)
J Biol Chem
, vol.272
, pp. 16644-16651
-
-
Ho, Y.-S.1
Magnenat, J.-L.2
Bronson, R.T.3
Cao, J.4
Gargano, M.5
Sugawara, M.6
Funk, C.D.7
-
34
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0031571663
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Superoxide-mediated cytotoxicity in superoxide dismutase-deficient fetal fibroblasts
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Huang TT, Yasunami M, Carlson EJ, Gillespie AM, Reaume AG, Hoffman EK, Chan PH, Scott RW, Epstein CJ: Superoxide-mediated cytotoxicity in superoxide dismutase-deficient fetal fibroblasts. Arch Biochem Biophys 1997, 344:424-432.
-
(1997)
Arch Biochem Biophys
, vol.344
, pp. 424-432
-
-
Huang, T.T.1
Yasunami, M.2
Carlson, E.J.3
Gillespie, A.M.4
Reaume, A.G.5
Hoffman, E.K.6
Chan, P.H.7
Scott, R.W.8
Epstein, C.J.9
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35
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15844429977
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Superoxide dismutase activity is essential for stationary phase survival in Saccharomyces cerevisiae. Mitochondrial production of toxic oxygen species in vivo
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Longo VD, Gralla EB, Valentine JS: Superoxide dismutase activity is essential for stationary phase survival in Saccharomyces cerevisiae. Mitochondrial production of toxic oxygen species in vivo. J Biol Chem 1996, 271:12275-12280.
-
(1996)
J Biol Chem
, vol.271
, pp. 12275-12280
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-
Longo, V.D.1
Gralla, E.B.2
Valentine, J.S.3
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36
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0028827252
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Dilated cardiomyopathy and neonatal lethality in mutant mice lacking manganese superoxide dismutase
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Li Y, Huang TT, Carlson EJ, Melov S, Ursell PC, Olson JL, Noble LJ, Yoshimura MP, Berger C, Chan PH et al.: Dilated cardiomyopathy and neonatal lethality in mutant mice lacking manganese superoxide dismutase. Nat Genet 1995, 11:376-381.
-
(1995)
Nat Genet
, vol.11
, pp. 376-381
-
-
Li, Y.1
Huang, T.T.2
Carlson, E.J.3
Melov, S.4
Ursell, P.C.5
Olson, J.L.6
Noble, L.J.7
Yoshimura, M.P.8
Berger, C.9
Chan, P.H.10
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37
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0029838063
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Neurodegeneration, myocardial injury, and perinatal death in mitochondrial superoxide dismutase-deficient mice
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Lebovitz RM, Zhang H, Vogel H, Cartwright J Jr, Dionne L, Lu N, Huang S, Matzuk MM: Neurodegeneration, myocardial injury, and perinatal death in mitochondrial superoxide dismutase-deficient mice. Proc Natl Acad Sci USA 1996, 93:9782-9787.
-
(1996)
Proc Natl Acad Sci USA
, vol.93
, pp. 9782-9787
-
-
Lebovitz, R.M.1
Zhang, H.2
Vogel, H.3
Cartwright J., Jr.4
Dionne, L.5
Lu, N.6
Huang, S.7
Matzuk, M.M.8
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38
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0030800997
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2 and is indispensable for stress defense in C3 plants
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In this paper the authors demonstrated that catalase deficient transgenic tobacco plants were sensitive to elevated light levels; however, this increase in sensitivity was not accompanied by an increase in hydrogen peroxide levels, but was accompanied by a decrease in ascorbate and increased levels of oxidized glutathione. They conclude that catalase functions as a cellular sink for hydrogen peroxide, including peroxide produced outside the peroxisomes
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2 and is indispensable for stress defense in C3 plants. EMBO J 1997, 16:4806-4816. In this paper the authors demonstrated that catalase deficient transgenic tobacco plants were sensitive to elevated light levels; however, this increase in sensitivity was not accompanied by an increase in hydrogen peroxide levels, but was accompanied by a decrease in ascorbate and increased levels of oxidized glutathione. They conclude that catalase functions as a cellular sink for hydrogen peroxide, including peroxide produced outside the peroxisomes.
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(1997)
EMBO J
, vol.16
, pp. 4806-4816
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-
Willekens, H.1
Chamnongpol, S.2
Davey, M.3
Schraudner, M.4
Langebartels, C.5
Van Montagu, M.6
Inze, D.7
Van Camp, W.8
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39
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0030925516
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Use of transgenic plants to study antioxidant defenses
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Allen RD, Webb RP, Schake SA: Use of transgenic plants to study antioxidant defenses. Free Radic Biol Med 1997, 23:473-479.
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(1997)
Free Radic Biol Med
, vol.23
, pp. 473-479
-
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Allen, R.D.1
Webb, R.P.2
Schake, S.A.3
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40
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0029815740
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Environmental stress sensitivity of an ascorbic acid-deficient Arabidopsis mutant
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Conklin PL, Williams EH, Last RL: Environmental stress sensitivity of an ascorbic acid-deficient Arabidopsis mutant Proc Natl Acad Sci USA 1996, 93:9970-9974.
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(1996)
Proc Natl Acad Sci USA
, vol.93
, pp. 9970-9974
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Conklin, P.L.1
Williams, E.H.2
Last, R.L.3
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41
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0031010242
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The regulation and function of tobacco superoxide dismutases
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Van Camp W, Inzé D, Van Montagu M: The regulation and function of tobacco superoxide dismutases. Free Radic Biol Med 1997, 23:515-520.
-
(1997)
Free Radic Biol Med
, vol.23
, pp. 515-520
-
-
Van Camp, W.1
Inzé, D.2
Van Montagu, M.3
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42
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0029849183
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Differential expression of superoxide dismutases containing Ni and Fe/Zn in Streptomyces coelicolor
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Kim EJ, Kim HP, Hah YC, Roe JH: Differential expression of superoxide dismutases containing Ni and Fe/Zn in Streptomyces coelicolor. Eur J Biochem 1996, 241:178-185.
-
(1996)
Eur J Biochem
, vol.241
, pp. 178-185
-
-
Kim, E.J.1
Kim, H.P.2
Hah, Y.C.3
Roe, J.H.4
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43
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0030588257
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Unique isozymes of superoxide dismutase in Streptomyces griseus
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Two unique isozymes of SOD from S. griseus are described. SOD I was composed of four identical subunits of molecular weight 13 000 kDa. It was found to contain 0.9 nickel ions per subunit. Its absorption and electron paramagnetic resonance (EPR) spectra were characteristic of Ni(III). SOD II was composed of four identical subunits of molecular weight 22 000 kDa. It was found to contain both iron and zinc. Nickel SOD was found to be widely distributed in Streptomyces. For many years it was thought that all SODs contained either Fe, Mn, or Cu and Zn. One wonders what other novel SODs will be found in the future
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Youn HD, Youn H, Lee JW, Yim YI, Lee JK, Hah YC, Kang SO: Unique isozymes of superoxide dismutase in Streptomyces griseus. Arch Biochem Biophys 1996, 334:341-348. Two unique isozymes of SOD from S. griseus are described. SOD I was composed of four identical subunits of molecular weight 13 000 kDa. It was found to contain 0.9 nickel ions per subunit. Its absorption and electron paramagnetic resonance (EPR) spectra were characteristic of Ni(III). SOD II was composed of four identical subunits of molecular weight 22 000 kDa. It was found to contain both iron and zinc. Nickel SOD was found to be widely distributed in Streptomyces. For many years it was thought that all SODs contained either Fe, Mn, or Cu and Zn. One wonders what other novel SODs will be found in the future.
-
(1996)
Arch Biochem Biophys
, vol.334
, pp. 341-348
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Youn, H.D.1
Youn, H.2
Lee, J.W.3
Yim, Y.I.4
Lee, J.K.5
Hah, Y.C.6
Kang, S.O.7
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44
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0029778889
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A novel nickel-containing superoxide dismutase from Streptomyces spp
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Youn HD, Kim EJ, Roe JH, Hah YC, Kang SO: A novel nickel-containing superoxide dismutase from Streptomyces spp. Biochem J 1996, 318:889-896.
-
(1996)
Biochem J
, vol.318
, pp. 889-896
-
-
Youn, H.D.1
Kim, E.J.2
Roe, J.H.3
Hah, Y.C.4
Kang, S.O.5
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45
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0031569871
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The copper- And zinc-containing superoxide dismutase from Escherichia coli: Molecular weight and stability
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This paper reports further characterization of the periplasmic CuZnSOD from E. coli, which was found by sedimentation equilibrium analysis to be a monomer with a molecular weight of approximately 17 000 kDa. Studies of thermal inactivation of this enzyme in the presence and absence of excess copper and zinc ions suggest that these metal ions are relatively loosely held in this enzyme. Hg(II) was found to inactivate the enzyme, presumably by displacing metal ions from the active site. Not long ago, CuZnSODs were believed to be restricted to eukaryotes and one or two atypical prokaryotes. This is obviously no longer the case and new examples of prokaryotic CuZn-SODs continue to be found
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Benov L, Sage H, Fridovich I: The copper- and zinc-containing superoxide dismutase from Escherichia coli: molecular weight and stability. Arch Biochem Biophys 1997, 340:305-310. This paper reports further characterization of the periplasmic CuZnSOD from E. coli, which was found by sedimentation equilibrium analysis to be a monomer with a molecular weight of approximately 17 000 kDa. Studies of thermal inactivation of this enzyme in the presence and absence of excess copper and zinc ions suggest that these metal ions are relatively loosely held in this enzyme. Hg(II) was found to inactivate the enzyme, presumably by displacing metal ions from the active site. Not long ago, CuZnSODs were believed to be restricted to eukaryotes and one or two atypical prokaryotes. This is obviously no longer the case and new examples of prokaryotic CuZn-SODs continue to be found.
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(1997)
Arch Biochem Biophys
, vol.340
, pp. 305-310
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Benov, L.1
Sage, H.2
Fridovich, I.3
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46
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0029759409
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Superoxide dismutase protects calcineurin from inactivation
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Wang X, Culotta VC, Klee CB: Superoxide dismutase protects calcineurin from inactivation. Nature 1996, 383:434-437.
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(1996)
Nature
, vol.383
, pp. 434-437
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Wang, X.1
Culotta, V.C.2
Klee, C.B.3
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47
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0030802648
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The copper chaperone for superoxide dismutase
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In this paper the authors showed that a specific protein carrier of copper, Lys7p, was required for the proper metallation of CuZnSOD in Saccharomyces cerevisiae. A lys7 knockout strain showed an oxygen sensitive phenotype characteristic of CuZnSOD deficiency. This strain contained copper-deficient CuZnSOD protein but showed normal processing of other copper proteins. The oxygen sensitivity of the lys7 knockout strain is particularly striking since both the CuZnSOD protein and the copper ions are present in sufficient amounts but the copper is not inserted into the protein
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Culotta VC, Klomp LW, Strain J, Casareno RL, Krems B, Gitlin JD: The copper chaperone for superoxide dismutase. J Biol Chem 1997, 272:23469-23472. In this paper the authors showed that a specific protein carrier of copper, Lys7p, was required for the proper metallation of CuZnSOD in Saccharomyces cerevisiae. A lys7 knockout strain showed an oxygen sensitive phenotype characteristic of CuZnSOD deficiency. This strain contained copper-deficient CuZnSOD protein but showed normal processing of other copper proteins. The oxygen sensitivity of the lys7 knockout strain is particularly striking since both the CuZnSOD protein and the copper ions are present in sufficient amounts but the copper is not inserted into the protein.
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(1997)
J Biol Chem
, vol.272
, pp. 23469-23472
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Culotta, V.C.1
Klomp, L.W.2
Strain, J.3
Casareno, R.L.4
Krems, B.5
Gitlin, J.D.6
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48
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0030474295
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Rubrerythrin from Clostridium perfringens: Cloning of the gene, purification of the protein, and characterization of its superoxide dismutase function
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Lehmann Y, Meile L, Teuber M: Rubrerythrin from Clostridium perfringens: cloning of the gene, purification of the protein, and characterization of its superoxide dismutase function. J Bacteriol 1996, 178:7152-7158.
-
(1996)
J Bacteriol
, vol.178
, pp. 7152-7158
-
-
Lehmann, Y.1
Meile, L.2
Teuber, M.3
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49
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0030867832
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A mechanism for complementation of the sodA sodB defect in Escherichia coli by overproduction of the rbo gene product (desulfoferridoxin) from Desulfoarculus baarsii
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Liochev SI, Fridovich I: A mechanism for complementation of the sodA sodB defect in Escherichia coli by overproduction of the rbo gene product (desulfoferridoxin) from Desulfoarculus baarsii. J Biol Chem 1997, 272:25573-25575.
-
(1997)
J Biol Chem
, vol.272
, pp. 25573-25575
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Liochev, S.I.1
Fridovich, I.2
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50
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0031571101
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A potent superoxide dismutase mimic: Manganese β-octabromo-mesotetrakis-(N-methylpyridinium-4-yl) porphyrin
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Batinic-Haberle I, Liochev SI, Spasojevic I, Fridovich I: A potent superoxide dismutase mimic: manganese β-octabromo-mesotetrakis-(N-methylpyridinium-4-yl) porphyrin. Arch Biochem Biophys 1997, 343:225-233.
-
(1997)
Arch Biochem Biophys
, vol.343
, pp. 225-233
-
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Batinic-Haberle, I.1
Liochev, S.I.2
Spasojevic, I.3
Fridovich, I.4
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51
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0029979718
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Manganese-based superoxide dismutase mimetics inhibit neutrophil infiltration in vivo
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This paper describes in vivo studies of several manganese-containing synthetic SODs which had previously been shown to have high SOD activity and to inhibit neutrophil-mediated cell injury in vitro. These drugs were found to inhibit colonic tissue injury and neutrophil accumulation in a dose-dependent manner. Similar manganese-containing compounds with little or no SOD activity were ineffective. These results support a proinflammatory role for superoxide in tissue injury and provide further encouragement for development of synthetic SODs as drugs
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Weiss RH, Fretland DJ, Baron DA, Ryan US, Riley DP: Manganese-based superoxide dismutase mimetics inhibit neutrophil infiltration in vivo. J Biol Chem 1996, 271:26149-26156. This paper describes in vivo studies of several manganese-containing synthetic SODs which had previously been shown to have high SOD activity and to inhibit neutrophil-mediated cell injury in vitro. These drugs were found to inhibit colonic tissue injury and neutrophil accumulation in a dose-dependent manner. Similar manganese-containing compounds with little or no SOD activity were ineffective. These results support a proinflammatory role for superoxide in tissue injury and provide further encouragement for development of synthetic SODs as drugs.
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(1996)
J Biol Chem
, vol.271
, pp. 26149-26156
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Weiss, R.H.1
Fretland, D.J.2
Baron, D.A.3
Ryan, U.S.4
Riley, D.P.5
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53
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0030955353
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The yeast peptide-methionine sulfoxide reductase functions as an antioxidant in vivo
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This paper reports identification and characterization of the enzyme methionine sulfoxide reductase (MsrA) in the yeast S. cerevisiae. Interruption of the yeast gene resulted in a null mutant, which totally lost its cellular MsrA activity and was more susceptible to oxidative stress than its wild type parent strain. Under various oxidative stresses, high levels of free and protein-bound methionine sulfoxide were found in extracts of the null mutant cells relative to their wild type parent cells. These results suggest that methionine plus MsrA constitutes an antioxidant system in which free or external methionine residues act as scavengers of reactive oxygen species followed by re-reduction of the resulting methionine residues in a reaction catalyzed by MsrA. MsrA should thus be added to the list of antioxidant enzymes in the cell
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Moskovitz J, Berlett BS, Poston JM, Stadtman ER: The yeast peptide-methionine sulfoxide reductase functions as an antioxidant in vivo. Proc Natl Acad Sci USA 1997, 94:9585-9589. This paper reports identification and characterization of the enzyme methionine sulfoxide reductase (MsrA) in the yeast S. cerevisiae. Interruption of the yeast gene resulted in a null mutant, which totally lost its cellular MsrA activity and was more susceptible to oxidative stress than its wild type parent strain. Under various oxidative stresses, high levels of free and protein-bound methionine sulfoxide were found in extracts of the null mutant cells relative to their wild type parent cells. These results suggest that methionine plus MsrA constitutes an antioxidant system in which free or external methionine residues act as scavengers of reactive oxygen species followed by re-reduction of the resulting methionine residues in a reaction catalyzed by MsrA. MsrA should thus be added to the list of antioxidant enzymes in the cell.
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(1997)
Proc Natl Acad Sci USA
, vol.94
, pp. 9585-9589
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Moskovitz, J.1
Berlett, B.S.2
Poston, J.M.3
Stadtman, E.R.4
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54
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0030449173
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Methionine residues as endogenous antioxidants in proteins
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Levine RL, Mosoni L, Berlett BS, Stadtman ER: Methionine residues as endogenous antioxidants in proteins. Proc Natl Acad Sci USA 1996, 93:15036-15040.
-
(1996)
Proc Natl Acad Sci USA
, vol.93
, pp. 15036-15040
-
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Levine, R.L.1
Mosoni, L.2
Berlett, B.S.3
Stadtman, E.R.4
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55
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0031042252
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Toward site specificity of oxidative damage in proteins: C-H and C-C bond dissociation energies and reduction potentials of the radicals of alanine, serine, and threonine residues - An ab initio study
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This paper addresses the issue of whether the susceptibility to oxidative damage of individual amino acid residues in proteins depends upon the secondary structure in which they occur. Ab initio calculations indicated that amino acid residues in β sheet structures would be more susceptible to hydrogen atom abstraction at the α-carbon position relative to those in α-helical structures. Theoretical calculations also indicated that sensitivity increases in the series alanine
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Rauk A, Yu D, Armstrong DA: Toward site specificity of oxidative damage in proteins: C-H and C-C bond dissociation energies and reduction potentials of the radicals of alanine, serine, and threonine residues - an ab initio study. J Am Chem Soc 1997, 119:208-217. This paper addresses the issue of whether the susceptibility to oxidative damage of individual amino acid residues in proteins depends upon the secondary structure in which they occur. Ab initio calculations indicated that amino acid residues in β sheet structures would be more susceptible to hydrogen atom abstraction at the α-carbon position relative to those in α-helical structures. Theoretical calculations also indicated that sensitivity increases in the series alanine
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(1997)
J am Chem Soc
, vol.119
, pp. 208-217
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Rauk, A.1
Yu, D.2
Armstrong, D.A.3
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56
-
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0030952676
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Modification of protein surface hydrophobicity and methionine oxidation by oxidative systems
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Chao CC, Ma YS, Stadtman ER: Modification of protein surface hydrophobicity and methionine oxidation by oxidative systems. Proc Natl Acad Sci USA 1997, 94:2969-2974.
-
(1997)
Proc Natl Acad Sci USA
, vol.94
, pp. 2969-2974
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Chao, C.C.1
Ma, Y.S.2
Stadtman, E.R.3
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58
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0030942257
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Differences in the regulation of iron regulatory protein-1 (IRP-1) by extra- And intracellular oxidative stress
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Pantopoulos K, Mueller S, Atzberger A, Ansorge W, Stremmel W, Hentze MW: Differences in the regulation of iron regulatory protein-1 (IRP-1) by extra- and intracellular oxidative stress. J Biol Chem 1997, 272:9802-9808.
-
(1997)
J Biol Chem
, vol.272
, pp. 9802-9808
-
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Pantopoulos, K.1
Mueller, S.2
Atzberger, A.3
Ansorge, W.4
Stremmel, W.5
Hentze, M.W.6
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59
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0030751667
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Prooxidant-initiated lipid peroxidation in isolated rat hepatocytes: Detection of 4-hydroxynonenal- And malondialdehyde-protein adducts
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4 nor iron/ascorbate elicited changes in 4-HNE or induced 4-HNE-modified proteins. Experiments of the type described in this paper will be very useful in establishing the details of oxidative damage pathways occurring in vivo
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4 nor iron/ascorbate elicited changes in 4-HNE or induced 4-HNE-modified proteins. Experiments of the type described in this paper will be very useful in establishing the details of oxidative damage pathways occurring in vivo.
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(1997)
Chem Res Toxicol
, vol.10
, pp. 895-905
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Hartley, D.P.1
Kroll, D.J.2
Petersen, D.R.3
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60
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0030882878
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Metabolic activation of trans-4-hydroxy-2-nonenal, a toxic product of membrane lipid peroxidation and inhibitor of P450 cytochromes
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Kuo CL, Vaz ADN, Coon MJ: Metabolic activation of trans-4-hydroxy-2-nonenal, a toxic product of membrane lipid peroxidation and inhibitor of P450 cytochromes. J Biol Chem 1997, 272:22611-22616.
-
(1997)
J Biol Chem
, vol.272
, pp. 22611-22616
-
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Kuo, C.L.1
Vaz, A.D.N.2
Coon, M.J.3
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61
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0030857377
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Iron homeostasis, oxidative stress, and DNA damage
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Meneghini R: Iron homeostasis, oxidative stress, and DNA damage. Free Radic Biol Med 1997, 23:783-792.
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(1997)
Free Radic Biol Med
, vol.23
, pp. 783-792
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Meneghini, R.1
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62
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0029920828
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Site-specific DNA damage induced by NADH in the presence of copper(II): Role of active oxygen species
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DNA damage was induced by NAD(P)H in the presence of Cu(II). The damage was inhibited by catalase as well as by chelation of Cu(I) but not by hydroxyl radical scavengers. These results suggest that NAD(P)H can act as an endogenous reductant of DNA-bound Cu(II) to Cu(I) which then reacts with hydrogen peroxide to give oxidation of DNA. The oxidation is proposed to occur via a DNA-Cu(I)OOH complex or by generation of hydroxyl radicals in a site-specific manner
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Oikawa S, Kawanishi S: Site-specific DNA damage induced by NADH in the presence of copper(II): Role of active oxygen species. Biochemistry 1996, 35:4584-4590. DNA damage was induced by NAD(P)H in the presence of Cu(II). The damage was inhibited by catalase as well as by chelation of Cu(I) but not by hydroxyl radical scavengers. These results suggest that NAD(P)H can act as an endogenous reductant of DNA-bound Cu(II) to Cu(I) which then reacts with hydrogen peroxide to give oxidation of DNA. The oxidation is proposed to occur via a DNA-Cu(I)OOH complex or by generation of hydroxyl radicals in a site-specific manner.
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(1996)
Biochemistry
, vol.35
, pp. 4584-4590
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Oikawa, S.1
Kawanishi, S.2
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63
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0029682487
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Reactions of nitric oxide with metalloproteins
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A comprehensive review of reactions of NO and species derived from it with metalloproteins
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Radi R: Reactions of nitric oxide with metalloproteins. Chem Res Toxicol 1996, 9:828-835. A comprehensive review of reactions of NO and species derived from it with metalloproteins.
-
(1996)
Chem Res Toxicol
, vol.9
, pp. 828-835
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Radi, R.1
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64
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0029682870
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Oxidative damage and tyrosine nitration from peroxynitrite
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Peroxynitrite, formed from the reaction of nitric oxide (NO) with superoxide, has been implicated as a major agent of NO-induced cytotoxicity. This comprehensive review describes the experiments in support of this hypothesis
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Beckman JS: Oxidative damage and tyrosine nitration from peroxynitrite. Chem Res Toxicol 1996, 9:836-844. Peroxynitrite, formed from the reaction of nitric oxide (NO) with superoxide, has been implicated as a major agent of NO-induced cytotoxicity. This comprehensive review describes the experiments in support of this hypothesis.
-
(1996)
Chem Res Toxicol
, vol.9
, pp. 836-844
-
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Beckman, J.S.1
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65
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0000892477
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-OONO) play a major role in cytotoxicity?
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This commentary critically evaluates the hypothesis that peroxynitrite plays a major role in cytotoxicity in vivo and concludes that the evidence currently available is not sufficient to reach that conclusion
-
-OONO) play a major role in cytotoxicity? Accounts Chem Res 1997, 30:149-152. This commentary critically evaluates the hypothesis that peroxynitrite plays a major role in cytotoxicity in vivo and concludes that the evidence currently available is not sufficient to reach that conclusion.
-
(1997)
Accounts Chem Res
, vol.30
, pp. 149-152
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Fukuto, J.M.1
Ignarro, L.J.2
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66
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0031567576
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What nitrates tyrosine? Is nitrotyrosine specific as a biomarker of peroxynitrite formation in vivo?
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This paper concludes that the evidence is not conclusive that nitrotyrosine is specific as a biomarker of peroxynitrite formation in vivo and suggests that the nitrating agent be referred to as a reactive nitrogen species
-
Halliwell B: What nitrates tyrosine? Is nitrotyrosine specific as a biomarker of peroxynitrite formation in vivo? FEBS Lett 1997, 411:157-160. This paper concludes that the evidence is not conclusive that nitrotyrosine is specific as a biomarker of peroxynitrite formation in vivo and suggests that the nitrating agent be referred to as a reactive nitrogen species.
-
(1997)
FEBS Lett
, vol.411
, pp. 157-160
-
-
Halliwell, B.1
-
67
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0029680493
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Carbon dioxide: Physiological catalyst for peroxynitrite-mediated cellular damage or cellular protectant?
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-. This reaction occurs at physiologically relevant concentrations and may represent the major fate of peroxynitrite when it is formed in vivo. This paper reviews this topic and concludes that considerably more knowledge about the lifetime and reactivity of this adduct is required before its biological significance can be assessed
-
-. This reaction occurs at physiologically relevant concentrations and may represent the major fate of peroxynitrite when it is formed in vivo. This paper reviews this topic and concludes that considerably more knowledge about the lifetime and reactivity of this adduct is required before its biological significance can be assessed.
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(1996)
Chem Res Toxicol
, vol.9
, pp. 845-850
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Lymar, S.V.1
Hurst, J.K.2
-
68
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0030456218
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Inhibition of the catalytic activity of alcohol dehydrogenase by nitric oxide is associated with S-nitrosylation and the release of zinc
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Gergel D, Cederbaum Al: Inhibition of the catalytic activity of alcohol dehydrogenase by nitric oxide is associated with S-nitrosylation and the release of zinc. Biochemistry 1996, 35:16186-16194.
-
(1996)
Biochemistry
, vol.35
, pp. 16186-16194
-
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Gergel, D.1
Cederbaum, A.2
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69
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0031054520
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ras interaction
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Nitric oxide (NO) stimulates Ras by increasing its guanine nucleotide exchange activity by nitrosothiol formation. In this report the authors determine that this S-nitrosylation specifically occurs at Cys118 of the protein. Mutation of this residue to a serine prevents NO induction of guanine nucleotide exchange and two mitogen-activated protein (MAP) kinases downstream of Ras
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ras interaction. J Biol Chem 1997, 272:4323-4326. Nitric oxide (NO) stimulates Ras by increasing its guanine nucleotide exchange activity by nitrosothiol formation. In this report the authors determine that this S-nitrosylation specifically occurs at Cys118 of the protein. Mutation of this residue to a serine prevents NO induction of guanine nucleotide exchange and two mitogen-activated protein (MAP) kinases downstream of Ras.
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(1997)
J Biol Chem
, vol.272
, pp. 4323-4326
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Lander, H.M.1
Hajjar, D.P.2
Hempstead, B.L.3
Mirza, U.A.4
Chait, B.T.5
Campbell, S.6
Quilliam, L.A.7
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70
-
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0031029150
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A novel reaction mechanism for the formation of S-nitrosothiol in vivo
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2 to give RS-N=O plus superoxide. Chemical evidence in support of the feasibility of this mechanism is presented
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2 to give RS-N=O plus superoxide. Chemical evidence in support of the feasibility of this mechanism is presented.
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(1997)
J Biol Chem
, vol.272
, pp. 2841-2845
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Gow, A.J.1
Buerk, D.G.2
Ischiropoulos, H.3
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71
-
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0030822507
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Nitric oxide sensitivity of the aconitases
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Gardner PR, Costantino G, Szabo C, Salzman AL: Nitric oxide sensitivity of the aconitases. J Biol Chem 1997, 272:25071-25076.
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(1997)
J Biol Chem
, vol.272
, pp. 25071-25076
-
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Gardner, P.R.1
Costantino, G.2
Szabo, C.3
Salzman, A.L.4
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72
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0030950713
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Interplay between NO and [Fe-S] clusters: Relevance to biological systems
-
Drapier J-C: Interplay between NO and [Fe-S] clusters: relevance to biological systems. Methods 1997, 11:319-329.
-
(1997)
Methods
, vol.11
, pp. 319-329
-
-
Drapier, J.-C.1
-
73
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0030731929
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Interplay between ferritin metabolism, reactive oxygen species and nitric oxide
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Lipinski P, Drapier J-C: Interplay between ferritin metabolism, reactive oxygen species and nitric oxide. J Biol Inorg Chem 1997, 2:559-566.
-
(1997)
J Biol Inorg Chem
, vol.2
, pp. 559-566
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Lipinski, P.1
Drapier, J.-C.2
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75
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0030827975
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Reactive oxygen species and Alzheimer's disease
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This commentary describes evidence suggesting that the presence of amyloid peptide βA4, which is derived from the amyloid precursor protein (APP), leads to oxidative stress by a mechanism that involves complexation and reduction of Cu(II) to Cu(I). The paper is marred by the failure of the authors to address satisfactorily earlier criticisms of the use of bathocuprein as a method for detection of Cu(I) formation [76]
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Multhaup G, Ruppert T, Schlicksupp A, Hesse L, Beher D, Masters CL, Beyreuther K: Reactive oxygen species and Alzheimer's disease. Biochem Pharmacol 1997, 54:533-539. This commentary describes evidence suggesting that the presence of amyloid peptide βA4, which is derived from the amyloid precursor protein (APP), leads to oxidative stress by a mechanism that involves complexation and reduction of Cu(II) to Cu(I). The paper is marred by the failure of the authors to address satisfactorily earlier criticisms of the use of bathocuprein as a method for detection of Cu(I) formation [76].
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(1997)
Biochem Pharmacol
, vol.54
, pp. 533-539
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Multhaup, G.1
Ruppert, T.2
Schlicksupp, A.3
Hesse, L.4
Beher, D.5
Masters, C.L.6
Beyreuther, K.7
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76
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0030474926
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Alzheimer's precursor protein and the use of bathocuproine for determining reduction of copper(II)
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Sayre LM, Multhaup G: Alzheimer's precursor protein and the use of bathocuproine for determining reduction of copper(II). Science 1996, 274:1933-1934.
-
(1996)
Science
, vol.274
, pp. 1933-1934
-
-
Sayre, L.M.1
Multhaup, G.2
-
77
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0030983405
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Mechanisms of neurotoxicity associated with amyloid βdeposition and the role of free radicals in the pathogenesis of Alzheimer's disease: A critical appraisal
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A comprehensive review of proposed mechanisms of neurotoxicity associated with amyloid deposition in Alzheimer's disease
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Sayre LM, Zagorski MG, Surewicz WK, Krafft GA, Perry G: Mechanisms of neurotoxicity associated with amyloid βdeposition and the role of free radicals in the pathogenesis of Alzheimer's disease: a critical appraisal. Chem Res Toxicol 1997, 10:518-526. A comprehensive review of proposed mechanisms of neurotoxicity associated with amyloid deposition in Alzheimer's disease.
-
(1997)
Chem Res Toxicol
, vol.10
, pp. 518-526
-
-
Sayre, L.M.1
Zagorski, M.G.2
Surewicz, W.K.3
Krafft, G.A.4
Perry, G.5
-
79
-
-
0031567601
-
Deletion of the yeast homologue of the human gene associated with Friedreich's ataxia elicits iron accumulation in mitochondria
-
Foury F, Cazzalini O: Deletion of the yeast homologue of the human gene associated with Friedreich's ataxia elicits iron accumulation in mitochondria. FEBS Lett 1997, 411:373-377.
-
(1997)
FEBS Lett
, vol.411
, pp. 373-377
-
-
Foury, F.1
Cazzalini, O.2
-
80
-
-
0031253821
-
Aconitase and mitochondrial iron-sulphur protein deficiency in Friedreich ataxia
-
Friedreich ataxia is a degenerative disease linked to mutations in the frataxin gene. This gene is believed to be involved in mitochondrial iron transport, based on studies of a homologous protein in yeast. In this report, the authors show that the activities of aconitase and complexes I, II, and III of the electron transport chain, which are Fe-S cluster containing enzymes, are reduced in heart tissue from two Freidreich ataxia patients relative to the average control activities
-
Rotig A, de Lonlay P, Chretien D, Foury F, Koenig M, Sidi D, Munnich A, Rustin P: Aconitase and mitochondrial iron-sulphur protein deficiency in Friedreich ataxia. Nat Genet 1997, 17:215-217. Friedreich ataxia is a degenerative disease linked to mutations in the frataxin gene. This gene is believed to be involved in mitochondrial iron transport, based on studies of a homologous protein in yeast. In this report, the authors show that the activities of aconitase and complexes I, II, and III of the electron transport chain, which are Fe-S cluster containing enzymes, are reduced in heart tissue from two Freidreich ataxia patients relative to the average control activities.
-
(1997)
Nat Genet
, vol.17
, pp. 215-217
-
-
Rotig, A.1
De Lonlay, P.2
Chretien, D.3
Foury, F.4
Koenig, M.5
Sidi, D.6
Munnich, A.7
Rustin, P.8
-
81
-
-
0031215133
-
Copper-binding motifs in catalysis, transport, detoxification and signaling
-
Koch KA, Pena MM, Thiele DJ: Copper-binding motifs in catalysis, transport, detoxification and signaling. Chem Biol 1997, 4:549-560.
-
(1997)
Chem Biol
, vol.4
, pp. 549-560
-
-
Koch, K.A.1
Pena, M.M.2
Thiele, D.J.3
-
82
-
-
15844366271
-
Involvement of hydrogen peroxide in collagen cross-linking by high glucose in vitro and in vivo
-
Elgawish A, Glomb M, Friedlander M, Monnier VM: Involvement of hydrogen peroxide in collagen cross-linking by high glucose in vitro and in vivo. J Biol Chem 1996, 271:12964-12971.
-
(1996)
J Biol Chem
, vol.271
, pp. 12964-12971
-
-
Elgawish, A.1
Glomb, M.2
Friedlander, M.3
Monnier, V.M.4
-
83
-
-
0029996734
-
Compensatory ahpC gene expression in isoniazid-resistant Mycobacterium tuberculosis
-
The catalase-peroxidase KatG in Mycobacterium tuberculosis activates the drug isoniazid to a form toxic to this bacterium. Loss of KatG function results in isoniazid resistance, but results in increased peroxide sensitivity. In this report, the authors show that isoniazid-resistant KatG mutants compensate for the loss of KatG function by mutations resulting in the overexpression of Ahp C, a putative alkyl hydroperoxidase
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Sherman DR, Mdluli K, Hickey MJ, Arain TM, Morris SL, Barry CE III, Stover CK: Compensatory ahpC gene expression in isoniazid-resistant Mycobacterium tuberculosis. Science 1996, 272:1641-1643. The catalase-peroxidase KatG in Mycobacterium tuberculosis activates the drug isoniazid to a form toxic to this bacterium. Loss of KatG function results in isoniazid resistance, but results in increased peroxide sensitivity. In this report, the authors show that isoniazid-resistant KatG mutants compensate for the loss of KatG function by mutations resulting in the overexpression of Ahp C, a putative alkyl hydroperoxidase.
-
(1996)
Science
, vol.272
, pp. 1641-1643
-
-
Sherman, D.R.1
Mdluli, K.2
Hickey, M.J.3
Arain, T.M.4
Morris, S.L.5
Barry C.E. III6
Stover, C.K.7
-
84
-
-
0031439957
-
Oxidative DNA cleavage by the antitumor antibiotic leinamycin and simple 1,2-dithiolan-3-one 1-oxides: Evidence for thiol-dependent conversion of molecular oxygen to DNA-cleaving oxygen radicals mediated by polysulfides
-
Mitra K, Kim W, Daniels JS, Gates KS: Oxidative DNA cleavage by the antitumor antibiotic leinamycin and simple 1,2-dithiolan-3-one 1-oxides: evidence for thiol-dependent conversion of molecular oxygen to DNA-cleaving oxygen radicals mediated by polysulfides. J Am Chem Soc 1997, 119:11691-11692.
-
(1997)
J am Chem Soc
, vol.119
, pp. 11691-11692
-
-
Mitra, K.1
Kim, W.2
Daniels, J.S.3
Gates, K.S.4
-
85
-
-
0030237186
-
Structure and biodistribution relationships of photodynamic sensitizers
-
Boyle RW, Dolphin D: Structure and biodistribution relationships of photodynamic sensitizers. Photochem Photobiol 1996, 64:469-485.
-
(1996)
Photochem Photobiol
, vol.64
, pp. 469-485
-
-
Boyle, R.W.1
Dolphin, D.2
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