PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 34266485-1 2021 BACKGROUND: Superoxide dismutase (SOD), a central component of the antioxidant defence system of most organisms, removes excess superoxide anions by converting them to oxygen and hydrogen peroxide. Hydrogen Peroxide 179-196 superoxide dismutase 1 Homo sapiens 34-37 35630540-5 2022 By activating antioxidant enzymes such as superoxide dismutases (SOD), catalase (CAT) and phenylalanine ammonia-lyase (PAL) and subsequently eliminating reactive oxygen species (ROS) in a timely manner, the rate of O-2 production and H2O2 content of wheat seedlings were reduced, and the dynamic balance of free radical metabolism in the plant body was maintained. Hydrogen Peroxide 234-238 superoxide dismutase 1 Homo sapiens 42-63 34821332-5 2021 In a cell assay, this nanoplatform could function as an antagonist of GPX4 and agonist of SOD-1, resulting in intracellular ROS and H2O2 accumulation. Hydrogen Peroxide 132-136 superoxide dismutase 1 Homo sapiens 90-95 35472363-6 2022 Specifically, they effectively protected SH-SY5Y cells from H2O2-induced damage by enhancing antioxidant enzyme activities (SOD), total antioxidant capacity (T-AOC) and suppressing malondialdehyde (MDA) levels. Hydrogen Peroxide 60-64 superoxide dismutase 1 Homo sapiens 124-127 35630540-5 2022 By activating antioxidant enzymes such as superoxide dismutases (SOD), catalase (CAT) and phenylalanine ammonia-lyase (PAL) and subsequently eliminating reactive oxygen species (ROS) in a timely manner, the rate of O-2 production and H2O2 content of wheat seedlings were reduced, and the dynamic balance of free radical metabolism in the plant body was maintained. Hydrogen Peroxide 234-238 superoxide dismutase 1 Homo sapiens 65-68 35483970-5 2022 CFS treatment fundamentally reduced the intracellular reactive oxygen species (ROS) and malondialdehyde (MDA) contents and improved the activities of antioxidant enzymes (CAT, SOD and GSH-Px) in H2 O2 -treated HaCaT cells. Hydrogen Peroxide 195-200 superoxide dismutase 1 Homo sapiens 176-179 35624792-1 2022 The superoxide dismutase (SOD) family functions as a reactive oxygen species (ROS)-scavenging system by converting superoxide anions into hydrogen peroxide in the cytosol (SOD1), mitochondria (SOD2), and extracellular matrix (SOD3). Hydrogen Peroxide 138-155 superoxide dismutase 1 Homo sapiens 4-24 35624792-1 2022 The superoxide dismutase (SOD) family functions as a reactive oxygen species (ROS)-scavenging system by converting superoxide anions into hydrogen peroxide in the cytosol (SOD1), mitochondria (SOD2), and extracellular matrix (SOD3). Hydrogen Peroxide 138-155 superoxide dismutase 1 Homo sapiens 26-29 35624792-1 2022 The superoxide dismutase (SOD) family functions as a reactive oxygen species (ROS)-scavenging system by converting superoxide anions into hydrogen peroxide in the cytosol (SOD1), mitochondria (SOD2), and extracellular matrix (SOD3). Hydrogen Peroxide 138-155 superoxide dismutase 1 Homo sapiens 172-176 35191133-8 2022 Moreover, it significantly attenuated H2O2-induced oxidative stress as measured by malondialdehyde (MDA), glutathione (GSH), nitrite and superoxide dismutase (SOD) level. Hydrogen Peroxide 38-42 superoxide dismutase 1 Homo sapiens 137-157 35191133-8 2022 Moreover, it significantly attenuated H2O2-induced oxidative stress as measured by malondialdehyde (MDA), glutathione (GSH), nitrite and superoxide dismutase (SOD) level. Hydrogen Peroxide 38-42 superoxide dismutase 1 Homo sapiens 159-162 35515703-1 2022 Vitamin B12 (B12) is an essential co-factor for two enzymes in mammalian metabolism and can also act as a mimetic of superoxide dismutase (SOD) converting superoxide (O2 -) to hydrogen peroxide (H2O2). Hydrogen Peroxide 177-194 superoxide dismutase 1 Homo sapiens 117-137 35566156-6 2022 They also restore SOD activity reduced by H2O2. Hydrogen Peroxide 42-46 superoxide dismutase 1 Homo sapiens 18-21 35515703-1 2022 Vitamin B12 (B12) is an essential co-factor for two enzymes in mammalian metabolism and can also act as a mimetic of superoxide dismutase (SOD) converting superoxide (O2 -) to hydrogen peroxide (H2O2). Hydrogen Peroxide 177-194 superoxide dismutase 1 Homo sapiens 139-142 35515703-1 2022 Vitamin B12 (B12) is an essential co-factor for two enzymes in mammalian metabolism and can also act as a mimetic of superoxide dismutase (SOD) converting superoxide (O2 -) to hydrogen peroxide (H2O2). Hydrogen Peroxide 196-200 superoxide dismutase 1 Homo sapiens 117-137 35515703-1 2022 Vitamin B12 (B12) is an essential co-factor for two enzymes in mammalian metabolism and can also act as a mimetic of superoxide dismutase (SOD) converting superoxide (O2 -) to hydrogen peroxide (H2O2). Hydrogen Peroxide 196-200 superoxide dismutase 1 Homo sapiens 139-142 35204309-1 2022 SOD1 is the major superoxide dismutase responsible for catalyzing dismutation of superoxide to hydrogen peroxide and molecular oxygen. Hydrogen Peroxide 95-112 superoxide dismutase 1 Homo sapiens 0-4 35198094-10 2022 In addition, luteolin significantly increased the activities of SOD and GSH-PX and decreased intracellular levels of ROS and MDA in H2O2-treated ARPE-19 cells. Hydrogen Peroxide 132-136 superoxide dismutase 1 Homo sapiens 64-67 35125733-2 2022 Superoxide dismutase (SOD) has been commonly identified as dismutase enzyme catalyzes the conversion of superoxide to hydrogen peroxide and elemental oxygen, and could serve as an important biomarker in this direction. Hydrogen Peroxide 118-135 superoxide dismutase 1 Homo sapiens 0-20 35125733-2 2022 Superoxide dismutase (SOD) has been commonly identified as dismutase enzyme catalyzes the conversion of superoxide to hydrogen peroxide and elemental oxygen, and could serve as an important biomarker in this direction. Hydrogen Peroxide 118-135 superoxide dismutase 1 Homo sapiens 22-25 34981336-5 2022 The cytotoxic effect of H2O2 and expression of LDH, caspase-3, MDA and SOD was analyzed by assay kit. Hydrogen Peroxide 24-28 superoxide dismutase 1 Homo sapiens 71-74 2703311-6 1989 The addition of superoxide dismutase (SOD) to the protein solution prior to photolysis increased the amount of H2O2 generated by 3- to 4-fold. Hydrogen Peroxide 111-115 superoxide dismutase 1 Homo sapiens 16-36 34969852-8 2022 Altogether, Sod1-derived H2O2 is important for antioxidant defense and a master regulator of metabolism and the thiol redoxome. Hydrogen Peroxide 25-29 superoxide dismutase 1 Homo sapiens 12-16 2556228-8 1989 Superoxide dismutase (SOD) produced increases in the iodination reaction in stimulated PMN by increasing the availability of H2O2. Hydrogen Peroxide 125-129 superoxide dismutase 1 Homo sapiens 0-20 2556228-8 1989 Superoxide dismutase (SOD) produced increases in the iodination reaction in stimulated PMN by increasing the availability of H2O2. Hydrogen Peroxide 125-129 superoxide dismutase 1 Homo sapiens 22-25 34969852-1 2022 Cu/Zn superoxide dismutase (Sod1) is a highly conserved and abundant antioxidant enzyme that detoxifies superoxide (O2 -) by catalyzing its conversion to dioxygen (O2) and hydrogen peroxide (H2O2). Hydrogen Peroxide 173-190 superoxide dismutase 1 Homo sapiens 0-26 34969852-1 2022 Cu/Zn superoxide dismutase (Sod1) is a highly conserved and abundant antioxidant enzyme that detoxifies superoxide (O2 -) by catalyzing its conversion to dioxygen (O2) and hydrogen peroxide (H2O2). Hydrogen Peroxide 173-190 superoxide dismutase 1 Homo sapiens 28-32 34969852-1 2022 Cu/Zn superoxide dismutase (Sod1) is a highly conserved and abundant antioxidant enzyme that detoxifies superoxide (O2 -) by catalyzing its conversion to dioxygen (O2) and hydrogen peroxide (H2O2). Hydrogen Peroxide 192-196 superoxide dismutase 1 Homo sapiens 0-26 34969852-1 2022 Cu/Zn superoxide dismutase (Sod1) is a highly conserved and abundant antioxidant enzyme that detoxifies superoxide (O2 -) by catalyzing its conversion to dioxygen (O2) and hydrogen peroxide (H2O2). Hydrogen Peroxide 192-196 superoxide dismutase 1 Homo sapiens 28-32 34969852-3 2022 The mechanism involves Sod1-derived H2O2 oxidatively inactivating the glycolytic enzyme, GAPDH, which in turn reroutes carbohydrate flux to the oxidative phase of the pentose phosphate pathway (oxPPP) to generate NADPH. Hydrogen Peroxide 36-40 superoxide dismutase 1 Homo sapiens 23-27 34949154-5 2022 Our results exhibited that H2O2 treatment of A549 cells reduced the level of SOD and increased the level of ROS. Hydrogen Peroxide 27-31 superoxide dismutase 1 Homo sapiens 77-80 2760616-7 1989 Alternatively, increased SOD activity may induce cell death through the accumulation of hydrogen peroxide. Hydrogen Peroxide 88-105 superoxide dismutase 1 Homo sapiens 25-28 2722888-0 1989 The interaction between Cu(I) superoxide dismutase and hydrogen peroxide. Hydrogen Peroxide 55-72 superoxide dismutase 1 Homo sapiens 30-50 2703311-6 1989 The addition of superoxide dismutase (SOD) to the protein solution prior to photolysis increased the amount of H2O2 generated by 3- to 4-fold. Hydrogen Peroxide 111-115 superoxide dismutase 1 Homo sapiens 38-41 2596324-2 1989 Biochemical mechanisms of this free radical generation include: xanthine oxidase dependent O.- production, hydrogen peroxide (H2O2) formation by superoxide dismutase (SOD), hydroxyl radical (OH-) production via the Haber-Weiss reaction, and lipid radical formation from membrane peroxidation. Hydrogen Peroxide 107-124 superoxide dismutase 1 Homo sapiens 145-165 2492791-19 1989 At elevated concentrations of H2O2, a second nonaffinity mechanism of inactivation of both SODR143 and SODK143 was found, in which a second equivalent of H2O2 reacts with the Cu,ZnSOD.HO2- complex to give a competing second-order inactivation. Hydrogen Peroxide 30-34 superoxide dismutase 1 Homo sapiens 175-183 2492791-19 1989 At elevated concentrations of H2O2, a second nonaffinity mechanism of inactivation of both SODR143 and SODK143 was found, in which a second equivalent of H2O2 reacts with the Cu,ZnSOD.HO2- complex to give a competing second-order inactivation. Hydrogen Peroxide 154-158 superoxide dismutase 1 Homo sapiens 175-183 2596324-2 1989 Biochemical mechanisms of this free radical generation include: xanthine oxidase dependent O.- production, hydrogen peroxide (H2O2) formation by superoxide dismutase (SOD), hydroxyl radical (OH-) production via the Haber-Weiss reaction, and lipid radical formation from membrane peroxidation. Hydrogen Peroxide 126-130 superoxide dismutase 1 Homo sapiens 145-165 2596324-2 1989 Biochemical mechanisms of this free radical generation include: xanthine oxidase dependent O.- production, hydrogen peroxide (H2O2) formation by superoxide dismutase (SOD), hydroxyl radical (OH-) production via the Haber-Weiss reaction, and lipid radical formation from membrane peroxidation. Hydrogen Peroxide 126-130 superoxide dismutase 1 Homo sapiens 167-170 3191186-3 1988 Similar effect of the red light was also observed when SOD was inactivated with hydrogen peroxide: laser irradiation brought about the reduction of initial absorption spectrum of the enzyme. Hydrogen Peroxide 80-97 superoxide dismutase 1 Homo sapiens 55-58 2557982-17 1989 It is noteworthy that addition of SOD does not only result in a decrease in the amount of H2O2 formed during the regeneration of Mn3+, but, in fact, prevents H2O2 formation. Hydrogen Peroxide 90-94 superoxide dismutase 1 Homo sapiens 34-37 2557982-17 1989 It is noteworthy that addition of SOD does not only result in a decrease in the amount of H2O2 formed during the regeneration of Mn3+, but, in fact, prevents H2O2 formation. Hydrogen Peroxide 158-162 superoxide dismutase 1 Homo sapiens 34-37 2855027-1 1988 Like superoxide dismutase (SOD), human ceruloplasmin (Cp) scavenges superoxide anion radicals injected into the solution with the aid a high-voltage generator, hydrogen peroxide being the product of reaction. Hydrogen Peroxide 160-177 superoxide dismutase 1 Homo sapiens 5-25 2855027-1 1988 Like superoxide dismutase (SOD), human ceruloplasmin (Cp) scavenges superoxide anion radicals injected into the solution with the aid a high-voltage generator, hydrogen peroxide being the product of reaction. Hydrogen Peroxide 160-177 superoxide dismutase 1 Homo sapiens 27-30 3218146-3 1988 These data suggest that reduced NAD- and NADP-containing oxidoreductases alpha-GPD and G6PD are donors of H+ used in biosynthesis of H2O2 catalyzed by SOD. Hydrogen Peroxide 133-137 superoxide dismutase 1 Homo sapiens 151-154 2987038-4 1985 Since hydrogen peroxide and a ferric-EDTA chelate are themselves a hydroxyl radical-generating system, it follows that SOD must also protect against damage done by this reaction. Hydrogen Peroxide 6-23 superoxide dismutase 1 Homo sapiens 119-122 2843167-3 1988 The hydroxyl-radical formation enhanced by SOD was inhibited by catalase and desferrioxamine, and stimulated by EDTA and diethylenetriaminepenta-acetic acid, suggesting that both hydrogen peroxide and iron ions participate in the reaction. Hydrogen Peroxide 179-196 superoxide dismutase 1 Homo sapiens 43-46 2843167-7 1988 Secondly, the superoxide anions formed in the first step are dismuted by SOD to generate hydrogen peroxide and molecular oxygen, and hence the equilibrium in the first step is displaced in favour of the formation of superoxide anions. Hydrogen Peroxide 89-106 superoxide dismutase 1 Homo sapiens 73-76 2838554-4 1988 For detection of granulocyte activation the following assay systems were used: 1) lucigenin-dependent chemiluminescence (CL), 2) superoxide-dismutase (SOD) inhibitable cytochrome C-reduction (superoxide), 3) horseradish peroxidase-mediated oxidation of phenol red (hydrogen peroxide), 4) release of myeloperoxidase, 5) ultrastructural detection of hydrogen peroxide-production, and 6) scanning and transmission electron microscopy (SEM and TEM, respectively). Hydrogen Peroxide 265-282 superoxide dismutase 1 Homo sapiens 151-154 2838554-4 1988 For detection of granulocyte activation the following assay systems were used: 1) lucigenin-dependent chemiluminescence (CL), 2) superoxide-dismutase (SOD) inhibitable cytochrome C-reduction (superoxide), 3) horseradish peroxidase-mediated oxidation of phenol red (hydrogen peroxide), 4) release of myeloperoxidase, 5) ultrastructural detection of hydrogen peroxide-production, and 6) scanning and transmission electron microscopy (SEM and TEM, respectively). Hydrogen Peroxide 348-365 superoxide dismutase 1 Homo sapiens 151-154 2843172-10 1988 This inhibition is explained by myeloperoxidase undergoing a cycle of reactions with O2-, H2O2 and O2-, with compounds III and II as intermediates, i.e., by myeloperoxidase acting as a combined SOD/catalase enzyme. Hydrogen Peroxide 90-94 superoxide dismutase 1 Homo sapiens 194-197 2828775-7 1987 The superoxide radical-caused effect could be partially prevented by co-addition of superoxide dismutase (SOD) which dismutates O2- to H2O2 and O2. Hydrogen Peroxide 135-139 superoxide dismutase 1 Homo sapiens 84-104 2828775-7 1987 The superoxide radical-caused effect could be partially prevented by co-addition of superoxide dismutase (SOD) which dismutates O2- to H2O2 and O2. Hydrogen Peroxide 135-139 superoxide dismutase 1 Homo sapiens 106-109 2987038-5 1985 The ability of SOD to inhibit damage to deoxyribose caused by hydrogen peroxide and a ferric-EDTA chelate is experimentally demonstrated in this paper. Hydrogen Peroxide 62-79 superoxide dismutase 1 Homo sapiens 15-18 6466333-0 1984 Destruction of tryptophan residues by hydrogen peroxide in iron-superoxide dismutase. Hydrogen Peroxide 38-55 superoxide dismutase 1 Homo sapiens 64-84 6466333-1 1984 Reaction of H2O2 with iron containing superoxide dismutase (SOD) was studied by absorption spectroscopy, activity measurement and amino acid analysis. Hydrogen Peroxide 12-16 superoxide dismutase 1 Homo sapiens 38-58 6466333-1 1984 Reaction of H2O2 with iron containing superoxide dismutase (SOD) was studied by absorption spectroscopy, activity measurement and amino acid analysis. Hydrogen Peroxide 12-16 superoxide dismutase 1 Homo sapiens 60-63 33900756-2 2021 Nonheme iron enzymes, superoxide reductase (SOR) and superoxide dismutase (SOD), detoxify O2 - via reduction to afford H2O2 and disproportionation to afford O2 and H2O2, respectively. Hydrogen Peroxide 119-123 superoxide dismutase 1 Homo sapiens 53-73 6666195-9 1983 The enzyme superoxide dismutase (SOD) converts peroxide radicals (O-2) into hydrogen peroxide (H2O2) which can be inactivated by catalase or peroxidase. Hydrogen Peroxide 76-93 superoxide dismutase 1 Homo sapiens 33-36 6666195-9 1983 The enzyme superoxide dismutase (SOD) converts peroxide radicals (O-2) into hydrogen peroxide (H2O2) which can be inactivated by catalase or peroxidase. Hydrogen Peroxide 95-99 superoxide dismutase 1 Homo sapiens 33-36 6265012-0 1981 Inactivation of human CuZn superoxide dismutase during exposure to superoxide radical and hydrogen peroxide. Hydrogen Peroxide 90-107 superoxide dismutase 1 Homo sapiens 22-47 199619-4 1977 This inhibitory effect was reversed by the simultaneous addition of superoxide dismutase (SOD), whereas the addition of SOD alone increased the amount of detectable H(2)O(2) in the medium. Hydrogen Peroxide 165-173 superoxide dismutase 1 Homo sapiens 68-88 199619-4 1977 This inhibitory effect was reversed by the simultaneous addition of superoxide dismutase (SOD), whereas the addition of SOD alone increased the amount of detectable H(2)O(2) in the medium. Hydrogen Peroxide 165-173 superoxide dismutase 1 Homo sapiens 90-93 199619-4 1977 This inhibitory effect was reversed by the simultaneous addition of superoxide dismutase (SOD), whereas the addition of SOD alone increased the amount of detectable H(2)O(2) in the medium. Hydrogen Peroxide 165-173 superoxide dismutase 1 Homo sapiens 120-123 169293-2 1975 This was accomplished by allowing them to phagocytize latex particles coated with superoxide dismutase (SOD), which catalyzes the generation of H2O2 from O2. Hydrogen Peroxide 144-148 superoxide dismutase 1 Homo sapiens 82-102 169293-2 1975 This was accomplished by allowing them to phagocytize latex particles coated with superoxide dismutase (SOD), which catalyzes the generation of H2O2 from O2. Hydrogen Peroxide 144-148 superoxide dismutase 1 Homo sapiens 104-107 33901885-7 2021 Quantitative real-time PCR (qRT-PCR) and biochemical assays showed that HRW induced the transcripts and enzymatic activities of superoxide dismutase (SOD), ascorbate peroxidase (APX), and catalase (CAT) that metabolize reactive oxygen species (ROS); these increases coincided with the observed changes in O2.-, H2O2 and OH accumulation upon GA treatment. Hydrogen Peroxide 311-315 superoxide dismutase 1 Homo sapiens 128-148 6457303-5 1981 Rather, the elevation of GSHPxase in Down syndrome may represent an adaptive metabolic response to the increased hydrogen peroxide produced by the triplicated SOD-1 gene dose in trisomy 21. Hydrogen Peroxide 113-130 superoxide dismutase 1 Homo sapiens 159-164 225679-4 1979 The chemical and biological reactivity of superoxide is high and includes a leading role in bacterial killing caused by radiation, in which superoxide dismutase (SOD), an enzyme that catalyses the reaction: O2 + O2 +2H leads to H2O2 +O2 protected markedly. Hydrogen Peroxide 228-232 superoxide dismutase 1 Homo sapiens 140-160 225679-4 1979 The chemical and biological reactivity of superoxide is high and includes a leading role in bacterial killing caused by radiation, in which superoxide dismutase (SOD), an enzyme that catalyses the reaction: O2 + O2 +2H leads to H2O2 +O2 protected markedly. Hydrogen Peroxide 228-232 superoxide dismutase 1 Homo sapiens 162-165 421692-1 1979 Superoxide dismutase (SOD) and glutathione peroxidase (GPX) protect aerobic organisms against the toxic superoxide anion and hydrogen peroxide, which are generated during phagocytosis by polymorphonuclear leucocytes (PMNs). Hydrogen Peroxide 125-142 superoxide dismutase 1 Homo sapiens 0-20 421692-1 1979 Superoxide dismutase (SOD) and glutathione peroxidase (GPX) protect aerobic organisms against the toxic superoxide anion and hydrogen peroxide, which are generated during phagocytosis by polymorphonuclear leucocytes (PMNs). Hydrogen Peroxide 125-142 superoxide dismutase 1 Homo sapiens 22-25 421692-5 1979 Since SOD generates bactericidal hydrogen peroxide and regulates the release of the toxic superoxide radical into the surrounding tissues, this study may add new understanding to the pathophysiological aspects of acute and chronic inflammatory processes. Hydrogen Peroxide 33-50 superoxide dismutase 1 Homo sapiens 6-9 1228339-1 1975 Superoxide dismutase (SOD), widely distributed in aerobic organisms, catalyzes dismutation of the superoxide free radical, O2-, to oxygen and hydrogen peroxide and apparently protects against oxygen toxicity. Hydrogen Peroxide 142-159 superoxide dismutase 1 Homo sapiens 0-20 1228339-1 1975 Superoxide dismutase (SOD), widely distributed in aerobic organisms, catalyzes dismutation of the superoxide free radical, O2-, to oxygen and hydrogen peroxide and apparently protects against oxygen toxicity. Hydrogen Peroxide 142-159 superoxide dismutase 1 Homo sapiens 22-25 33900756-2 2021 Nonheme iron enzymes, superoxide reductase (SOR) and superoxide dismutase (SOD), detoxify O2 - via reduction to afford H2O2 and disproportionation to afford O2 and H2O2, respectively. Hydrogen Peroxide 119-123 superoxide dismutase 1 Homo sapiens 75-78 33900756-2 2021 Nonheme iron enzymes, superoxide reductase (SOR) and superoxide dismutase (SOD), detoxify O2 - via reduction to afford H2O2 and disproportionation to afford O2 and H2O2, respectively. Hydrogen Peroxide 164-168 superoxide dismutase 1 Homo sapiens 53-73 33900756-2 2021 Nonheme iron enzymes, superoxide reductase (SOR) and superoxide dismutase (SOD), detoxify O2 - via reduction to afford H2O2 and disproportionation to afford O2 and H2O2, respectively. Hydrogen Peroxide 164-168 superoxide dismutase 1 Homo sapiens 75-78 33923136-6 2021 CeO2NPs have been reported to act as a ROS and reactive nitrogen species (RNS) scavenger and to have multi-enzyme mimetic activity, including SOD activity (deprotionation of superoxide anion into oxygen and hydrogen peroxide), catalase activity (conversion of hydrogen peroxide into oxygen and water), and peroxidase activity (reducing hydrogen peroxide into hydroxyl radicals). Hydrogen Peroxide 260-277 superoxide dismutase 1 Homo sapiens 142-145 33923136-6 2021 CeO2NPs have been reported to act as a ROS and reactive nitrogen species (RNS) scavenger and to have multi-enzyme mimetic activity, including SOD activity (deprotionation of superoxide anion into oxygen and hydrogen peroxide), catalase activity (conversion of hydrogen peroxide into oxygen and water), and peroxidase activity (reducing hydrogen peroxide into hydroxyl radicals). Hydrogen Peroxide 260-277 superoxide dismutase 1 Homo sapiens 142-145 33511387-5 2021 The alleviated-tumor hypoxia can not only elevate H2O2 content via the Dox-activated cascade reaction of nicotinamide adenine dinucleotide phosphate (NADPH) oxidases (NOXs) and superoxide dismutase (SOD), but also improve the efficacy of Dox. Hydrogen Peroxide 50-54 superoxide dismutase 1 Homo sapiens 177-197 33838689-13 2021 Moreover, downregulation of SOD, NO, BCL2, and GAPDH, and upregulation of VEGFA, ET1, and PARP1 were discovered after cells were exposed to 0.5 mM H2O2 in this study, which could be improved by PARP1 inhibitor and SDMM capsule in a dose-dependent way, whereas worsened by PARP1 activation and GAPDH inhibitor. Hydrogen Peroxide 147-151 superoxide dismutase 1 Homo sapiens 28-31 33511387-5 2021 The alleviated-tumor hypoxia can not only elevate H2O2 content via the Dox-activated cascade reaction of nicotinamide adenine dinucleotide phosphate (NADPH) oxidases (NOXs) and superoxide dismutase (SOD), but also improve the efficacy of Dox. Hydrogen Peroxide 50-54 superoxide dismutase 1 Homo sapiens 199-202 33548866-16 2021 In terms of SOD content and apoptotic rate, the SOD level showed the opposite trend compared with H2O2 group. Hydrogen Peroxide 98-102 superoxide dismutase 1 Homo sapiens 48-51 33271327-6 2021 HuD regulation of SOD1 mRNA was also found to be oxidative stress (OS)-dependent, as shown by the increased HuD binding and upregulation of this mRNA after H2O2 exposure. Hydrogen Peroxide 156-160 superoxide dismutase 1 Homo sapiens 18-22 33218686-1 2021 Cu/Zn Superoxide Dismutase (Sod1) catalyzes the disproportionation of cytotoxic superoxide radicals (O2 -) into oxygen (O2) and hydrogen peroxide (H2O2), a key signaling molecule. Hydrogen Peroxide 128-145 superoxide dismutase 1 Homo sapiens 0-26 33218686-1 2021 Cu/Zn Superoxide Dismutase (Sod1) catalyzes the disproportionation of cytotoxic superoxide radicals (O2 -) into oxygen (O2) and hydrogen peroxide (H2O2), a key signaling molecule. Hydrogen Peroxide 128-145 superoxide dismutase 1 Homo sapiens 28-32 33218686-1 2021 Cu/Zn Superoxide Dismutase (Sod1) catalyzes the disproportionation of cytotoxic superoxide radicals (O2 -) into oxygen (O2) and hydrogen peroxide (H2O2), a key signaling molecule. Hydrogen Peroxide 147-151 superoxide dismutase 1 Homo sapiens 0-26 33218686-1 2021 Cu/Zn Superoxide Dismutase (Sod1) catalyzes the disproportionation of cytotoxic superoxide radicals (O2 -) into oxygen (O2) and hydrogen peroxide (H2O2), a key signaling molecule. Hydrogen Peroxide 147-151 superoxide dismutase 1 Homo sapiens 28-32 33259795-2 2021 To combat this threat, the cell employs the enzyme Cu/Zn Superoxide Dismutase (SOD1), which can convert the radical superoxide into molecular oxygen and hydrogen peroxide, through redox reactions. Hydrogen Peroxide 153-170 superoxide dismutase 1 Homo sapiens 51-77 33259795-2 2021 To combat this threat, the cell employs the enzyme Cu/Zn Superoxide Dismutase (SOD1), which can convert the radical superoxide into molecular oxygen and hydrogen peroxide, through redox reactions. Hydrogen Peroxide 153-170 superoxide dismutase 1 Homo sapiens 79-83 33161248-6 2020 Additionally, 14q decreased the apoptotic percentage of HepG2 cells, reduced the ROS produce and LDH release, and improved GSH and SOD levels in H2O2-treated HepG2 cells. Hydrogen Peroxide 145-149 superoxide dismutase 1 Homo sapiens 131-134 33297791-6 2021 Results: H2O2 induced oxidative damage in SRA01/04 cells by inhibiting the activity of SOD and CAT and reducing total GSH levels. Hydrogen Peroxide 9-13 superoxide dismutase 1 Homo sapiens 87-90 33297791-7 2021 Treatment of SRA01/04 cells with NR significantly increased cell viability and reduced cell apoptosis and ROS generation, whereas SOD and CAT activities and total GSH and MMP levels were improved by the NR treatment in an H2O2-exposed cell model. Hydrogen Peroxide 222-226 superoxide dismutase 1 Homo sapiens 130-133 32780285-8 2020 C3G interference memorably and dose-dependently inhibited H2O2-induced intracellular ROS and MDA overproduction, while C3G treatment markedly increased H2O2-induced the activities of intracellular SOD, GSH-Px and CAT. Hydrogen Peroxide 152-156 superoxide dismutase 1 Homo sapiens 197-200 33173962-11 2020 H2O2-mediated increases in MDA, proinflammatory cytokine and endothelial cell adhesion factor levels were decreased by Mtp treatment, whereas Mtp reversed H2O2-mediated downregulation of SOD and GSH-Px activity. Hydrogen Peroxide 0-4 superoxide dismutase 1 Homo sapiens 187-190 33173962-11 2020 H2O2-mediated increases in MDA, proinflammatory cytokine and endothelial cell adhesion factor levels were decreased by Mtp treatment, whereas Mtp reversed H2O2-mediated downregulation of SOD and GSH-Px activity. Hydrogen Peroxide 155-159 superoxide dismutase 1 Homo sapiens 187-190 33256538-13 2022 Aloperine greatly decreased the production of ROS and MDA, and increased the activities of SOD and GSH-PX in H2O2-stimulated ARPE-19 cells. Hydrogen Peroxide 109-113 superoxide dismutase 1 Homo sapiens 91-94 32758663-6 2020 Melatonin relieved H2O2-induced oxidative stress by significantly reducing intracellular ROS, MDA and 8-OHdG levels and increasing SOD and GSH-Px activities. Hydrogen Peroxide 19-23 superoxide dismutase 1 Homo sapiens 131-134 32774685-6 2020 Additionally, H2O2 at 1 mM significantly decreased the mRNA expression levels of Nrf2, CAT, SOD1, SOD2, HO-1, GST-pi, NQO1, and GLCM in ARPE-19 cells; however, treatment with EE-TT reversed the downregulated mRNA expression levels of all these genes induced by H2O2. Hydrogen Peroxide 14-18 superoxide dismutase 1 Homo sapiens 92-96 33000859-8 2020 The reduced glutathione (GSH) level and superoxide dismutase (SOD) activity in H2O2-induced ARPE-19 cells were elevated after MADE treatment. Hydrogen Peroxide 79-83 superoxide dismutase 1 Homo sapiens 40-60 33000859-8 2020 The reduced glutathione (GSH) level and superoxide dismutase (SOD) activity in H2O2-induced ARPE-19 cells were elevated after MADE treatment. Hydrogen Peroxide 79-83 superoxide dismutase 1 Homo sapiens 62-65 32955857-3 2020 Mechanistic studies show that the catalysis consists of a three-step reaction: the oxidation of NADPH to produce O2- via oxidase-like activity, the subsequent dismutation of O2- to H2O2 via SOD-like activity, followed by H2O2-mediated oxidation of L-arginine to produce NO via a non-enzymatic pathway. Hydrogen Peroxide 181-185 superoxide dismutase 1 Homo sapiens 190-193 32955857-3 2020 Mechanistic studies show that the catalysis consists of a three-step reaction: the oxidation of NADPH to produce O2- via oxidase-like activity, the subsequent dismutation of O2- to H2O2 via SOD-like activity, followed by H2O2-mediated oxidation of L-arginine to produce NO via a non-enzymatic pathway. Hydrogen Peroxide 221-225 superoxide dismutase 1 Homo sapiens 190-193 32993995-10 2020 The antioxidative properties of PLGA-nanoceria-SOD particles were verified by adding H2O2 to cell culture and imaging with fluorescent markers of oxidative stress. Hydrogen Peroxide 85-89 superoxide dismutase 1 Homo sapiens 47-50 33120873-2 2020 They are closely interconnected in the catabolism of reactive oxygen species because one product of SOD reaction (hydrogen peroxide) is the main substrate of CAT reaction finally leading to harmless products (i.e., molecular oxygen and water). Hydrogen Peroxide 114-131 superoxide dismutase 1 Homo sapiens 100-103 32439943-5 2020 Furthermore, the ERPHs effectively suppressed H2O2-induced ROS production and lipid peroxidation and increased the protein expression levels of the intracellular antioxidant enzymes SOD, GSH-Px and CAT in H2O2-stressed HepG-2 cells. Hydrogen Peroxide 205-209 superoxide dismutase 1 Homo sapiens 182-185 32483451-7 2020 The released SOD-Fe0 and Lapa were further endocytosed by tumor cells and the Lapa produces superoxide anion (O2 - ) through the catalysis of NQO1 that is overexpressed in tumor cells, while O2 - is converted to H2O2 via SOD. Hydrogen Peroxide 213-217 superoxide dismutase 1 Homo sapiens 13-20 32483451-7 2020 The released SOD-Fe0 and Lapa were further endocytosed by tumor cells and the Lapa produces superoxide anion (O2 - ) through the catalysis of NQO1 that is overexpressed in tumor cells, while O2 - is converted to H2O2 via SOD. Hydrogen Peroxide 213-217 superoxide dismutase 1 Homo sapiens 13-16 32335580-7 2020 Treatment of the H2O2-stressed epithelial cells with myricetin caused significant (P<0.05) increased levels of SOD, CAT, and GSH. Hydrogen Peroxide 17-21 superoxide dismutase 1 Homo sapiens 111-114 32191862-1 2020 The folding reaction of a stable monomeric variant of Cu/Zn superoxide dismutase (mSOD1), an enzyme responsible for the conversion of superoxide free radicals into hydrogen peroxide and oxygen, is known to be among the slowest folding processes that adhere to two-state behavior. Hydrogen Peroxide 164-181 superoxide dismutase 1 Homo sapiens 54-80 31579960-3 2020 Further analysis evidenced that Genistein enhanced the activities of antioxidant enzymes superoxide dismutase (SOD), GSH-peroxidase (GSH-Px), and catalase (CAT) in H2 O2 -treated GCs, but this enhancement was attenuated by H89. Hydrogen Peroxide 164-169 superoxide dismutase 1 Homo sapiens 89-109 32023550-6 2020 In Dex- and H2O2-treated MG63 cells, AU also enhanced the expression of anti-oxidative stress-associated factors in the nuclear respiratory factor 2 signaling pathway, including superoxide dismutases 1 and 2, heme oxygenases 1 and 2, and catalase. Hydrogen Peroxide 12-16 superoxide dismutase 1 Homo sapiens 178-232 32016568-6 2020 In the sensing process, SOD and CuInZnS QDs on a glassy carbon electrode (GCE) competed with each other for hydrogen peroxide to produce superoxide during electrochemical luminescence, thus quenching the ECL signal of CuInZnS QDs. Hydrogen Peroxide 108-125 superoxide dismutase 1 Homo sapiens 24-27 31579960-3 2020 Further analysis evidenced that Genistein enhanced the activities of antioxidant enzymes superoxide dismutase (SOD), GSH-peroxidase (GSH-Px), and catalase (CAT) in H2 O2 -treated GCs, but this enhancement was attenuated by H89. Hydrogen Peroxide 164-169 superoxide dismutase 1 Homo sapiens 111-114 31863908-4 2020 Here, we show that a thiol group of Cys111 in SOD1 is oxidized to a sulfenic acid with hydrogen peroxide and reveal that further dissociation of the bound metal ions from the oxidized SOD1 allows another free Cys residue (Cys6) to nucleophilically attack the sulfenylated Cys111. Hydrogen Peroxide 87-104 superoxide dismutase 1 Homo sapiens 46-50 31863908-4 2020 Here, we show that a thiol group of Cys111 in SOD1 is oxidized to a sulfenic acid with hydrogen peroxide and reveal that further dissociation of the bound metal ions from the oxidized SOD1 allows another free Cys residue (Cys6) to nucleophilically attack the sulfenylated Cys111. Hydrogen Peroxide 87-104 superoxide dismutase 1 Homo sapiens 184-188 30890424-8 2019 In contrast, the H2O2 + 100 mumol/L ICA and H2O2 + 100 mumol/L ICA + DTT groups had significant inhibitory effects on the expressions of GRP78, ATF4 and eIF2alpha proteins, showing enhanced cell viability and SOD and GSH-Px activity. Hydrogen Peroxide 17-21 superoxide dismutase 1 Homo sapiens 209-212 32323267-3 2020 H2O2 is generated by superoxide dismutase (SOD)-mediated conversion of superoxide produced by membrane-localized NADPH oxidases (NOXes). Hydrogen Peroxide 0-4 superoxide dismutase 1 Homo sapiens 21-41 32323267-3 2020 H2O2 is generated by superoxide dismutase (SOD)-mediated conversion of superoxide produced by membrane-localized NADPH oxidases (NOXes). Hydrogen Peroxide 0-4 superoxide dismutase 1 Homo sapiens 43-46 30839137-9 2019 We found that H2 O2 could significantly induce the apoptosis of NSCs, increase LDH, MDA levels, and decrease SOD activity by activating the Notch1 signaling pathway. Hydrogen Peroxide 14-19 superoxide dismutase 1 Homo sapiens 109-112 31692944-11 2019 GSH, glutathione peroxidase (Gpx), and superoxide dismutase (SOD) neutralize H2O2-induced oxidative damage in mitochondria. Hydrogen Peroxide 77-81 superoxide dismutase 1 Homo sapiens 39-59 31692944-11 2019 GSH, glutathione peroxidase (Gpx), and superoxide dismutase (SOD) neutralize H2O2-induced oxidative damage in mitochondria. Hydrogen Peroxide 77-81 superoxide dismutase 1 Homo sapiens 61-64 31258517-4 2019 After host cell invasion, mycobacteria induces the expression of NADPH oxidase 2 (NOX2) to generate superoxide radicals ( O 2 - ), which are then converted to more toxic hydrogen peroxide (H2O2) by superoxide dismutase (SOD) and subsequently reduced to water by catalase. Hydrogen Peroxide 173-190 superoxide dismutase 1 Homo sapiens 201-221 31258517-4 2019 After host cell invasion, mycobacteria induces the expression of NADPH oxidase 2 (NOX2) to generate superoxide radicals ( O 2 - ), which are then converted to more toxic hydrogen peroxide (H2O2) by superoxide dismutase (SOD) and subsequently reduced to water by catalase. Hydrogen Peroxide 173-190 superoxide dismutase 1 Homo sapiens 223-226 31258517-4 2019 After host cell invasion, mycobacteria induces the expression of NADPH oxidase 2 (NOX2) to generate superoxide radicals ( O 2 - ), which are then converted to more toxic hydrogen peroxide (H2O2) by superoxide dismutase (SOD) and subsequently reduced to water by catalase. Hydrogen Peroxide 192-196 superoxide dismutase 1 Homo sapiens 201-221 31258517-4 2019 After host cell invasion, mycobacteria induces the expression of NADPH oxidase 2 (NOX2) to generate superoxide radicals ( O 2 - ), which are then converted to more toxic hydrogen peroxide (H2O2) by superoxide dismutase (SOD) and subsequently reduced to water by catalase. Hydrogen Peroxide 192-196 superoxide dismutase 1 Homo sapiens 223-226 31724066-3 2020 The superoxide dismutase (SOD), an antioxidant enzyme, plays an essential pathogenic role in the inflammatory diseases by not only catalyzing the conversion of the superoxide to hydrogen peroxide and oxygen but also affecting immune responses. Hydrogen Peroxide 178-195 superoxide dismutase 1 Homo sapiens 4-24 31724066-3 2020 The superoxide dismutase (SOD), an antioxidant enzyme, plays an essential pathogenic role in the inflammatory diseases by not only catalyzing the conversion of the superoxide to hydrogen peroxide and oxygen but also affecting immune responses. Hydrogen Peroxide 178-195 superoxide dismutase 1 Homo sapiens 26-29 31273612-7 2019 In antioxidant defence system, the superoxide dismutase (SOD) family is a first line antioxidant enzyme group involved in catalysing reactive oxygen species (ROS) to hydrogen peroxide and molecular oxygen. Hydrogen Peroxide 166-183 superoxide dismutase 1 Homo sapiens 35-55 31273612-7 2019 In antioxidant defence system, the superoxide dismutase (SOD) family is a first line antioxidant enzyme group involved in catalysing reactive oxygen species (ROS) to hydrogen peroxide and molecular oxygen. Hydrogen Peroxide 166-183 superoxide dismutase 1 Homo sapiens 57-60 31346243-0 2019 Cu/Zn-superoxide dismutase and wild-type like fALS SOD1 mutants produce cytotoxic quantities of H2O2 via cysteine-dependent redox short-circuit. Hydrogen Peroxide 96-100 superoxide dismutase 1 Homo sapiens 51-55 31346243-1 2019 The Cu/Zn-superoxide dismutase (SOD1) is a ubiquitous enzyme that catalyzes the dismutation of superoxide radicals to oxygen and hydrogen peroxide. Hydrogen Peroxide 129-146 superoxide dismutase 1 Homo sapiens 32-36 31346243-5 2019 Here, we demonstrated that metal-saturated SOD1WT (holo-SOD1WT) and a familial ALS (fALS) catalytically active SOD1 mutant, SOD1G93A, are capable, under defined metabolic circumstances, to generate cytotoxic quantities of H2O2 through cysteine (CSH)/glutathione (GSH) redox short-circuit. Hydrogen Peroxide 222-226 superoxide dismutase 1 Homo sapiens 43-47 30890424-7 2019 ERS activators H2O2 and dl-dithiothreitol (DTT) significantly increased GRP78, ATF4 and eIF2alpha expressions, decreased cell activity and reduced SOD and GSH-Px activity. Hydrogen Peroxide 15-19 superoxide dismutase 1 Homo sapiens 147-150 30890424-8 2019 In contrast, the H2O2 + 100 mumol/L ICA and H2O2 + 100 mumol/L ICA + DTT groups had significant inhibitory effects on the expressions of GRP78, ATF4 and eIF2alpha proteins, showing enhanced cell viability and SOD and GSH-Px activity. Hydrogen Peroxide 44-48 superoxide dismutase 1 Homo sapiens 209-212 30502329-8 2019 Furthermore, under H2O2-induced oxidative stress, M2G down-regulated Sod1, Cat, and Nrf2 expression. Hydrogen Peroxide 19-23 superoxide dismutase 1 Homo sapiens 69-73 30911355-1 2019 Multiple signaling pathways including ERK, PI3K-Akt, and NF-kappaB, which are essential for onset and development of cancer, can be activated by intracellularly sustained high levels of H2O2 provided by elevated activity and expression of copper/zinc superoxide dismutase (SOD1) that catalyzes the dismutation of O2 - into H2O2. Hydrogen Peroxide 186-190 superoxide dismutase 1 Homo sapiens 273-277 30911355-1 2019 Multiple signaling pathways including ERK, PI3K-Akt, and NF-kappaB, which are essential for onset and development of cancer, can be activated by intracellularly sustained high levels of H2O2 provided by elevated activity and expression of copper/zinc superoxide dismutase (SOD1) that catalyzes the dismutation of O2 - into H2O2. Hydrogen Peroxide 324-328 superoxide dismutase 1 Homo sapiens 273-277 30584457-6 2018 Kaempferol also inhibits the upregulated vascular endothelial growth factor (VEGF) mRNA expression levels induced by H2O2 in ARPE-19 cells and affects the oxidation and antioxidant imbalanced system in ARPE-19 cells treated by H2O2 through the regulations of both the activities of reactive oxygen species (ROS) and superoxide dismutase (SOD). Hydrogen Peroxide 117-121 superoxide dismutase 1 Homo sapiens 316-336 30680088-10 2019 Scutellarin alleviated the H2O2-induced oxidative stress in ARPE-19 cells, which was illustrated by reduced levels of ROS and MDA, accompanied by increased SOD activity and GSH level. Hydrogen Peroxide 27-31 superoxide dismutase 1 Homo sapiens 156-159 30262281-7 2018 Furthermore, downregulation of CAT mRNA and SOD1 and PRX2 proteins induced by H2O2, was minimal after the Na2SeO3+H2O2 treatment. Hydrogen Peroxide 78-82 superoxide dismutase 1 Homo sapiens 44-48 30262281-7 2018 Furthermore, downregulation of CAT mRNA and SOD1 and PRX2 proteins induced by H2O2, was minimal after the Na2SeO3+H2O2 treatment. Hydrogen Peroxide 114-118 superoxide dismutase 1 Homo sapiens 44-48 30584457-6 2018 Kaempferol also inhibits the upregulated vascular endothelial growth factor (VEGF) mRNA expression levels induced by H2O2 in ARPE-19 cells and affects the oxidation and antioxidant imbalanced system in ARPE-19 cells treated by H2O2 through the regulations of both the activities of reactive oxygen species (ROS) and superoxide dismutase (SOD). Hydrogen Peroxide 117-121 superoxide dismutase 1 Homo sapiens 338-341 29860626-2 2018 We demonstrated that H2O2 decreases PDLSC viability by 40 and 50% with the concentrations of 400 and 500 muM, respectively, with an observed downregulation of Pellino-1 mRNA and protein; we further concluded that overexpression of Pellino-1 significantly lowers 8-hydroxy-2"-deoxyguanosine levels by 10% and upregulates superoxide dismutase 1, glutathione peroxidase levels, and catalase mRNA levels by 200, 40, and 250%, respectively. Hydrogen Peroxide 21-25 superoxide dismutase 1 Homo sapiens 320-342 30350732-0 2018 Light-induced intracellular hydrogen peroxide generation through genetically encoded photosensitizer KillerRed-SOD1. Hydrogen Peroxide 28-45 superoxide dismutase 1 Homo sapiens 111-115 30350732-3 2018 To analyse the effects of H2O2 and its diffusion within the cell we developed the new genetically encoded photosensitizer KillerRed-SOD1 which enables a light-induced spatially and temporally controlled generation of H2O2 in living cells. Hydrogen Peroxide 26-30 superoxide dismutase 1 Homo sapiens 132-136 30350732-3 2018 To analyse the effects of H2O2 and its diffusion within the cell we developed the new genetically encoded photosensitizer KillerRed-SOD1 which enables a light-induced spatially and temporally controlled generation of H2O2 in living cells. Hydrogen Peroxide 217-221 superoxide dismutase 1 Homo sapiens 132-136 30350732-5 2018 Light irradiation at a wavelength of 560 nm induced superoxide radical formation at the KR domain which was transformed to H2O2 at the SOD1 domain. Hydrogen Peroxide 123-127 superoxide dismutase 1 Homo sapiens 135-139 30350732-8 2018 Herein, it was exemplarily shown that the peroxisomal targeting sequence 1 directed the photosensitizer KR-SOD1 to the peroxisomes and enabled H2O2 formation specifically in these organelles. Hydrogen Peroxide 143-147 superoxide dismutase 1 Homo sapiens 107-111 30350732-9 2018 In summary, with the photosensitizer KR-SOD1 a new valuable tool was established which allows a controlled intracellular H2O2 generation for the analysis of H2O2 effects on a subcellular level. Hydrogen Peroxide 121-125 superoxide dismutase 1 Homo sapiens 40-44 30350732-9 2018 In summary, with the photosensitizer KR-SOD1 a new valuable tool was established which allows a controlled intracellular H2O2 generation for the analysis of H2O2 effects on a subcellular level. Hydrogen Peroxide 157-161 superoxide dismutase 1 Homo sapiens 40-44 29845280-9 2018 Pretreatment of A549 cells with H2O2 prior to RSV infection upregulated the mRNA and protein expression of TLR3 and NF-kappaB, and downregulated the mRNA expression of IRF3 and SOD1, as well as the total SOD activity. Hydrogen Peroxide 32-36 superoxide dismutase 1 Homo sapiens 177-181 29845280-9 2018 Pretreatment of A549 cells with H2O2 prior to RSV infection upregulated the mRNA and protein expression of TLR3 and NF-kappaB, and downregulated the mRNA expression of IRF3 and SOD1, as well as the total SOD activity. Hydrogen Peroxide 32-36 superoxide dismutase 1 Homo sapiens 177-180 30459328-7 2018 Hydrogen peroxide outclassed all the other regulators in increasing leaf SOD, CAT activity, chlorophyll contents, net photosynthetic rate, number of sympodial branches, boll weight and fiber quality components. Hydrogen Peroxide 0-17 superoxide dismutase 1 Homo sapiens 73-76 29648877-15 2018 We identify that, in liver tissue from ALF patients and mice models, manganese-dependent SOD was overexpressed, and show lipopolysaccharide/H2O2 inhibits mitophagy via reactive oxygen species in hepatic stellate cells (HSCs). Hydrogen Peroxide 140-144 superoxide dismutase 1 Homo sapiens 89-92 29953407-2 2018 Superoxide dismutase (SOD) is the first line of defense against reactive oxygen species (ROS), eliminating the strong superoxide radical and producing H2O2, which can then be degraded by catalase (CAT). Hydrogen Peroxide 151-155 superoxide dismutase 1 Homo sapiens 0-20 29953407-2 2018 Superoxide dismutase (SOD) is the first line of defense against reactive oxygen species (ROS), eliminating the strong superoxide radical and producing H2O2, which can then be degraded by catalase (CAT). Hydrogen Peroxide 151-155 superoxide dismutase 1 Homo sapiens 22-25 29842900-7 2018 Evidences showed that the mutant hSOD1 resulted in the increased oxidative stress, abnormal antioxidant signaling and pathological behaviors in motor performance and survival compared with non-mutant hSOD1 models, treatment with LA improved motor activity and survival in transgenic flies, prevented NSC34 cells from mutant hSOD1 or H2O2 induced decreased antioxidant enzymes as well as increased ROS levels. Hydrogen Peroxide 333-337 superoxide dismutase 1 Homo sapiens 33-38 28986302-6 2018 The mRNA levels of Nrf2, catalase, superoxide dismutase 1 (SOD1), and 8-Oxoguanine DNA glycosylase (OGG1) were elevated by H2O2, and DMF treatment showed similar but pronounced effects through activation of Nrf2. Hydrogen Peroxide 123-127 superoxide dismutase 1 Homo sapiens 35-57 28986302-6 2018 The mRNA levels of Nrf2, catalase, superoxide dismutase 1 (SOD1), and 8-Oxoguanine DNA glycosylase (OGG1) were elevated by H2O2, and DMF treatment showed similar but pronounced effects through activation of Nrf2. Hydrogen Peroxide 123-127 superoxide dismutase 1 Homo sapiens 59-63 29410551-7 2018 Furthermore, there was 149-221% increase in hydrogen peroxide (H<sub>2</sub>O<sub>2</sub>) concentration, and 26-38% increase in SOD activity in the case of workers compared to the control group. Hydrogen Peroxide 44-61 superoxide dismutase 1 Homo sapiens 153-156 29512729-3 2018 Our recent study demonstrated that superoxide dismutase (SOD)-dependent production of hydrogen peroxide (H2O2) promoted the invasive and migratory activity of pancreatic cancer cells. Hydrogen Peroxide 86-103 superoxide dismutase 1 Homo sapiens 35-55 29512729-3 2018 Our recent study demonstrated that superoxide dismutase (SOD)-dependent production of hydrogen peroxide (H2O2) promoted the invasive and migratory activity of pancreatic cancer cells. Hydrogen Peroxide 86-103 superoxide dismutase 1 Homo sapiens 57-60 29512729-3 2018 Our recent study demonstrated that superoxide dismutase (SOD)-dependent production of hydrogen peroxide (H2O2) promoted the invasive and migratory activity of pancreatic cancer cells. Hydrogen Peroxide 105-109 superoxide dismutase 1 Homo sapiens 35-55 29512729-3 2018 Our recent study demonstrated that superoxide dismutase (SOD)-dependent production of hydrogen peroxide (H2O2) promoted the invasive and migratory activity of pancreatic cancer cells. Hydrogen Peroxide 105-109 superoxide dismutase 1 Homo sapiens 57-60 29512729-11 2018 The findings of the present study demonstrated that curcumin decreased SOD-induced production of ROS and H2O2 in BxPC-3 and Panc-1 cells. Hydrogen Peroxide 105-109 superoxide dismutase 1 Homo sapiens 71-74 29512729-15 2018 To summarize, these results demonstrated that curcumin was able to prevent SOD-driven H2O2-induced pancreatic cancer metastasis by blocking the PI3K/Akt/NF-kappaB signaling pathway. Hydrogen Peroxide 86-90 superoxide dismutase 1 Homo sapiens 75-78 29725495-4 2018 The 24 h ORY exposure significantly prevented hydrogen peroxide- (H2O2-) induced ROS/RNS production at 3 h, and this effect was sustained for at least 24 h. ORY pretreatment also enhanced the activity of antioxidant enzymes: superoxide dismutase (SOD) and glutathione peroxidase (GPX). Hydrogen Peroxide 46-63 superoxide dismutase 1 Homo sapiens 225-245 29220697-10 2018 These experiments suggest that, unlike the well-known SOD-mediated dismutation of two O2 - to form H2O2 and O2, SOD catalyzes a reaction using H2S and O2 to form persulfide. Hydrogen Peroxide 99-103 superoxide dismutase 1 Homo sapiens 54-57 29220697-10 2018 These experiments suggest that, unlike the well-known SOD-mediated dismutation of two O2 - to form H2O2 and O2, SOD catalyzes a reaction using H2S and O2 to form persulfide. Hydrogen Peroxide 99-103 superoxide dismutase 1 Homo sapiens 112-115 29702613-6 2018 Lipophilic electrophiles rapidly bind to SOD1 and induce stable and functionally active dimers, which produce excess hydrogen peroxide leading to aberrant cell signalling. Hydrogen Peroxide 117-134 superoxide dismutase 1 Homo sapiens 41-45 29725495-4 2018 The 24 h ORY exposure significantly prevented hydrogen peroxide- (H2O2-) induced ROS/RNS production at 3 h, and this effect was sustained for at least 24 h. ORY pretreatment also enhanced the activity of antioxidant enzymes: superoxide dismutase (SOD) and glutathione peroxidase (GPX). Hydrogen Peroxide 46-63 superoxide dismutase 1 Homo sapiens 247-250 29725495-4 2018 The 24 h ORY exposure significantly prevented hydrogen peroxide- (H2O2-) induced ROS/RNS production at 3 h, and this effect was sustained for at least 24 h. ORY pretreatment also enhanced the activity of antioxidant enzymes: superoxide dismutase (SOD) and glutathione peroxidase (GPX). Hydrogen Peroxide 66-70 superoxide dismutase 1 Homo sapiens 225-245 29725495-4 2018 The 24 h ORY exposure significantly prevented hydrogen peroxide- (H2O2-) induced ROS/RNS production at 3 h, and this effect was sustained for at least 24 h. ORY pretreatment also enhanced the activity of antioxidant enzymes: superoxide dismutase (SOD) and glutathione peroxidase (GPX). Hydrogen Peroxide 66-70 superoxide dismutase 1 Homo sapiens 247-250 29351198-0 2018 Superoxide Dismutase Mimetic GC4419 Enhances the Oxidation of Pharmacological Ascorbate and Its Anticancer Effects in an H2O2-Dependent Manner. Hydrogen Peroxide 121-125 superoxide dismutase 1 Homo sapiens 0-20 29358575-0 2018 Pathological hydrogen peroxide triggers the fibrillization of wild-type SOD1 via sulfenic acid modification of Cys-111. Hydrogen Peroxide 13-30 superoxide dismutase 1 Homo sapiens 72-76 29358575-2 2018 However, how SOD1-catalyzed reaction product hydrogen peroxide affects amyloid formation of SOD1 and TDP-43 remains elusory. Hydrogen Peroxide 45-62 superoxide dismutase 1 Homo sapiens 13-17 29358575-2 2018 However, how SOD1-catalyzed reaction product hydrogen peroxide affects amyloid formation of SOD1 and TDP-43 remains elusory. Hydrogen Peroxide 45-62 superoxide dismutase 1 Homo sapiens 92-96 29358575-4 2018 In this paper, we demonstrate that H2O2 at pathological concentrations triggers the fibrillization of wild-type SOD1 both in vitro and in SH-SY5Y cells. Hydrogen Peroxide 35-39 superoxide dismutase 1 Homo sapiens 112-116 29351198-5 2018 The current study demonstrates that the Mn(II)-containing pentaazamacrocyclic selective SOD mimetic GC4419 may serve as an AscH-/O2 - oxidoreductase as evidenced by the increased rate of oxygen consumption, steady-state concentrations of ascorbate radical, and H2O2 production in complete cell culture media. Hydrogen Peroxide 261-265 superoxide dismutase 1 Homo sapiens 88-91 28603086-4 2017 SOD catalyzes the dismutation of the superoxide anion (O2 -) to oxygen (O2) and hydrogen peroxide (H2O2). Hydrogen Peroxide 80-97 superoxide dismutase 1 Homo sapiens 0-3 29351198-7 2018 This enhanced cancer cell killing was dependent upon the catalytic activity of the SOD mimetic and the generation of H2O2, as determined using conditional overexpression of catalase in H1299T cells. Hydrogen Peroxide 117-121 superoxide dismutase 1 Homo sapiens 83-86 29851012-6 2018 Superoxide dismutase (MnSOD, SOD2) from the mitochondrial matrix, as well as superoxide dismutase (Cu/ZnSOD, SOD1) present in small amounts in the mitochondrial intramembrane space, converts superoxide anion to hydrogen peroxide, which can be then converted by catalase to harmless H2O.In the chapter we describe a relation between mitochondrial membrane potential and the rate of ROS formation. Hydrogen Peroxide 211-228 superoxide dismutase 1 Homo sapiens 109-113 29358575-5 2018 Using an anti-dimedone antibody that detects sulfenic acid modification of proteins, we found that Cys-111 in wild-type SOD1 is oxidized to C-SOH by pathological concentration of H2O2, followed by the formation of sulfenic acid modified SOD1 oligomers. Hydrogen Peroxide 179-183 superoxide dismutase 1 Homo sapiens 120-124 29358575-7 2018 Thus, we propose that H2O2 at pathological concentrations triggers the fibrillization of wild-type SOD1 and subsequently induces SOD1 toxicity and TDP-43 toxicity in neuronal cells via sulfenic acid modification of Cys-111 in SOD1. Hydrogen Peroxide 22-26 superoxide dismutase 1 Homo sapiens 99-103 29358575-7 2018 Thus, we propose that H2O2 at pathological concentrations triggers the fibrillization of wild-type SOD1 and subsequently induces SOD1 toxicity and TDP-43 toxicity in neuronal cells via sulfenic acid modification of Cys-111 in SOD1. Hydrogen Peroxide 22-26 superoxide dismutase 1 Homo sapiens 129-133 29358575-7 2018 Thus, we propose that H2O2 at pathological concentrations triggers the fibrillization of wild-type SOD1 and subsequently induces SOD1 toxicity and TDP-43 toxicity in neuronal cells via sulfenic acid modification of Cys-111 in SOD1. Hydrogen Peroxide 22-26 superoxide dismutase 1 Homo sapiens 129-133 29358575-9 2018 These findings can explain how H2O2 at pathologic concentrations regulates the misfolding and toxicity of SOD1 and TDP-43 associated with ALS, and suggest that sulfenic acid modification of wild-type SOD1 should play pivotal roles in the pathogenesis of sporadic ALS. Hydrogen Peroxide 31-35 superoxide dismutase 1 Homo sapiens 106-110 29358575-9 2018 These findings can explain how H2O2 at pathologic concentrations regulates the misfolding and toxicity of SOD1 and TDP-43 associated with ALS, and suggest that sulfenic acid modification of wild-type SOD1 should play pivotal roles in the pathogenesis of sporadic ALS. Hydrogen Peroxide 31-35 superoxide dismutase 1 Homo sapiens 200-204 29850654-1 2018 Superoxide dismutase 1 (SOD1) is a metalloenzyme that catalyzes the disproportionation of superoxide into molecular oxygen and hydrogen peroxide. Hydrogen Peroxide 127-144 superoxide dismutase 1 Homo sapiens 0-22 29850654-1 2018 Superoxide dismutase 1 (SOD1) is a metalloenzyme that catalyzes the disproportionation of superoxide into molecular oxygen and hydrogen peroxide. Hydrogen Peroxide 127-144 superoxide dismutase 1 Homo sapiens 24-28 28676971-2 2017 In the present study non-cytotoxic dose of oxidants, H2O2 (100 muM) and GO (10 muU/ml) was used to induce moderate oxidative stress via generating ROS in human glioblastoma cell line U-87 MG cells, which showed a marked increase in the antioxidant capacity as studied by measuring the modulation in expression levels and activities of superoxide dismutase (SOD1 and SOD2) and catalase (CAT) enzymes, and the GSH content. Hydrogen Peroxide 53-57 superoxide dismutase 1 Homo sapiens 357-361 28603086-4 2017 SOD catalyzes the dismutation of the superoxide anion (O2 -) to oxygen (O2) and hydrogen peroxide (H2O2). Hydrogen Peroxide 99-103 superoxide dismutase 1 Homo sapiens 0-3 28686251-2 2017 Sod1 dismutes superoxide anions to hydrogen peroxide and oxygen. Hydrogen Peroxide 35-52 superoxide dismutase 1 Homo sapiens 0-4 28074522-9 2017 RESULTS: In comparison with the control group, the viability of MCs and SOD activity were significantly decreased in the H2 O2 group (P < 0.05) and significantly increased in the tacalcitol group (P < 0.05). Hydrogen Peroxide 121-126 superoxide dismutase 1 Homo sapiens 72-75 28112004-3 2017 Pretreatment with these two carotenoids significantly attenuated H2O2-induced apoptosis in WPMY-1 cells through the inhibition of intracellular reactive oxygen species (ROS) and malondialdehyde (MDA) overproduction, as well as the activation of the activities in catalase (CAT), superoxide dismutase (SOD), and glutathione peroxidase (GSH-Px). Hydrogen Peroxide 65-69 superoxide dismutase 1 Homo sapiens 279-299 28112004-3 2017 Pretreatment with these two carotenoids significantly attenuated H2O2-induced apoptosis in WPMY-1 cells through the inhibition of intracellular reactive oxygen species (ROS) and malondialdehyde (MDA) overproduction, as well as the activation of the activities in catalase (CAT), superoxide dismutase (SOD), and glutathione peroxidase (GSH-Px). Hydrogen Peroxide 65-69 superoxide dismutase 1 Homo sapiens 301-304 27914828-0 2017 Oleuropein protects L-02 cells against H2O2-induced oxidative stress by increasing SOD1, GPx1 and CAT expression. Hydrogen Peroxide 39-43 superoxide dismutase 1 Homo sapiens 83-87 27112417-5 2017 Meanwhile, the added 200 U/mL SOD group showed lower MDA content and H2 O2 content. Hydrogen Peroxide 69-74 superoxide dismutase 1 Homo sapiens 30-33 28445874-2 2017 In the neonate, superoxide dismutase (SOD) overexpression worsens hypoxic-ischemic injury due to H2O2 accumulation in the brain. Hydrogen Peroxide 97-101 superoxide dismutase 1 Homo sapiens 38-41 27842206-3 2016 In addition, H2O2 decreased the transcription levels of catalase (CAT), glutathione peroxidase (GPx), and superoxide dismutase (SOD) 5.43-, 2.89-, and 5.33-fold, respectively, while it increased Bax, NF-kappabeta, TNF-alpha, and iNOS expression 1.57-, 1.32-, 1.40-, and 1.41-fold, respectively. Hydrogen Peroxide 13-17 superoxide dismutase 1 Homo sapiens 106-126 27842206-3 2016 In addition, H2O2 decreased the transcription levels of catalase (CAT), glutathione peroxidase (GPx), and superoxide dismutase (SOD) 5.43-, 2.89-, and 5.33-fold, respectively, while it increased Bax, NF-kappabeta, TNF-alpha, and iNOS expression 1.57-, 1.32-, 1.40-, and 1.41-fold, respectively. Hydrogen Peroxide 13-17 superoxide dismutase 1 Homo sapiens 128-131 27842206-5 2016 Moreover, intracellular glutathione (GSH) level and SOD activity were decreased by 46.2% and 45.0% in the H2O2 treatment group, and OOP recovered 58.5% and 20.1% of the decreases caused by H2O2. Hydrogen Peroxide 106-110 superoxide dismutase 1 Homo sapiens 52-55 27773815-3 2016 By utilizing cumate inducible SOD1 cells, we also showed that knock-down or pharmacologic depletion of cIAPs leads to H2O2 induced cytotoxicity in mSOD1 expressing cells. Hydrogen Peroxide 118-122 superoxide dismutase 1 Homo sapiens 30-34 27671770-10 2016 To confirm this, we measured the production of H2O2 following overexpression of SOD1 or catalase with MnTE-2-PyP treatment in the presence or absence of radiation. Hydrogen Peroxide 47-51 superoxide dismutase 1 Homo sapiens 80-84 26699812-3 2016 Because Cu,Zn-superoxide dismutase-induced H2O2 can polarize macrophages to a profibrotic M2 phenotype, we hypothesized that modulation of the redox state of the cell is involved in the epigenetic modulation of the macrophage phenotype. Hydrogen Peroxide 43-47 superoxide dismutase 1 Homo sapiens 8-34 30034766-2 2016 Intracellular H2O2 is formed mainly via the catalytic dismutation of O2 - by SODs including SOD1, SOD2 and SOD3. Hydrogen Peroxide 14-18 superoxide dismutase 1 Homo sapiens 92-96 30034766-3 2016 Thus, the intracellular levels of O2 - and H2O2 can directly be controlled through regulating SOD1 activity. Hydrogen Peroxide 43-47 superoxide dismutase 1 Homo sapiens 94-98 30034766-4 2016 Here, based on the active site structure and catalytic mechanism of SOD1, we developed a new type of efficient and specific SOD1 inhibitors which can directly change the intracellular levels of H2O2 and O2 -. Hydrogen Peroxide 194-198 superoxide dismutase 1 Homo sapiens 68-72 30034766-4 2016 Here, based on the active site structure and catalytic mechanism of SOD1, we developed a new type of efficient and specific SOD1 inhibitors which can directly change the intracellular levels of H2O2 and O2 -. Hydrogen Peroxide 194-198 superoxide dismutase 1 Homo sapiens 124-128 30034766-6 2016 The reduced ERK1/2 phosphorylation induced by the specific SOD1 inactivation-mediated decrease of intracellular H2O2 levels reveals the potential of these specific SOD1 inhibitors in understanding and regulating ROS signaling. Hydrogen Peroxide 112-116 superoxide dismutase 1 Homo sapiens 59-63 30034766-6 2016 The reduced ERK1/2 phosphorylation induced by the specific SOD1 inactivation-mediated decrease of intracellular H2O2 levels reveals the potential of these specific SOD1 inhibitors in understanding and regulating ROS signaling. Hydrogen Peroxide 112-116 superoxide dismutase 1 Homo sapiens 164-168 26891889-8 2016 All antioxidants tested, except SOD, effectively reduced neuronal damage and DNA breakage caused by the toxic H2O2/SNAP combination. Hydrogen Peroxide 110-114 superoxide dismutase 1 Homo sapiens 32-35 27083311-5 2016 Furthermore, in HaCaT keratinocytes treated with H2O2, 1,25(OH)2D3, 21(OH)pD and calcipotriol stimulated the expression of SOD1 and CAT genes, but not SOD2, indicating a possible role of mitochondria in ROS-modulated cell death. Hydrogen Peroxide 49-53 superoxide dismutase 1 Homo sapiens 123-127 27086975-8 2016 Furthermore, superoxide dismutase (SOD1 and 2) enzymes, localised within cerebellar neurons, are up-regulated, yet the activation of subsequent enzymes responsible for the detoxification of hydrogen peroxide, catalase and glutathione peroxidase are relatively deficient. Hydrogen Peroxide 190-207 superoxide dismutase 1 Homo sapiens 35-45 27187356-8 2016 Moreover, the decreased level of DNA-PKcs was associated with the production of intracellular hydrogen peroxide by stable dimeric forms of Cu/Zn SOD1 induced by NSC. Hydrogen Peroxide 94-111 superoxide dismutase 1 Homo sapiens 145-149 26843356-5 2016 The survival of cells and the activities of superoxide dismutase (SOD) and glutathione peroxidase (GSH-Px) were significantly increased through the pre-incubation of HepG-2 cells with RDPHs before H2O2 exposure. Hydrogen Peroxide 197-201 superoxide dismutase 1 Homo sapiens 44-64 26843356-5 2016 The survival of cells and the activities of superoxide dismutase (SOD) and glutathione peroxidase (GSH-Px) were significantly increased through the pre-incubation of HepG-2 cells with RDPHs before H2O2 exposure. Hydrogen Peroxide 197-201 superoxide dismutase 1 Homo sapiens 66-69 26356671-1 2015 HIGHLIGHTS: BACKGROUND: Cu/Zn superoxide dismutases (SODs) like the extracellular SOD3 and cytoplasmic SOD1 regulate cell proliferation by generating hydrogen peroxide (H2O2). Hydrogen Peroxide 151-168 superoxide dismutase 1 Homo sapiens 104-108 26883293-0 2016 Activation of EGFR by small compounds through coupling the generation of hydrogen peroxide to stable dimerization of Cu/Zn SOD1. Hydrogen Peroxide 73-90 superoxide dismutase 1 Homo sapiens 123-127 26883293-4 2016 Production of H2O2 during redox transformation of NBD compounds is associated with the transition of a monomeric form of Cu/Zn superoxide dismutase 1 (SOD1) to stable dimers. Hydrogen Peroxide 14-18 superoxide dismutase 1 Homo sapiens 151-155 26883293-5 2016 The highly stable and functionally active SOD1 dimer, in the absence of adequate activities in downstream reactions, promotes the disproportionate production and accumulation of intracellular hydrogen peroxide shortly after exposure to NBD compounds. Hydrogen Peroxide 192-209 superoxide dismutase 1 Homo sapiens 42-46 26629876-4 2016 Here, we implement an electrochemical setup and use the specificity of superoxide dismutase-1 (SOD1) to show, for the first time, that H2O2 production by Cu-Abeta in the presence of ascorbate occurs mainly via a free O2 (-) intermediate. Hydrogen Peroxide 135-139 superoxide dismutase 1 Homo sapiens 71-93 26629876-4 2016 Here, we implement an electrochemical setup and use the specificity of superoxide dismutase-1 (SOD1) to show, for the first time, that H2O2 production by Cu-Abeta in the presence of ascorbate occurs mainly via a free O2 (-) intermediate. Hydrogen Peroxide 135-139 superoxide dismutase 1 Homo sapiens 95-99 26898904-7 2016 SOD and D-mannitol scavengers also reduced DNA damage by 30% indicating that O(2)(-)* and OH* are involved in H2O2 formation. Hydrogen Peroxide 110-114 superoxide dismutase 1 Homo sapiens 0-3 26619801-0 2016 Hydrogen peroxide-mediated induction of SOD1 gene transcription is independent from Nrf2 in a cellular model of neurodegeneration. Hydrogen Peroxide 0-17 superoxide dismutase 1 Homo sapiens 40-44 26619801-2 2016 Previously we demonstrated the accumulation of reactive oxygen species (ROS) and increased SOD1 gene expression in H2O2-treated SH-SY5Y cells, recapitulating pathological features of Amyotrophic Lateral Sclerosis (ALS). Hydrogen Peroxide 115-119 superoxide dismutase 1 Homo sapiens 91-95 26619801-4 2016 RESULTS: In response to H2O2 treatment, PolII increased its association to SOD1 promoter. Hydrogen Peroxide 24-28 superoxide dismutase 1 Homo sapiens 75-79 26356671-1 2015 HIGHLIGHTS: BACKGROUND: Cu/Zn superoxide dismutases (SODs) like the extracellular SOD3 and cytoplasmic SOD1 regulate cell proliferation by generating hydrogen peroxide (H2O2). Hydrogen Peroxide 170-174 superoxide dismutase 1 Homo sapiens 104-108 26356671-6 2015 RESULTS: a) without copper supplementation, exogenous SOD potentiated sub-toxic DSF toxicity antagonized by sub-toxic TTM or by the anti-oxidant N-acetylcysteine; b) exogenous glucose oxidase, another H2O2 generator resembled exogenous SOD in potentiating sub-toxic DSF. Hydrogen Peroxide 201-205 superoxide dismutase 1 Homo sapiens 54-57 25794772-2 2015 In the present study, we have evaluated the effects of the superoxide dismutase (SOD) mimetic MnTmPyP and the SOD/catalase mimetic EUK 134 on superoxide and H2O2 formation as well as proliferation, adhesion, and migration of MCF-7 and MDA-MB-231 cells. Hydrogen Peroxide 157-161 superoxide dismutase 1 Homo sapiens 110-113 25863213-5 2015 The highest H2O2 content was accompanied by a significant decrease of SOD and CAT activity and an elevated level of GPx. Hydrogen Peroxide 12-16 superoxide dismutase 1 Homo sapiens 70-73 26354208-5 2015 The gene for Cu/Zn superoxide dismutase (SOD1) is coded on chromosome 21 and it is overexpressed (~50%) resulting in an increase of reactive oxygen species (ROS) due to overproduction of hydrogen peroxide (H 2 O 2 ). Hydrogen Peroxide 187-204 superoxide dismutase 1 Homo sapiens 13-39 26354208-5 2015 The gene for Cu/Zn superoxide dismutase (SOD1) is coded on chromosome 21 and it is overexpressed (~50%) resulting in an increase of reactive oxygen species (ROS) due to overproduction of hydrogen peroxide (H 2 O 2 ). Hydrogen Peroxide 187-204 superoxide dismutase 1 Homo sapiens 41-45 25928076-0 2015 Oligomerization of Cu,Zn-Superoxide Dismutase (SOD1) by Docosahexaenoic Acid and Its Hydroperoxides In Vitro: Aggregation Dependence on Fatty Acid Unsaturation and Thiols. Hydrogen Peroxide 85-99 superoxide dismutase 1 Homo sapiens 19-45 25928076-0 2015 Oligomerization of Cu,Zn-Superoxide Dismutase (SOD1) by Docosahexaenoic Acid and Its Hydroperoxides In Vitro: Aggregation Dependence on Fatty Acid Unsaturation and Thiols. Hydrogen Peroxide 85-99 superoxide dismutase 1 Homo sapiens 47-51 25928076-4 2015 Here we investigated the effect of DHA and its hydroperoxides (DHAOOH) on human SOD1 oligomerization in vitro. Hydrogen Peroxide 47-61 superoxide dismutase 1 Homo sapiens 80-84 25660330-9 2015 The stability of SOD1 activity was further tested through in vitro incubation with H2O2 and scanning of its electrophoretic profiles. Hydrogen Peroxide 83-87 superoxide dismutase 1 Homo sapiens 17-21 25660330-13 2015 Treatment with 20 muM also elevated GR activity after in vitro incubation at 37 C. Electrophoretic profiles revealed that incubation with ibogaine mitigates H2O2 mediated suppression of SOD1 activity. Hydrogen Peroxide 157-161 superoxide dismutase 1 Homo sapiens 186-190 25825208-0 2015 Superoxide dismutase promotes the epithelial-mesenchymal transition of pancreatic cancer cells via activation of the H2O2/ERK/NF-kappaB axis. Hydrogen Peroxide 117-121 superoxide dismutase 1 Homo sapiens 0-20 25419347-10 2014 Wogonin also upregulated the mRNA expression of CAT, SOD-1 and GSR in oxidative stress induced by H2O2 EA.hy926 cells. Hydrogen Peroxide 98-102 superoxide dismutase 1 Homo sapiens 53-58 24877629-9 2014 The mRNA levels of SIRT3, catalase, and superoxide dismutase 1 were up-regulated by hydrogen peroxide in both COV434 cells and human GCs and down-regulated by human chorionic gonadotropin. Hydrogen Peroxide 84-101 superoxide dismutase 1 Homo sapiens 40-62 25371520-8 2014 Superoxide dismutase (SOD) is the main enzyme, which neutralizes ROS into less noxious hydrogen peroxide. Hydrogen Peroxide 87-104 superoxide dismutase 1 Homo sapiens 0-20 25371520-8 2014 Superoxide dismutase (SOD) is the main enzyme, which neutralizes ROS into less noxious hydrogen peroxide. Hydrogen Peroxide 87-104 superoxide dismutase 1 Homo sapiens 22-25 24368505-6 2014 According to the suggested concept, the intrinsically higher superoxide dismutase (SOD) levels in halophytes are required for rapid induction of the H2O2 "signature", and to trigger a cascade of adaptive responses (both genetic and physiological), while the role of other enzymatic antioxidants may be in decreasing the basal levels of H2O2, once the signalling has been processed. Hydrogen Peroxide 149-153 superoxide dismutase 1 Homo sapiens 61-81 24123071-4 2014 Our results showed that during osteoblast adhesion/spreading (30 min and 2 h of seeding) the intracellular ROS content (hydrogen peroxide) is finely regulated by an effective anti-oxidant system [catalase and Superoxide Dismutase (SOD) activities were evaluated]. Hydrogen Peroxide 120-137 superoxide dismutase 1 Homo sapiens 209-229 24123071-4 2014 Our results showed that during osteoblast adhesion/spreading (30 min and 2 h of seeding) the intracellular ROS content (hydrogen peroxide) is finely regulated by an effective anti-oxidant system [catalase and Superoxide Dismutase (SOD) activities were evaluated]. Hydrogen Peroxide 120-137 superoxide dismutase 1 Homo sapiens 231-234 24535002-13 2014 Overall, SOD1 is upregulated in response to selenite-mediated ROS generation, and this likely leads to an accumulation of toxic hydrogen peroxide that is temporally related to decreased cancer cell viability. Hydrogen Peroxide 128-145 superoxide dismutase 1 Homo sapiens 9-13 24647101-1 2014 Superoxide dismutase 1 (Sod1) has been known for nearly half a century for catalysis of superoxide to hydrogen peroxide. Hydrogen Peroxide 102-119 superoxide dismutase 1 Homo sapiens 0-22 24647101-1 2014 Superoxide dismutase 1 (Sod1) has been known for nearly half a century for catalysis of superoxide to hydrogen peroxide. Hydrogen Peroxide 102-119 superoxide dismutase 1 Homo sapiens 24-28 24647101-3 2014 Interestingly, H2O2 is sufficient to promote Sod1 nuclear localization, indicating that it is responding to general ROS rather than Sod1 substrate superoxide. Hydrogen Peroxide 15-19 superoxide dismutase 1 Homo sapiens 45-49 24368505-6 2014 According to the suggested concept, the intrinsically higher superoxide dismutase (SOD) levels in halophytes are required for rapid induction of the H2O2 "signature", and to trigger a cascade of adaptive responses (both genetic and physiological), while the role of other enzymatic antioxidants may be in decreasing the basal levels of H2O2, once the signalling has been processed. Hydrogen Peroxide 149-153 superoxide dismutase 1 Homo sapiens 83-86 24368505-6 2014 According to the suggested concept, the intrinsically higher superoxide dismutase (SOD) levels in halophytes are required for rapid induction of the H2O2 "signature", and to trigger a cascade of adaptive responses (both genetic and physiological), while the role of other enzymatic antioxidants may be in decreasing the basal levels of H2O2, once the signalling has been processed. Hydrogen Peroxide 336-340 superoxide dismutase 1 Homo sapiens 61-81 24368505-6 2014 According to the suggested concept, the intrinsically higher superoxide dismutase (SOD) levels in halophytes are required for rapid induction of the H2O2 "signature", and to trigger a cascade of adaptive responses (both genetic and physiological), while the role of other enzymatic antioxidants may be in decreasing the basal levels of H2O2, once the signalling has been processed. Hydrogen Peroxide 336-340 superoxide dismutase 1 Homo sapiens 83-86 24001508-11 2014 Pretreatment of HeLa cells with quercetin alleviated H2O2-induced cell injury by improving redox balance as indicated by the increase in glutathione content and SOD (superoxide dismutase) levels as well as by the decrease in ROS level. Hydrogen Peroxide 53-57 superoxide dismutase 1 Homo sapiens 166-186 24724445-3 2014 RESULTS: SOD, which catalyzes the reduction of superoxide anions to hydrogen peroxide and has anti-oxidative effects, was significantly lower in E group at the end of surgery whereas the levels of myeloperoxydase were not different between the groups. Hydrogen Peroxide 68-85 superoxide dismutase 1 Homo sapiens 9-12 24292713-5 2014 ATN-224-dependent SOD1 inhibition increased superoxide, which diminished enzyme activity of the antioxidant glutathione peroxidase, leading to an increase in intracellular hydrogen peroxide (H(2)O(2)) levels. Hydrogen Peroxide 172-189 superoxide dismutase 1 Homo sapiens 18-22 23969235-7 2013 We also observed that the treatment with H2O2 induced a significant increase of the amount of SOD1 mRNA bound by ELAVs and an up-regulation of SOD1 protein levels. Hydrogen Peroxide 41-45 superoxide dismutase 1 Homo sapiens 94-98 24080119-3 2013 We report that peroxidase and H2O2 induce superoxide dismutase (SOD)-sensitive, L-012-derived CL in the presence of oxygen. Hydrogen Peroxide 30-34 superoxide dismutase 1 Homo sapiens 42-62 24080119-3 2013 We report that peroxidase and H2O2 induce superoxide dismutase (SOD)-sensitive, L-012-derived CL in the presence of oxygen. Hydrogen Peroxide 30-34 superoxide dismutase 1 Homo sapiens 64-67 24564604-7 2014 Superoxide dismutase (SOD) was then added to the inflowing perfusion media to convert any superoxide crossing the microdialysis membrane to H(2)O(2) within the microdialysis probe. Hydrogen Peroxide 140-148 superoxide dismutase 1 Homo sapiens 0-20 24564604-7 2014 Superoxide dismutase (SOD) was then added to the inflowing perfusion media to convert any superoxide crossing the microdialysis membrane to H(2)O(2) within the microdialysis probe. Hydrogen Peroxide 140-148 superoxide dismutase 1 Homo sapiens 22-25 24389620-2 2014 The enzyme, superoxide dismutase (SOD) catalyses the dismutation of superoxide anion to hydrogen peroxide. Hydrogen Peroxide 88-105 superoxide dismutase 1 Homo sapiens 34-37 24036105-3 2013 This study examined the role of the enzymatic antioxidant SOD, which converts the pro-oxidant superoxide into H2O2, in vitiligo pathogenesis. Hydrogen Peroxide 110-114 superoxide dismutase 1 Homo sapiens 58-61 24036105-14 2013 Overall, our results suggest that increased activity of SOD isoforms under the influence of genetic factors may lead to accumulation of H2O2 in cytoplasmic, mitochondrial, and extracellular compartments resulting in oxidative damage to the melanocytes. Hydrogen Peroxide 136-140 superoxide dismutase 1 Homo sapiens 56-59 24103366-4 2013 The interaction between the tested Cu(II)-RSSR and superoxide, led to the generation and recovery of concentrations of hydrogen peroxide and oxygen that were, respectively, below and above those theoretically-expected from a sole SOD mimetic action. Hydrogen Peroxide 119-136 superoxide dismutase 1 Homo sapiens 230-233 23969235-7 2013 We also observed that the treatment with H2O2 induced a significant increase of the amount of SOD1 mRNA bound by ELAVs and an up-regulation of SOD1 protein levels. Hydrogen Peroxide 41-45 superoxide dismutase 1 Homo sapiens 143-147 24324479-7 2013 However, in senescence, superoxide dismutase (SOD), that converts superoxide anion radical ([Formula: see text]) to hydrogen peroxide (H2O2,) decreases, while the thylakoid Ndh complex, that favors the generation of singlet oxygen ((1)O2) and [Formula: see text], and peroxidase (PX), that consumes H2O2, increase. Hydrogen Peroxide 116-133 superoxide dismutase 1 Homo sapiens 24-44 24324479-7 2013 However, in senescence, superoxide dismutase (SOD), that converts superoxide anion radical ([Formula: see text]) to hydrogen peroxide (H2O2,) decreases, while the thylakoid Ndh complex, that favors the generation of singlet oxygen ((1)O2) and [Formula: see text], and peroxidase (PX), that consumes H2O2, increase. Hydrogen Peroxide 299-303 superoxide dismutase 1 Homo sapiens 24-44 24324479-7 2013 However, in senescence, superoxide dismutase (SOD), that converts superoxide anion radical ([Formula: see text]) to hydrogen peroxide (H2O2,) decreases, while the thylakoid Ndh complex, that favors the generation of singlet oxygen ((1)O2) and [Formula: see text], and peroxidase (PX), that consumes H2O2, increase. Hydrogen Peroxide 299-303 superoxide dismutase 1 Homo sapiens 46-49 24324479-7 2013 However, in senescence, superoxide dismutase (SOD), that converts superoxide anion radical ([Formula: see text]) to hydrogen peroxide (H2O2,) decreases, while the thylakoid Ndh complex, that favors the generation of singlet oxygen ((1)O2) and [Formula: see text], and peroxidase (PX), that consumes H2O2, increase. Hydrogen Peroxide 116-133 superoxide dismutase 1 Homo sapiens 46-49 24324479-7 2013 However, in senescence, superoxide dismutase (SOD), that converts superoxide anion radical ([Formula: see text]) to hydrogen peroxide (H2O2,) decreases, while the thylakoid Ndh complex, that favors the generation of singlet oxygen ((1)O2) and [Formula: see text], and peroxidase (PX), that consumes H2O2, increase. Hydrogen Peroxide 135-139 superoxide dismutase 1 Homo sapiens 24-44 24324479-7 2013 However, in senescence, superoxide dismutase (SOD), that converts superoxide anion radical ([Formula: see text]) to hydrogen peroxide (H2O2,) decreases, while the thylakoid Ndh complex, that favors the generation of singlet oxygen ((1)O2) and [Formula: see text], and peroxidase (PX), that consumes H2O2, increase. Hydrogen Peroxide 135-139 superoxide dismutase 1 Homo sapiens 46-49 23768398-5 2013 The addition of catalase and superoxide dismutase (SOD) prevented the hydroxyl radical driven-degradation of beta-glucan induced by iron(II) or ascorbic acid/iron(II), demonstrating the involvement of both superoxide and hydrogen peroxide in the hydroxyl radical formation. Hydrogen Peroxide 221-238 superoxide dismutase 1 Homo sapiens 29-49 23578882-11 2013 The results further revealed that exposure to Cd, Pb, and a co-stimulation of H2O2 with Hg resulted in the increased expression of antioxidant gene SOD. Hydrogen Peroxide 78-82 superoxide dismutase 1 Homo sapiens 148-151 23768398-5 2013 The addition of catalase and superoxide dismutase (SOD) prevented the hydroxyl radical driven-degradation of beta-glucan induced by iron(II) or ascorbic acid/iron(II), demonstrating the involvement of both superoxide and hydrogen peroxide in the hydroxyl radical formation. Hydrogen Peroxide 221-238 superoxide dismutase 1 Homo sapiens 51-54 23768398-6 2013 SOD, which catalyses the dismutation of superoxide into hydrogen peroxide, should have stimulated the formation of radicals, since these radicals are generated from the reaction between hydrogen peroxide and iron(II). Hydrogen Peroxide 56-73 superoxide dismutase 1 Homo sapiens 0-3 23768398-6 2013 SOD, which catalyses the dismutation of superoxide into hydrogen peroxide, should have stimulated the formation of radicals, since these radicals are generated from the reaction between hydrogen peroxide and iron(II). Hydrogen Peroxide 186-203 superoxide dismutase 1 Homo sapiens 0-3 23919400-1 2013 The metalloenzyme Cu/Zn-superoxide dismutase (SOD1) catalyzes the reduction of superoxide anions into molecular oxygen and hydrogen peroxide. Hydrogen Peroxide 123-140 superoxide dismutase 1 Homo sapiens 18-44 23855710-4 2013 The chosen oxidizing system was the bicarbonate-dependent peroxidase activity of hSOD1 that consumes H2O2 to produce carbonate radical, which oxidizes the enzyme. Hydrogen Peroxide 101-105 superoxide dismutase 1 Homo sapiens 81-86 23919400-1 2013 The metalloenzyme Cu/Zn-superoxide dismutase (SOD1) catalyzes the reduction of superoxide anions into molecular oxygen and hydrogen peroxide. Hydrogen Peroxide 123-140 superoxide dismutase 1 Homo sapiens 46-50 23927036-2 2013 To remove ROS, cells have developed ROS-specific defense mechanisms, including the enzyme Cu/Zn superoxide dismutase (SOD1), which catalyzes the disproportionation of superoxide anions into molecular oxygen and hydrogen peroxide. Hydrogen Peroxide 211-228 superoxide dismutase 1 Homo sapiens 118-122 23919400-2 2013 Hydrogen peroxide can oxidize SOD1, resulting in aberrant protein conformational changes, disruption of SOD1 function, and DNA damage. Hydrogen Peroxide 0-17 superoxide dismutase 1 Homo sapiens 30-34 23927036-3 2013 Although hydrogen peroxide is less reactive than superoxide, it is still capable of oxidizing, unfolding, and inactivating SOD1, at least in vitro. Hydrogen Peroxide 9-26 superoxide dismutase 1 Homo sapiens 123-127 23919400-2 2013 Hydrogen peroxide can oxidize SOD1, resulting in aberrant protein conformational changes, disruption of SOD1 function, and DNA damage. Hydrogen Peroxide 0-17 superoxide dismutase 1 Homo sapiens 104-108 23984825-5 2013 The results showed that farrerol significantly inhibited the loss of cell viability and enhanced superoxide dismutase (SOD) and glutathione peroxidase (GSH-Px) activities in H2O2-induced EA.hy926 cells. Hydrogen Peroxide 174-178 superoxide dismutase 1 Homo sapiens 97-117 23984825-5 2013 The results showed that farrerol significantly inhibited the loss of cell viability and enhanced superoxide dismutase (SOD) and glutathione peroxidase (GSH-Px) activities in H2O2-induced EA.hy926 cells. Hydrogen Peroxide 174-178 superoxide dismutase 1 Homo sapiens 119-122 23832989-1 2013 The electron transport system required for energy transduction in mitochondria releases free electrons to generate superoxide, which is converted to hydrogen peroxide either spontaneously or by superoxide dismutase (SOD). Hydrogen Peroxide 149-166 superoxide dismutase 1 Homo sapiens 194-214 23831194-6 2013 Compared with the H2O2 treatment alone cells group, 200 mg/L of the extract increased the activity of superoxide dismutase (SOD) in cells by 397.3%, and decreased the concentration of malondialdehyde (MDA) and the activity of lactate acid dehydrogenase (LDH) by 47.8% and 69.6%, respectively. Hydrogen Peroxide 18-22 superoxide dismutase 1 Homo sapiens 102-122 23831194-6 2013 Compared with the H2O2 treatment alone cells group, 200 mg/L of the extract increased the activity of superoxide dismutase (SOD) in cells by 397.3%, and decreased the concentration of malondialdehyde (MDA) and the activity of lactate acid dehydrogenase (LDH) by 47.8% and 69.6%, respectively. Hydrogen Peroxide 18-22 superoxide dismutase 1 Homo sapiens 124-127 23832989-1 2013 The electron transport system required for energy transduction in mitochondria releases free electrons to generate superoxide, which is converted to hydrogen peroxide either spontaneously or by superoxide dismutase (SOD). Hydrogen Peroxide 149-166 superoxide dismutase 1 Homo sapiens 216-219 23832989-3 2013 In the absence of SOD, hydrogen peroxide can be converted to highly toxic hydroxyl radicals, in particular, in the presence of transition metals such as the free form of iron. Hydrogen Peroxide 23-40 superoxide dismutase 1 Homo sapiens 18-21 23755211-5 2013 As evidenced by mass spectrometry and SDS-PAGE, Cys-111 is a primary target for oxidative modification of pathological human SOD1 mutant A4V by either excess Cu(2+) or hydrogen peroxide. Hydrogen Peroxide 168-185 superoxide dismutase 1 Homo sapiens 125-129 23755211-7 2013 Furthermore, Cu(2+) binds to wild-type SOD1 oxidized by hydrogen peroxide in a way similar to A4V, triggering the aggregation of such an oxidized form. Hydrogen Peroxide 56-73 superoxide dismutase 1 Homo sapiens 39-43 23522069-6 2013 The activity of the SOD form was the highest at pH 10 within the temperature range between 20 and 45 C. The enzymatic activity of form released after cold shock was inhibited by H2O2 and diethyldithiocarbamate (DDC; by 65 and 40%, respectively). Hydrogen Peroxide 178-182 superoxide dismutase 1 Homo sapiens 20-23 23456297-9 2013 We postulate that the disproportional up-regulation of SOD, CAT and GPX expression and enzymatic activity in cancer cells results in the mitochondrial accumulation of H2O2, which in turn induces cancer cell apoptosis. Hydrogen Peroxide 167-171 superoxide dismutase 1 Homo sapiens 55-58 23522069-7 2013 The SOD form released by homogenization was inhibited by H2O2 and DDC (40%). Hydrogen Peroxide 57-61 superoxide dismutase 1 Homo sapiens 4-7 23124725-3 2013 SOD1 activity profile following native polyacrylamide gel electrophoresis indicates that aripiprazole and quetiapine protect enzyme activity from inhibition with hydrogen peroxide. Hydrogen Peroxide 162-179 superoxide dismutase 1 Homo sapiens 0-4 23365008-7 2013 Pre-treatment of human dermal fibroblasts with Oatp significantly reversed the H(2)O(2)-induced decrease of superoxide dismutase (SOD) and the inhibition of malondialdehyde (MDA). Hydrogen Peroxide 79-87 superoxide dismutase 1 Homo sapiens 108-128 23365008-7 2013 Pre-treatment of human dermal fibroblasts with Oatp significantly reversed the H(2)O(2)-induced decrease of superoxide dismutase (SOD) and the inhibition of malondialdehyde (MDA). Hydrogen Peroxide 79-87 superoxide dismutase 1 Homo sapiens 130-133 23365008-8 2013 The results demonstrate that oat peptides possess antioxidant activity and are effective against H(2)O(2)-induced human dermal fibroblast injury by the enhanced activity of SOD and decrease in MDA level. Hydrogen Peroxide 97-105 superoxide dismutase 1 Homo sapiens 173-176 23449129-6 2013 Treatment of human dermal fibroblasts with EGCG significantly reversed the H2O2-induced decrease of superoxide dismutase (SOD) and glutathione peroxidase (GSH-px), and the inhibition of malondialdehyde (MDA) levels. Hydrogen Peroxide 75-79 superoxide dismutase 1 Homo sapiens 100-120 23921602-3 2013 Superoxide dismutase (SOD) is the first-line and only antioxidant enzyme that converts superoxide to hydrogen peroxide. Hydrogen Peroxide 101-118 superoxide dismutase 1 Homo sapiens 0-20 23921602-3 2013 Superoxide dismutase (SOD) is the first-line and only antioxidant enzyme that converts superoxide to hydrogen peroxide. Hydrogen Peroxide 101-118 superoxide dismutase 1 Homo sapiens 22-25 23449129-6 2013 Treatment of human dermal fibroblasts with EGCG significantly reversed the H2O2-induced decrease of superoxide dismutase (SOD) and glutathione peroxidase (GSH-px), and the inhibition of malondialdehyde (MDA) levels. Hydrogen Peroxide 75-79 superoxide dismutase 1 Homo sapiens 122-125 23449129-7 2013 These results showed that EGCG possessed antioxidant activity and was effective against H2O2-induced human dermal fibroblast injury by enhancing the activity of SOD and GSH-px, and by decreasing the MDA level. Hydrogen Peroxide 88-92 superoxide dismutase 1 Homo sapiens 161-164 23089226-5 2012 EC stimulation by micromolar concentrations of H2O2 was inhibited by catalase, but also unexpectedly by SOD. Hydrogen Peroxide 47-51 superoxide dismutase 1 Homo sapiens 104-107 22846601-8 2012 SOD must favor reduction of oxygen by the INH radical to give superoxide and ultimately hydrogen peroxide. Hydrogen Peroxide 88-105 superoxide dismutase 1 Homo sapiens 0-3 22842628-9 2012 The Cu-dependent enzyme SOD1 is responsible for generating the hydrogen peroxide in response to RTK activation that serves to inhibit phosphatases that normally limit RTK signaling. Hydrogen Peroxide 63-80 superoxide dismutase 1 Homo sapiens 24-28 23026387-7 2012 The addition of exogenous CAT and SOD significantly protected the capacity for glucose uptake and respiration, suggesting that superoxide and H(2)O(2) are involved in the impairment of activity during UV-B exposure. Hydrogen Peroxide 142-150 superoxide dismutase 1 Homo sapiens 34-37 23259324-7 2012 Our findings revealed that exposure of non-irradiated cells to these factors induced increased in SOD and catalase activities which reverted to normal levels by 8 h. During this period, the released factors-treated cells were resistant to killing by UVC or H2O2 and induced DNA damage and lipid peroxidation were also lowered. Hydrogen Peroxide 257-261 superoxide dismutase 1 Homo sapiens 98-101 22459774-2 2012 Superoxide dismutase (SOD) catalyses the dismutation of superoxide anion to hydrogen peroxide. Hydrogen Peroxide 76-93 superoxide dismutase 1 Homo sapiens 22-25 22542526-5 2012 Here, we present evidence that hydrogen peroxide treatment, which generates free radical species at the SOD1 active site, causes oxidative damage to active-site histidine residues, leading to major structural changes and non-amyloid aggregation similar to that seen in ALS. Hydrogen Peroxide 31-48 superoxide dismutase 1 Homo sapiens 104-108 22294351-2 2012 Generation of H2O2 was pH dependent, increasing at alkaline pH, and was lowered in the presence of catalase and, to a lesser extent, of superoxide dismutase (SOD). Hydrogen Peroxide 14-18 superoxide dismutase 1 Homo sapiens 136-156 22294351-2 2012 Generation of H2O2 was pH dependent, increasing at alkaline pH, and was lowered in the presence of catalase and, to a lesser extent, of superoxide dismutase (SOD). Hydrogen Peroxide 14-18 superoxide dismutase 1 Homo sapiens 158-161 22352897-4 2012 Therefore, the present review summarizes experimental data supporting a neuroprotective potential of H2O2 in ischaemic stroke that has been principally achieved by means of pharmacological and genetic strategies that modify either the activity or the expression of the superoxide dismutase (SOD), glutathione peroxidase (GPx) and CAT enzymes, which are key regulators of H2O2 metabolism. Hydrogen Peroxide 101-105 superoxide dismutase 1 Homo sapiens 269-289 22352897-4 2012 Therefore, the present review summarizes experimental data supporting a neuroprotective potential of H2O2 in ischaemic stroke that has been principally achieved by means of pharmacological and genetic strategies that modify either the activity or the expression of the superoxide dismutase (SOD), glutathione peroxidase (GPx) and CAT enzymes, which are key regulators of H2O2 metabolism. Hydrogen Peroxide 101-105 superoxide dismutase 1 Homo sapiens 291-294 22352897-4 2012 Therefore, the present review summarizes experimental data supporting a neuroprotective potential of H2O2 in ischaemic stroke that has been principally achieved by means of pharmacological and genetic strategies that modify either the activity or the expression of the superoxide dismutase (SOD), glutathione peroxidase (GPx) and CAT enzymes, which are key regulators of H2O2 metabolism. Hydrogen Peroxide 371-375 superoxide dismutase 1 Homo sapiens 269-289 22200861-7 2012 Furthermore, a significant decrease in the SOD/CAT ratio was observed following lithium treatment, which was associated with decreased OxS by lowering hydrogen peroxide levels. Hydrogen Peroxide 151-168 superoxide dismutase 1 Homo sapiens 43-46 22292618-4 2012 The system is composed of superoxide dismutase (SOD) conjugated to oxidation-sensitive amphiphilic polysulfide/PEG block copolymers; the conjugate combines the SOD reactivity toward superoxide with that of hydrophobic thioethers toward hydrogen peroxide. Hydrogen Peroxide 236-253 superoxide dismutase 1 Homo sapiens 26-46 22292618-4 2012 The system is composed of superoxide dismutase (SOD) conjugated to oxidation-sensitive amphiphilic polysulfide/PEG block copolymers; the conjugate combines the SOD reactivity toward superoxide with that of hydrophobic thioethers toward hydrogen peroxide. Hydrogen Peroxide 236-253 superoxide dismutase 1 Homo sapiens 48-51 22292618-5 2012 Specifically, here we have demonstrated how this hybrid system can efficiently convert superoxide into hydrogen peroxide, which is then "mopped-up" by the polysulfides: this modus operandi is functionally analogous to the SOD/catalase combination, with the advantages of (a) being based on a single and more stable system, and (b) a higher overall efficiency due the physical proximity of the two ROS-reactive centers (SOD and polysulfides). Hydrogen Peroxide 103-120 superoxide dismutase 1 Homo sapiens 222-225 22292618-5 2012 Specifically, here we have demonstrated how this hybrid system can efficiently convert superoxide into hydrogen peroxide, which is then "mopped-up" by the polysulfides: this modus operandi is functionally analogous to the SOD/catalase combination, with the advantages of (a) being based on a single and more stable system, and (b) a higher overall efficiency due the physical proximity of the two ROS-reactive centers (SOD and polysulfides). Hydrogen Peroxide 103-120 superoxide dismutase 1 Homo sapiens 419-422 22322977-9 2012 In contrast, enhanced dismutation of superoxide to hydrogen peroxide with SOD had no effect on ANG II-dependent stimulation of L-type calcium channels. Hydrogen Peroxide 51-68 superoxide dismutase 1 Homo sapiens 74-77 22370236-11 2012 Induced SOD expression after H(2)O(2) stimulation was diminished by CAPE pretreatment. Hydrogen Peroxide 29-37 superoxide dismutase 1 Homo sapiens 8-11 22200861-8 2012 This reduction in the SOD/CAT ratio may lead to lower OxS, indicated primarily by a decrease in the concentration of cell hydrogen peroxide. Hydrogen Peroxide 122-139 superoxide dismutase 1 Homo sapiens 22-25 22508043-8 2012 Exogenous catalase or SOD1 did not alter cytotoxicity, while over-expression of either catalase or SOD1 did, pointing to the importance of intracellular hydrogen peroxide generation in cell killing. Hydrogen Peroxide 153-170 superoxide dismutase 1 Homo sapiens 99-103 22139847-2 2012 The presence of p38alpha increases basal and H(2)O(2)-induced expression of the antioxidant enzymes: superoxide-dismutase 1 (SOD-1), SOD-2, and catalase through different mechanisms, which protects from reactive oxygen species (ROS) accumulation and prevents cell death. Hydrogen Peroxide 45-53 superoxide dismutase 1 Homo sapiens 101-123 22139847-2 2012 The presence of p38alpha increases basal and H(2)O(2)-induced expression of the antioxidant enzymes: superoxide-dismutase 1 (SOD-1), SOD-2, and catalase through different mechanisms, which protects from reactive oxygen species (ROS) accumulation and prevents cell death. Hydrogen Peroxide 45-53 superoxide dismutase 1 Homo sapiens 125-130 23049256-6 2012 Under the same conditions, LMWP-SOD1 abolished activation of the cell cycle regulator proteins, p53 and p21(Cip1), induced by hydrogen peroxide. Hydrogen Peroxide 126-143 superoxide dismutase 1 Homo sapiens 27-36 23049256-7 2012 In addition, LMWP-SOD1 reversed the inhibition of osteoblastic differentiation and downregulation of osteogenic gene markers induced by hydrogen peroxide. Hydrogen Peroxide 136-153 superoxide dismutase 1 Homo sapiens 13-22 21865594-1 2011 Superoxide dismutase 1 (Sod1) is an important antioxidative enzyme that converts superoxide anions to hydrogen peroxide and water. Hydrogen Peroxide 102-119 superoxide dismutase 1 Homo sapiens 0-22 22984565-3 2012 SOD also reacts with H(2)O(2), leading to the formation of a strong copper-bound oxidant species that can either inactivate the enzyme or oxidise other substrates. Hydrogen Peroxide 21-29 superoxide dismutase 1 Homo sapiens 0-3 21905722-6 2011 H(2)O(2)-induced stress decreased CuZn superoxide dismutase (CuZn-SOD) and glutathione peroxidase (GPx) activities, whereas this effect was prevented by incubation with TCs in a concentration-dependent manner. Hydrogen Peroxide 0-8 superoxide dismutase 1 Homo sapiens 34-59 21905722-6 2011 H(2)O(2)-induced stress decreased CuZn superoxide dismutase (CuZn-SOD) and glutathione peroxidase (GPx) activities, whereas this effect was prevented by incubation with TCs in a concentration-dependent manner. Hydrogen Peroxide 0-8 superoxide dismutase 1 Homo sapiens 61-69 22057568-6 2012 Superoxide dismutase (MnSOD, SOD2) from the mitochondrial matrix as well as superoxide dismutase (Cu/ZnSOD, SOD1) present in small amounts in the mitochondrial intramembrane space, convert superoxide anion to hydrogen peroxide, which can be then converted by catalase to harmless H(2)O. Hydrogen Peroxide 209-226 superoxide dismutase 1 Homo sapiens 108-112 21865594-1 2011 Superoxide dismutase 1 (Sod1) is an important antioxidative enzyme that converts superoxide anions to hydrogen peroxide and water. Hydrogen Peroxide 102-119 superoxide dismutase 1 Homo sapiens 24-28 21393238-0 2011 Mitochondrial Cu,Zn-superoxide dismutase mediates pulmonary fibrosis by augmenting H2O2 generation. Hydrogen Peroxide 83-87 superoxide dismutase 1 Homo sapiens 14-40 21419845-7 2011 The suppression of oxygen consumption by addition of SOD or catalase further confirmed the production of superoxide and hydrogen peroxide. Hydrogen Peroxide 120-137 superoxide dismutase 1 Homo sapiens 53-56 19701650-5 2009 We also explored the consequences of a pre-treatment with SOD on the afferent nerve response to H2O2 injection or electrical muscle stimulation (MS). Hydrogen Peroxide 96-100 superoxide dismutase 1 Homo sapiens 58-61 21731194-8 2010 Superoxide dismutase (SOD), glutathione peroxidase and catalase are termed as primary antioxidants as these scavenge superoxide anion and hydrogen peroxide. Hydrogen Peroxide 138-155 superoxide dismutase 1 Homo sapiens 0-20 20110684-5 2010 The hydroperoxide donor TBHP increased SOD1 levels but did not change catalase levels. Hydrogen Peroxide 4-17 superoxide dismutase 1 Homo sapiens 39-43 22272128-3 2011 SOD-1 catalyses the superoxide radical (O(-2)) into hydrogen peroxide and molecular oxygen. Hydrogen Peroxide 52-69 superoxide dismutase 1 Homo sapiens 0-5 21172066-4 2010 Moreover NGAL levels increase in correlation with the age, and showed a significantly correlation between the increase with the severity of disease.DS is characterized by an enhancement of gene production such as GART, SOD-1 and CBS that encode specific protein and enzyme involved in hydrogen peroxide and superoxide production, species highly cytotoxic implicated in inflammation and ageing.NGAL may have the potential application to ameliorate the toxicity induced by oxidative stress conditions such as Alzheimer"s disease, thalassemia, cardiovascular disease, burn injury, transplantation, diabetes, and aging. Hydrogen Peroxide 285-302 superoxide dismutase 1 Homo sapiens 219-224 20806083-0 2010 Resveratrol protects human lens epithelial cells against H2O2-induced oxidative stress by increasing catalase, SOD-1, and HO-1 expression. Hydrogen Peroxide 57-61 superoxide dismutase 1 Homo sapiens 111-116 20184893-1 2010 Cu,Zn superoxide dismutase (SOD1) is a dimeric metal-binding enzyme responsible for the dismutation of toxic superoxide to hydrogen peroxide and oxygen in cells. Hydrogen Peroxide 123-140 superoxide dismutase 1 Homo sapiens 0-26 20184893-1 2010 Cu,Zn superoxide dismutase (SOD1) is a dimeric metal-binding enzyme responsible for the dismutation of toxic superoxide to hydrogen peroxide and oxygen in cells. Hydrogen Peroxide 123-140 superoxide dismutase 1 Homo sapiens 28-32 20034962-3 2010 Superoxide dismutase (SOD) catalyzes the dismutation of superoxide anion to hydrogen peroxide, which is subsequently detoxified by catalase. Hydrogen Peroxide 76-93 superoxide dismutase 1 Homo sapiens 22-25 19701650-8 2009 SOD injection lowered the baseline activity of 50 out of 70 afferent units, suppressed the afferent response to H2O2 injection, and delayed and reduced the MS-induced activation of all recorded units. Hydrogen Peroxide 112-116 superoxide dismutase 1 Homo sapiens 0-3 19286663-5 2009 In view of recent observations, we hypothesized that the SOD1 peroxidase cycle relies on two steps: 1) reduction of SOD-Cu(II) by hydrogen peroxide followed by 2) oxidation of SOD-Cu(I) by peroxymonocarbonate, the product of the spontaneous reaction of bicarbonate with hydrogen peroxide, to produce SOD-Cu(II) and carbonate radical anion. Hydrogen Peroxide 130-147 superoxide dismutase 1 Homo sapiens 57-61 19379729-6 2009 Incubation of cells with H(2)O(2) caused a marked decrease in superoxide dismutase (SOD) activity; this decrease was significantly inhibited by morroniside. Hydrogen Peroxide 25-33 superoxide dismutase 1 Homo sapiens 62-82 19379729-6 2009 Incubation of cells with H(2)O(2) caused a marked decrease in superoxide dismutase (SOD) activity; this decrease was significantly inhibited by morroniside. Hydrogen Peroxide 25-33 superoxide dismutase 1 Homo sapiens 84-87 20083859-3 2009 NADPH oxidases (Nox) are the predominant producers of superoxide in the vasculature, whereas superoxide dismutase (SOD) and glutathione peroxidase 1 (GPx1) are the major enzymes responsible for the inactivation of superoxide and hydrogen peroxide, respectively. Hydrogen Peroxide 229-246 superoxide dismutase 1 Homo sapiens 115-118 19286663-5 2009 In view of recent observations, we hypothesized that the SOD1 peroxidase cycle relies on two steps: 1) reduction of SOD-Cu(II) by hydrogen peroxide followed by 2) oxidation of SOD-Cu(I) by peroxymonocarbonate, the product of the spontaneous reaction of bicarbonate with hydrogen peroxide, to produce SOD-Cu(II) and carbonate radical anion. Hydrogen Peroxide 270-287 superoxide dismutase 1 Homo sapiens 57-61 19042137-10 2009 SOD and CAT induced by H(2)O(2) could be blocked by scavenger of NO and inhibitors of NO generation, while SOD and CAT induced by NO could not be blocked by scavenger of H(2)O(2) and inhibitor of H(2)O(2). Hydrogen Peroxide 23-31 superoxide dismutase 1 Homo sapiens 0-3 19243126-6 2009 Kinetic analyses of hydrogen peroxide consumption and of nitrite, formate, and bicarbonate-carbon dioxide oxidation showed that the Sod1-bound hydroxyl-like oxidant functions in the presence of nitrite and formate. Hydrogen Peroxide 20-37 superoxide dismutase 1 Homo sapiens 132-136 19243126-12 2009 In the presence of bicarbonate-carbon dioxide, sustained hSod1-mediated oxidations occurred with low steady-state concentrations of hydrogen peroxide (4-10 microM). Hydrogen Peroxide 132-149 superoxide dismutase 1 Homo sapiens 57-62 18764780-1 2009 The understanding of the mechanism, oxidant(s) involved and how and what protein radicals are produced during the reaction of wild-type SOD1 (Cu,Zn-superoxide dismutase) with H2O2 and their fate is incomplete, but a better understanding of the role of this reaction is needed. Hydrogen Peroxide 175-179 superoxide dismutase 1 Homo sapiens 136-140 18764780-7 2009 The CO(*-) produced by the reaction of hSOD1 with H2O2 also produced distinctive DMPO (5,5-dimethylpyrroline-N-oxide) nitrone adduct-positive protein bands in the mBH. Hydrogen Peroxide 50-54 superoxide dismutase 1 Homo sapiens 39-44 18764780-8 2009 Finally, we propose a biochemical mechanism to explain CO(*-) production from CO2, enhanced protein radical formation and protection by (bi)carbonate against H2O2-induced fragmentation of the SOD1 active site. Hydrogen Peroxide 158-162 superoxide dismutase 1 Homo sapiens 192-196 18764780-9 2009 Our present study is important for establishing experimental conditions for studying the molecular mechanism and targets of oxidation during the reverse reaction of SOD1 with H2O2; these results are the first step in analysing the critical targets of SOD1-driven oxidation during pathological processes such as neuroinflammation. Hydrogen Peroxide 175-179 superoxide dismutase 1 Homo sapiens 165-169 18764780-9 2009 Our present study is important for establishing experimental conditions for studying the molecular mechanism and targets of oxidation during the reverse reaction of SOD1 with H2O2; these results are the first step in analysing the critical targets of SOD1-driven oxidation during pathological processes such as neuroinflammation. Hydrogen Peroxide 175-179 superoxide dismutase 1 Homo sapiens 251-255 18509606-1 2008 The objective of our study was to investigate the neuroprotective efficacy of superoxide dismutase (SOD), loaded in poly(D,L-lactide co-glycolide; PLGA) nanoparticles (NPs), in cultured human neurons challenged with hydrogen peroxide (H(2)O(2))-induced oxidative stress. Hydrogen Peroxide 216-233 superoxide dismutase 1 Homo sapiens 78-98 18927353-9 2009 Accumulation of hydrogen peroxide was observed with the administration of high doses of PC-SOD, an effect that was suppressed by the simultaneous administration of catalase. Hydrogen Peroxide 16-33 superoxide dismutase 1 Homo sapiens 88-94 18927353-11 2009 These results suggest that PC-SOD achieves its ameliorative effect against colitis through decreasing the colonic level of ROS and that its ineffectiveness at higher doses is because of the accumulation of hydrogen peroxide. Hydrogen Peroxide 206-223 superoxide dismutase 1 Homo sapiens 27-33 18927353-2 2009 Superoxide dismutase (SOD) catalyzes dismutation of superoxide anion to hydrogen peroxide, which is subsequently detoxified by catalase. Hydrogen Peroxide 72-89 superoxide dismutase 1 Homo sapiens 22-25 18509606-1 2008 The objective of our study was to investigate the neuroprotective efficacy of superoxide dismutase (SOD), loaded in poly(D,L-lactide co-glycolide; PLGA) nanoparticles (NPs), in cultured human neurons challenged with hydrogen peroxide (H(2)O(2))-induced oxidative stress. Hydrogen Peroxide 235-244 superoxide dismutase 1 Homo sapiens 100-103 18509606-6 2008 The neuroprotective effect of SOD-NPs was seen up to 6 h after H(2)O(2)-induced oxidative stress, but the effect diminished thereafter. Hydrogen Peroxide 63-71 superoxide dismutase 1 Homo sapiens 30-33 18509606-1 2008 The objective of our study was to investigate the neuroprotective efficacy of superoxide dismutase (SOD), loaded in poly(D,L-lactide co-glycolide; PLGA) nanoparticles (NPs), in cultured human neurons challenged with hydrogen peroxide (H(2)O(2))-induced oxidative stress. Hydrogen Peroxide 216-233 superoxide dismutase 1 Homo sapiens 100-103 18509606-1 2008 The objective of our study was to investigate the neuroprotective efficacy of superoxide dismutase (SOD), loaded in poly(D,L-lactide co-glycolide; PLGA) nanoparticles (NPs), in cultured human neurons challenged with hydrogen peroxide (H(2)O(2))-induced oxidative stress. Hydrogen Peroxide 235-244 superoxide dismutase 1 Homo sapiens 78-98 18957292-6 2008 In addition, experiments with SOD mimic, catalase, and exogenous H2O2 provided evidence that the presence of H2O2 down-regulated the amount of HIF-2alpha protein. Hydrogen Peroxide 109-113 superoxide dismutase 1 Homo sapiens 30-33 18826240-1 2008 Cu, Zn-superoxide dismutase (SOD-1), an enzyme that catalyzes the disproportionation reaction of superoxide to produce oxygen and hydrogen peroxide, thereby protecting cells from oxidative stress, is a homodimer that coordinates one copper and one zinc ion per monomer. Hydrogen Peroxide 130-147 superoxide dismutase 1 Homo sapiens 29-34 18480265-0 2008 Superoxide dismutase 1 (SOD1) is essential for H2O2-mediated oxidation and inactivation of phosphatases in growth factor signaling. Hydrogen Peroxide 47-51 superoxide dismutase 1 Homo sapiens 0-22 18395249-5 2008 X-ray photoelectron spectroscopy (XPS) and UV-visible analyses of nanoceria treated with hydrogen peroxide demonstrate that a decrease in the Ce 3(+)/4(+) ratio correlates directly with a loss of SOD mimetic activity. Hydrogen Peroxide 89-106 superoxide dismutase 1 Homo sapiens 196-199 18480265-0 2008 Superoxide dismutase 1 (SOD1) is essential for H2O2-mediated oxidation and inactivation of phosphatases in growth factor signaling. Hydrogen Peroxide 47-51 superoxide dismutase 1 Homo sapiens 24-28 18480265-1 2008 Superoxide dismutase 1 (SOD1) is an abundant copper/zinc enzyme found in the cytoplasm that converts superoxide into hydrogen peroxide and molecular oxygen. Hydrogen Peroxide 117-134 superoxide dismutase 1 Homo sapiens 0-22 18480265-1 2008 Superoxide dismutase 1 (SOD1) is an abundant copper/zinc enzyme found in the cytoplasm that converts superoxide into hydrogen peroxide and molecular oxygen. Hydrogen Peroxide 117-134 superoxide dismutase 1 Homo sapiens 24-28 18480265-7 2008 Pretreatment with exogenous H(2)O(2) or with the phosphatase inhibitor vanadate abrogates the inhibition of ERK1/2 phosphorylation induced by ATN-224 or SOD1 siRNA treatments. Hydrogen Peroxide 28-36 superoxide dismutase 1 Homo sapiens 153-157 19093460-2 2007 Superoxide dismutase (SOD) catalyzes the conversion of superoxide radical to hydrogen peroxide (H2O2) and molecular oxygen (O2) thus providing a biological defense against oxygen toxicity. Hydrogen Peroxide 77-94 superoxide dismutase 1 Homo sapiens 0-20 17657594-14 2008 In addition, the H2O2 produced in the cell system was about 2 microM for the low-dose combination which was scavenged to about 1 microM in the presence of SOD. Hydrogen Peroxide 17-21 superoxide dismutase 1 Homo sapiens 155-158 17915203-8 2007 The percentage of residual damage after H(2)O(2) treatment followed by 3h of post-incubation is significantly higher in patients and also correlates positively with SOD activity, ER and PR expression and negatively with the basal DNA damage. Hydrogen Peroxide 40-48 superoxide dismutase 1 Homo sapiens 165-168 17951132-6 2007 In addition, this oil inhibited H(2)O(2)-induced depletion of antioxidant defense components, such as superoxide dismutase and catalase. Hydrogen Peroxide 32-40 superoxide dismutase 1 Homo sapiens 102-122 18366234-5 2008 On the basis of the above results, the co-induction of the SOD and POD activities to eliminate the superoxide and also hydrogen peroxide as a one-pot reaction was finally performed by using the Mn-HPyP-modified DMPC liposome, resulting in an increase in the efficiency of the elimination of both superoxide and hydrogen peroxide. Hydrogen Peroxide 119-136 superoxide dismutase 1 Homo sapiens 59-62 18366234-5 2008 On the basis of the above results, the co-induction of the SOD and POD activities to eliminate the superoxide and also hydrogen peroxide as a one-pot reaction was finally performed by using the Mn-HPyP-modified DMPC liposome, resulting in an increase in the efficiency of the elimination of both superoxide and hydrogen peroxide. Hydrogen Peroxide 311-328 superoxide dismutase 1 Homo sapiens 59-62 18386505-1 2008 A Notable decrease of the peak intensity of the capillary electrophoregram due to the dimeric SOD molecule was observed when a solution containing copper(II) chloride and ascorbic acid was added to the SOD solution, indicating that the capillary electrophoresis method is useful to detect the dissociation of the dimeric SOD molecule in solution, and that dissociation of the dimeric SOD molecule is induced by the presence of hydrogen peroxide. Hydrogen Peroxide 427-444 superoxide dismutase 1 Homo sapiens 94-97 18386505-1 2008 A Notable decrease of the peak intensity of the capillary electrophoregram due to the dimeric SOD molecule was observed when a solution containing copper(II) chloride and ascorbic acid was added to the SOD solution, indicating that the capillary electrophoresis method is useful to detect the dissociation of the dimeric SOD molecule in solution, and that dissociation of the dimeric SOD molecule is induced by the presence of hydrogen peroxide. Hydrogen Peroxide 427-444 superoxide dismutase 1 Homo sapiens 202-205 18386505-1 2008 A Notable decrease of the peak intensity of the capillary electrophoregram due to the dimeric SOD molecule was observed when a solution containing copper(II) chloride and ascorbic acid was added to the SOD solution, indicating that the capillary electrophoresis method is useful to detect the dissociation of the dimeric SOD molecule in solution, and that dissociation of the dimeric SOD molecule is induced by the presence of hydrogen peroxide. Hydrogen Peroxide 427-444 superoxide dismutase 1 Homo sapiens 202-205 18386505-1 2008 A Notable decrease of the peak intensity of the capillary electrophoregram due to the dimeric SOD molecule was observed when a solution containing copper(II) chloride and ascorbic acid was added to the SOD solution, indicating that the capillary electrophoresis method is useful to detect the dissociation of the dimeric SOD molecule in solution, and that dissociation of the dimeric SOD molecule is induced by the presence of hydrogen peroxide. Hydrogen Peroxide 427-444 superoxide dismutase 1 Homo sapiens 202-205 17913710-5 2007 Wild-type SOD1 was more sensitive to oxidation by hydrogen peroxide-generating fragments, oligomers, and charge isomers compared with 2-ME-SOD1. Hydrogen Peroxide 50-67 superoxide dismutase 1 Homo sapiens 10-14 19093460-2 2007 Superoxide dismutase (SOD) catalyzes the conversion of superoxide radical to hydrogen peroxide (H2O2) and molecular oxygen (O2) thus providing a biological defense against oxygen toxicity. Hydrogen Peroxide 77-94 superoxide dismutase 1 Homo sapiens 22-25 19093460-2 2007 Superoxide dismutase (SOD) catalyzes the conversion of superoxide radical to hydrogen peroxide (H2O2) and molecular oxygen (O2) thus providing a biological defense against oxygen toxicity. Hydrogen Peroxide 96-100 superoxide dismutase 1 Homo sapiens 0-20 19093460-2 2007 Superoxide dismutase (SOD) catalyzes the conversion of superoxide radical to hydrogen peroxide (H2O2) and molecular oxygen (O2) thus providing a biological defense against oxygen toxicity. Hydrogen Peroxide 96-100 superoxide dismutase 1 Homo sapiens 22-25 17122956-3 2006 Under the conditions of oxidative stress, superoxide dismutase (SOD) acts as an endogenous cellular defense system to degrade superoxide (O2-) into oxygen and hydrogen peroxide. Hydrogen Peroxide 159-176 superoxide dismutase 1 Homo sapiens 42-62 17223784-4 2006 It was found that SOD in the hydrogel was more resistant to H2O2 inactivation than the native enzyme and at the same time it reduced the time necessary for wound healing. Hydrogen Peroxide 60-64 superoxide dismutase 1 Homo sapiens 18-21 17020816-1 2006 The mitochondrial enzyme manganese superoxide dismutase (mitMn-SOD) is one of the antioxidant enzymes involved in cellular defense against oxidative stress and catalyzes the conversion of O(2)(-) into the stabler H(2)O(2). Hydrogen Peroxide 213-221 superoxide dismutase 1 Homo sapiens 63-66 17048802-1 2006 For some time it has been claimed that trisomic cells are more sensitive to oxidative stress since there is an imbalance in hydrogen peroxide metabolism due to an increase in superoxide dismutase (SOD) catalytic activity. Hydrogen Peroxide 124-141 superoxide dismutase 1 Homo sapiens 175-195 17048802-1 2006 For some time it has been claimed that trisomic cells are more sensitive to oxidative stress since there is an imbalance in hydrogen peroxide metabolism due to an increase in superoxide dismutase (SOD) catalytic activity. Hydrogen Peroxide 124-141 superoxide dismutase 1 Homo sapiens 197-200 17015180-2 2006 However, the nature of the effect of SOD on the cellular production of H(2)O(2) is not widely appreciated. Hydrogen Peroxide 71-79 superoxide dismutase 1 Homo sapiens 37-40 17015180-9 2006 We found that the higher the level of SOD, the greater the rate of accumulation of H(2)O(2). Hydrogen Peroxide 83-91 superoxide dismutase 1 Homo sapiens 38-41 17015180-12 2006 Thus, the current paradigm that SOD will lower the flux of H(2)O(2) does not hold for the ETC. Hydrogen Peroxide 59-67 superoxide dismutase 1 Homo sapiens 32-35 17122956-3 2006 Under the conditions of oxidative stress, superoxide dismutase (SOD) acts as an endogenous cellular defense system to degrade superoxide (O2-) into oxygen and hydrogen peroxide. Hydrogen Peroxide 159-176 superoxide dismutase 1 Homo sapiens 64-67 16495003-5 2006 Exposure to H2O2 induced a time-dependent decrease of Bcl-2 and SOD1 in control lymphocytes. Hydrogen Peroxide 12-16 superoxide dismutase 1 Homo sapiens 64-68 16431026-10 2006 Finally, we show that the motor neuron-like cells expressing mutant SOD1 are more susceptible to H2O2 induced cell death compared to the cells expressing WT SOD1. Hydrogen Peroxide 97-101 superoxide dismutase 1 Homo sapiens 68-72 16085106-1 2006 One of the most important antioxidant enzymes is superoxide dismutase (SOD), which catalyses the dismutation of superoxide radicals to hydrogen peroxide. Hydrogen Peroxide 135-152 superoxide dismutase 1 Homo sapiens 49-69 16511360-0 2006 Cu,Zn-superoxide dismutase is an intracellular catalyst for the H(2)O(2)-dependent oxidation of dichlorodihydrofluorescein. Hydrogen Peroxide 64-72 superoxide dismutase 1 Homo sapiens 0-26 16511360-9 2006 We propose that CuZnSOD is a potential intracellular catalyst for the H(2)O(2)-dependent oxidation of DCFH(2). Hydrogen Peroxide 70-78 superoxide dismutase 1 Homo sapiens 16-23 16085106-1 2006 One of the most important antioxidant enzymes is superoxide dismutase (SOD), which catalyses the dismutation of superoxide radicals to hydrogen peroxide. Hydrogen Peroxide 135-152 superoxide dismutase 1 Homo sapiens 71-74 16085106-9 2006 This short-circuiting of the SOD cycle could lead to an increased hydrogen peroxide production. Hydrogen Peroxide 66-83 superoxide dismutase 1 Homo sapiens 29-32 15652492-4 2005 Overexpression of human superoxide dismutase (SOD) by adenovirus-mediated gene transfer or addition of exogenous hydrogen peroxide (H(2)O(2)) significantly enhanced TNF-alpha-induced IL-8 mRNA expression. Hydrogen Peroxide 113-130 superoxide dismutase 1 Homo sapiens 24-44 16046449-5 2005 In this study, we modified Cu,Zn-superoxide dismutase by using a combination of myeloperoxidase, hydrogen peroxide, and nitrite. Hydrogen Peroxide 97-114 superoxide dismutase 1 Homo sapiens 27-53 15777089-4 2005 The addition of catalase inhibited the SOD1 peroxidase activity stimulated by the thiol oxidase actvity, implicating an intermediary role for H2O2 in SOD1/Cys/HCO3(-)-mediated oxidation and hydroxylation reactions. Hydrogen Peroxide 142-146 superoxide dismutase 1 Homo sapiens 39-43 15777089-4 2005 The addition of catalase inhibited the SOD1 peroxidase activity stimulated by the thiol oxidase actvity, implicating an intermediary role for H2O2 in SOD1/Cys/HCO3(-)-mediated oxidation and hydroxylation reactions. Hydrogen Peroxide 142-146 superoxide dismutase 1 Homo sapiens 150-154 15652492-4 2005 Overexpression of human superoxide dismutase (SOD) by adenovirus-mediated gene transfer or addition of exogenous hydrogen peroxide (H(2)O(2)) significantly enhanced TNF-alpha-induced IL-8 mRNA expression. Hydrogen Peroxide 113-130 superoxide dismutase 1 Homo sapiens 46-49 16729589-2 2006 Based on this fact, it has become apparent that the hydrogen peroxide molecule induces the dissociation of the dimeric structure of SOD, and this should give reasonable explanation for the inactivation of SOD by hydrogen peroxide. Hydrogen Peroxide 52-69 superoxide dismutase 1 Homo sapiens 132-135 16729589-2 2006 Based on this fact, it has become apparent that the hydrogen peroxide molecule induces the dissociation of the dimeric structure of SOD, and this should give reasonable explanation for the inactivation of SOD by hydrogen peroxide. Hydrogen Peroxide 52-69 superoxide dismutase 1 Homo sapiens 205-208 16729589-2 2006 Based on this fact, it has become apparent that the hydrogen peroxide molecule induces the dissociation of the dimeric structure of SOD, and this should give reasonable explanation for the inactivation of SOD by hydrogen peroxide. Hydrogen Peroxide 212-229 superoxide dismutase 1 Homo sapiens 132-135 16729589-2 2006 Based on this fact, it has become apparent that the hydrogen peroxide molecule induces the dissociation of the dimeric structure of SOD, and this should give reasonable explanation for the inactivation of SOD by hydrogen peroxide. Hydrogen Peroxide 212-229 superoxide dismutase 1 Homo sapiens 205-208 16686997-6 2006 This may due to the enzymatic ability of over-expressed CuZn-superoxide dismutase in Down syndrome to catalyze the formation of H2O2 from O2*-, thereby increasing the availability of substrate H2O2 for the iron-dependent generation of HO* via the Fenton reaction, suggesting that HO* generated from DS-GF may be involved in progressive periodontitis of Down syndrome. Hydrogen Peroxide 128-132 superoxide dismutase 1 Homo sapiens 56-81 16686997-6 2006 This may due to the enzymatic ability of over-expressed CuZn-superoxide dismutase in Down syndrome to catalyze the formation of H2O2 from O2*-, thereby increasing the availability of substrate H2O2 for the iron-dependent generation of HO* via the Fenton reaction, suggesting that HO* generated from DS-GF may be involved in progressive periodontitis of Down syndrome. Hydrogen Peroxide 193-197 superoxide dismutase 1 Homo sapiens 56-81 16254550-12 2005 Lenses overexpressing SOD1 remained clear after H2O2 treatment at 100 muM for 24 h, similar to control. Hydrogen Peroxide 48-52 superoxide dismutase 1 Homo sapiens 22-26 16254550-13 2005 Overexpression of SOD1 diminished the effect of H2O2 on PKCgamma activation and subsequent inhibition of gap junctions, indicating that overexpression of SOD1 may reduce reactive oxygen species (ROS) production, and this would prevent the normal H2O2 effect on cataract formation. Hydrogen Peroxide 48-52 superoxide dismutase 1 Homo sapiens 18-22 16254550-13 2005 Overexpression of SOD1 diminished the effect of H2O2 on PKCgamma activation and subsequent inhibition of gap junctions, indicating that overexpression of SOD1 may reduce reactive oxygen species (ROS) production, and this would prevent the normal H2O2 effect on cataract formation. Hydrogen Peroxide 48-52 superoxide dismutase 1 Homo sapiens 154-158 16254550-13 2005 Overexpression of SOD1 diminished the effect of H2O2 on PKCgamma activation and subsequent inhibition of gap junctions, indicating that overexpression of SOD1 may reduce reactive oxygen species (ROS) production, and this would prevent the normal H2O2 effect on cataract formation. Hydrogen Peroxide 246-250 superoxide dismutase 1 Homo sapiens 18-22 16254550-13 2005 Overexpression of SOD1 diminished the effect of H2O2 on PKCgamma activation and subsequent inhibition of gap junctions, indicating that overexpression of SOD1 may reduce reactive oxygen species (ROS) production, and this would prevent the normal H2O2 effect on cataract formation. Hydrogen Peroxide 246-250 superoxide dismutase 1 Homo sapiens 154-158 16254550-14 2005 CONCLUSIONS: Overexpression of SOD1 in whole lens prevents H2O2-induced oxidative damage (cataract formation) to the lens and subsequent control of gap junctions by protein kinase Cgamma. Hydrogen Peroxide 59-63 superoxide dismutase 1 Homo sapiens 31-35 16036355-7 2005 Spontaneous apoptosis, hydrogen peroxide and anti-Fas antibody-induced apoptosis of neutrophils were accelerated in Down"s syndrome patients, in whom the SOD gene is overexpressed. Hydrogen Peroxide 23-40 superoxide dismutase 1 Homo sapiens 154-157 15590679-8 2005 In the presence of Cu,Zn-superoxide dismutase, an enzyme that induces the rapid catalytic dismutation of superoxide to the less reactive H(2)O(2) and O(2), the yields of the dehydroguanidinohydantion lesions become negligible. Hydrogen Peroxide 137-145 superoxide dismutase 1 Homo sapiens 19-45 15839099-4 2005 Cell responses against both superoxide and peroxide stresses include enhanced expression of superoxide dismutase (SOD) and catalase, however, the extent was different: treatment with PQ increased mainly SOD, whereas exogenous H2O2 led to enhanced catalase. Hydrogen Peroxide 226-230 superoxide dismutase 1 Homo sapiens 114-117 15683235-7 2005 Notably, attempts to generate a stable hydroperoxo-Mn3+ SOD species by protonation of the proximal O atom of the hydroperoxo ligand resulted in dissociation of HOO- and eventual H+ transfer from Tyr34 to HOO-, generating deprotonated Tyr34 and H2O2. Hydrogen Peroxide 244-248 superoxide dismutase 1 Homo sapiens 51-59 15544920-1 2004 Previously, we showed that oxidation of tryptophan-32 (Trp-32) residue was crucial for H(2)O(2)/bicarbonate (HCO(3)(-))-dependent covalent aggregation of human Cu,Zn SOD1 (hSOD1). Hydrogen Peroxide 87-95 superoxide dismutase 1 Homo sapiens 166-170 15607903-4 2005 These species produced immuno-spin trapping-detectable SOD1-centered radicals associated with H2O2-induced active site ( approximately 5 and approximately 10 kDa fragments) and non-active site (smearing between 3 and 16 kDa) copper-dependent backbone oxidations and subsequent fragmentation of SOD1. Hydrogen Peroxide 94-98 superoxide dismutase 1 Homo sapiens 55-59 15607903-4 2005 These species produced immuno-spin trapping-detectable SOD1-centered radicals associated with H2O2-induced active site ( approximately 5 and approximately 10 kDa fragments) and non-active site (smearing between 3 and 16 kDa) copper-dependent backbone oxidations and subsequent fragmentation of SOD1. Hydrogen Peroxide 94-98 superoxide dismutase 1 Homo sapiens 294-298 15607903-5 2005 Second, in the presence of DTPA, which inhibits H2O2-induced SOD1 non-active site fragmentation, (bi)carbonate scavenged the enzyme-bound oxidant at the SOD1 active site to produce the carbonate radical anion, CO3*-, thus protecting against active site SOD1 fragmentation. Hydrogen Peroxide 48-52 superoxide dismutase 1 Homo sapiens 61-65 15607903-5 2005 Second, in the presence of DTPA, which inhibits H2O2-induced SOD1 non-active site fragmentation, (bi)carbonate scavenged the enzyme-bound oxidant at the SOD1 active site to produce the carbonate radical anion, CO3*-, thus protecting against active site SOD1 fragmentation. Hydrogen Peroxide 48-52 superoxide dismutase 1 Homo sapiens 153-157 15607903-5 2005 Second, in the presence of DTPA, which inhibits H2O2-induced SOD1 non-active site fragmentation, (bi)carbonate scavenged the enzyme-bound oxidant at the SOD1 active site to produce the carbonate radical anion, CO3*-, thus protecting against active site SOD1 fragmentation. Hydrogen Peroxide 48-52 superoxide dismutase 1 Homo sapiens 153-157 15607903-8 2005 In addition, (bi)carbonate enhanced H2O2-induced SOD1 turnover as demonstrated by an enhancement in oxygen evolution and SOD1 inactivation. Hydrogen Peroxide 36-40 superoxide dismutase 1 Homo sapiens 49-53 15607903-8 2005 In addition, (bi)carbonate enhanced H2O2-induced SOD1 turnover as demonstrated by an enhancement in oxygen evolution and SOD1 inactivation. Hydrogen Peroxide 36-40 superoxide dismutase 1 Homo sapiens 121-125 15607903-9 2005 These results help clarify the free radical chemistry involved in the functional and structural oxidative damage to SOD1 by H2O2 with the intermediacy of copper- and CO3*--mediated oxidations. Hydrogen Peroxide 124-128 superoxide dismutase 1 Homo sapiens 116-120 15617860-3 2005 Some of the cognitive impairments are likely due to post-natal hydrogen peroxide-mediated oxidative stress caused by overexpression of the superoxide dismutase (SOD-1) gene, which is located on the triplicated 21st chromosome and known to be 50% overexpressed. Hydrogen Peroxide 63-80 superoxide dismutase 1 Homo sapiens 161-166 15607903-1 2005 We have reinvestigated the biochemistry of H2O2-induced Cu,Zn-superoxide dismutase (SOD1)-centered radicals, detecting them by immuno-spin trapping. Hydrogen Peroxide 43-47 superoxide dismutase 1 Homo sapiens 84-88 15607903-2 2005 These radicals are involved in H2O2-induced structural and functional damage to SOD1, and their mechanism of generation depends on copper and/or (bi)carbonate (i.e., CO2, CO3(-2), or HCO3-). Hydrogen Peroxide 31-35 superoxide dismutase 1 Homo sapiens 80-84 15589971-10 2005 Thus, it appeared that inhibition of SOD might be the major cause for the production of cellular superoxide with concomitant decrease of H(2)O(2) in DPD-treated cells. Hydrogen Peroxide 137-145 superoxide dismutase 1 Homo sapiens 37-40 15544920-1 2004 Previously, we showed that oxidation of tryptophan-32 (Trp-32) residue was crucial for H(2)O(2)/bicarbonate (HCO(3)(-))-dependent covalent aggregation of human Cu,Zn SOD1 (hSOD1). Hydrogen Peroxide 87-95 superoxide dismutase 1 Homo sapiens 172-177 15525277-9 2004 We suggest that SOD1 overexpression has beneficial effects on astrocytes, as it does in other systems with similarly high disposal of hydroperoxides. Hydrogen Peroxide 134-148 superoxide dismutase 1 Homo sapiens 16-20 15000391-7 2004 Superoxide dismutase (SOD) increased NO accumulation, suggesting that endogenous NO may modulate the level of H2O2 by interacting with O2- in the HR lesion. Hydrogen Peroxide 110-114 superoxide dismutase 1 Homo sapiens 0-20 15544046-6 2004 Overexpression of human SOD1 in mouse NIH 3T3 fibroblasts increased SOD activity, enhanced intracellular generation of H2O2 and significantly stimulated VEGF production as determined by increase in VEGF promoter activity, VEGF mRNA expression and VEGF protein synthesis. Hydrogen Peroxide 119-123 superoxide dismutase 1 Homo sapiens 24-28 15544046-6 2004 Overexpression of human SOD1 in mouse NIH 3T3 fibroblasts increased SOD activity, enhanced intracellular generation of H2O2 and significantly stimulated VEGF production as determined by increase in VEGF promoter activity, VEGF mRNA expression and VEGF protein synthesis. Hydrogen Peroxide 119-123 superoxide dismutase 1 Homo sapiens 24-27 15129738-5 2004 For EPR, potassium superoxide (KO2) was used as a source of O2- where qualitative results suggested that CpCpx and AcylCpCpx were SOD mimics, which catalyze the conversion of O2- to dioxygen and hydrogen peroxide (H2O2). Hydrogen Peroxide 195-212 superoxide dismutase 1 Homo sapiens 130-133 15129738-5 2004 For EPR, potassium superoxide (KO2) was used as a source of O2- where qualitative results suggested that CpCpx and AcylCpCpx were SOD mimics, which catalyze the conversion of O2- to dioxygen and hydrogen peroxide (H2O2). Hydrogen Peroxide 214-218 superoxide dismutase 1 Homo sapiens 130-133 15086540-1 2004 Abnormal production of reactive oxygen species (ROS) induces tissue damage and superoxide dismutase (SOD) that converts superoxide radicals to hydrogen peroxide functions as defense against ROS. Hydrogen Peroxide 143-160 superoxide dismutase 1 Homo sapiens 79-99 15086540-1 2004 Abnormal production of reactive oxygen species (ROS) induces tissue damage and superoxide dismutase (SOD) that converts superoxide radicals to hydrogen peroxide functions as defense against ROS. Hydrogen Peroxide 143-160 superoxide dismutase 1 Homo sapiens 101-104 15000391-7 2004 Superoxide dismutase (SOD) increased NO accumulation, suggesting that endogenous NO may modulate the level of H2O2 by interacting with O2- in the HR lesion. Hydrogen Peroxide 110-114 superoxide dismutase 1 Homo sapiens 22-25 15388232-3 2004 When disassembled NF-L was incubated with Cu,Zn-SOD and H2O2, the aggregation of protein was proportional to the concentration of hydrogen peroxide. Hydrogen Peroxide 130-147 superoxide dismutase 1 Homo sapiens 48-51 15388232-4 2004 Cu,Zn-SOD/H2O2-mediated modification of NF-L was significantly inhibited by radical scavenger, spin trap agents and copper chelators. Hydrogen Peroxide 10-14 superoxide dismutase 1 Homo sapiens 6-9 15388232-5 2004 Dityrosine crosslink formation was obtained in Cu,Zn-SOD/H2O2-mediated NF-L aggregates. Hydrogen Peroxide 57-61 superoxide dismutase 1 Homo sapiens 53-56 15258675-4 2004 Based on our observation, it can be concluded that the defensive capacity of cells against H2O2 depends on the ratio between catalase/GPx/SOD and H2O2, especially at high-stress situations, and the intracellular balance of these enzymes are more important than the influence of the single component. Hydrogen Peroxide 91-95 superoxide dismutase 1 Homo sapiens 138-141 12686560-2 2003 Higher molecular weight species (apparent dimers and trimers) of hSOD1WT were formed from incubation mixtures containing hSOD1WT, H2O2, and HCO3-. Hydrogen Peroxide 130-134 superoxide dismutase 1 Homo sapiens 65-70 14717588-2 2004 The mechanism by which Cu,Zn-SOD/hydrogen peroxide/bicarbonate is able to oxidize substrates has been proposed to be dependent on an oxidant whose nature, diffusible carbonate radical anion or enzyme-bound peroxycarbonate, remains debatable. Hydrogen Peroxide 33-50 superoxide dismutase 1 Homo sapiens 23-32 12843619-10 2003 H(2)O(2)-induced cytotoxicity was completely blocked by catalase (CAT), while it was enhanced by superoxide dismutase (SOD). Hydrogen Peroxide 0-8 superoxide dismutase 1 Homo sapiens 97-117 12843619-10 2003 H(2)O(2)-induced cytotoxicity was completely blocked by catalase (CAT), while it was enhanced by superoxide dismutase (SOD). Hydrogen Peroxide 0-8 superoxide dismutase 1 Homo sapiens 119-122 14744629-5 2004 The results show that survival rates were increased in sod+ xth- nfo+ cells compared with sod- xth- ape-, sod- xth- ape-, and sod+ xth- ape- cells under oxidative stress generated with 0.1 mM paraquat or 3 mM H2O2. Hydrogen Peroxide 209-213 superoxide dismutase 1 Homo sapiens 55-58 14644319-2 2003 The immediate products of such reactions, superoxide anion radicals and hydrogen peroxide can be metabolised by enzymes such as superoxide dismutase (SOD) and catalase (CAT), respectively, and depending on its concentration by Vitamin C (Vit C). Hydrogen Peroxide 72-89 superoxide dismutase 1 Homo sapiens 128-148 14644319-2 2003 The immediate products of such reactions, superoxide anion radicals and hydrogen peroxide can be metabolised by enzymes such as superoxide dismutase (SOD) and catalase (CAT), respectively, and depending on its concentration by Vitamin C (Vit C). Hydrogen Peroxide 72-89 superoxide dismutase 1 Homo sapiens 150-153 14644319-8 2003 The variable responses with SOD indicate a lesser involvement of superoxide anion radicals due to SOD-mediated conversion of superoxide to hydrogen peroxide generally causing a lower level of DNA damage than other ROS. Hydrogen Peroxide 139-156 superoxide dismutase 1 Homo sapiens 28-31 14644319-8 2003 The variable responses with SOD indicate a lesser involvement of superoxide anion radicals due to SOD-mediated conversion of superoxide to hydrogen peroxide generally causing a lower level of DNA damage than other ROS. Hydrogen Peroxide 139-156 superoxide dismutase 1 Homo sapiens 98-101 12810837-2 2003 One of the major factors in the protection from superoxide anions is the enzyme superoxide dismutase (SOD), which catalyzes the dismutation of superoxide to hydrogen peroxide. Hydrogen Peroxide 157-174 superoxide dismutase 1 Homo sapiens 102-105 12686560-11 2003 Molecular oxygen was needed for HCO3-/H2O2-dependent aggregation of hSOD1WT, implicating a role for a Trp-32-dependent peroxidative reaction in the covalent aggregation of hSOD1WT. Hydrogen Peroxide 38-42 superoxide dismutase 1 Homo sapiens 68-73 12686560-11 2003 Molecular oxygen was needed for HCO3-/H2O2-dependent aggregation of hSOD1WT, implicating a role for a Trp-32-dependent peroxidative reaction in the covalent aggregation of hSOD1WT. Hydrogen Peroxide 38-42 superoxide dismutase 1 Homo sapiens 68-75 12686560-2 2003 Higher molecular weight species (apparent dimers and trimers) of hSOD1WT were formed from incubation mixtures containing hSOD1WT, H2O2, and HCO3-. Hydrogen Peroxide 130-134 superoxide dismutase 1 Homo sapiens 65-72 12649272-1 2003 Hydrogen peroxide can interact with the active site of copper-zinc superoxide dismutase (SOD1) to generate a powerful oxidant. Hydrogen Peroxide 0-17 superoxide dismutase 1 Homo sapiens 89-93 12770950-2 2003 2 SOD (200 U ml(-1)) increased the production of H(2)O(2) in smooth muscle cells (as indicated by the use of an H(2)O(2)-sensitive fluorescent dye). Hydrogen Peroxide 49-57 superoxide dismutase 1 Homo sapiens 2-5 12626432-7 2003 The mutated Cu, Zn-SOD incubated with glucose generated higher levels of hydrogen peroxide than the wild-type enzyme. Hydrogen Peroxide 73-90 superoxide dismutase 1 Homo sapiens 19-22 12496163-1 2003 Superoxide dismutase (SOD) is an enzyme that converts superoxide radicals into hydrogen peroxide and molecular oxygen and has been shown to contribute to the virulence of many human-pathogenic bacteria through its ability to neutralize toxic levels of reactive oxygen species generated by the host. Hydrogen Peroxide 79-96 superoxide dismutase 1 Homo sapiens 0-20 12551919-0 2003 Differential effects of superoxide dismutase isoform expression on hydroperoxide-induced apoptosis in PC-12 cells. Hydrogen Peroxide 67-80 superoxide dismutase 1 Homo sapiens 24-44 12496163-1 2003 Superoxide dismutase (SOD) is an enzyme that converts superoxide radicals into hydrogen peroxide and molecular oxygen and has been shown to contribute to the virulence of many human-pathogenic bacteria through its ability to neutralize toxic levels of reactive oxygen species generated by the host. Hydrogen Peroxide 79-96 superoxide dismutase 1 Homo sapiens 22-25 12437574-6 2002 Furthermore, the treatment of hSOD1-expressing cells with hydrogen peroxide promoted the oligomerization, and detergent-insolubility of mutant SOD1 alone, and the oxidized mutant SOD1 proteins were more heavily poly-ubiquitinated. Hydrogen Peroxide 58-75 superoxide dismutase 1 Homo sapiens 30-35 12184785-6 2002 SOD and catalase inhibited the DNA damage, suggesting that DNA damage involved superoxide anion and hydrogen peroxide. Hydrogen Peroxide 100-117 superoxide dismutase 1 Homo sapiens 0-16 12458889-8 2002 The authors speculate that in BD patients, serum superoxide radicals may be dismutated to H2O2 by increased CuZn-SOD activity and the conversion of H2O2 to hydroxyl radical may be enhanced by iron, owing to diminished serum Trf; these mechanisms may contribute to the increased serum lipid peroxidation. Hydrogen Peroxide 90-94 superoxide dismutase 1 Homo sapiens 108-116 13677623-14 2002 SOD converts O2*- to H2O2, which is further converted to H2O with the help of GPx and CAT. Hydrogen Peroxide 21-25 superoxide dismutase 1 Homo sapiens 0-3 12218958-3 2002 Superoxide dismutase (SOD) catalyzes the conversion of single electron reduced species of molecular oxygen to hydrogen peroxide and oxygen. Hydrogen Peroxide 110-127 superoxide dismutase 1 Homo sapiens 0-20 12218958-3 2002 Superoxide dismutase (SOD) catalyzes the conversion of single electron reduced species of molecular oxygen to hydrogen peroxide and oxygen. Hydrogen Peroxide 110-127 superoxide dismutase 1 Homo sapiens 22-25 12057773-0 2002 Why does SOD overexpression sometimes enhance, sometimes decrease, hydrogen peroxide production? Hydrogen Peroxide 67-84 superoxide dismutase 1 Homo sapiens 9-12 12057773-2 2002 Toxic effects of superoxide dismutase (SOD) overexpression are commonly attributed to increased hydrogen peroxide (H(2)O(2)) production. Hydrogen Peroxide 96-113 superoxide dismutase 1 Homo sapiens 17-37 12057773-2 2002 Toxic effects of superoxide dismutase (SOD) overexpression are commonly attributed to increased hydrogen peroxide (H(2)O(2)) production. Hydrogen Peroxide 96-113 superoxide dismutase 1 Homo sapiens 39-42 12057773-2 2002 Toxic effects of superoxide dismutase (SOD) overexpression are commonly attributed to increased hydrogen peroxide (H(2)O(2)) production. Hydrogen Peroxide 115-124 superoxide dismutase 1 Homo sapiens 17-37 12057773-2 2002 Toxic effects of superoxide dismutase (SOD) overexpression are commonly attributed to increased hydrogen peroxide (H(2)O(2)) production. Hydrogen Peroxide 115-124 superoxide dismutase 1 Homo sapiens 39-42 12057773-6 2002 Even within this simple framework, SOD overexpression may increase, hold constant, or decrease H(2)O(2) production. Hydrogen Peroxide 95-103 superoxide dismutase 1 Homo sapiens 35-38 12057773-8 2002 In cells or cellular compartments where this ratio is exceptionally low (< 1), a modest decrease in H(2)O(2) production upon SOD overexpression is expected. Hydrogen Peroxide 103-111 superoxide dismutase 1 Homo sapiens 128-131 12057773-9 2002 Where the ratio is higher than unity, H(2)O(2) production should increase, but at most linearly, with SOD activity. Hydrogen Peroxide 38-46 superoxide dismutase 1 Homo sapiens 102-105 12057773-11 2002 According to the minimal model, only where most superoxide is eliminated through H(2)O(2)-free processes does SOD activity have the moderately large influence on H(2)O(2) production observed in some experiments. Hydrogen Peroxide 81-89 superoxide dismutase 1 Homo sapiens 110-113 12057773-11 2002 According to the minimal model, only where most superoxide is eliminated through H(2)O(2)-free processes does SOD activity have the moderately large influence on H(2)O(2) production observed in some experiments. Hydrogen Peroxide 162-170 superoxide dismutase 1 Homo sapiens 110-113 12123083-1 2002 A superoxide dismutase (SOD)-modified electrode, in which SOD is oriented on the gold electrode via a self-assembled monolayer of cysteine so as to allow its direct electrode reaction, possesses a bi-directional electrocatalysis for both the oxidation of superoxide ion (O2-) to O2 and the reduction of O2- to H2O2 and functions as a third generation O2- biosensor. Hydrogen Peroxide 310-314 superoxide dismutase 1 Homo sapiens 2-22 12123083-1 2002 A superoxide dismutase (SOD)-modified electrode, in which SOD is oriented on the gold electrode via a self-assembled monolayer of cysteine so as to allow its direct electrode reaction, possesses a bi-directional electrocatalysis for both the oxidation of superoxide ion (O2-) to O2 and the reduction of O2- to H2O2 and functions as a third generation O2- biosensor. Hydrogen Peroxide 310-314 superoxide dismutase 1 Homo sapiens 24-27 12123083-1 2002 A superoxide dismutase (SOD)-modified electrode, in which SOD is oriented on the gold electrode via a self-assembled monolayer of cysteine so as to allow its direct electrode reaction, possesses a bi-directional electrocatalysis for both the oxidation of superoxide ion (O2-) to O2 and the reduction of O2- to H2O2 and functions as a third generation O2- biosensor. Hydrogen Peroxide 310-314 superoxide dismutase 1 Homo sapiens 58-61 11312732-3 2001 The complex M40403 was previously shown to be a superoxide dismutase (SOD) catalyst with rates for the catalytic dismutation of superoxide to oxygen and hydrogen peroxide at pH = 7.4 of 1.2 x 10(+7) M(-1) s(-1). Hydrogen Peroxide 153-170 superoxide dismutase 1 Homo sapiens 48-68 12038771-4 2002 At SOD/Cys/Au, O2- could be specifically oxidized and reduced to O2 and hydrogen peroxide, respectively, through the inherent catalytic reaction of SOD. Hydrogen Peroxide 72-89 superoxide dismutase 1 Homo sapiens 3-6 12038771-4 2002 At SOD/Cys/Au, O2- could be specifically oxidized and reduced to O2 and hydrogen peroxide, respectively, through the inherent catalytic reaction of SOD. Hydrogen Peroxide 72-89 superoxide dismutase 1 Homo sapiens 148-151 12060292-3 2001 Excess electrons from the photosynthetic and respiratory electron transport chains can be used for the reduction of oxygen, thus producing superoxide radicals (O2.-); these are subsequently transformed to H2O2 via superoxide dismutase (SOD; EC 1.15.1.1). Hydrogen Peroxide 205-209 superoxide dismutase 1 Homo sapiens 214-234 12060292-3 2001 Excess electrons from the photosynthetic and respiratory electron transport chains can be used for the reduction of oxygen, thus producing superoxide radicals (O2.-); these are subsequently transformed to H2O2 via superoxide dismutase (SOD; EC 1.15.1.1). Hydrogen Peroxide 205-209 superoxide dismutase 1 Homo sapiens 236-239 11461912-9 2001 Cu,Zn-SOD plus H(2)O(2) caused the HCO(3)(-)-dependent oxidation of DCF, casting doubt on the validity of using DCF oxidation as a reliable measure of intracellular H(2)O(2) production. Hydrogen Peroxide 165-173 superoxide dismutase 1 Homo sapiens 6-9 11461956-6 2001 Overexpression of either SOD1 mutant tended to increase levels of lipid peroxidation, protein carbonyls, and 3-nitrotyrosine and accelerated viability loss induced by serum withdrawal, H2O2 or HNE, accompanied by greater rises in oxidative damage parameters. Hydrogen Peroxide 185-189 superoxide dismutase 1 Homo sapiens 25-29 11461956-8 2001 By contrast, expression of wild-type SOD1 rendered cells more resistant to loss of viability induced by serum deprivation, HNE or H2O2. Hydrogen Peroxide 130-134 superoxide dismutase 1 Homo sapiens 37-41 11351106-11 2001 Simulated loss of SOD resulted in higher H2O2 production rates, thereby affecting all subsequent steps of the Asc-GSH-cycle. Hydrogen Peroxide 41-45 superoxide dismutase 1 Homo sapiens 18-21 11677273-9 2001 and the subsequently formed H(2)O(2) by superoxide dismutase (SOD) plus catalase likewise prevented the nitration of protein-bound tyrosine but actually enhanced the cytotoxicity of SIN-1, indicating that cortical cells can cope with the oxidative but not the nitrosative stress generated. Hydrogen Peroxide 28-36 superoxide dismutase 1 Homo sapiens 40-60 11677273-9 2001 and the subsequently formed H(2)O(2) by superoxide dismutase (SOD) plus catalase likewise prevented the nitration of protein-bound tyrosine but actually enhanced the cytotoxicity of SIN-1, indicating that cortical cells can cope with the oxidative but not the nitrosative stress generated. Hydrogen Peroxide 28-36 superoxide dismutase 1 Homo sapiens 62-65 11410240-6 2001 These findings suggest that FeMPy(4)P as SOD mimic converts intracellular O2(*-) to H(2)O(2) and that it rapidly reacts with H(2)O(2) to form *OH, causing DNA damage and inducing cell death. Hydrogen Peroxide 84-92 superoxide dismutase 1 Homo sapiens 41-44 11312732-3 2001 The complex M40403 was previously shown to be a superoxide dismutase (SOD) catalyst with rates for the catalytic dismutation of superoxide to oxygen and hydrogen peroxide at pH = 7.4 of 1.2 x 10(+7) M(-1) s(-1). Hydrogen Peroxide 153-170 superoxide dismutase 1 Homo sapiens 70-73 11245904-2 2001 Antioxidant enzymes, superoxide dismutases (SOD, converting superoxide anion into H2O2) and catalase (converting H2O2 into water), are candidate drugs for augmentation of antioxidant defenses in endothelium. Hydrogen Peroxide 82-86 superoxide dismutase 1 Homo sapiens 44-47 11246233-2 2001 Prior studies have shown, however, that SOD1 overexpression can reduce neuronal survival during exposure to superoxide generators by a mechanism involving excess H(2)O(2) accumulation. Hydrogen Peroxide 162-170 superoxide dismutase 1 Homo sapiens 40-44 11246233-7 2001 Surprisingly, increased survival in SOD1 overexpressing cultures remained evident even when H(2)O(2) catabolism was inhibited by preincubation with aminotriazole (to block catalase) and buthionine sulfoximine (to deplete glutathione). Hydrogen Peroxide 92-100 superoxide dismutase 1 Homo sapiens 36-40 11245904-2 2001 Antioxidant enzymes, superoxide dismutases (SOD, converting superoxide anion into H2O2) and catalase (converting H2O2 into water), are candidate drugs for augmentation of antioxidant defenses in endothelium. Hydrogen Peroxide 113-117 superoxide dismutase 1 Homo sapiens 44-47 15256925-4 2001 On the other hand, a significant improvement in sperm parameter recovery was seen in the aliquot with both SOD and catalase supplementation; perhaps because of their combined and simultaneous action on superoxide anion and hydrogen peroxide. Hydrogen Peroxide 223-240 superoxide dismutase 1 Homo sapiens 107-110 10574920-1 1999 Prior spin trapping studies reported that H(2)O(2) is metabolized by copper,zinc-superoxide dismutase (SOD) to form (. Hydrogen Peroxide 42-50 superoxide dismutase 1 Homo sapiens 69-101 11217146-1 2001 BACKGROUND: The antioxidant enzyme Cu/Zn-superoxide dismutase-1 (SOD1) gene is localized to chromosome 21q22.1 and catalyzes the dismutation of superoxide anions to hydrogen peroxide, which may lead to the increased production of active oxygen species in Down Syndrome (DS), trisomy 21. Hydrogen Peroxide 165-182 superoxide dismutase 1 Homo sapiens 35-63 11217146-1 2001 BACKGROUND: The antioxidant enzyme Cu/Zn-superoxide dismutase-1 (SOD1) gene is localized to chromosome 21q22.1 and catalyzes the dismutation of superoxide anions to hydrogen peroxide, which may lead to the increased production of active oxygen species in Down Syndrome (DS), trisomy 21. Hydrogen Peroxide 165-182 superoxide dismutase 1 Homo sapiens 65-69 10940382-0 2000 Nitric oxide protects Cu,Zn-superoxide dismutase from hydrogen peroxide-induced inactivation. Hydrogen Peroxide 54-71 superoxide dismutase 1 Homo sapiens 22-48 10940382-1 2000 Reaction of Cu,Zn-superoxide dismutase (SOD1) and hydrogen peroxide generates a putative oxidant SOD-Cu2+-.OH that can inactivate the enzyme and oxidize 5,5"-dimethyl-1-pyrroline-N-oxide (DMPO) to DMPO-.OH. Hydrogen Peroxide 50-67 superoxide dismutase 1 Homo sapiens 12-38 10940382-1 2000 Reaction of Cu,Zn-superoxide dismutase (SOD1) and hydrogen peroxide generates a putative oxidant SOD-Cu2+-.OH that can inactivate the enzyme and oxidize 5,5"-dimethyl-1-pyrroline-N-oxide (DMPO) to DMPO-.OH. Hydrogen Peroxide 50-67 superoxide dismutase 1 Homo sapiens 40-44 10940382-1 2000 Reaction of Cu,Zn-superoxide dismutase (SOD1) and hydrogen peroxide generates a putative oxidant SOD-Cu2+-.OH that can inactivate the enzyme and oxidize 5,5"-dimethyl-1-pyrroline-N-oxide (DMPO) to DMPO-.OH. Hydrogen Peroxide 50-67 superoxide dismutase 1 Homo sapiens 40-43 10940382-2 2000 In the presence of nitric oxide (.NO), the SOD1/H2O2 system is known to produce peroxynitrite (ONOO-). Hydrogen Peroxide 48-52 superoxide dismutase 1 Homo sapiens 43-47 10940382-7 2000 We propose that .NO protects SOD1 from H2O2-induced inactivation by reducing SOD-Cu2+.OH to the active SOD-Cu2+ with concomitant production of NO+ which reacts with H2O2 to give ONOO-. Hydrogen Peroxide 39-43 superoxide dismutase 1 Homo sapiens 29-33 10940382-7 2000 We propose that .NO protects SOD1 from H2O2-induced inactivation by reducing SOD-Cu2+.OH to the active SOD-Cu2+ with concomitant production of NO+ which reacts with H2O2 to give ONOO-. Hydrogen Peroxide 39-43 superoxide dismutase 1 Homo sapiens 29-32 10940382-7 2000 We propose that .NO protects SOD1 from H2O2-induced inactivation by reducing SOD-Cu2+.OH to the active SOD-Cu2+ with concomitant production of NO+ which reacts with H2O2 to give ONOO-. Hydrogen Peroxide 39-43 superoxide dismutase 1 Homo sapiens 77-80 10940382-7 2000 We propose that .NO protects SOD1 from H2O2-induced inactivation by reducing SOD-Cu2+.OH to the active SOD-Cu2+ with concomitant production of NO+ which reacts with H2O2 to give ONOO-. Hydrogen Peroxide 165-169 superoxide dismutase 1 Homo sapiens 29-33 10940382-7 2000 We propose that .NO protects SOD1 from H2O2-induced inactivation by reducing SOD-Cu2+.OH to the active SOD-Cu2+ with concomitant production of NO+ which reacts with H2O2 to give ONOO-. Hydrogen Peroxide 165-169 superoxide dismutase 1 Homo sapiens 29-32 10940382-7 2000 We propose that .NO protects SOD1 from H2O2-induced inactivation by reducing SOD-Cu2+.OH to the active SOD-Cu2+ with concomitant production of NO+ which reacts with H2O2 to give ONOO-. Hydrogen Peroxide 165-169 superoxide dismutase 1 Homo sapiens 77-80 10823352-2 2000 In these preparations, H2O2 (30 microM) induced a fast and transient contraction, which could be abolished by pretreatment of catalase (800 U/ml), but not affected by superoxide anion scavenger, superoxide dismutase (SOD; 150 U/ml) or the hydroxyl free radical scavenger, DMSO/mannitol (each 3 mM). Hydrogen Peroxide 23-27 superoxide dismutase 1 Homo sapiens 217-220 10898156-1 2000 A superoxide dismutase biosensor was used to determine the antioxidant properties of scavenger molecules and the antiradical activity of healthy and diseased human kidney tissues; this biosensor is based on the use of the enzyme superoxide dismutase (SOD), which is physically entrapped in a kappa-carrageenan gel membrane, and of a transducer consisting of an amperometric hydrogen peroxide electrode. Hydrogen Peroxide 374-391 superoxide dismutase 1 Homo sapiens 2-22 10898156-1 2000 A superoxide dismutase biosensor was used to determine the antioxidant properties of scavenger molecules and the antiradical activity of healthy and diseased human kidney tissues; this biosensor is based on the use of the enzyme superoxide dismutase (SOD), which is physically entrapped in a kappa-carrageenan gel membrane, and of a transducer consisting of an amperometric hydrogen peroxide electrode. Hydrogen Peroxide 374-391 superoxide dismutase 1 Homo sapiens 229-249 10898156-1 2000 A superoxide dismutase biosensor was used to determine the antioxidant properties of scavenger molecules and the antiradical activity of healthy and diseased human kidney tissues; this biosensor is based on the use of the enzyme superoxide dismutase (SOD), which is physically entrapped in a kappa-carrageenan gel membrane, and of a transducer consisting of an amperometric hydrogen peroxide electrode. Hydrogen Peroxide 374-391 superoxide dismutase 1 Homo sapiens 251-254 10930123-2 2000 Pyrogallol, a O2 generator and precursor of hydrogen peroxide (H2O2), had potent cytotoxic effects on the endothelial cells, but this effect was completely abolished by SOD/CAT. Hydrogen Peroxide 44-61 superoxide dismutase 1 Homo sapiens 169-172 10930123-2 2000 Pyrogallol, a O2 generator and precursor of hydrogen peroxide (H2O2), had potent cytotoxic effects on the endothelial cells, but this effect was completely abolished by SOD/CAT. Hydrogen Peroxide 63-67 superoxide dismutase 1 Homo sapiens 169-172 10574920-1 1999 Prior spin trapping studies reported that H(2)O(2) is metabolized by copper,zinc-superoxide dismutase (SOD) to form (. Hydrogen Peroxide 42-50 superoxide dismutase 1 Homo sapiens 103-106 10564779-0 1999 Hydrogen peroxide-mediated Cu,Zn-superoxide dismutase fragmentation: protection by carnosine, homocarnosine and anserine. Hydrogen Peroxide 0-17 superoxide dismutase 1 Homo sapiens 27-53 10705716-5 1999 The superoxide dismutase enzyme (SOD) catalyzes dismutation of the superoxide radical into hydrogen peroxide and oxygen hydrogen peroxide is in turn reduced to water and oxygen by peroxidase glutathione and catalase enzymes. Hydrogen Peroxide 91-108 superoxide dismutase 1 Homo sapiens 4-31 10705716-5 1999 The superoxide dismutase enzyme (SOD) catalyzes dismutation of the superoxide radical into hydrogen peroxide and oxygen hydrogen peroxide is in turn reduced to water and oxygen by peroxidase glutathione and catalase enzymes. Hydrogen Peroxide 91-108 superoxide dismutase 1 Homo sapiens 33-36 10705716-5 1999 The superoxide dismutase enzyme (SOD) catalyzes dismutation of the superoxide radical into hydrogen peroxide and oxygen hydrogen peroxide is in turn reduced to water and oxygen by peroxidase glutathione and catalase enzymes. Hydrogen Peroxide 120-137 superoxide dismutase 1 Homo sapiens 4-31 10705716-5 1999 The superoxide dismutase enzyme (SOD) catalyzes dismutation of the superoxide radical into hydrogen peroxide and oxygen hydrogen peroxide is in turn reduced to water and oxygen by peroxidase glutathione and catalase enzymes. Hydrogen Peroxide 120-137 superoxide dismutase 1 Homo sapiens 33-36 10564779-3 1999 These results suggested that *OH was implicated in the hydrogen peroxide-mediated Cu,Zn-SOD fragmentation. Hydrogen Peroxide 55-72 superoxide dismutase 1 Homo sapiens 88-91 10564779-5 1999 We investigated whether three compounds could protect the fragmentation of Cu,Zn-SOD induced by H(2)O(2). Hydrogen Peroxide 96-104 superoxide dismutase 1 Homo sapiens 81-84 10564779-9 1999 These results suggest that carnosine and related compounds can protect the hydrogen peroxide-mediated Cu,Zn-SOD fragmentation through the scavenging of *OH. Hydrogen Peroxide 75-92 superoxide dismutase 1 Homo sapiens 108-111 10440583-4 1999 Superoxide dismutase (SOD), but not catalase or sodium formate, inhibited this NF-kappaB activation, suggesting that O2*- rather than H2O2 or *OH, radicals play the most critical role in this induction. Hydrogen Peroxide 134-138 superoxide dismutase 1 Homo sapiens 0-20 10446418-8 1999 In order to apply a permanent H(2)O(2)-induced oxidative stress to astroglial cells the generation of H(2)O(2) by the coupled reactions of xanthine oxidase (XO) and superoxide dismutase (SOD) was studied and this system was applied to cultured astroglial cells. Hydrogen Peroxide 30-38 superoxide dismutase 1 Homo sapiens 165-185 10446418-8 1999 In order to apply a permanent H(2)O(2)-induced oxidative stress to astroglial cells the generation of H(2)O(2) by the coupled reactions of xanthine oxidase (XO) and superoxide dismutase (SOD) was studied and this system was applied to cultured astroglial cells. Hydrogen Peroxide 30-38 superoxide dismutase 1 Homo sapiens 187-190 10596413-3 1999 SOD and catalase catalyse the transformation of oxygen radicals and hydrogen peroxide to less toxic metabolites. Hydrogen Peroxide 68-85 superoxide dismutase 1 Homo sapiens 0-3 10493305-4 1999 SOD and catalase activities were determined by the spectrophotometric monitoring of the inhibition of pyrogallol autoxidation and the hydrogen peroxide decomposition rate, respectively. Hydrogen Peroxide 134-151 superoxide dismutase 1 Homo sapiens 0-3 10440583-4 1999 Superoxide dismutase (SOD), but not catalase or sodium formate, inhibited this NF-kappaB activation, suggesting that O2*- rather than H2O2 or *OH, radicals play the most critical role in this induction. Hydrogen Peroxide 134-138 superoxide dismutase 1 Homo sapiens 22-25 9817920-2 1998 About 20% of familial cases are associated with mutations in the gene for copper/zinc superoxide dismutase ( SOD1 ), which catalyses the dismutation of the superoxide radical to hydrogen peroxide and oxygen. Hydrogen Peroxide 178-195 superoxide dismutase 1 Homo sapiens 109-113 10343179-8 1999 Reminiscent of the data obtained from H2O2-treated tissues, hypothalami and NIL from SOD1 mutants displayed decreased cGMP accumulation and increased AVP release, compared with tissues from wild-type littermates. Hydrogen Peroxide 38-42 superoxide dismutase 1 Homo sapiens 85-89 10319417-1 1999 Cu,Zn-superoxide dismutase (SOD) can catalyze hydroxyl radical generation using H2O2 as a substrate. Hydrogen Peroxide 80-84 superoxide dismutase 1 Homo sapiens 0-26 10319417-1 1999 Cu,Zn-superoxide dismutase (SOD) can catalyze hydroxyl radical generation using H2O2 as a substrate. Hydrogen Peroxide 80-84 superoxide dismutase 1 Homo sapiens 28-31 10319417-6 1999 These results suggest that lipid peroxidation is mediated by the Cu,Zn-SOD and H2O2 system via the generation of hydroxyl radicals by a combination of the peroxidative reaction of Cu,Zn-SOD and the Fenton-like reaction of free copper released from oxidatively damaged SOD. Hydrogen Peroxide 79-83 superoxide dismutase 1 Homo sapiens 186-189 10319417-6 1999 These results suggest that lipid peroxidation is mediated by the Cu,Zn-SOD and H2O2 system via the generation of hydroxyl radicals by a combination of the peroxidative reaction of Cu,Zn-SOD and the Fenton-like reaction of free copper released from oxidatively damaged SOD. Hydrogen Peroxide 79-83 superoxide dismutase 1 Homo sapiens 186-189 9880490-1 1999 Cu,Zn-superoxide dismutase (SOD1) acts as a peroxidase in the presence of H2O2 at high pH (pH > 9). Hydrogen Peroxide 74-78 superoxide dismutase 1 Homo sapiens 28-32 9880490-3 1999 However, recent EPR studies of the enzyme performed in the physiological pH range 7.4-7.6 with the spin trap 5,5"-dimethyl-1-pyrolline-N-oxide attributed the intense EPR signal of 5, 5"-dimethyl-1-pyrolline-N-oxide-OH obtained from SOD1 and H2O2 to the peroxidase activity of the enzyme. Hydrogen Peroxide 241-245 superoxide dismutase 1 Homo sapiens 232-236 9789014-3 1998 We report in this study that lipid peroxidation of L-alpha-lecithin liposomes was enhanced greatly during the SOD/H2O2 reaction in the presence of nitrite anion (NO2-) with or without the metal ion chelator, diethylenetriaminepentacetic acid. Hydrogen Peroxide 114-118 superoxide dismutase 1 Homo sapiens 110-113 9796619-5 1998 The observations that both SOD and catalase reduced (in the case of LPC) or totally prevented (in the other cases) the acrosome reaction of capacitated spermatozoa and that hydrogen peroxide (H2O2) or ROS generated by the combination of xanthine and xanthine oxidase (O2.-, which dismutates to H2O2) triggered the acrosome reaction indicated the involvement of ROS in this process. Hydrogen Peroxide 173-190 superoxide dismutase 1 Homo sapiens 27-30 9789014-8 1998 NO2- inhibited H2O2-dependent inactivation of SOD. Hydrogen Peroxide 15-19 superoxide dismutase 1 Homo sapiens 46-49 9796619-5 1998 The observations that both SOD and catalase reduced (in the case of LPC) or totally prevented (in the other cases) the acrosome reaction of capacitated spermatozoa and that hydrogen peroxide (H2O2) or ROS generated by the combination of xanthine and xanthine oxidase (O2.-, which dismutates to H2O2) triggered the acrosome reaction indicated the involvement of ROS in this process. Hydrogen Peroxide 294-298 superoxide dismutase 1 Homo sapiens 27-30 9618471-0 1998 Reexamination of the mechanism of hydroxyl radical adducts formed from the reaction between familial amyotrophic lateral sclerosis-associated Cu,Zn superoxide dismutase mutants and H2O2. Hydrogen Peroxide 181-185 superoxide dismutase 1 Homo sapiens 148-168 9618471-2 1998 Mutations to Cu,Zn superoxide dismutase (SOD) linked with familial ALS are reported to increase hydroxyl radical adduct formation from hydrogen peroxide as measured by spin trapping with 5, 5"-dimethyl-1-pyrrolline N-oxide (DMPO). Hydrogen Peroxide 135-152 superoxide dismutase 1 Homo sapiens 19-39 9618471-2 1998 Mutations to Cu,Zn superoxide dismutase (SOD) linked with familial ALS are reported to increase hydroxyl radical adduct formation from hydrogen peroxide as measured by spin trapping with 5, 5"-dimethyl-1-pyrrolline N-oxide (DMPO). Hydrogen Peroxide 135-152 superoxide dismutase 1 Homo sapiens 41-44 9796506-3 1998 Superoxide dismutase (SOD) is responsible for the dismutation of the superoxide radicals into hydrogen peroxide and molecular oxygen. Hydrogen Peroxide 94-111 superoxide dismutase 1 Homo sapiens 0-20 9796506-3 1998 Superoxide dismutase (SOD) is responsible for the dismutation of the superoxide radicals into hydrogen peroxide and molecular oxygen. Hydrogen Peroxide 94-111 superoxide dismutase 1 Homo sapiens 22-25 9345297-6 1997 It is reasonable to postulate that the thyroidal SOD in homeotherms serves a dual role, firstly as a strategic antioxidant enzyme to protect the thyroid gland against the degenerative influence of toxic oxyradicals and secondly to provide H2O2 for thyroid hormone biosynthesis. Hydrogen Peroxide 239-243 superoxide dismutase 1 Homo sapiens 49-52 9422377-5 1998 Catalase effectively reduced C-DCDHF-DA but not HEt fluorescence, whereas SOD reduced HEt but not C-DCDHF-DA fluorescence, indicating that HEt and C-DCDHF-DA fluorescence correlated with O2- and hydrogen peroxide, respectively. Hydrogen Peroxide 195-212 superoxide dismutase 1 Homo sapiens 74-77 9473738-1 1997 We investigated the generation of nitric oxide (NO) by H2O2-dependent peroxidation of hydroxyurea in the presence of copper-containing proteins such as Cu,Zn-superoxide dismutase (Cu,Zn-SOD) or ceruloplasmin as a catalyst. Hydrogen Peroxide 55-59 superoxide dismutase 1 Homo sapiens 152-178 9473738-5 1997 ESR spin trapping with 5,5-dimethyl-1-pyrroline N-oxide (DMPO) showed hydroxy radical (OH) generation in the reaction of H2O2 with either Cu,Zn-SOD or ceruloplasmin. Hydrogen Peroxide 121-125 superoxide dismutase 1 Homo sapiens 138-147 9473738-8 1997 Incubation of hydroxyurea and Cu,Zn-SOD with xanthine oxidase and hypoxanthine in a system forming O2- -->H2O2 also resulted in appreciable NO production. Hydrogen Peroxide 109-113 superoxide dismutase 1 Homo sapiens 30-39 9618471-8 1998 Contrary to earlier reports, the present results indicate that a significant fraction of DMPO/.OH formed during the reaction of SOD and familial ALS SOD mutants with H2O2 is derived from the incorporation of oxygen from water due to oxidation of DMPO to DMPO/.OH presumably via DMPO radical cation. Hydrogen Peroxide 166-170 superoxide dismutase 1 Homo sapiens 128-131 9546325-5 1998 In addition, SOD1-FALS fibroblasts were more sensitive to H2O2 than SALS fibroblasts and than fibroblasts of controls. Hydrogen Peroxide 58-62 superoxide dismutase 1 Homo sapiens 13-17 9546325-6 1998 These results suggest that the mechanism underlying both SOD1-FALS and SALS jeopardizes the cell"s defense against free radical stress, and that SOD1-FALS cells are particularly sensitive to H2O2. Hydrogen Peroxide 191-195 superoxide dismutase 1 Homo sapiens 145-149 9509420-1 1997 To study the catalytic activity of Cu,Zn-superoxide dismutase (SOD) in the generation of hydroxyl radical (.OH) from H2O2, we investigated the mechanism of DNA cleavage mediated by human Cu,Zn-SOD and H2O2. Hydrogen Peroxide 117-121 superoxide dismutase 1 Homo sapiens 35-61 9509420-1 1997 To study the catalytic activity of Cu,Zn-superoxide dismutase (SOD) in the generation of hydroxyl radical (.OH) from H2O2, we investigated the mechanism of DNA cleavage mediated by human Cu,Zn-SOD and H2O2. Hydrogen Peroxide 117-121 superoxide dismutase 1 Homo sapiens 63-66 9509420-1 1997 To study the catalytic activity of Cu,Zn-superoxide dismutase (SOD) in the generation of hydroxyl radical (.OH) from H2O2, we investigated the mechanism of DNA cleavage mediated by human Cu,Zn-SOD and H2O2. Hydrogen Peroxide 201-205 superoxide dismutase 1 Homo sapiens 35-61 9509420-1 1997 To study the catalytic activity of Cu,Zn-superoxide dismutase (SOD) in the generation of hydroxyl radical (.OH) from H2O2, we investigated the mechanism of DNA cleavage mediated by human Cu,Zn-SOD and H2O2. Hydrogen Peroxide 201-205 superoxide dismutase 1 Homo sapiens 63-66 9509420-3 1997 A spectrophotometric study using a 2,2"-azinobis-(3-ethylbenzthiazoline-6-sulfonate) (ABTS) showed that free .OH formation was proportional to concentrations of Cu,Zn-SOD and H2O2. Hydrogen Peroxide 175-179 superoxide dismutase 1 Homo sapiens 167-170 9509420-5 1997 These results indicated that .OH generated early in the peroxidative reaction of Cu,Zn-SOD with H2O2 was implicated in DNA cleavage. Hydrogen Peroxide 96-100 superoxide dismutase 1 Homo sapiens 87-90 9509420-6 1997 Incubation with H2O2 resulted in a time-dependent release of copper ions from the Cu,Zn-SOD molecule. Hydrogen Peroxide 16-20 superoxide dismutase 1 Homo sapiens 88-91 9509420-8 1997 Evidence that DTPA protected the DNA cleavage induced by the Cu,Zn-SOD/H2O2 system supports this mechanism. Hydrogen Peroxide 71-75 superoxide dismutase 1 Homo sapiens 67-70 9509420-9 1997 We suggest that DNA cleavage is mediated in the Cu,Zn-SOD/H2O2 system via the generation of .OH by a combination of the peroxidative reaction of Cu,Zn-SOD and the Fenton-like reaction of free copper ions released from oxidatively damaged SOD. Hydrogen Peroxide 58-62 superoxide dismutase 1 Homo sapiens 54-57 9509420-9 1997 We suggest that DNA cleavage is mediated in the Cu,Zn-SOD/H2O2 system via the generation of .OH by a combination of the peroxidative reaction of Cu,Zn-SOD and the Fenton-like reaction of free copper ions released from oxidatively damaged SOD. Hydrogen Peroxide 58-62 superoxide dismutase 1 Homo sapiens 151-154 9509420-9 1997 We suggest that DNA cleavage is mediated in the Cu,Zn-SOD/H2O2 system via the generation of .OH by a combination of the peroxidative reaction of Cu,Zn-SOD and the Fenton-like reaction of free copper ions released from oxidatively damaged SOD. Hydrogen Peroxide 58-62 superoxide dismutase 1 Homo sapiens 151-154 9294870-1 1997 Key charged residues in Cu,Zn superoxide dismutase (Cu,Zn SOD) promote electrostatic steering of the superoxide substrate to the active site Cu ion, resulting in dismutation of superoxide to oxygen and hydrogen peroxide, Lys-136, along with the adjacent residues Glu-132 and Glu-133, forms a proposed electrostatic triad contributing to substrate recognition. Hydrogen Peroxide 202-219 superoxide dismutase 1 Homo sapiens 24-50 9357549-7 1997 When compared with the non-enzyme protein, bovine serum albumin (BSA), SOD had a protective effect against BT, H2O2 and BLM; in the presence of GSH, SOD diminished the effect of HQ, BQ and Vit C but enhanced the effect of BT, H2O2 and BLM. Hydrogen Peroxide 111-115 superoxide dismutase 1 Homo sapiens 71-74 9357549-7 1997 When compared with the non-enzyme protein, bovine serum albumin (BSA), SOD had a protective effect against BT, H2O2 and BLM; in the presence of GSH, SOD diminished the effect of HQ, BQ and Vit C but enhanced the effect of BT, H2O2 and BLM. Hydrogen Peroxide 226-230 superoxide dismutase 1 Homo sapiens 149-152 9357549-8 1997 With both GSH and Fe and compared with BSA, SOD enhanced the effect of HQ, BQ and BLM, ameliorated the effect of H2O2, and did not affect the others. Hydrogen Peroxide 113-117 superoxide dismutase 1 Homo sapiens 44-47 9360150-10 1997 With cuprophan, instead the reduced SOD/catalase ratio causes a greater H2O2 generation and a lower conversion to water. Hydrogen Peroxide 72-76 superoxide dismutase 1 Homo sapiens 36-39 9339903-1 1997 We investigated the fragmentation of human Cu,Zn-superoxide dismutase (SOD) by H2O2. Hydrogen Peroxide 79-83 superoxide dismutase 1 Homo sapiens 43-69 9339903-1 1997 We investigated the fragmentation of human Cu,Zn-superoxide dismutase (SOD) by H2O2. Hydrogen Peroxide 79-83 superoxide dismutase 1 Homo sapiens 71-74 9339903-2 1997 When Cu,Zn-SOD was incubated with H2O2, the fragmentation of protein proceeded rapidly within 1 min. Hydrogen Peroxide 34-38 superoxide dismutase 1 Homo sapiens 11-14 9339903-3 1997 The amounts of .OH radical formed in the Cu,Zn-SOD/H2O2 system reached a maximum in about 3 min. Hydrogen Peroxide 51-55 superoxide dismutase 1 Homo sapiens 47-50 9339903-5 1997 Copper ions released from Cu,Zn-SOD were gradually increased up to 30 min after starting the incubation with H2O2 in a time-dependent manner. Hydrogen Peroxide 109-113 superoxide dismutase 1 Homo sapiens 32-35 9339903-7 1997 The results suggested that the fragmentation of Cu,Zn-SOD by H2O2 was due to the peroxidative reaction of SOD rather than the Fenton-like reaction by free copper released from oxidatively damaged SOD. Hydrogen Peroxide 61-65 superoxide dismutase 1 Homo sapiens 54-57 9339903-7 1997 The results suggested that the fragmentation of Cu,Zn-SOD by H2O2 was due to the peroxidative reaction of SOD rather than the Fenton-like reaction by free copper released from oxidatively damaged SOD. Hydrogen Peroxide 61-65 superoxide dismutase 1 Homo sapiens 106-109 9339903-7 1997 The results suggested that the fragmentation of Cu,Zn-SOD by H2O2 was due to the peroxidative reaction of SOD rather than the Fenton-like reaction by free copper released from oxidatively damaged SOD. Hydrogen Peroxide 61-65 superoxide dismutase 1 Homo sapiens 106-109 9344593-7 1997 Measurements of ROS production during PH indicate that overexpression of SOD leads to the decreased production of O2- and elevation of H2O2. Hydrogen Peroxide 135-139 superoxide dismutase 1 Homo sapiens 73-76 9375974-10 1997 Superoxide dismutase (SOD), which catalyzes the conversion of superoxide anion to H2O2 had no significant effect on LTB4 production by human neutrophils. Hydrogen Peroxide 82-86 superoxide dismutase 1 Homo sapiens 0-20 9375974-10 1997 Superoxide dismutase (SOD), which catalyzes the conversion of superoxide anion to H2O2 had no significant effect on LTB4 production by human neutrophils. Hydrogen Peroxide 82-86 superoxide dismutase 1 Homo sapiens 22-25 9339903-10 1997 Thus we conclude that the fragmentation of Cu,Zn-SOD by H2O2, is due to the oxidative damage resulting from free .OH radicals generated by the peroxidative reaction of SOD. Hydrogen Peroxide 56-60 superoxide dismutase 1 Homo sapiens 49-52 9339903-10 1997 Thus we conclude that the fragmentation of Cu,Zn-SOD by H2O2, is due to the oxidative damage resulting from free .OH radicals generated by the peroxidative reaction of SOD. Hydrogen Peroxide 56-60 superoxide dismutase 1 Homo sapiens 168-171 9294870-1 1997 Key charged residues in Cu,Zn superoxide dismutase (Cu,Zn SOD) promote electrostatic steering of the superoxide substrate to the active site Cu ion, resulting in dismutation of superoxide to oxygen and hydrogen peroxide, Lys-136, along with the adjacent residues Glu-132 and Glu-133, forms a proposed electrostatic triad contributing to substrate recognition. Hydrogen Peroxide 202-219 superoxide dismutase 1 Homo sapiens 52-61 22062129-6 1997 Using the sensitive test with cyanide and hydrogen peroxide, the acrylamide gel of the SOD showed this enzyme was of the Cu Zn type. Hydrogen Peroxide 42-59 superoxide dismutase 1 Homo sapiens 87-90 9223111-1 1997 The human Cu/Zn superoxide dismutase (hSOD-1) gene, catalyses the dismutation of O2 to H2O2 and O2. Hydrogen Peroxide 87-91 superoxide dismutase 1 Homo sapiens 10-36 9223111-1 1997 The human Cu/Zn superoxide dismutase (hSOD-1) gene, catalyses the dismutation of O2 to H2O2 and O2. Hydrogen Peroxide 87-91 superoxide dismutase 1 Homo sapiens 38-44 9237246-10 1997 The variability arises from the variability in SOD activity: all H2O2 produced is from O2- due to the action of SOD. Hydrogen Peroxide 65-69 superoxide dismutase 1 Homo sapiens 47-50 9237246-10 1997 The variability arises from the variability in SOD activity: all H2O2 produced is from O2- due to the action of SOD. Hydrogen Peroxide 65-69 superoxide dismutase 1 Homo sapiens 112-115 9085276-1 1997 In addition to the usual superoxide dismutation activity, Cu,Zn-superoxide dismutase (SOD) has a peroxidative function that utilizes its own dismutation product, H2O2 as a substrate. Hydrogen Peroxide 162-166 superoxide dismutase 1 Homo sapiens 58-84 9085276-1 1997 In addition to the usual superoxide dismutation activity, Cu,Zn-superoxide dismutase (SOD) has a peroxidative function that utilizes its own dismutation product, H2O2 as a substrate. Hydrogen Peroxide 162-166 superoxide dismutase 1 Homo sapiens 86-89 9413891-3 1997 Superoxide dismutase (SOD), a primary antioxidant, accelerates the dismutation of the toxic superoxide radical produced during the oxidative energy processes into the less harmful molecules, hydrogen peroxide and molecular oxygen. Hydrogen Peroxide 191-208 superoxide dismutase 1 Homo sapiens 0-20 9020024-7 1997 The addition of SOD exacerbated but that of catalase attenuated peroxynitrite-induced DNA fragmentation, suggesting that this H2O2 production contributes to the apoptotic process. Hydrogen Peroxide 126-130 superoxide dismutase 1 Homo sapiens 16-19 9383636-4 1997 produce hydrogen peroxide (H2O2) by the action of superoxide dismutase (SOD). Hydrogen Peroxide 8-25 superoxide dismutase 1 Homo sapiens 50-70 9383636-4 1997 produce hydrogen peroxide (H2O2) by the action of superoxide dismutase (SOD). Hydrogen Peroxide 8-25 superoxide dismutase 1 Homo sapiens 72-75 9383636-4 1997 produce hydrogen peroxide (H2O2) by the action of superoxide dismutase (SOD). Hydrogen Peroxide 27-31 superoxide dismutase 1 Homo sapiens 50-70 9383636-4 1997 produce hydrogen peroxide (H2O2) by the action of superoxide dismutase (SOD). Hydrogen Peroxide 27-31 superoxide dismutase 1 Homo sapiens 72-75 9006926-10 1997 In the presence of Cu,Zn-superoxide dismutase, the reaction of .NO with cysteine generates hydrogen peroxide, indicating that the reaction generates O-2. Hydrogen Peroxide 91-108 superoxide dismutase 1 Homo sapiens 19-45 27396880-0 1997 Superoxide Dismutase Inhibition of Oxidation of Ubiquinol and Concomitant Formation of Hydrogen Peroxide. Hydrogen Peroxide 87-104 superoxide dismutase 1 Homo sapiens 0-20 27396880-2 1997 We found that copper-zinc superoxide dismutase and manganese superoxide dismutase inhibited both the CoQ0 formation and the H2O2 formation only in the presence of chelators such as DTPA (diethylenetriaminepentaacetic acid). Hydrogen Peroxide 124-128 superoxide dismutase 1 Homo sapiens 26-46 27396880-2 1997 We found that copper-zinc superoxide dismutase and manganese superoxide dismutase inhibited both the CoQ0 formation and the H2O2 formation only in the presence of chelators such as DTPA (diethylenetriaminepentaacetic acid). Hydrogen Peroxide 124-128 superoxide dismutase 1 Homo sapiens 61-81 9413891-3 1997 Superoxide dismutase (SOD), a primary antioxidant, accelerates the dismutation of the toxic superoxide radical produced during the oxidative energy processes into the less harmful molecules, hydrogen peroxide and molecular oxygen. Hydrogen Peroxide 191-208 superoxide dismutase 1 Homo sapiens 22-25 8724785-6 1996 The reciprocal action of catalase and SOD on their operational stabilities in enzymatic reactions of H2O2 decomposition is discussed. Hydrogen Peroxide 101-105 superoxide dismutase 1 Homo sapiens 38-41 27406670-9 1996 The generation of hydrogen peroxide was increased by low pH (pH 6.25) with lgG-1 but reduced with Cu-Zn SOD. Hydrogen Peroxide 18-35 superoxide dismutase 1 Homo sapiens 104-107 8858989-10 1996 Moreover, the inactivation rate of Suc-ker-SOD by H2O2 was less than those of native SOD and polyethylene glycol-conjugated SOD. Hydrogen Peroxide 50-54 superoxide dismutase 1 Homo sapiens 43-46 8858989-11 1996 The effect of H2O2 on liganded Cu++ in the active site of Suc-ker-SOD was much less than those of other SOD derivatives. Hydrogen Peroxide 14-18 superoxide dismutase 1 Homo sapiens 66-69 8806769-6 1996 Peroxynitrite-induced LCL was 80 and 55% inhibitable by SOD and catalase, respectively, showing that there were O2.- and H2O2-dependent routes of chemiexcitation. Hydrogen Peroxide 121-125 superoxide dismutase 1 Homo sapiens 56-59 8925565-3 1996 to hydrogen peroxide by the enzyme superoxide dismutase (SOD). Hydrogen Peroxide 3-20 superoxide dismutase 1 Homo sapiens 35-55 8925565-3 1996 to hydrogen peroxide by the enzyme superoxide dismutase (SOD). Hydrogen Peroxide 3-20 superoxide dismutase 1 Homo sapiens 57-60 8932447-1 1996 PURPOSE: Superoxide dismutase (SOD), an antioxidant enzyme, converts peroxide radicals into hydrogen peroxide. Hydrogen Peroxide 92-109 superoxide dismutase 1 Homo sapiens 9-29 8824885-2 1996 In this study we investigate the effects of a perturbation in the ratio of Cu/Zn-superoxide dismutase activity (Sod1 dismutases .O2-to H2O2) to glutathione peroxidase activity (Gpx1 catalyses H2O2 conversion to H2O) on cell growth and development. Hydrogen Peroxide 135-139 superoxide dismutase 1 Homo sapiens 75-101 8824885-2 1996 In this study we investigate the effects of a perturbation in the ratio of Cu/Zn-superoxide dismutase activity (Sod1 dismutases .O2-to H2O2) to glutathione peroxidase activity (Gpx1 catalyses H2O2 conversion to H2O) on cell growth and development. Hydrogen Peroxide 135-139 superoxide dismutase 1 Homo sapiens 112-116 8824885-2 1996 In this study we investigate the effects of a perturbation in the ratio of Cu/Zn-superoxide dismutase activity (Sod1 dismutases .O2-to H2O2) to glutathione peroxidase activity (Gpx1 catalyses H2O2 conversion to H2O) on cell growth and development. Hydrogen Peroxide 192-196 superoxide dismutase 1 Homo sapiens 75-101 8824885-2 1996 In this study we investigate the effects of a perturbation in the ratio of Cu/Zn-superoxide dismutase activity (Sod1 dismutases .O2-to H2O2) to glutathione peroxidase activity (Gpx1 catalyses H2O2 conversion to H2O) on cell growth and development. Hydrogen Peroxide 192-196 superoxide dismutase 1 Homo sapiens 112-116 8824885-3 1996 Our data demonstrate that Sod1 transfected cell lines that have an elevation in the ratio of Sod1 activity to Gpx1 activity produce higher levels of H2O2 and exhibit well characterised markers of cellular senescence viz. Hydrogen Peroxide 149-153 superoxide dismutase 1 Homo sapiens 26-30 8824885-3 1996 Our data demonstrate that Sod1 transfected cell lines that have an elevation in the ratio of Sod1 activity to Gpx1 activity produce higher levels of H2O2 and exhibit well characterised markers of cellular senescence viz. Hydrogen Peroxide 149-153 superoxide dismutase 1 Homo sapiens 93-97 8824885-5 1996 On the contrary, Sod1 transfected cell lines that have an unaltered ratio in the activity of these two enzymes, have unaltered levels of H2O2 and fail to show characteristics of senescence. Hydrogen Peroxide 137-141 superoxide dismutase 1 Homo sapiens 17-21 8824885-0 1996 Elevation in the ratio of Cu/Zn-superoxide dismutase to glutathione peroxidase activity induces features of cellular senescence and this effect is mediated by hydrogen peroxide. Hydrogen Peroxide 159-176 superoxide dismutase 1 Homo sapiens 26-52 8932447-1 1996 PURPOSE: Superoxide dismutase (SOD), an antioxidant enzyme, converts peroxide radicals into hydrogen peroxide. Hydrogen Peroxide 92-109 superoxide dismutase 1 Homo sapiens 31-34 7488137-1 1995 We established an effective monoepoxide-generating system by combining cytochrome-c (Cyt-c) with a hydrogen peroxide (H2O2)-generating system comprising hypoxanthine (HX), xanthine oxidase (XO) and superoxide dismutase (SOD; HX-XO-SOD-Cyt-c system). Hydrogen Peroxide 99-116 superoxide dismutase 1 Homo sapiens 198-218 8886800-5 1996 We conclude that while SOD may play a physiological role in maintaining a balance between O2.- and H2O2, high levels of this enzyme are associated with impaired sperm function because (a) the human spermatozoon is highly susceptible to the cytotoxic effects of H2O2, (b) O2.- is an important mediator of normal sperm function, and (c) high SOD activities reflect errors in spermatogenesis associated with germ cell exfoliation and the retention of excess residual cytoplasm by the spermatozoa. Hydrogen Peroxide 99-103 superoxide dismutase 1 Homo sapiens 23-26 8886800-5 1996 We conclude that while SOD may play a physiological role in maintaining a balance between O2.- and H2O2, high levels of this enzyme are associated with impaired sperm function because (a) the human spermatozoon is highly susceptible to the cytotoxic effects of H2O2, (b) O2.- is an important mediator of normal sperm function, and (c) high SOD activities reflect errors in spermatogenesis associated with germ cell exfoliation and the retention of excess residual cytoplasm by the spermatozoa. Hydrogen Peroxide 261-265 superoxide dismutase 1 Homo sapiens 23-26 7488137-1 1995 We established an effective monoepoxide-generating system by combining cytochrome-c (Cyt-c) with a hydrogen peroxide (H2O2)-generating system comprising hypoxanthine (HX), xanthine oxidase (XO) and superoxide dismutase (SOD; HX-XO-SOD-Cyt-c system). Hydrogen Peroxide 99-116 superoxide dismutase 1 Homo sapiens 220-223 7488137-1 1995 We established an effective monoepoxide-generating system by combining cytochrome-c (Cyt-c) with a hydrogen peroxide (H2O2)-generating system comprising hypoxanthine (HX), xanthine oxidase (XO) and superoxide dismutase (SOD; HX-XO-SOD-Cyt-c system). Hydrogen Peroxide 99-116 superoxide dismutase 1 Homo sapiens 231-234 7488137-1 1995 We established an effective monoepoxide-generating system by combining cytochrome-c (Cyt-c) with a hydrogen peroxide (H2O2)-generating system comprising hypoxanthine (HX), xanthine oxidase (XO) and superoxide dismutase (SOD; HX-XO-SOD-Cyt-c system). Hydrogen Peroxide 118-122 superoxide dismutase 1 Homo sapiens 198-218 7488137-1 1995 We established an effective monoepoxide-generating system by combining cytochrome-c (Cyt-c) with a hydrogen peroxide (H2O2)-generating system comprising hypoxanthine (HX), xanthine oxidase (XO) and superoxide dismutase (SOD; HX-XO-SOD-Cyt-c system). Hydrogen Peroxide 118-122 superoxide dismutase 1 Homo sapiens 220-223 7488137-1 1995 We established an effective monoepoxide-generating system by combining cytochrome-c (Cyt-c) with a hydrogen peroxide (H2O2)-generating system comprising hypoxanthine (HX), xanthine oxidase (XO) and superoxide dismutase (SOD; HX-XO-SOD-Cyt-c system). Hydrogen Peroxide 118-122 superoxide dismutase 1 Homo sapiens 231-234 7673115-12 1995 In contrast, Cu,Zn-SOD increased H2O2 accumulation from SIN-1 at low but not high concentrations of the enzyme, suggesting that high concentrations of the Cu,Zn-SOD interacted with the H2O2. Hydrogen Peroxide 33-37 superoxide dismutase 1 Homo sapiens 19-22 7673115-12 1995 In contrast, Cu,Zn-SOD increased H2O2 accumulation from SIN-1 at low but not high concentrations of the enzyme, suggesting that high concentrations of the Cu,Zn-SOD interacted with the H2O2. Hydrogen Peroxide 33-37 superoxide dismutase 1 Homo sapiens 161-164 7673115-12 1995 In contrast, Cu,Zn-SOD increased H2O2 accumulation from SIN-1 at low but not high concentrations of the enzyme, suggesting that high concentrations of the Cu,Zn-SOD interacted with the H2O2. Hydrogen Peroxide 185-189 superoxide dismutase 1 Homo sapiens 19-22 7673115-12 1995 In contrast, Cu,Zn-SOD increased H2O2 accumulation from SIN-1 at low but not high concentrations of the enzyme, suggesting that high concentrations of the Cu,Zn-SOD interacted with the H2O2. Hydrogen Peroxide 185-189 superoxide dismutase 1 Homo sapiens 161-164 7673115-13 1995 EPR spin trapping studies demonstrated the formation of hydroxyl radical from the decomposition of H2O2 by high concentrations of the Cu,Zn-SOD. Hydrogen Peroxide 99-103 superoxide dismutase 1 Homo sapiens 140-143 7673115-17 1995 These results suggest that the potentiation of SIN-1 toxicity by SOD is due to enhanced production of H2O2, followed by site-specific damage of critical cellular sites by a transition metal-catalyzed reaction. Hydrogen Peroxide 102-106 superoxide dismutase 1 Homo sapiens 65-68 7673115-18 1995 These results also emphasize that the role of SOD as a protectant against oxidant damage is complex and dependent, in part, on the subsequent fate and reactivity of the generated H2O2. Hydrogen Peroxide 179-183 superoxide dismutase 1 Homo sapiens 46-49 7670947-8 1995 In the absence of paracetamol, SOD and catalase inhibited the modification of LDL (P < .05), suggesting that superoxide anions and hydrogen peroxide might be involved in the cell-mediated modification pathway. Hydrogen Peroxide 134-151 superoxide dismutase 1 Homo sapiens 31-34 7638274-5 1995 The UVA-dependent H2O2 formation was increased 50% by superoxide dismutase (SOD) and abolished by catalase, arguing for the initial generation of superoxide anion. Hydrogen Peroxide 18-22 superoxide dismutase 1 Homo sapiens 76-79 7814447-4 1995 The [Ca2+]i response to X-XO was essentially diminished by superoxide dismutase (SOD) (200 U/ml) and catalase (CAT) (200 U/ml), which scavenge the superoxide anion, O2-, or H2O2, respectively. Hydrogen Peroxide 173-177 superoxide dismutase 1 Homo sapiens 59-79 7814447-4 1995 The [Ca2+]i response to X-XO was essentially diminished by superoxide dismutase (SOD) (200 U/ml) and catalase (CAT) (200 U/ml), which scavenge the superoxide anion, O2-, or H2O2, respectively. Hydrogen Peroxide 173-177 superoxide dismutase 1 Homo sapiens 81-84 7814447-5 1995 The [Ca2+]i increase stimulated by 10 nmol H2O2/ml/min, generated from the glucose-glucose oxidase system, or 10 microM H2O2, given as bolus, was about a third of that induced by X-XO (10 nmol O2-/ml/min) but was comparable to that induced by X-XO in the presence of SOD. Hydrogen Peroxide 43-47 superoxide dismutase 1 Homo sapiens 267-270 7814447-5 1995 The [Ca2+]i increase stimulated by 10 nmol H2O2/ml/min, generated from the glucose-glucose oxidase system, or 10 microM H2O2, given as bolus, was about a third of that induced by X-XO (10 nmol O2-/ml/min) but was comparable to that induced by X-XO in the presence of SOD. Hydrogen Peroxide 120-124 superoxide dismutase 1 Homo sapiens 267-270 7998936-2 1994 Released Cu2+ from the glycated Cu,Zn-SOD probably facilitates a Fenton reaction to convert H2O2 into hydroxy radical, which then participates in the non-specific fragmentation [Ookawara et al. Hydrogen Peroxide 92-96 superoxide dismutase 1 Homo sapiens 32-41 7604223-1 1995 Exposure of cupro-zinc superoxide dismutase (SOD) to hydrogen peroxide or ascorbate-Fe(III) gives rise to the extensively oxidative modification of SOD. Hydrogen Peroxide 53-70 superoxide dismutase 1 Homo sapiens 45-48 7604223-1 1995 Exposure of cupro-zinc superoxide dismutase (SOD) to hydrogen peroxide or ascorbate-Fe(III) gives rise to the extensively oxidative modification of SOD. Hydrogen Peroxide 53-70 superoxide dismutase 1 Homo sapiens 148-151 7998936-14 1994 These results suggest that hydroxy radical is produced through a Fenton reaction by Cu2+ and H2O2 released from the glycated Cu,Zn-SOD, and participates in nuclear DNA cleavage. Hydrogen Peroxide 93-97 superoxide dismutase 1 Homo sapiens 125-134 8031841-7 1994 Elimination of the effects of superoxide radicals, manganese and H2O2 on autoxidation of hydroquinone by addition of SOD, catalase and DETAPAC to the incubation mixture resulted in a 79% inhibition of NADH oxidation, suggesting that 21% of the autoxidation is oxygen-dependent. Hydrogen Peroxide 65-69 superoxide dismutase 1 Homo sapiens 117-120 7850993-3 1994 However, Cu,Zn-SOD can increase intra- and extracellular H2O2. Hydrogen Peroxide 57-61 superoxide dismutase 1 Homo sapiens 9-18 7850993-5 1994 With a non-physiological concentration of H2O2 (0.8 mmol/l) to stimulate chemiluminescence (CL) at a level < 2 mV, it was observed that the addition of Cu,Zn-SOD (100 micrograms/ml) yielded an increase of 204.7 +/- 78.2 mV (P < 0.05). Hydrogen Peroxide 42-46 superoxide dismutase 1 Homo sapiens 155-164 7850993-10 1994 In electron paramagnetic resonance, with the use of the spin-trap dimethylpyrroline-N-oxide (DMPO), it was demonstrated that, in the reaction between H2O2 and Cu,Zn-SOD, .OH was generated. Hydrogen Peroxide 150-154 superoxide dismutase 1 Homo sapiens 159-168 7850993-11 1994 The oxidation of keto-methylthiobutyric acid (KMB) to ethylene, assessed by gas chromatography, demonstrated that H2O2/Cu,Zn-SOD-generated .OH can react with KMB and not only with the SOD molecule itself. Hydrogen Peroxide 114-118 superoxide dismutase 1 Homo sapiens 119-128 7850993-11 1994 The oxidation of keto-methylthiobutyric acid (KMB) to ethylene, assessed by gas chromatography, demonstrated that H2O2/Cu,Zn-SOD-generated .OH can react with KMB and not only with the SOD molecule itself. Hydrogen Peroxide 114-118 superoxide dismutase 1 Homo sapiens 125-128 7841338-5 1994 The impact of purified superoxide dismutase (SOD) upon the production of hydrogen peroxide produced as a consequence of 3,4-EQ metabolism was evaluated; surprisingly, SOD inhibited the hydrogen peroxide produced by this o-quinone. Hydrogen Peroxide 73-90 superoxide dismutase 1 Homo sapiens 23-43 7841338-5 1994 The impact of purified superoxide dismutase (SOD) upon the production of hydrogen peroxide produced as a consequence of 3,4-EQ metabolism was evaluated; surprisingly, SOD inhibited the hydrogen peroxide produced by this o-quinone. Hydrogen Peroxide 73-90 superoxide dismutase 1 Homo sapiens 45-48 7841338-5 1994 The impact of purified superoxide dismutase (SOD) upon the production of hydrogen peroxide produced as a consequence of 3,4-EQ metabolism was evaluated; surprisingly, SOD inhibited the hydrogen peroxide produced by this o-quinone. Hydrogen Peroxide 73-90 superoxide dismutase 1 Homo sapiens 167-170 7841338-5 1994 The impact of purified superoxide dismutase (SOD) upon the production of hydrogen peroxide produced as a consequence of 3,4-EQ metabolism was evaluated; surprisingly, SOD inhibited the hydrogen peroxide produced by this o-quinone. Hydrogen Peroxide 185-202 superoxide dismutase 1 Homo sapiens 23-43 7841338-5 1994 The impact of purified superoxide dismutase (SOD) upon the production of hydrogen peroxide produced as a consequence of 3,4-EQ metabolism was evaluated; surprisingly, SOD inhibited the hydrogen peroxide produced by this o-quinone. Hydrogen Peroxide 185-202 superoxide dismutase 1 Homo sapiens 45-48 7841338-5 1994 The impact of purified superoxide dismutase (SOD) upon the production of hydrogen peroxide produced as a consequence of 3,4-EQ metabolism was evaluated; surprisingly, SOD inhibited the hydrogen peroxide produced by this o-quinone. Hydrogen Peroxide 185-202 superoxide dismutase 1 Homo sapiens 167-170 7850993-12 1994 We conclude that H2O2 reduces SOD-bound Cu2+ to Cu1+ which, in reaction with H2O2 catalyses its reduction to OH. Hydrogen Peroxide 17-21 superoxide dismutase 1 Homo sapiens 30-33 7850993-12 1994 We conclude that H2O2 reduces SOD-bound Cu2+ to Cu1+ which, in reaction with H2O2 catalyses its reduction to OH. Hydrogen Peroxide 77-81 superoxide dismutase 1 Homo sapiens 30-33 8185613-1 1994 Superoxide dismutase (SOD), which breaks down superoxide to oxygen and hydrogen peroxide, is generally considered an antioxidant enzyme. Hydrogen Peroxide 71-88 superoxide dismutase 1 Homo sapiens 0-20 8185613-1 1994 Superoxide dismutase (SOD), which breaks down superoxide to oxygen and hydrogen peroxide, is generally considered an antioxidant enzyme. Hydrogen Peroxide 71-88 superoxide dismutase 1 Homo sapiens 22-25 8312381-8 1994 LPO in this system was decreased in the presence of free radical scavengers and enzymes that degrade H2O2 (EDTA, SOD, L-carnosine, chelated iron and catalase). Hydrogen Peroxide 101-105 superoxide dismutase 1 Homo sapiens 113-116 8260663-8 1993 The SOD activity of LR strains was irreversibly inhibited 100% by 5 mM H2O2, and exhibited greater sensitivity to NaN3, suggesting the presence of iron in the enzyme. Hydrogen Peroxide 71-75 superoxide dismutase 1 Homo sapiens 4-7 8232185-1 1993 The localization of Cu/Zn and Mn superoxide dismutase (SOD), which catalyzes the dismutation of superoxide radicals (O2-) to O2 and H2O2, in various thyroid disorders was studied by an immunohistochemical technique in 20% formalin fixed paraffin embedded thin sections using anti-human Cu/Zn and Mn-SOD antibodies. Hydrogen Peroxide 132-136 superoxide dismutase 1 Homo sapiens 55-58 8382025-10 1993 Under CWF light, catalase inhibited and superoxide dismutase (SOD) stimulated formation of DNA SSB, indicating H2O2 was generated from O2-. Hydrogen Peroxide 111-115 superoxide dismutase 1 Homo sapiens 40-60 7686874-12 1993 Experiments with MPO-H2O2 in SOD- and Cl(-)-free conditions showed the formation of DFO radical and confirmed the hypothesis of the involvement of compound II. Hydrogen Peroxide 21-25 superoxide dismutase 1 Homo sapiens 29-32 8390449-7 1993 The results of inhibition studies on the NADH oxidation with SOD and catalase suggested that the reaction mixture containing stannum (IV) chloride contained a greater amount of H2O2 and a lower amount of O2- than that containing only vanadium (IV). Hydrogen Peroxide 177-181 superoxide dismutase 1 Homo sapiens 61-64 8403808-13 1993 Cu/Zn superoxide dismutase can catalyse the dismutation of O2 into H2O2 and generate OH.. Hydrogen Peroxide 67-71 superoxide dismutase 1 Homo sapiens 0-26 8446170-6 1993 Here we report tight genetic linkage between FALS and a gene that encodes a cytosolic, Cu/Zn-binding superoxide dismutase (SOD1), a homodimeric metalloenzyme that catalyzes the dismutation of the toxic superoxide anion O2.- to O2 and H2O2 (ref. Hydrogen Peroxide 234-238 superoxide dismutase 1 Homo sapiens 123-127 8382025-10 1993 Under CWF light, catalase inhibited and superoxide dismutase (SOD) stimulated formation of DNA SSB, indicating H2O2 was generated from O2-. Hydrogen Peroxide 111-115 superoxide dismutase 1 Homo sapiens 62-65 1334093-1 1992 To elaborate the catalytic activity of Cu2+ of Cu,Zn-superoxide dismutase (SOD) in the generation of hydroxyl radical (.OH) from H2O2, we investigated the mechanism of inactivation of alpha 1-protease inhibitor (alpha 1-PI), mediated by H2O2 and Cu,Zn-SOD. Hydrogen Peroxide 129-133 superoxide dismutase 1 Homo sapiens 47-73 8117850-10 1993 Oxidative challenge with H2O2 resulted in minimal changes in the absorbance spectra of PolyHb-SOD-catalase. Hydrogen Peroxide 25-29 superoxide dismutase 1 Homo sapiens 94-97 8117850-12 1993 Furthermore, the amount of iron released, after incubation with 250 microM H2O2, was 6.8 +/- 1.8 micrograms/dl for PolyHb-SOD-catalase and 76.6 +/- 1.0 micrograms/dl for PolyHb. Hydrogen Peroxide 75-79 superoxide dismutase 1 Homo sapiens 122-125 8225030-13 1993 free radicals derived from H2O2, produced by the action of SOD, may be a necessary prerequisite for differentiation, whereas an overproduction of OH. Hydrogen Peroxide 27-31 superoxide dismutase 1 Homo sapiens 59-62 1334093-6 1992 SOD activity decreased rapidly during the reaction with H2O2 for the initial 30 min. Hydrogen Peroxide 56-60 superoxide dismutase 1 Homo sapiens 0-3 1334093-7 1992 Time-dependent changes in the ESR signal of SOD showed the destruction of ligands for Cu2+ in SOD by H2O2 within this initial period. Hydrogen Peroxide 101-105 superoxide dismutase 1 Homo sapiens 44-47 1334093-7 1992 Time-dependent changes in the ESR signal of SOD showed the destruction of ligands for Cu2+ in SOD by H2O2 within this initial period. Hydrogen Peroxide 101-105 superoxide dismutase 1 Homo sapiens 94-97 1334093-8 1992 Thus we conclude that inactivation of alpha 1-PI is mediated in the H2O2/Cu,Zn-SOD system via the generation of .OH by free Cu2+ released from oxidatively damaged SOD. Hydrogen Peroxide 68-72 superoxide dismutase 1 Homo sapiens 79-82 1334093-8 1992 Thus we conclude that inactivation of alpha 1-PI is mediated in the H2O2/Cu,Zn-SOD system via the generation of .OH by free Cu2+ released from oxidatively damaged SOD. Hydrogen Peroxide 68-72 superoxide dismutase 1 Homo sapiens 163-166 1334093-1 1992 To elaborate the catalytic activity of Cu2+ of Cu,Zn-superoxide dismutase (SOD) in the generation of hydroxyl radical (.OH) from H2O2, we investigated the mechanism of inactivation of alpha 1-protease inhibitor (alpha 1-PI), mediated by H2O2 and Cu,Zn-SOD. Hydrogen Peroxide 129-133 superoxide dismutase 1 Homo sapiens 75-78 1334093-1 1992 To elaborate the catalytic activity of Cu2+ of Cu,Zn-superoxide dismutase (SOD) in the generation of hydroxyl radical (.OH) from H2O2, we investigated the mechanism of inactivation of alpha 1-protease inhibitor (alpha 1-PI), mediated by H2O2 and Cu,Zn-SOD. Hydrogen Peroxide 237-241 superoxide dismutase 1 Homo sapiens 47-73 1334093-1 1992 To elaborate the catalytic activity of Cu2+ of Cu,Zn-superoxide dismutase (SOD) in the generation of hydroxyl radical (.OH) from H2O2, we investigated the mechanism of inactivation of alpha 1-protease inhibitor (alpha 1-PI), mediated by H2O2 and Cu,Zn-SOD. Hydrogen Peroxide 237-241 superoxide dismutase 1 Homo sapiens 75-78 1334093-3 1992 ESR spin trapping using 5,5-dimethyl-1-pyrroline N-oxide showed that free .OH was indeed generated in the reaction of Cu,Zn-SOD/H2O2; this was substantiated by the almost complete eradication of .OH by either ethanol or dimethyl sulfoxide accompanied by the generation of carbon-centered radicals. Hydrogen Peroxide 128-132 superoxide dismutase 1 Homo sapiens 124-127 1581040-8 1992 Cells pretreated with desferrioxamine (Des) and superoxide dismutase (SOD) or Des, SOD and catalase (CAT) to induce partial (H2O2 formation only) or almost full protection (no ROS formation) showed about the same reactions as when cells were exposed to alloxan and cysteine without scavengers (O2-, H2O2 and OH. Hydrogen Peroxide 299-303 superoxide dismutase 1 Homo sapiens 48-68 1304602-3 1992 Inhibition of the formation of H2O2 by SOD indicates that the formation of H2O2 and the consequent decrease of the cell survival was enhanced by O2-. Hydrogen Peroxide 31-35 superoxide dismutase 1 Homo sapiens 39-42 1304602-3 1992 Inhibition of the formation of H2O2 by SOD indicates that the formation of H2O2 and the consequent decrease of the cell survival was enhanced by O2-. Hydrogen Peroxide 75-79 superoxide dismutase 1 Homo sapiens 39-42 1581040-8 1992 Cells pretreated with desferrioxamine (Des) and superoxide dismutase (SOD) or Des, SOD and catalase (CAT) to induce partial (H2O2 formation only) or almost full protection (no ROS formation) showed about the same reactions as when cells were exposed to alloxan and cysteine without scavengers (O2-, H2O2 and OH. Hydrogen Peroxide 125-129 superoxide dismutase 1 Homo sapiens 83-86 1324124-7 1992 This effect of SOD was reversed by catalase, indicating involvement of hydrogen peroxide in this effect. Hydrogen Peroxide 71-88 superoxide dismutase 1 Homo sapiens 15-18 1328424-10 1992 SOD is the enzyme that catalyzes the dismutation reaction of superoxide anion radicals: 2O2- + 2H(+)----H2O2 + O2. Hydrogen Peroxide 97-108 superoxide dismutase 1 Homo sapiens 0-3 1581040-8 1992 Cells pretreated with desferrioxamine (Des) and superoxide dismutase (SOD) or Des, SOD and catalase (CAT) to induce partial (H2O2 formation only) or almost full protection (no ROS formation) showed about the same reactions as when cells were exposed to alloxan and cysteine without scavengers (O2-, H2O2 and OH. Hydrogen Peroxide 299-303 superoxide dismutase 1 Homo sapiens 83-86 1584206-1 1992 The activities of superoxide dismutase (SOD; EC 1.15.1.1) and glutathione peroxidase (GSHPx; EC 1.11.1.9), the enzymes that metabolize the superoxide anion and hydrogen peroxide, respectively, were measured in serum from healthy subjects and patients with Parkinson"s disease (PD). Hydrogen Peroxide 160-177 superoxide dismutase 1 Homo sapiens 18-38 1317004-1 1992 The oxidation of NADH and accompanying reduction of oxygen to H2O2 stimulated by polyvanadate was markedly inhibited by SOD and cytochrome c. Hydrogen Peroxide 62-66 superoxide dismutase 1 Homo sapiens 120-123 1584206-1 1992 The activities of superoxide dismutase (SOD; EC 1.15.1.1) and glutathione peroxidase (GSHPx; EC 1.11.1.9), the enzymes that metabolize the superoxide anion and hydrogen peroxide, respectively, were measured in serum from healthy subjects and patients with Parkinson"s disease (PD). Hydrogen Peroxide 160-177 superoxide dismutase 1 Homo sapiens 40-43 1627273-5 1992 The SOD mimetic activity of PS-K was demonstrated by quantitative analysis of hydrogen peroxide as the end product of O2-., its formation being assisted catalytically by SOD or PS-K. Hydrogen Peroxide 78-95 superoxide dismutase 1 Homo sapiens 4-7 1627273-5 1992 The SOD mimetic activity of PS-K was demonstrated by quantitative analysis of hydrogen peroxide as the end product of O2-., its formation being assisted catalytically by SOD or PS-K. Hydrogen Peroxide 78-95 superoxide dismutase 1 Homo sapiens 170-173 2164216-1 1990 Cu,Zn superoxide dismutase (Cu,Zn-SOD; EC 1.15.1.1) is known to be inhibited slowly by H2O2. Hydrogen Peroxide 87-91 superoxide dismutase 1 Homo sapiens 0-26 1563647-3 1992 This CL is inhibited by catalase and deferoxamine, unaffected by mannitol, and stimulated by superoxide dismutase (SOD), suggesting that it is mediated by H2O2. Hydrogen Peroxide 155-159 superoxide dismutase 1 Homo sapiens 93-113 1563647-3 1992 This CL is inhibited by catalase and deferoxamine, unaffected by mannitol, and stimulated by superoxide dismutase (SOD), suggesting that it is mediated by H2O2. Hydrogen Peroxide 155-159 superoxide dismutase 1 Homo sapiens 115-118 1783856-3 1991 However, human tear film does contain the CuZn superoxide dismutase (103 +/- 32 ng/mg soluble protein), which is inactivated by hydrogen peroxide (0.2 mM). Hydrogen Peroxide 128-145 superoxide dismutase 1 Homo sapiens 42-67 1783856-6 1991 These results indicate that the tear film is lacking the enzyme systems to provide significant protection to the cornea, to the tear film itself, or to the SOD of the tear film from the oxidant action of hydrogen peroxide. Hydrogen Peroxide 204-221 superoxide dismutase 1 Homo sapiens 156-159 1910314-5 1991 Furthermore, superoxide dismutase-dependent platelet activation is fully prevented by catalase and/or aspirin, suggesting a role for H2O2 and the involvement of the cyclooxygenase pathway of arachidonic acid in such activation. Hydrogen Peroxide 133-137 superoxide dismutase 1 Homo sapiens 13-33 1649094-1 1991 The active site Cu ion in Cu,Zn superoxide dismutase is alternately oxidized and reduced during the enzymatic dismutation of superoxide to hydrogen peroxide and molecular oxygen. Hydrogen Peroxide 139-156 superoxide dismutase 1 Homo sapiens 26-52 2148198-4 1990 SOD, superoxide scavenger, and catalase (CAT), which destroy hydrogen peroxide, apparently reduced proteinuria on 14th day (18.5 +/- 3.17 mg/day, 20.7 +/- 7.35 mg/day, respectively, in comparison with control group, 29.5 +/- 4.21 mg/day), but there was no statistical significance. Hydrogen Peroxide 61-78 superoxide dismutase 1 Homo sapiens 0-3 2164216-1 1990 Cu,Zn superoxide dismutase (Cu,Zn-SOD; EC 1.15.1.1) is known to be inhibited slowly by H2O2. Hydrogen Peroxide 87-91 superoxide dismutase 1 Homo sapiens 28-37 2164216-2 1990 Using EPR and the spin traps 5,5-dimethyl-1-pyrroline 1-oxide (DMPO) and N-tert-butyl-alpha-phenylnitrone (PBN), we have shown that Cu,Zn-SOD catalyzes the formation of "free" .OH radicals from H2O2 in pH 7.6 bicarbonate buffer. Hydrogen Peroxide 194-198 superoxide dismutase 1 Homo sapiens 132-141 2164216-10 1990 The capacity of Cu,Zn-SOD to generate "free" .OH radicals from H2O2 may in part explain the biological damage associated with elevated intracellular SOD activity. Hydrogen Peroxide 63-67 superoxide dismutase 1 Homo sapiens 16-25 2164216-10 1990 The capacity of Cu,Zn-SOD to generate "free" .OH radicals from H2O2 may in part explain the biological damage associated with elevated intracellular SOD activity. Hydrogen Peroxide 63-67 superoxide dismutase 1 Homo sapiens 22-25 2308398-8 1990 SOD was inactivated by 50% by hydrogen peroxide at 4 x 10(-4) M (20 min, 37 degrees C), but organic peroxides and hydroxyl radicals were ineffective on this enzyme. Hydrogen Peroxide 30-47 superoxide dismutase 1 Homo sapiens 0-3 1963617-3 1990 A decrease in the bleaching rates was observed upon addition of SOD or hydroxyl radical scavengers, showing that the hydrogen peroxide/Ni(II)/glycyl-glycyl-L-histidine system generated superoxide anions as well as hydroxyl radicals. Hydrogen Peroxide 117-134 superoxide dismutase 1 Homo sapiens 64-67 33774064-3 2021 In this study, the effect of cadmium on SOD1, a CuZn metalloenzyme catalyzing superoxide conversion into hydrogen peroxide, has been investigated in three different biological models. Hydrogen Peroxide 105-122 superoxide dismutase 1 Homo sapiens 40-44 33798828-2 2021 Superoxide dismutase (SOD), catalase (CAT), and glutathione peroxidase are among the key enzymes that maintain the low nanomolar physiological concentrations of superoxide and hydrogen peroxide. Hydrogen Peroxide 176-193 superoxide dismutase 1 Homo sapiens 0-20 33798828-2 2021 Superoxide dismutase (SOD), catalase (CAT), and glutathione peroxidase are among the key enzymes that maintain the low nanomolar physiological concentrations of superoxide and hydrogen peroxide. Hydrogen Peroxide 176-193 superoxide dismutase 1 Homo sapiens 22-25 34776311-3 2022 The increase in SOD, CAT and GPX activities, reduce in ROS level and MDA content, and weaken in damage on cell membrane and DNA could be responsible for the protective effect of GSGH on H2O2-mediated oxidative injured HepG2 cells. Hydrogen Peroxide 186-190 superoxide dismutase 1 Homo sapiens 16-19 34943042-10 2021 Furthermore, hydrogen peroxide addition was observed to mimic, in vitro, the SOD-1 effect on IL-17 production. Hydrogen Peroxide 13-30 superoxide dismutase 1 Homo sapiens 77-82 34884437-5 2021 Its subsequent conversion into H2O2 by superoxide dismutase 1 and 3 (SOD1, SOD3) and production of ClO- from H2O2 by myeloperoxidase (MPO) was necessary for cell death induction. Hydrogen Peroxide 31-35 superoxide dismutase 1 Homo sapiens 39-67 34414854-10 2021 Transfection of p-LUCAT1 significantly reversed the decreased SOD levels, the increased MDA and ROS content, and the elevated tumor necrosis factor-alpha (TNF-alpha), interleukin-6 (IL-6), and interleukin-1 beta (IL-1beta) in H2O2-stimulated cells (P < 0.001). Hydrogen Peroxide 226-230 superoxide dismutase 1 Homo sapiens 62-65 34884437-5 2021 Its subsequent conversion into H2O2 by superoxide dismutase 1 and 3 (SOD1, SOD3) and production of ClO- from H2O2 by myeloperoxidase (MPO) was necessary for cell death induction. Hydrogen Peroxide 31-35 superoxide dismutase 1 Homo sapiens 69-73 34636556-4 2021 It is particularly noteworthy that SOD can effectively catalyze dismutation of the O2- to produce H2O2 and O2, and Au@PANI with a good reduction and catalytic property can catalyze the produced H2O2 into H2O and O2. Hydrogen Peroxide 99-103 superoxide dismutase 1 Homo sapiens 35-38 34558653-10 2021 RK1 treatment significantly improved cell viability, reduced the apoptotic rate and increased the activity levels of SOD, CAT and GSH-Px in the PIG1 cell line exposed to H2O2. Hydrogen Peroxide 170-174 superoxide dismutase 1 Homo sapiens 117-120 34476501-6 2021 H2O2-induced intracellular MDA was decreased by ANP, and the levels of SOD and NO were increased in the presence of ANP. Hydrogen Peroxide 0-4 superoxide dismutase 1 Homo sapiens 71-74 34636556-4 2021 It is particularly noteworthy that SOD can effectively catalyze dismutation of the O2- to produce H2O2 and O2, and Au@PANI with a good reduction and catalytic property can catalyze the produced H2O2 into H2O and O2. Hydrogen Peroxide 195-199 superoxide dismutase 1 Homo sapiens 35-38 34392045-10 2021 Taken together, these data support that H2O2 acts as a signaling molecule in the activation of antioxidant enzymes (specifically NOX, SOD, and CAT), regulation of both glutathione-related enzymes and total glutathione content, and upregulation of the cell wall-loosening protein gene TaEXPB23. Hydrogen Peroxide 40-44 superoxide dismutase 1 Homo sapiens 134-137 34318481-5 2021 Moreover, after treatment with decapeptide-ribose MRPs, the activities of cellular antioxidative enzymes, such as catalase (CAT), superoxide dismutase (SOD), glutathione peroxidase (GSH-Px), and glutathione reductase (GSH-Rx) were remarkably increased, while the content of malondialdehyde (MDA) was decreased compared with H2 O2 - treated group, thereby enhancing the intracellular antioxidant defenses. Hydrogen Peroxide 324-329 superoxide dismutase 1 Homo sapiens 130-150 34392045-7 2021 Moreover, these seedlings had significantly lower catalase (CAT), peroxidase (POX), and ascorbate peroxidase (APX) activities but higher NADPH oxidase (NOX) and superoxide dismutase (SOD) activities under the same conditions, which consequently induced greater H2O2 accumulation. Hydrogen Peroxide 261-265 superoxide dismutase 1 Homo sapiens 183-186 34318481-5 2021 Moreover, after treatment with decapeptide-ribose MRPs, the activities of cellular antioxidative enzymes, such as catalase (CAT), superoxide dismutase (SOD), glutathione peroxidase (GSH-Px), and glutathione reductase (GSH-Rx) were remarkably increased, while the content of malondialdehyde (MDA) was decreased compared with H2 O2 - treated group, thereby enhancing the intracellular antioxidant defenses. Hydrogen Peroxide 324-329 superoxide dismutase 1 Homo sapiens 152-155 34439550-6 2021 Then, these compounds, 4 and 6-11, with better antioxidant activity were further explored to protect the L02 cells from H2O2-induced oxidative injury by reducing the reactive oxygen species (ROS) and Malondialdehyde (MDA) production and activating the SOD enzyme. Hydrogen Peroxide 120-124 superoxide dismutase 1 Homo sapiens 252-255 34313971-12 2021 Moreover, A-EVs significantly upregulated the mRNA expression of Nrf2, HO-1, CAT, and SOD genes in H2O2-treated HaCaT cells. Hydrogen Peroxide 99-103 superoxide dismutase 1 Homo sapiens 86-89