PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 30849487-2 2019 Most of previous studies reported that Cu-Abeta could contribute to oxidative stress, as H2O2 and OH are catalytically generated by Cu-Abeta with the assistance of biological reductant, with only one recent report stated that free O2 - is also generated in the Cu-Abeta catalyzed processes, where an indirect technique was applied. Hydrogen Peroxide 89-93 amyloid beta precursor protein Homo sapiens 42-47 31187978-0 2019 Hydrogen Peroxide Modifies Abeta-Membrane Interactions with Implications for Abeta40 Aggregation. Hydrogen Peroxide 0-17 amyloid beta precursor protein Homo sapiens 27-32 31187978-10 2019 The impact of H2O2 on Abeta aggregation in the presence of lipids was associated with a reduced affinity of Abeta for the vesicle surface. Hydrogen Peroxide 14-18 amyloid beta precursor protein Homo sapiens 22-27 30849487-2 2019 Most of previous studies reported that Cu-Abeta could contribute to oxidative stress, as H2O2 and OH are catalytically generated by Cu-Abeta with the assistance of biological reductant, with only one recent report stated that free O2 - is also generated in the Cu-Abeta catalyzed processes, where an indirect technique was applied. Hydrogen Peroxide 89-93 amyloid beta precursor protein Homo sapiens 136-141 30849487-2 2019 Most of previous studies reported that Cu-Abeta could contribute to oxidative stress, as H2O2 and OH are catalytically generated by Cu-Abeta with the assistance of biological reductant, with only one recent report stated that free O2 - is also generated in the Cu-Abeta catalyzed processes, where an indirect technique was applied. Hydrogen Peroxide 89-93 amyloid beta precursor protein Homo sapiens 136-141 30849487-4 2019 All the experimental results obtained from the three methods demonstrated that Cu-Abeta in the biological reducing environment was not only able to catalyze the production of H2O2 and OH, but also to generate free O2 -. Hydrogen Peroxide 175-179 amyloid beta precursor protein Homo sapiens 82-87 31415717-14 2019 Even under stressed conditions (H2O2 treatment) where the Abeta production was higher, the peptide was still able to significantly reduce the effect of BACE1 while not effecting cell viability. Hydrogen Peroxide 32-36 amyloid beta precursor protein Homo sapiens 58-63 30385800-4 2018 Using fluorescence measurements and UV absorbance, we show that dityrosine can be formed aerobically when Abeta is incubated with Cu2+ and hydrogen-peroxide, or in a Cu2+ and ascorbate redox mixture. Hydrogen Peroxide 139-156 amyloid beta precursor protein Homo sapiens 106-111 29172520-1 2017 A component of the neurotoxicity of the beta amyloid peptide (Abeta) of Alzheimer"s disease is its ability to generate superoxide, hydrogen peroxide, and hydroxyl radicals by reaction of its reduced copper complex Abeta/Cu+ with molecular oxygen. Hydrogen Peroxide 131-148 amyloid beta precursor protein Homo sapiens 40-60 29172520-1 2017 A component of the neurotoxicity of the beta amyloid peptide (Abeta) of Alzheimer"s disease is its ability to generate superoxide, hydrogen peroxide, and hydroxyl radicals by reaction of its reduced copper complex Abeta/Cu+ with molecular oxygen. Hydrogen Peroxide 131-148 amyloid beta precursor protein Homo sapiens 62-67 29172520-1 2017 A component of the neurotoxicity of the beta amyloid peptide (Abeta) of Alzheimer"s disease is its ability to generate superoxide, hydrogen peroxide, and hydroxyl radicals by reaction of its reduced copper complex Abeta/Cu+ with molecular oxygen. Hydrogen Peroxide 131-148 amyloid beta precursor protein Homo sapiens 214-219 27270708-1 2016 Heme bound amyloid beta (Abeta) peptides, which have been associated with Alzheimer"s disease (AD), can catalytically oxidize ferrocytochrome c (Cyt c(II)) in the presence of hydrogen peroxide (H2O2). Hydrogen Peroxide 175-192 amyloid beta precursor protein Homo sapiens 25-30 28409157-2 2017 In the present study, we investigated the effects of ferulic acid on the Abeta levels in H2O2-stimulated human lens epithelial (HLE) SRA 01/04 cells. Hydrogen Peroxide 89-93 amyloid beta precursor protein Homo sapiens 73-78 28409157-4 2017 H2O2 stimulation augmented gene expression of the proteins related to Abeta production, resulting in the production of three types of Abeta peptides. Hydrogen Peroxide 0-4 amyloid beta precursor protein Homo sapiens 70-75 28409157-4 2017 H2O2 stimulation augmented gene expression of the proteins related to Abeta production, resulting in the production of three types of Abeta peptides. Hydrogen Peroxide 0-4 amyloid beta precursor protein Homo sapiens 134-139 28409157-5 2017 Treatment with 0.1 muM ferulic acid attenuated the augmentations of gene expression and production of the proteins related to the secretion of three types of Abeta peptides in the H2O2-stimulated HLE cells. Hydrogen Peroxide 180-184 amyloid beta precursor protein Homo sapiens 158-163 27844077-2 2016 Heme binds both amyloid beta (Abeta) and human islet amyloid polypeptide (hIAPP) to form heme-Abeta and heme-hIAPP complexes, respectively, and form reactive oxygen species (ROS) like H2O2, O2 -etc., which are known to cause oxidative damage. Hydrogen Peroxide 184-188 amyloid beta precursor protein Homo sapiens 30-35 27619837-4 2016 In this system, CQ is released only upon exposure to conditions in which H2O2 levels are high, such as those in Abeta plaques. Hydrogen Peroxide 73-77 amyloid beta precursor protein Homo sapiens 112-117 27619837-9 2016 STATEMENT OF SIGNIFICANCE: Due to the low ability to cross the blood-brain barrier (BBB) and non-specific interactions with metal ions necessary for normal cellular processes of metal chelator or Abeta inhibitors, we created a novel gold nanoparticle-capped mesoporous silica (MSN-AuNPs)-based H2O2-responsive controlled release system for targeted delivery of the metal chelator CQ and AuNPs (Abeta inhibitor). Hydrogen Peroxide 294-298 amyloid beta precursor protein Homo sapiens 196-201 27619837-10 2016 In this system, CQ and AuNPs are released only upon exposure to conditions in which H2O2 levels are high, such as those in Abeta plaques. Hydrogen Peroxide 84-88 amyloid beta precursor protein Homo sapiens 123-128 27108954-4 2016 In vitro oxidation of Abeta, by the physiological oxidant H2O2, was monitored using (1)H NMR and mass spectrometry. Hydrogen Peroxide 58-62 amyloid beta precursor protein Homo sapiens 22-27 27270708-1 2016 Heme bound amyloid beta (Abeta) peptides, which have been associated with Alzheimer"s disease (AD), can catalytically oxidize ferrocytochrome c (Cyt c(II)) in the presence of hydrogen peroxide (H2O2). Hydrogen Peroxide 194-198 amyloid beta precursor protein Homo sapiens 25-30 26629876-0 2016 Free Superoxide is an Intermediate in the Production of H2O2 by Copper(I)-Abeta Peptide and O2. Hydrogen Peroxide 56-60 amyloid beta precursor protein Homo sapiens 74-79 27055069-5 2016 Binding and microscopy studies support that these BAM agents target Abeta and inhibit the interactions of catalase with Abeta in cells, which, in turn, can account for an observed inhibition of Abeta-induced increases in hydrogen peroxide in cells treated with these compounds. Hydrogen Peroxide 221-238 amyloid beta precursor protein Homo sapiens 68-73 27055069-5 2016 Binding and microscopy studies support that these BAM agents target Abeta and inhibit the interactions of catalase with Abeta in cells, which, in turn, can account for an observed inhibition of Abeta-induced increases in hydrogen peroxide in cells treated with these compounds. Hydrogen Peroxide 221-238 amyloid beta precursor protein Homo sapiens 120-125 27055069-5 2016 Binding and microscopy studies support that these BAM agents target Abeta and inhibit the interactions of catalase with Abeta in cells, which, in turn, can account for an observed inhibition of Abeta-induced increases in hydrogen peroxide in cells treated with these compounds. Hydrogen Peroxide 221-238 amyloid beta precursor protein Homo sapiens 120-125 26699836-10 2016 Because copper and hydrogen peroxide are elevated in the AD brain, CHICUP-stabilized Abeta oligomers are biologically relevant and should be further explored as a new therapeutic target. Hydrogen Peroxide 19-36 amyloid beta precursor protein Homo sapiens 85-90 26629876-2 2016 Cu bound to the peptide amyloid-beta (Abeta) is found in AD brains, and Cu-Abeta could contribute to this oxidative stress, as it is able to produce in vitro H2O2 and HO in the presence of oxygen and biological reducing agents such as ascorbate. Hydrogen Peroxide 158-162 amyloid beta precursor protein Homo sapiens 38-43 26629876-2 2016 Cu bound to the peptide amyloid-beta (Abeta) is found in AD brains, and Cu-Abeta could contribute to this oxidative stress, as it is able to produce in vitro H2O2 and HO in the presence of oxygen and biological reducing agents such as ascorbate. Hydrogen Peroxide 158-162 amyloid beta precursor protein Homo sapiens 75-80 26629876-3 2016 The mechanism of Cu-Abeta-catalyzed H2O2 production is however not known, although it was proposed that H2O2 is directly formed from O2 via a 2-electron process. Hydrogen Peroxide 36-40 amyloid beta precursor protein Homo sapiens 20-25 26629876-3 2016 The mechanism of Cu-Abeta-catalyzed H2O2 production is however not known, although it was proposed that H2O2 is directly formed from O2 via a 2-electron process. Hydrogen Peroxide 104-108 amyloid beta precursor protein Homo sapiens 20-25 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 amyloid beta precursor protein Homo sapiens 157-162 26629876-5 2016 This finding radically changes the view on the catalytic mechanism of H2O2 production by Cu-Abeta, and opens the possibility that Cu-Abeta-catalyzed O2 (-) contributes to oxidative stress in AD, and hence may be of interest. Hydrogen Peroxide 70-74 amyloid beta precursor protein Homo sapiens 92-97 26629876-5 2016 This finding radically changes the view on the catalytic mechanism of H2O2 production by Cu-Abeta, and opens the possibility that Cu-Abeta-catalyzed O2 (-) contributes to oxidative stress in AD, and hence may be of interest. Hydrogen Peroxide 70-74 amyloid beta precursor protein Homo sapiens 133-138 25211009-6 2015 Under oxidative (H2O2) and nitrative (H2O2/NaNO2) stress conditions, the Abeta40-heme complexes caused oxidation and nitration of the Abeta Tyr-10 residue through promoting peroxidase-like reactions, which were different from the classic inhibitive effect of heme on Abeta aggregation. Hydrogen Peroxide 17-21 amyloid beta precursor protein Homo sapiens 73-78 25211009-6 2015 Under oxidative (H2O2) and nitrative (H2O2/NaNO2) stress conditions, the Abeta40-heme complexes caused oxidation and nitration of the Abeta Tyr-10 residue through promoting peroxidase-like reactions, which were different from the classic inhibitive effect of heme on Abeta aggregation. Hydrogen Peroxide 38-42 amyloid beta precursor protein Homo sapiens 73-78 25387246-3 2015 Recently, we found that increasing pseudoperoxidase activity induces elevated tyrosine nitration on Abeta in the presence of nitrite and hydrogen peroxide. Hydrogen Peroxide 137-154 amyloid beta precursor protein Homo sapiens 100-105 23836416-2 2014 Abeta has high affinity for iron and copper resulting in the generation of neurotoxic hydrogen peroxide, oxidative stress and free radical formation. Hydrogen Peroxide 86-103 amyloid beta precursor protein Homo sapiens 0-5 24523414-4 2014 Our photometric studies confirmed the production of ~60 muM hydrogen peroxide (H2O2) from a solution of 20 muM Cu(2+) ions in complex with Abeta(1-40) in fibrils ([Cu(2+)]/[Abeta] = 0.4) within 2 h of incubation after addition of biological reducing agent ascorbate at the physiological concentration (~1 mM). Hydrogen Peroxide 60-77 amyloid beta precursor protein Homo sapiens 139-144 24523414-4 2014 Our photometric studies confirmed the production of ~60 muM hydrogen peroxide (H2O2) from a solution of 20 muM Cu(2+) ions in complex with Abeta(1-40) in fibrils ([Cu(2+)]/[Abeta] = 0.4) within 2 h of incubation after addition of biological reducing agent ascorbate at the physiological concentration (~1 mM). Hydrogen Peroxide 60-77 amyloid beta precursor protein Homo sapiens 173-178 24523414-4 2014 Our photometric studies confirmed the production of ~60 muM hydrogen peroxide (H2O2) from a solution of 20 muM Cu(2+) ions in complex with Abeta(1-40) in fibrils ([Cu(2+)]/[Abeta] = 0.4) within 2 h of incubation after addition of biological reducing agent ascorbate at the physiological concentration (~1 mM). Hydrogen Peroxide 79-83 amyloid beta precursor protein Homo sapiens 139-144 24523414-4 2014 Our photometric studies confirmed the production of ~60 muM hydrogen peroxide (H2O2) from a solution of 20 muM Cu(2+) ions in complex with Abeta(1-40) in fibrils ([Cu(2+)]/[Abeta] = 0.4) within 2 h of incubation after addition of biological reducing agent ascorbate at the physiological concentration (~1 mM). Hydrogen Peroxide 79-83 amyloid beta precursor protein Homo sapiens 173-178 24313818-3 2013 Moreover, Cu-Abeta complexes are able to catalyze the production of hydrogen peroxide and hydroxyl radicals, and oligomeric Cu-Abeta was reported to be more reactive. Hydrogen Peroxide 68-85 amyloid beta precursor protein Homo sapiens 13-18 24313818-3 2013 Moreover, Cu-Abeta complexes are able to catalyze the production of hydrogen peroxide and hydroxyl radicals, and oligomeric Cu-Abeta was reported to be more reactive. Hydrogen Peroxide 68-85 amyloid beta precursor protein Homo sapiens 127-132 21359283-6 2011 Copper ions entrapped in Abeta fibrils are electrochemically active and can generate ROS in the presence of hydrogen peroxide and reducing agents. Hydrogen Peroxide 108-125 amyloid beta precursor protein Homo sapiens 25-30 23770394-5 2013 Pre-incubation of the mAb-covered electrode with native Abeta decreased the amount of Abeta(1-16)-heme-AuNPs immobilized onto the electrode, resulting in the decrease of the reduction current of O2 to H2O2. Hydrogen Peroxide 201-205 amyloid beta precursor protein Homo sapiens 56-61 23726866-0 2013 Time course study of Abeta formation and neurite outgrowth disruption in differentiated human neuroblastoma cells exposed to H2O2: protective role of autophagy. Hydrogen Peroxide 125-129 amyloid beta precursor protein Homo sapiens 21-26 23726866-2 2013 We found that H2O2 disrupted neurite outgrowth concomitant with production of Abeta. Hydrogen Peroxide 14-18 amyloid beta precursor protein Homo sapiens 78-83 23726866-7 2013 Our results showed that autophagy could internalize and degrade intra- and extracellular Abeta after 3h treatment with H2O2. Hydrogen Peroxide 119-123 amyloid beta precursor protein Homo sapiens 89-94 22982299-6 2013 Amyloid beta can become pro-oxidant and when complexed to copper or iron it can generate hydrogen peroxide. Hydrogen Peroxide 89-106 amyloid beta precursor protein Homo sapiens 0-12 23203093-5 2012 Moreover, the addition of copper sulfate or hydrogen peroxide, used to mimic the oxidative stress observed in AD-affected brains, potentiates Abeta-mediated perturbation of DNA damage/repair systems in the "Abeta cell line". Hydrogen Peroxide 44-61 amyloid beta precursor protein Homo sapiens 142-147 23203093-5 2012 Moreover, the addition of copper sulfate or hydrogen peroxide, used to mimic the oxidative stress observed in AD-affected brains, potentiates Abeta-mediated perturbation of DNA damage/repair systems in the "Abeta cell line". Hydrogen Peroxide 44-61 amyloid beta precursor protein Homo sapiens 207-212 21790829-8 2012 In human neuroblastoma cells exposed to Abeta, tunicamycin or H2O2, PACT and pPKR concentrations are increased. Hydrogen Peroxide 62-66 amyloid beta precursor protein Homo sapiens 40-45 22437427-9 2012 60% reduction in the amount of hydrogen peroxide (H(2)O(2)) generated by Cu(2+)-Abeta in the presence of dioxygen (O(2)) and a reducing agent. Hydrogen Peroxide 31-48 amyloid beta precursor protein Homo sapiens 80-85 22437427-9 2012 60% reduction in the amount of hydrogen peroxide (H(2)O(2)) generated by Cu(2+)-Abeta in the presence of dioxygen (O(2)) and a reducing agent. Hydrogen Peroxide 50-58 amyloid beta precursor protein Homo sapiens 80-85 21708232-10 2011 We observed that human neuroblastoma (SK-N-SH) cells treated with FITC conjugated Abeta1-40 localized Abeta to the nucleus in the presence of H2O2-mediated oxidative stress. Hydrogen Peroxide 142-146 amyloid beta precursor protein Homo sapiens 82-87 20923778-4 2010 This report demonstrates that exposure of human neuroblastoma cells to cytotoxic preparations of aggregated Abeta peptides results in significant intracellular co-localization of Abeta with catalase, an anti-oxidant enzyme responsible for catalyzing the degradation of the ROS intermediate hydrogen peroxide (H(2)O(2)). Hydrogen Peroxide 290-307 amyloid beta precursor protein Homo sapiens 108-113 20923778-6 2010 Furthermore, small molecule inhibitors of catalase-amyloid interactions protect the hydrogen peroxide-degrading activity of catalase in Abeta-rich environments, leading to reduction of the co-localization of catalase and Abeta in cells, inhibition of Abeta-induced increases in cellular levels of H(2)O(2), and reduction of the toxicity of Abeta peptides. Hydrogen Peroxide 84-101 amyloid beta precursor protein Homo sapiens 221-226 20923778-6 2010 Furthermore, small molecule inhibitors of catalase-amyloid interactions protect the hydrogen peroxide-degrading activity of catalase in Abeta-rich environments, leading to reduction of the co-localization of catalase and Abeta in cells, inhibition of Abeta-induced increases in cellular levels of H(2)O(2), and reduction of the toxicity of Abeta peptides. Hydrogen Peroxide 84-101 amyloid beta precursor protein Homo sapiens 221-226 20923778-6 2010 Furthermore, small molecule inhibitors of catalase-amyloid interactions protect the hydrogen peroxide-degrading activity of catalase in Abeta-rich environments, leading to reduction of the co-localization of catalase and Abeta in cells, inhibition of Abeta-induced increases in cellular levels of H(2)O(2), and reduction of the toxicity of Abeta peptides. Hydrogen Peroxide 84-101 amyloid beta precursor protein Homo sapiens 221-226 20923778-4 2010 This report demonstrates that exposure of human neuroblastoma cells to cytotoxic preparations of aggregated Abeta peptides results in significant intracellular co-localization of Abeta with catalase, an anti-oxidant enzyme responsible for catalyzing the degradation of the ROS intermediate hydrogen peroxide (H(2)O(2)). Hydrogen Peroxide 290-307 amyloid beta precursor protein Homo sapiens 179-184 20923778-6 2010 Furthermore, small molecule inhibitors of catalase-amyloid interactions protect the hydrogen peroxide-degrading activity of catalase in Abeta-rich environments, leading to reduction of the co-localization of catalase and Abeta in cells, inhibition of Abeta-induced increases in cellular levels of H(2)O(2), and reduction of the toxicity of Abeta peptides. Hydrogen Peroxide 84-101 amyloid beta precursor protein Homo sapiens 136-141 21061469-0 2010 Paeonol attenuates H2O2-induced NF-kappaB-associated amyloid precursor protein expression. Hydrogen Peroxide 19-23 amyloid beta precursor protein Homo sapiens 53-78 19685013-6 2010 Wild-type Abeta alone is more cytotoxic but produced less amount of H(2)O(2) than AbetaH13R-copper complexes, suggesting that Abeta-membrane interaction may also implicated in the pathologic progress. Hydrogen Peroxide 68-76 amyloid beta precursor protein Homo sapiens 10-15 20203192-5 2010 Abeta increased hydrogen peroxide production as well as glutathione release into the extracellular space without affecting intracellular glutathione content. Hydrogen Peroxide 16-33 amyloid beta precursor protein Homo sapiens 0-5 21061469-7 2010 Moreover, using network analysis to investigate genes that were altered by H2O2 and reversely regulated by paeonol, we found that NF-kappaB was the primary center of the network and amyloid precursor protein (APP) was the secondary center. Hydrogen Peroxide 75-79 amyloid beta precursor protein Homo sapiens 182-207 19574031-1 2009 Molecular physicobiochemical calculations indicated that the metallic ion binding to beta-amyloids (Abeta) may induce production of hydrogen peroxide, which triggers the Ca ion redistribution from the extracellular to the intracellular compartmentation, resulting in a transient membrane electropotential drop by at least 208.06 mV. Hydrogen Peroxide 132-149 amyloid beta precursor protein Homo sapiens 100-105 20213540-5 2010 Increasing evidence suggests that cholesterol oxidation products are of importance in generation of Alzheimer"s disease, possibly induced by Abeta-produced hydrogen peroxide. Hydrogen Peroxide 156-173 amyloid beta precursor protein Homo sapiens 141-146 19631265-2 2009 Though the exact mode of action is not known, it is suggested that A beta induces cell death through induction of oxidative stress possibly through hydrogen peroxide generation. Hydrogen Peroxide 148-165 amyloid beta precursor protein Homo sapiens 67-73 18436531-0 2008 Hydrogen peroxide promotes Abeta production through JNK-dependent activation of gamma-secretase. Hydrogen Peroxide 0-17 amyloid beta precursor protein Homo sapiens 27-32 18847222-3 2008 There have been a number of studies monitoring reactive oxygen species (ROS) generation by copper and ascorbate that suggest that Abeta acts as a prooxidant producing H2O2. Hydrogen Peroxide 167-171 amyloid beta precursor protein Homo sapiens 130-135 18607649-1 2008 One of the many hypotheses on the pathogenesis of Alzheimer"s disease is that the amyloid-beta peptide (Abeta) binds CuII and can catalytically generate H2O2, leading to oxidative damage in brain tissues. Hydrogen Peroxide 153-157 amyloid beta precursor protein Homo sapiens 104-109 19542222-2 2009 Abeta.copper complexes have been identified in AD and catalytically oxidize cholesterol and lipid to generate H2O2 and lipid peroxides. Hydrogen Peroxide 110-114 amyloid beta precursor protein Homo sapiens 0-5 19123835-1 2009 The amyloid beta peptide (Abeta) of Alzheimer"s disease evolves hydrogen peroxide in vitro in the presence of Cu(II), external reducing agents, and molecular oxygen, without producing detectable amounts of the one-electron reduced intermediate, superoxide, O(2)(-*). Hydrogen Peroxide 64-81 amyloid beta precursor protein Homo sapiens 26-31 17846500-2 2007 Amyloid beta peptide (Abeta) is the major component of senile plaques and is known to exert its cytotoxic effect mainly by producing H2O2. Hydrogen Peroxide 133-137 amyloid beta precursor protein Homo sapiens 22-27 17969218-5 2008 Their strong chelating capacities allow them to inhibit more efficiently than the corresponding monomers the precipitation of Abeta-peptides induced by Cu II and Zn II and also to inhibit the toxic formation of H2O2 due to copper complexes of Abeta. Hydrogen Peroxide 211-215 amyloid beta precursor protein Homo sapiens 126-131 17969218-5 2008 Their strong chelating capacities allow them to inhibit more efficiently than the corresponding monomers the precipitation of Abeta-peptides induced by Cu II and Zn II and also to inhibit the toxic formation of H2O2 due to copper complexes of Abeta. Hydrogen Peroxide 211-215 amyloid beta precursor protein Homo sapiens 243-248 17846500-5 2007 We found that Abeta induced the production of H2O2 in vitro. Hydrogen Peroxide 46-50 amyloid beta precursor protein Homo sapiens 14-19 17846500-6 2007 Comparison of the amount of H2O2 required to induce VEGF synthesis in HN33 cells and the amount of H2O2 produced by 10 muM Abeta1-42 in vitro suggested that a toxic concentration of Abeta might induce VEGF synthesis in these cells. Hydrogen Peroxide 99-103 amyloid beta precursor protein Homo sapiens 123-128 17277887-4 2007 Abeta(1-40)Cu(II) complexes generate neurotoxic hydrogen peroxide (H(2)O(2)) from O(2) via Cu(2+) reduction, though the precise reaction mechanism is unclear. Hydrogen Peroxide 48-65 amyloid beta precursor protein Homo sapiens 0-5 17277887-7 2007 These findings indicate that copper binding to Abeta(1-40) can give rise to greater production of H(2)O(2), which leads to a breakdown in the integrity of the plasma membrane and subsequent neuronal death. Hydrogen Peroxide 98-106 amyloid beta precursor protein Homo sapiens 47-52 16814100-6 2006 We found that prefibrillar and oligomeric A beta(1-42) resulted in a more dramatic increase in the oxidative stress markers 4-hydroxynonenal and hydrogen peroxide compared to fibrillar A beta(1-42). Hydrogen Peroxide 145-162 amyloid beta precursor protein Homo sapiens 42-48 16945610-1 2006 BACKGROUND: Growing evidence suggests that oxidative damage caused by the beta-amyloid peptide in the pathogenesis of Alzheimer"s disease may be hydrogen peroxide mediated. Hydrogen Peroxide 145-162 amyloid beta precursor protein Homo sapiens 74-94 15635660-0 2005 Methionine regulates copper/hydrogen peroxide oxidation products of Abeta. Hydrogen Peroxide 28-45 amyloid beta precursor protein Homo sapiens 68-73 15025502-1 2004 It has been proposed that the Met residue in the C-terminal domain of the Alzheimer"s disease beta-amyloid peptide (betaA) serves as a source of electrons for the Cu(II)-catalyzed reduction of molecular oxygen to hydrogen peroxide. Hydrogen Peroxide 213-230 amyloid beta precursor protein Homo sapiens 94-114 15826313-2 2005 These include: i) the precipitation and aggregation of amyloid beta (Abeta) peptides to form senile plaques and neurofibrillary tangles, and/or ii) the augmentation of oxidative stress by metal ion mediated production and activation of hydrogen peroxide. Hydrogen Peroxide 236-253 amyloid beta precursor protein Homo sapiens 55-67 15668252-3 2005 Abeta coordinates the redox active metal ion Cu2+ to catalytically generate H2O2. Hydrogen Peroxide 76-80 amyloid beta precursor protein Homo sapiens 0-5 15699049-0 2005 Catechol oxidase-like oxidation chemistry of the 1-20 and 1-16 fragments of Alzheimer"s disease-related beta-amyloid peptide: their structure-activity correlation and the fate of hydrogen peroxide. Hydrogen Peroxide 179-196 amyloid beta precursor protein Homo sapiens 104-124 15614428-8 2005 Furthermore, hydrogen peroxide treatment facilitated beta-secretase activity and A(beta) generation. Hydrogen Peroxide 13-30 amyloid beta precursor protein Homo sapiens 81-88 13130517-0 2003 Overexpression of amyloid precursor protein is associated with degeneration, decreased viability, and increased damage caused by neurotoxins (prostaglandins A1 and E2, hydrogen peroxide, and nitric oxide) in differentiated neuroblastoma cells. Hydrogen Peroxide 168-185 amyloid beta precursor protein Homo sapiens 18-43 14675907-5 2003 Abeta peptides have been shown to exhibit superoxide dismutase activity, producing hydrogen peroxide which may be responsible for the neurotoxicity exhibited by this peptide in vitro. Hydrogen Peroxide 83-100 amyloid beta precursor protein Homo sapiens 0-5 14709077-2 2004 A model C-(4a)-flavinhydroperoxide (FlHOOH) is described that contains the tricyclic isoalloxazine moiety, the C-4a-hydroperoxide functionality, and a beta-hydroxyethyl group to model the effect of the 2"-OH group of the ribityl side chain of native FADHOOH. Hydrogen Peroxide 21-34 amyloid beta precursor protein Homo sapiens 149-155 14624024-4 2003 A rise in levels of hydrogen peroxide (H2O2) was observed in both in vitro and in vivo AD-associated transgenic models expressing the Abeta peptide compared with the wild type controls. Hydrogen Peroxide 20-37 amyloid beta precursor protein Homo sapiens 134-139 14624024-4 2003 A rise in levels of hydrogen peroxide (H2O2) was observed in both in vitro and in vivo AD-associated transgenic models expressing the Abeta peptide compared with the wild type controls. Hydrogen Peroxide 39-43 amyloid beta precursor protein Homo sapiens 134-139 10683851-3 2000 The cellular A beta 42 increase was caused by 3-day treatments with H2O2, etoposide or melphalan, all of which induce genotoxic apoptosis, but not by treatment with sodium azide, which causes necrosis. Hydrogen Peroxide 68-72 amyloid beta precursor protein Homo sapiens 13-19 12470799-4 2002 The abnormal combination of Abeta with Cu or Fe induces the production of hydrogen peroxide, which may mediate the conspicuous oxidative damage to the brain in AD. Hydrogen Peroxide 74-91 amyloid beta precursor protein Homo sapiens 28-33 12470799-5 2002 We have developed metal-binding compounds that inhibit the in vitro generation of hydrogen peroxide by Abeta, as well as reverse the aggregation of the peptide in vitro and from human brain post-mortem specimens. Hydrogen Peroxide 82-99 amyloid beta precursor protein Homo sapiens 103-108 11238735-9 2001 Homocysteine also generated high levels of hydrogen peroxide in the presence of Cu (II) and promoted Abeta/Cu-mediated hydrogen peroxide production and neurotoxicity. Hydrogen Peroxide 119-136 amyloid beta precursor protein Homo sapiens 101-106 10801964-7 2000 In addition, Abeta produces hydrogen peroxide in a Cu(II)/Fe(III)-dependent manner, and the hydrogen peroxide formation is quenched by Zn(II). Hydrogen Peroxide 28-45 amyloid beta precursor protein Homo sapiens 13-18 10801964-7 2000 In addition, Abeta produces hydrogen peroxide in a Cu(II)/Fe(III)-dependent manner, and the hydrogen peroxide formation is quenched by Zn(II). Hydrogen Peroxide 92-109 amyloid beta precursor protein Homo sapiens 13-18 12031892-0 2002 Formation of hydrogen peroxide and hydroxyl radicals from A(beta) and alpha-synuclein as a possible mechanism of cell death in Alzheimer"s disease and Parkinson"s disease. Hydrogen Peroxide 13-30 amyloid beta precursor protein Homo sapiens 58-65 12031892-6 2002 Our results suggest that hydrogen peroxide accumulates during the incubation of A(beta) or alpha-synuclein, by a metal-dependent mechanism, and that this is subsequently converted to hydroxyl radicals, on addition of Fe (II), by Fenton"s reaction. Hydrogen Peroxide 25-42 amyloid beta precursor protein Homo sapiens 80-87 11130184-7 2000 We therefore also investigated the proteasome inhibitory action of Abeta1-40 (a peptide comprising the first 40 residues of Abeta) modified by the intracellular oxidant hydrogen peroxide, and by the lipid peroxidation product 4-hydroxynonenal (HNE). Hydrogen Peroxide 169-186 amyloid beta precursor protein Homo sapiens 67-72 10959032-3 2000 Abeta converts molecular oxygen into hydrogen peroxide by reducing copper or iron, and this may lead to Fenton chemistry. Hydrogen Peroxide 37-54 amyloid beta precursor protein Homo sapiens 0-5 10386999-0 1999 The A beta peptide of Alzheimer"s disease directly produces hydrogen peroxide through metal ion reduction. Hydrogen Peroxide 60-77 amyloid beta precursor protein Homo sapiens 4-10 10386999-3 1999 We now show that human A beta directly produces hydrogen peroxide (H2O2) by a mechanism that involves the reduction of metal ions, Fe(III) or Cu(II), setting up conditions for Fenton-type chemistry. Hydrogen Peroxide 48-65 amyloid beta precursor protein Homo sapiens 23-29 10386999-3 1999 We now show that human A beta directly produces hydrogen peroxide (H2O2) by a mechanism that involves the reduction of metal ions, Fe(III) or Cu(II), setting up conditions for Fenton-type chemistry. Hydrogen Peroxide 67-71 amyloid beta precursor protein Homo sapiens 23-29 9761460-1 1998 The neurotoxic beta-amyloid (Abeta) peptide fragment Abeta(25-35) has been suggested to exert its deleterious effects on cells via production of hydrogen peroxide. Hydrogen Peroxide 145-162 amyloid beta precursor protein Homo sapiens 4-35 9175113-2 1997 A beta stimulated H2O2 production in neural (B12) and non-neural (HepG2) cells and stimulated PPP activity, the source of the main intracellular reductant NADPH, in HepG2 cells (67% increase). Hydrogen Peroxide 18-22 amyloid beta precursor protein Homo sapiens 0-6 9585534-0 1998 Copper-binding amyloid precursor protein undergoes a site-specific fragmentation in the reduction of hydrogen peroxide. Hydrogen Peroxide 101-118 amyloid beta precursor protein Homo sapiens 15-40 9207249-0 1997 Processing of Alzheimer"s amyloid precursor protein during H2O2-induced apoptosis in human neuronal cells. Hydrogen Peroxide 59-63 amyloid beta precursor protein Homo sapiens 26-51 9207249-1 1997 The processing of Alzheimer"s amyloid precursor protein was studied by Western blotting during H2O2 induced apoptosis in cultures of human neuroblastoma cells. Hydrogen Peroxide 95-99 amyloid beta precursor protein Homo sapiens 30-55 9175113-3 1997 Catalase blocked the A beta-induced increase in PPP, demonstrating that H2O2 mediated the increase in PPP activity. Hydrogen Peroxide 72-76 amyloid beta precursor protein Homo sapiens 21-27 9499162-0 1996 A beta (25-35) peptide displays H2O2-like reactivity towards aqueous Fe2+, nitroxide spin probes, and synaptosomal membrane proteins. Hydrogen Peroxide 32-36 amyloid beta precursor protein Homo sapiens 0-6 9266422-3 1997 A beta causes increased levels of H2O2 and lipid peroxides to accumulate in cells. Hydrogen Peroxide 34-38 amyloid beta precursor protein Homo sapiens 0-6 9266422-4 1997 The H2O2 degrading enzyme catalase protects cells from A beta toxicity. Hydrogen Peroxide 4-8 amyloid beta precursor protein Homo sapiens 55-61 9266422-5 1997 Clonal cell lines selected for their resistance to A beta toxicity also become resistant to the cytolytic action of H2O2. Hydrogen Peroxide 116-120 amyloid beta precursor protein Homo sapiens 51-57 9266422-7 1997 Finally, A beta induced H2O2 production and A beta toxicity are blocked by reagents which inhibit flavin oxidases, suggesting that A beta activates a member of this class of enzymes. Hydrogen Peroxide 24-28 amyloid beta precursor protein Homo sapiens 9-15 8626578-3 1996 Here we demonstrate that Alzheimer"s precursor protein (betaAPP) and A beta are present at low levels in normal lenses and increase in intact cultured monkey lenses treated with H2O2 or UV radiation (known cataractogenic agents), and with phorbol 12-myristate 13-acetate. Hydrogen Peroxide 178-182 amyloid beta precursor protein Homo sapiens 69-75 8626578-8 1996 Our data show that betaAPP and Abeta increase in mammalian lenses as part of a response to H2O2 or UV radiation and suggest that they may contribute to the mechanism by which oxidative damage leads to lens opacification. Hydrogen Peroxide 91-95 amyloid beta precursor protein Homo sapiens 31-36 33803786-8 2021 Our results strongly suggest that the H2O2 generated in the solution by CAP irradiation is responsible for Met oxidation, which inhibits Abeta amyloid formation. Hydrogen Peroxide 38-42 amyloid beta precursor protein Homo sapiens 137-142 8004671-3 1994 A beta causes increased levels of H2O2 and lipid peroxides to accumulate in cells. Hydrogen Peroxide 34-38 amyloid beta precursor protein Homo sapiens 0-6 8004671-4 1994 The H2O2-degrading enzyme catalase protects cells from A beta toxicity. Hydrogen Peroxide 4-8 amyloid beta precursor protein Homo sapiens 55-61 8004671-5 1994 Clonal cell lines selected for their resistance to A beta toxicity also become resistant to the cytolytic action of H2O2. Hydrogen Peroxide 116-120 amyloid beta precursor protein Homo sapiens 51-57 8004671-7 1994 Finally, A beta-induced H2O2 production and A beta toxicity are blocked by reagents that inhibit flavin oxidases, suggesting that A beta activates a member of this class of enzymes. Hydrogen Peroxide 24-28 amyloid beta precursor protein Homo sapiens 9-15 7826691-1 1994 Hydrogen peroxide mediates amyloid beta protein toxicity. Hydrogen Peroxide 0-17 amyloid beta precursor protein Homo sapiens 27-39 35468173-1 2022 beta-Amyloid (Abeta) peptides can bind both Cu2+ and heme cofactors simultaneously to form heme-Cu2+-Abeta complexes, which are proposed to generate toxic partially reduced oxygen species (PROS, e.g., H2O2) and play a vital role in Alzheimer"s disease (AD). Hydrogen Peroxide 201-205 amyloid beta precursor protein Homo sapiens 14-19 35468173-5 2022 When the concentration of the target Abeta is low, the synergistic enhancement effect arising from K2S2O8 with in situ generated H2O2 is predominant, resulting in an increase in the ECL signal of g-C3N4. Hydrogen Peroxide 129-133 amyloid beta precursor protein Homo sapiens 37-42 34467355-3 2021 This study has pioneered a singular pathway used to radicalize surface NO3 - functionalities anchored on polymorphic alpha-/gamma-MnO2 surfaces (alpha-/gamma-MnO2-N), in which Lewis acidic Mn2+/3+ and NO3 - served to form OH via H2O2 dissection and NO3 via radical transfer from OH to NO3 - ( OH NO3 ), respectively. Hydrogen Peroxide 230-234 amyloid beta precursor protein Homo sapiens 25-26 35468173-1 2022 beta-Amyloid (Abeta) peptides can bind both Cu2+ and heme cofactors simultaneously to form heme-Cu2+-Abeta complexes, which are proposed to generate toxic partially reduced oxygen species (PROS, e.g., H2O2) and play a vital role in Alzheimer"s disease (AD). Hydrogen Peroxide 201-205 amyloid beta precursor protein Homo sapiens 101-106