PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 34834681-6 2021 The enzymatic antioxidants, including superoxide dismutase (SOD), ascorbate peroxidase (APX), catalase (CAT) and peroxidase (POX) were improved by Cys application. Cysteine 147-150 superoxide dismutase 1 Homo sapiens 38-58 34834681-6 2021 The enzymatic antioxidants, including superoxide dismutase (SOD), ascorbate peroxidase (APX), catalase (CAT) and peroxidase (POX) were improved by Cys application. Cysteine 147-150 superoxide dismutase 1 Homo sapiens 60-63 34986524-0 2022 Nitric oxide inhibits endothelial cell apoptosis by inhibiting cysteine-dependent SOD1 monomerization. Cysteine 63-71 superoxide dismutase 1 Homo sapiens 82-86 34416109-4 2021 We report here a bioinspired NiII complex built on an ATCUN-like binding motif modulated with one cysteine, which demonstrates catalytic SOD activity in water (kcat = 8.4(2) x 105 M-1 s-1 at pH = 8.1). Cysteine 98-106 superoxide dismutase 1 Homo sapiens 137-140 35123243-2 2022 SOD biosensors were constructed employing three immobilization methods: cross-linking with EDC/NHS at a cysteine self-assembled monolayer (PCl/Au/SODCYS), biopolymer encapsulation with chitosan (PCl/Au/SODCHI) and cross-linking with glutaraldehyde (PCl/Au/SODGA). Cysteine 104-112 superoxide dismutase 1 Homo sapiens 0-3 34986524-8 2022 In summary, our data reveal that NO protects endothelial cells against apoptosis by inhibiting cysteine-dependent SOD1 monomerization to enhance SOD1 activity and inhibit oxidative stress. Cysteine 95-103 superoxide dismutase 1 Homo sapiens 114-118 34986524-8 2022 In summary, our data reveal that NO protects endothelial cells against apoptosis by inhibiting cysteine-dependent SOD1 monomerization to enhance SOD1 activity and inhibit oxidative stress. Cysteine 95-103 superoxide dismutase 1 Homo sapiens 145-149 6093188-12 1984 Superoxide dismutase (SOD) was found to stimulate the oxygen uptake in the case of MEA and cysteine, but had little or no effect with DTT and glutathione. Cysteine 91-99 superoxide dismutase 1 Homo sapiens 0-20 6093188-12 1984 Superoxide dismutase (SOD) was found to stimulate the oxygen uptake in the case of MEA and cysteine, but had little or no effect with DTT and glutathione. Cysteine 91-99 superoxide dismutase 1 Homo sapiens 22-25 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. Cysteine 105-113 superoxide dismutase 1 Homo sapiens 51-55 32862101-13 2020 The ability of these compounds to target cysteine 111 in SOD may have wider therapeutic applications targeting cysteines of enzymes involved in pathogenic and viral diseases including main protease of SARS-Cov-2 (COVID-19). Cysteine 41-49 superoxide dismutase 1 Homo sapiens 57-60 32862101-13 2020 The ability of these compounds to target cysteine 111 in SOD may have wider therapeutic applications targeting cysteines of enzymes involved in pathogenic and viral diseases including main protease of SARS-Cov-2 (COVID-19). Cysteine 111-120 superoxide dismutase 1 Homo sapiens 57-60 32598986-10 2020 Moreover, HHE and HNE induced extensive apo-SOD1 modifications, by forming Schiff bases or Michael adducts with Lys, His, and Cys residues. Cysteine 126-129 superoxide dismutase 1 Homo sapiens 44-48 32445072-0 2020 The Cysteine (Cys) Residues Cys-6 and Cys-111 in Mutant Superoxide Dismutase 1 (SOD1) A4V Are Required for Induction of Endoplasmic Reticulum Stress in Amyotrophic Lateral Sclerosis. Cysteine 4-12 superoxide dismutase 1 Homo sapiens 56-78 32445072-0 2020 The Cysteine (Cys) Residues Cys-6 and Cys-111 in Mutant Superoxide Dismutase 1 (SOD1) A4V Are Required for Induction of Endoplasmic Reticulum Stress in Amyotrophic Lateral Sclerosis. Cysteine 4-12 superoxide dismutase 1 Homo sapiens 80-84 32445072-0 2020 The Cysteine (Cys) Residues Cys-6 and Cys-111 in Mutant Superoxide Dismutase 1 (SOD1) A4V Are Required for Induction of Endoplasmic Reticulum Stress in Amyotrophic Lateral Sclerosis. Cysteine 4-7 superoxide dismutase 1 Homo sapiens 56-78 32445072-0 2020 The Cysteine (Cys) Residues Cys-6 and Cys-111 in Mutant Superoxide Dismutase 1 (SOD1) A4V Are Required for Induction of Endoplasmic Reticulum Stress in Amyotrophic Lateral Sclerosis. Cysteine 4-7 superoxide dismutase 1 Homo sapiens 80-84 32445072-0 2020 The Cysteine (Cys) Residues Cys-6 and Cys-111 in Mutant Superoxide Dismutase 1 (SOD1) A4V Are Required for Induction of Endoplasmic Reticulum Stress in Amyotrophic Lateral Sclerosis. Cysteine 14-17 superoxide dismutase 1 Homo sapiens 56-78 32445072-0 2020 The Cysteine (Cys) Residues Cys-6 and Cys-111 in Mutant Superoxide Dismutase 1 (SOD1) A4V Are Required for Induction of Endoplasmic Reticulum Stress in Amyotrophic Lateral Sclerosis. Cysteine 14-17 superoxide dismutase 1 Homo sapiens 80-84 32445072-0 2020 The Cysteine (Cys) Residues Cys-6 and Cys-111 in Mutant Superoxide Dismutase 1 (SOD1) A4V Are Required for Induction of Endoplasmic Reticulum Stress in Amyotrophic Lateral Sclerosis. Cysteine 14-17 superoxide dismutase 1 Homo sapiens 56-78 32445072-0 2020 The Cysteine (Cys) Residues Cys-6 and Cys-111 in Mutant Superoxide Dismutase 1 (SOD1) A4V Are Required for Induction of Endoplasmic Reticulum Stress in Amyotrophic Lateral Sclerosis. Cysteine 14-17 superoxide dismutase 1 Homo sapiens 80-84 32445072-6 2020 SOD1 contains four cysteine residues, two of which form an intra-subunit disulphide bond involving Cys-57 and Cys-146. Cysteine 19-27 superoxide dismutase 1 Homo sapiens 0-4 32445072-6 2020 SOD1 contains four cysteine residues, two of which form an intra-subunit disulphide bond involving Cys-57 and Cys-146. Cysteine 99-102 superoxide dismutase 1 Homo sapiens 0-4 32445072-6 2020 SOD1 contains four cysteine residues, two of which form an intra-subunit disulphide bond involving Cys-57 and Cys-146. Cysteine 110-113 superoxide dismutase 1 Homo sapiens 0-4 32445072-7 2020 The remaining two cysteines, Cys-6 and Cys-111, remain unpaired and have been implicated in mutant SOD1 aggregation. Cysteine 18-27 superoxide dismutase 1 Homo sapiens 99-103 32445072-7 2020 The remaining two cysteines, Cys-6 and Cys-111, remain unpaired and have been implicated in mutant SOD1 aggregation. Cysteine 29-32 superoxide dismutase 1 Homo sapiens 99-103 32445072-7 2020 The remaining two cysteines, Cys-6 and Cys-111, remain unpaired and have been implicated in mutant SOD1 aggregation. Cysteine 39-42 superoxide dismutase 1 Homo sapiens 99-103 32445072-8 2020 In this study, we examined the relationship between the SOD1 A4V cysteine residues and aggregation, ER stress induction and toxicity. Cysteine 65-73 superoxide dismutase 1 Homo sapiens 56-60 32445072-9 2020 We report here that mutation of Cys-6 and Cys-111 in mutant SOD1 A4V, but not Cys-57 or Cys-146, ameliorates ER stress, inclusion formation and apoptosis in neuronal cell lines. Cysteine 32-35 superoxide dismutase 1 Homo sapiens 60-64 32445072-9 2020 We report here that mutation of Cys-6 and Cys-111 in mutant SOD1 A4V, but not Cys-57 or Cys-146, ameliorates ER stress, inclusion formation and apoptosis in neuronal cell lines. Cysteine 42-45 superoxide dismutase 1 Homo sapiens 60-64 32445072-9 2020 We report here that mutation of Cys-6 and Cys-111 in mutant SOD1 A4V, but not Cys-57 or Cys-146, ameliorates ER stress, inclusion formation and apoptosis in neuronal cell lines. Cysteine 42-45 superoxide dismutase 1 Homo sapiens 60-64 32445072-9 2020 We report here that mutation of Cys-6 and Cys-111 in mutant SOD1 A4V, but not Cys-57 or Cys-146, ameliorates ER stress, inclusion formation and apoptosis in neuronal cell lines. Cysteine 42-45 superoxide dismutase 1 Homo sapiens 60-64 32529537-0 2020 Correction to: the Cysteine (Cys) Residues Cys-6 and Cys-111 in Mutant Superoxide Dismutase 1 (SOD1) A4V Are Required for Induction of Endoplasmic Reticulum Stress in Amyotrophic Lateral Sclerosis. Cysteine 19-27 superoxide dismutase 1 Homo sapiens 71-93 32529537-0 2020 Correction to: the Cysteine (Cys) Residues Cys-6 and Cys-111 in Mutant Superoxide Dismutase 1 (SOD1) A4V Are Required for Induction of Endoplasmic Reticulum Stress in Amyotrophic Lateral Sclerosis. Cysteine 19-27 superoxide dismutase 1 Homo sapiens 95-99 32529537-0 2020 Correction to: the Cysteine (Cys) Residues Cys-6 and Cys-111 in Mutant Superoxide Dismutase 1 (SOD1) A4V Are Required for Induction of Endoplasmic Reticulum Stress in Amyotrophic Lateral Sclerosis. Cysteine 19-22 superoxide dismutase 1 Homo sapiens 71-93 32529537-0 2020 Correction to: the Cysteine (Cys) Residues Cys-6 and Cys-111 in Mutant Superoxide Dismutase 1 (SOD1) A4V Are Required for Induction of Endoplasmic Reticulum Stress in Amyotrophic Lateral Sclerosis. Cysteine 19-22 superoxide dismutase 1 Homo sapiens 95-99 32529537-0 2020 Correction to: the Cysteine (Cys) Residues Cys-6 and Cys-111 in Mutant Superoxide Dismutase 1 (SOD1) A4V Are Required for Induction of Endoplasmic Reticulum Stress in Amyotrophic Lateral Sclerosis. Cysteine 29-32 superoxide dismutase 1 Homo sapiens 71-93 32529537-0 2020 Correction to: the Cysteine (Cys) Residues Cys-6 and Cys-111 in Mutant Superoxide Dismutase 1 (SOD1) A4V Are Required for Induction of Endoplasmic Reticulum Stress in Amyotrophic Lateral Sclerosis. Cysteine 29-32 superoxide dismutase 1 Homo sapiens 95-99 32529537-0 2020 Correction to: the Cysteine (Cys) Residues Cys-6 and Cys-111 in Mutant Superoxide Dismutase 1 (SOD1) A4V Are Required for Induction of Endoplasmic Reticulum Stress in Amyotrophic Lateral Sclerosis. Cysteine 29-32 superoxide dismutase 1 Homo sapiens 71-93 32529537-0 2020 Correction to: the Cysteine (Cys) Residues Cys-6 and Cys-111 in Mutant Superoxide Dismutase 1 (SOD1) A4V Are Required for Induction of Endoplasmic Reticulum Stress in Amyotrophic Lateral Sclerosis. Cysteine 29-32 superoxide dismutase 1 Homo sapiens 95-99 32207613-0 2020 The Role of the Cysteine Fragments of the Nickel Binding Loop in the Activity of the Ni(II)-Containing SOD Enzyme. Cysteine 16-24 superoxide dismutase 1 Homo sapiens 103-106 31545024-0 2019 Mononuclear Ni(II) Complexes with a S3O Coordination Sphere Based on a Tripodal Cysteine-Rich Ligand: pH Tuning of the Superoxide Dismutase Activity. Cysteine 80-88 superoxide dismutase 1 Homo sapiens 119-139 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. Cysteine 235-243 superoxide dismutase 1 Homo sapiens 43-47 30429951-4 2018 Oxa/cis-platin is able to interact with hSOD1 in the disulfide oxidized apo form by binding cysteine 111 (Cys111). Cysteine 92-100 superoxide dismutase 1 Homo sapiens 40-45 29703933-0 2018 The cysteine-reactive small molecule ebselen facilitates effective SOD1 maturation. Cysteine 4-12 superoxide dismutase 1 Homo sapiens 67-71 29220697-12 2018 It is also possible that H2S (or polysulfides) interact/react with SOD cysteines to affect catalytic activity or to directly contribute to sulfide metabolism. Cysteine 71-80 superoxide dismutase 1 Homo sapiens 67-70 29703933-4 2018 Here we report that the cysteine-reactive molecule ebselen efficiently confers the SOD1 intra-subunit disulphide and directs correct SOD1 folding, depopulating the globally unfolded precursor associated with aggregation and toxicity. Cysteine 24-32 superoxide dismutase 1 Homo sapiens 83-87 29703933-4 2018 Here we report that the cysteine-reactive molecule ebselen efficiently confers the SOD1 intra-subunit disulphide and directs correct SOD1 folding, depopulating the globally unfolded precursor associated with aggregation and toxicity. Cysteine 24-32 superoxide dismutase 1 Homo sapiens 133-137 29358575-0 2018 Pathological hydrogen peroxide triggers the fibrillization of wild-type SOD1 via sulfenic acid modification of Cys-111. Cysteine 111-114 superoxide dismutase 1 Homo sapiens 72-76 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. Cysteine 99-102 superoxide dismutase 1 Homo sapiens 120-124 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. Cysteine 99-102 superoxide dismutase 1 Homo sapiens 237-241 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. Cysteine 215-218 superoxide dismutase 1 Homo sapiens 99-103 28120938-5 2017 Cysteine mutations that attenuate SOD1 maturation prevented the SOD1-CCS heterodimer formation. Cysteine 0-8 superoxide dismutase 1 Homo sapiens 34-38 28585802-6 2017 A cysteine-free variant of SOD1 exhibits fibrillization behavior and fibril morphology identical to those of disulfide-reduced SOD1, firmly establishing that intermolecular disulfide bonds or intramolecular disulfide shuffling are not required for aggregation and fibril formation. Cysteine 2-10 superoxide dismutase 1 Homo sapiens 27-31 28603086-6 2017 In this study, human GPx1Ser and the Alvinella pompejana SOD (ApSOD) gene were used to design and generate several recombinant proteins with both GPx and SOD activities by combining traditional fusion protein technology, a cysteine auxotrophic expression system, and a single protein production (SPP) system. Cysteine 223-231 superoxide dismutase 1 Homo sapiens 57-60 28603086-6 2017 In this study, human GPx1Ser and the Alvinella pompejana SOD (ApSOD) gene were used to design and generate several recombinant proteins with both GPx and SOD activities by combining traditional fusion protein technology, a cysteine auxotrophic expression system, and a single protein production (SPP) system. Cysteine 223-231 superoxide dismutase 1 Homo sapiens 64-67 28120938-5 2017 Cysteine mutations that attenuate SOD1 maturation prevented the SOD1-CCS heterodimer formation. Cysteine 0-8 superoxide dismutase 1 Homo sapiens 64-68 25096579-4 2014 In human SOD1 (hSOD1), a conserved disulfide bond and two free cysteine residues can engage in anomalous thiol/disulfide exchange resulting in non-native disulfides, a hallmark of ALS that is related to protein misfolding and aggregation. Cysteine 63-71 superoxide dismutase 1 Homo sapiens 9-13 26511321-4 2015 Previously, we showed that the presence of apo-, disulfide-reduced SOD1, the most immature form of SOD1, results in initiation of fibrillation of more mature forms that have an intact Cys-57-Cys-146 disulfide bond and are partially metallated. Cysteine 184-187 superoxide dismutase 1 Homo sapiens 67-71 26511321-4 2015 Previously, we showed that the presence of apo-, disulfide-reduced SOD1, the most immature form of SOD1, results in initiation of fibrillation of more mature forms that have an intact Cys-57-Cys-146 disulfide bond and are partially metallated. Cysteine 184-187 superoxide dismutase 1 Homo sapiens 99-103 26511321-4 2015 Previously, we showed that the presence of apo-, disulfide-reduced SOD1, the most immature form of SOD1, results in initiation of fibrillation of more mature forms that have an intact Cys-57-Cys-146 disulfide bond and are partially metallated. Cysteine 191-194 superoxide dismutase 1 Homo sapiens 67-71 26511321-4 2015 Previously, we showed that the presence of apo-, disulfide-reduced SOD1, the most immature form of SOD1, results in initiation of fibrillation of more mature forms that have an intact Cys-57-Cys-146 disulfide bond and are partially metallated. Cysteine 191-194 superoxide dismutase 1 Homo sapiens 99-103 28167899-4 2017 Consolidated studies have demonstrated a fundamental role of cysteine residues in the aggregation process of SOD1 and TDP43, but disturbance of protein thiols homeostatic factors such as protein disulfide isomerases (PDI), glutathione, cysteine oxidation or palmitoylation might contribute to a general aberration of cysteine residues proteostasis in ALS. Cysteine 61-69 superoxide dismutase 1 Homo sapiens 109-113 27261461-2 2016 Human SOD1 (hSOD1) contains four cysteines, including Cys(57) and Cys(146), which have been linked to protein stability and folding via forming a disulfide bond, and Cys(6) and Cys(111) as free thiols. Cysteine 33-42 superoxide dismutase 1 Homo sapiens 6-10 27261461-2 2016 Human SOD1 (hSOD1) contains four cysteines, including Cys(57) and Cys(146), which have been linked to protein stability and folding via forming a disulfide bond, and Cys(6) and Cys(111) as free thiols. Cysteine 33-42 superoxide dismutase 1 Homo sapiens 12-17 27261461-2 2016 Human SOD1 (hSOD1) contains four cysteines, including Cys(57) and Cys(146), which have been linked to protein stability and folding via forming a disulfide bond, and Cys(6) and Cys(111) as free thiols. Cysteine 54-57 superoxide dismutase 1 Homo sapiens 6-10 27261461-2 2016 Human SOD1 (hSOD1) contains four cysteines, including Cys(57) and Cys(146), which have been linked to protein stability and folding via forming a disulfide bond, and Cys(6) and Cys(111) as free thiols. Cysteine 54-57 superoxide dismutase 1 Homo sapiens 12-17 27261461-2 2016 Human SOD1 (hSOD1) contains four cysteines, including Cys(57) and Cys(146), which have been linked to protein stability and folding via forming a disulfide bond, and Cys(6) and Cys(111) as free thiols. Cysteine 66-69 superoxide dismutase 1 Homo sapiens 6-10 27261461-2 2016 Human SOD1 (hSOD1) contains four cysteines, including Cys(57) and Cys(146), which have been linked to protein stability and folding via forming a disulfide bond, and Cys(6) and Cys(111) as free thiols. Cysteine 66-69 superoxide dismutase 1 Homo sapiens 12-17 27261461-2 2016 Human SOD1 (hSOD1) contains four cysteines, including Cys(57) and Cys(146), which have been linked to protein stability and folding via forming a disulfide bond, and Cys(6) and Cys(111) as free thiols. Cysteine 66-69 superoxide dismutase 1 Homo sapiens 6-10 27261461-2 2016 Human SOD1 (hSOD1) contains four cysteines, including Cys(57) and Cys(146), which have been linked to protein stability and folding via forming a disulfide bond, and Cys(6) and Cys(111) as free thiols. Cysteine 66-69 superoxide dismutase 1 Homo sapiens 12-17 27261461-2 2016 Human SOD1 (hSOD1) contains four cysteines, including Cys(57) and Cys(146), which have been linked to protein stability and folding via forming a disulfide bond, and Cys(6) and Cys(111) as free thiols. Cysteine 66-69 superoxide dismutase 1 Homo sapiens 6-10 27261461-2 2016 Human SOD1 (hSOD1) contains four cysteines, including Cys(57) and Cys(146), which have been linked to protein stability and folding via forming a disulfide bond, and Cys(6) and Cys(111) as free thiols. Cysteine 66-69 superoxide dismutase 1 Homo sapiens 12-17 25938783-3 2015 PKG1alpha can also be directly oxidized, forming a disulfide bond between homodimer subunits at cysteine 42 to enhance oxidant-stimulated vasorelaxation; however, the impact of PKG1alpha oxidation on myocardial regulation is unknown. Cysteine 96-104 superoxide dismutase 1 Homo sapiens 74-83 25096579-4 2014 In human SOD1 (hSOD1), a conserved disulfide bond and two free cysteine residues can engage in anomalous thiol/disulfide exchange resulting in non-native disulfides, a hallmark of ALS that is related to protein misfolding and aggregation. Cysteine 63-71 superoxide dismutase 1 Homo sapiens 15-20 24634066-3 2014 Cu/Zn-superoxide dismutase (SOD1) was chosen for this case study as it has a reactive surface cysteine residue, which is readily cysteinylated in vitro. Cysteine 94-102 superoxide dismutase 1 Homo sapiens 28-32 24094577-3 2014 In this study, we report a novel missense SOD1 mutation with a substitution of tryptophan for cysteine at the seventh amino acid (p.C7W, traditionally named p.C6W) based on HUGO Gene Nomenclature in a familial ALS pedigree. Cysteine 94-102 superoxide dismutase 1 Homo sapiens 42-46 24143259-11 2013 Disulfide scrambling thus appears to be an important event for misfolding and aggregation of SOD1, but may also be significant for protein function involving cysteines, e.g. mitochondrial import and copper loading. Cysteine 158-167 superoxide dismutase 1 Homo sapiens 93-97 23323266-0 2013 A solution 17O-NMR approach for observing an oxidized cysteine residue in Cu,Zn-superoxide dismutase. Cysteine 54-62 superoxide dismutase 1 Homo sapiens 74-100 23927036-6 2013 Many PTMs targeted a single reactive SOD1 cysteine, Cys111. Cysteine 42-50 superoxide dismutase 1 Homo sapiens 37-41 23927036-8 2013 To further characterize how cysteinylation may protect SOD1 from oxidation, cysteine-modified SOD1 was prepared in vitro and exposed to peroxide. Cysteine 76-84 superoxide dismutase 1 Homo sapiens 94-98 23919400-4 2013 We observed that cysteinylation of cysteine 111 (Cys111) of SOD1 prevents oxidation by peroxide (DOI 10.1021/bi4006122 ). Cysteine 35-43 superoxide dismutase 1 Homo sapiens 60-64 23919400-6 2013 The stoichiometry of binding was one cysteine per SOD1 dimer, and there does not appear to be free volume for a second cysteine without disrupting the dimer interface. Cysteine 37-45 superoxide dismutase 1 Homo sapiens 50-54 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. Cysteine 48-51 superoxide dismutase 1 Homo sapiens 125-129 23323266-2 2013 We describe here (17)O-NMR observation of the (17)O(2)-oxidized cysteine side chain of human Cu,Zn-superoxide dismutase in solution using selective (17)O(2) oxidation. Cysteine 64-72 superoxide dismutase 1 Homo sapiens 93-119 22677600-8 2012 Site-directed mutagenesis of the three cysteines present in the OvEC-SOD shows that enzyme activity is markedly reduced in the Cys-192 mutant. Cysteine 39-48 superoxide dismutase 1 Homo sapiens 69-72 23264618-4 2013 Here, we show that the structural destabilization of SOD1 scrambles a disulfide bond among four Cys residues in an SOD1 molecule. Cysteine 96-99 superoxide dismutase 1 Homo sapiens 53-57 23264618-4 2013 Here, we show that the structural destabilization of SOD1 scrambles a disulfide bond among four Cys residues in an SOD1 molecule. Cysteine 96-99 superoxide dismutase 1 Homo sapiens 115-119 23242317-4 2012 Here, we show that nodularin induces phosphorylation and possibly also cysteine oxidation of the antioxidant Cu,Zn superoxide dismutase (SOD1), without altering enzymatic SOD1 activity. Cysteine 71-79 superoxide dismutase 1 Homo sapiens 137-141 22677600-8 2012 Site-directed mutagenesis of the three cysteines present in the OvEC-SOD shows that enzyme activity is markedly reduced in the Cys-192 mutant. Cysteine 127-130 superoxide dismutase 1 Homo sapiens 69-72 22677600-9 2012 A homology model of the OvEC-SOD underlines the importance of Cys-192 for the stabilization of the adjacent active site channel. Cysteine 62-65 superoxide dismutase 1 Homo sapiens 29-32 22496122-7 2012 Mutation of cysteine-6 prevents palmitoylation, leads to reduction in superoxide dismutase-1 activity in vivo and in vitro, and inhibits nuclear localization, thereby supporting a functional role for superoxide dismutase-1 palmitoylation. Cysteine 12-20 superoxide dismutase 1 Homo sapiens 70-92 22869735-6 2012 Domain 3 is responsible for the catalytic formation of the hSOD1 Cys-57-Cys-146 disulfide bond, which involves both hCCS Cys-244 and Cys-246 via disulfide transfer. Cysteine 65-68 superoxide dismutase 1 Homo sapiens 59-64 22869735-6 2012 Domain 3 is responsible for the catalytic formation of the hSOD1 Cys-57-Cys-146 disulfide bond, which involves both hCCS Cys-244 and Cys-246 via disulfide transfer. Cysteine 72-75 superoxide dismutase 1 Homo sapiens 59-64 22869735-6 2012 Domain 3 is responsible for the catalytic formation of the hSOD1 Cys-57-Cys-146 disulfide bond, which involves both hCCS Cys-244 and Cys-246 via disulfide transfer. Cysteine 72-75 superoxide dismutase 1 Homo sapiens 59-64 22869735-6 2012 Domain 3 is responsible for the catalytic formation of the hSOD1 Cys-57-Cys-146 disulfide bond, which involves both hCCS Cys-244 and Cys-246 via disulfide transfer. Cysteine 72-75 superoxide dismutase 1 Homo sapiens 59-64 22496122-7 2012 Mutation of cysteine-6 prevents palmitoylation, leads to reduction in superoxide dismutase-1 activity in vivo and in vitro, and inhibits nuclear localization, thereby supporting a functional role for superoxide dismutase-1 palmitoylation. Cysteine 12-20 superoxide dismutase 1 Homo sapiens 200-222 22332887-0 2012 A novel variant of human superoxide dismutase 1 harboring amyotrophic lateral sclerosis-associated and experimental mutations in metal-binding residues and free cysteines lacks toxicity in vivo. Cysteine 161-170 superoxide dismutase 1 Homo sapiens 25-47 22471402-1 2012 cis-Diamminedichloroplatinum(II) (cisplatin) is able to interact with human superoxide dismutase (hSOD1) in the disulfide oxidized apo form with a dissociation constant of 37 +- 3 muM through binding cysteine 111 (Cys111) located at the edge of the subunit interface. Cysteine 200-208 superoxide dismutase 1 Homo sapiens 98-103 19299510-4 2009 Here we show, using SOD1 isolated from human erythrocytes, that human SOD1 is phosphorylated at threonine 2 and glutathionylated at cysteine 111. Cysteine 132-140 superoxide dismutase 1 Homo sapiens 70-74 22219129-0 2012 Oxidative modification of cysteine 111 promotes disulfide bond-independent aggregation of SOD1. Cysteine 26-34 superoxide dismutase 1 Homo sapiens 90-94 22219129-4 2012 Our data suggest that under normal circumstance, cysteine 111 residue in SOD1 is free; however, under oxidative stress, it is prone to oxidative modification by providing the thiolate anion (S-). Cysteine 49-57 superoxide dismutase 1 Homo sapiens 73-77 22219129-5 2012 With the progression of the disease, increased levels of oxidative insults facilitated the oxidation of thiol groups of cysteine residues; human mutant SOD1 could generate an upper shift band in reducing SDS-PAGE, which turned out to be a Cys111-peroxidized SOD1 species. Cysteine 120-128 superoxide dismutase 1 Homo sapiens 152-156 22219129-5 2012 With the progression of the disease, increased levels of oxidative insults facilitated the oxidation of thiol groups of cysteine residues; human mutant SOD1 could generate an upper shift band in reducing SDS-PAGE, which turned out to be a Cys111-peroxidized SOD1 species. Cysteine 120-128 superoxide dismutase 1 Homo sapiens 258-262 22219129-7 2012 This oxidative modification of cysteine 111 therefore promotes the formation of disulfide bond-independent aggregation of SOD1. Cysteine 31-39 superoxide dismutase 1 Homo sapiens 122-126 20367259-3 2010 Therefore, the cysteine residues of SOD1 play a fundamental role in its IMS localization. Cysteine 15-23 superoxide dismutase 1 Homo sapiens 36-40 23118898-6 2012 CONCLUSIONS/SIGNIFICANCE: Overall, this study is an extension of previous work demonstrating that cysteine residues in mutant SOD1 play a role in modulating aggregation and that intermolecular disulfide bonds are not required to produce large intracellular inclusion-like structures. Cysteine 98-106 superoxide dismutase 1 Homo sapiens 126-130 21739997-3 2011 Here we examine the effect of Cys-111 glutathionylation, a physiologically prevalent post-translational oxidative modification, on the stabilities of wild type SOD1 and two phenotypically diverse FALS mutants, A4V and I112T. Cysteine 30-33 superoxide dismutase 1 Homo sapiens 160-164 21739997-9 2011 Our experimental and computational results show that Cys-111 glutathionylation induces structural rearrangements that modulate stability of both wild type and FALS mutant SOD1. Cysteine 53-56 superoxide dismutase 1 Homo sapiens 171-175 21073275-1 2011 In this report we describe an ALS family with a novel missense SOD1 mutation with substitution of serine for cysteine at the sixth amino acid (C6S). Cysteine 109-117 superoxide dismutase 1 Homo sapiens 63-67 19299510-6 2009 Cysteine 111 glutathionylation promotes SOD1 monomer formation, a necessary initiating step in SOD1 aggregation, by causing a 2-fold increase in the K(d). Cysteine 0-8 superoxide dismutase 1 Homo sapiens 40-44 19299510-6 2009 Cysteine 111 glutathionylation promotes SOD1 monomer formation, a necessary initiating step in SOD1 aggregation, by causing a 2-fold increase in the K(d). Cysteine 0-8 superoxide dismutase 1 Homo sapiens 95-99 18301754-7 2008 These oligomers are formed through oxidation of the two free cysteines of SOD1 (6 and 111) and stabilized by hydrogen bonds, between beta strands, thus forming amyloid-like structures. Cysteine 61-70 superoxide dismutase 1 Homo sapiens 74-78 19052230-2 2008 Each SOD1 monomer binds to 1 copper and 1 zinc ion and maintains its disulfide bond (Cys-57-Cys-146) in the reducing cytoplasm of cell. Cysteine 85-88 superoxide dismutase 1 Homo sapiens 5-9 19052230-2 2008 Each SOD1 monomer binds to 1 copper and 1 zinc ion and maintains its disulfide bond (Cys-57-Cys-146) in the reducing cytoplasm of cell. Cysteine 92-95 superoxide dismutase 1 Homo sapiens 5-9 19070613-12 2009 SOD activity (21.4+/-2.9 U/g protein) was significantly elevated in the group with cysteine, compared to the other groups (P<0.001). Cysteine 83-91 superoxide dismutase 1 Homo sapiens 0-3 18703498-8 2008 Fourth, all of the cysteine residues in human SOD1 are critical for its retention in mitochondria due to their involvement in intramolecular disulfide bonds and in the interaction with CCS. Cysteine 19-27 superoxide dismutase 1 Homo sapiens 46-50 18316367-3 2008 In the present study, we used a panel of experimental and disease-linked mutations at cysteine residues of SOD1 (positions 6, 57, 111, and 146) in cell culture assays for aggregation to demonstrate that extensive disulfide cross-linking is not required for the formation of mutant SOD1 aggregates. Cysteine 86-94 superoxide dismutase 1 Homo sapiens 107-111 18316367-6 2008 Similar to other recent work, we found that cysteines 6 and 111, particularly the latter, play interesting roles in modulating the aggregation of human SOD1. Cysteine 44-53 superoxide dismutase 1 Homo sapiens 152-156 17466509-0 2007 One-step method embedding superoxide dismutase and gold nanoparticles in silica sol-gel network in the presence of cysteine for construction of third-generation biosensor. Cysteine 115-123 superoxide dismutase 1 Homo sapiens 26-46 17999779-7 2007 Cysteine derivatives administration prevented exercise-induced decline in SOD activity and increased in GPx activity during exercise. Cysteine 0-8 superoxide dismutase 1 Homo sapiens 74-77 17913710-3 2007 Only human and great ape SOD1s among mammals have the highly reactive free cysteine residue, Cys(111), at the surface of the SOD1 molecule. Cysteine 75-83 superoxide dismutase 1 Homo sapiens 25-29 17913710-3 2007 Only human and great ape SOD1s among mammals have the highly reactive free cysteine residue, Cys(111), at the surface of the SOD1 molecule. Cysteine 75-83 superoxide dismutase 1 Homo sapiens 125-129 17913710-3 2007 Only human and great ape SOD1s among mammals have the highly reactive free cysteine residue, Cys(111), at the surface of the SOD1 molecule. Cysteine 93-96 superoxide dismutase 1 Homo sapiens 25-29 17913710-3 2007 Only human and great ape SOD1s among mammals have the highly reactive free cysteine residue, Cys(111), at the surface of the SOD1 molecule. Cysteine 93-96 superoxide dismutase 1 Homo sapiens 125-129 17913710-4 2007 The purpose of this study was to investigate the role of Cys(111) in the oxidative damage of the SOD1 protein, by comparing the oxidative susceptibility of recombinant human SOD1 modified with 2-mercaptoethanol at Cys(111) (2-ME-SOD1) to wild-type SOD1. Cysteine 57-60 superoxide dismutase 1 Homo sapiens 97-101 17913710-4 2007 The purpose of this study was to investigate the role of Cys(111) in the oxidative damage of the SOD1 protein, by comparing the oxidative susceptibility of recombinant human SOD1 modified with 2-mercaptoethanol at Cys(111) (2-ME-SOD1) to wild-type SOD1. Cysteine 214-217 superoxide dismutase 1 Homo sapiens 97-101 17913710-7 2007 Using mass spectrometry and limited proteolysis, this upper band was identified as an oxidized subunit of SOD1; the sulfhydryl group (Cys-SH) of Cys(111) was selectively oxidized to cysteine sulfinic acid (Cys-SO(2)H) and to cysteine sulfonic acid (Cys-SO(3)H). Cysteine 134-137 superoxide dismutase 1 Homo sapiens 106-110 17913710-7 2007 Using mass spectrometry and limited proteolysis, this upper band was identified as an oxidized subunit of SOD1; the sulfhydryl group (Cys-SH) of Cys(111) was selectively oxidized to cysteine sulfinic acid (Cys-SO(2)H) and to cysteine sulfonic acid (Cys-SO(3)H). Cysteine 145-148 superoxide dismutase 1 Homo sapiens 106-110 17913710-8 2007 The antibody raised against a synthesized peptide containing Cys(111)-SO(3)H reacted with only the Cys(111)-peroxidized SOD1 by Western blot analysis and labeled Lewy body-like hyaline inclusions and vacuole rims in the spinal cord of human SOD1-mutated amyotrophic lateral sclerosis mice by immunohistochemical analysis. Cysteine 61-64 superoxide dismutase 1 Homo sapiens 120-124 17913710-8 2007 The antibody raised against a synthesized peptide containing Cys(111)-SO(3)H reacted with only the Cys(111)-peroxidized SOD1 by Western blot analysis and labeled Lewy body-like hyaline inclusions and vacuole rims in the spinal cord of human SOD1-mutated amyotrophic lateral sclerosis mice by immunohistochemical analysis. Cysteine 61-64 superoxide dismutase 1 Homo sapiens 241-245 17913710-8 2007 The antibody raised against a synthesized peptide containing Cys(111)-SO(3)H reacted with only the Cys(111)-peroxidized SOD1 by Western blot analysis and labeled Lewy body-like hyaline inclusions and vacuole rims in the spinal cord of human SOD1-mutated amyotrophic lateral sclerosis mice by immunohistochemical analysis. Cysteine 99-102 superoxide dismutase 1 Homo sapiens 120-124 17913710-9 2007 These results suggest that Cys(111) is a primary target for oxidative modification and plays an important role in oxidative damage to human SOD1, including familial amyotrophic lateral sclerosis mutants. Cysteine 27-30 superoxide dismutase 1 Homo sapiens 140-144 17157186-0 2006 Modification of cysteine 111 in human Cu,Zn-superoxide dismutase. Cysteine 16-24 superoxide dismutase 1 Homo sapiens 38-64 17070542-2 2007 Here, we present the crystal structure of fully cysteine-depleted human SOD (SOD(CallA)), representing a reduced, marginally stable intermediate on the folding pathway in vivo that has also been implicated as neurotoxic precursor state. Cysteine 48-56 superoxide dismutase 1 Homo sapiens 72-75 17157186-1 2006 Human Cu,Zn-superoxide dismutase (hSOD1) has 4 cysteines per subunit. Cysteine 47-56 superoxide dismutase 1 Homo sapiens 6-32 17157186-1 2006 Human Cu,Zn-superoxide dismutase (hSOD1) has 4 cysteines per subunit. Cysteine 47-56 superoxide dismutase 1 Homo sapiens 34-39 16945901-2 2006 Here we demonstrate that each of 12 different familial ALS-mutant SOD1s with widely differing biophysical properties are associated with mitochondria of motoneuronal cells to a much greater extent than wild-type SOD1, and that this effect may depend on the oxidation of Cys residues. Cysteine 270-273 superoxide dismutase 1 Homo sapiens 66-70 16909016-9 2005 For example, WTL SOD1 mutants are more susceptible than wild-type SOD1 to reduction of the intrasubunit disulfide bond between Cys-57 and Cys-146 at physiological pH and temperature. Cysteine 127-130 superoxide dismutase 1 Homo sapiens 17-21 16448070-2 2006 In this work, monomeric mutants of human Cu,Zn-SOD were engineered to contain one or two additional cysteine residues, which could be used to bind the protein to gold surfaces, thus making the use of promotor molecules unnecessary. Cysteine 100-108 superoxide dismutase 1 Homo sapiens 47-50 16301531-2 2005 We have mapped the homodimer interface in the dopamine D2 receptor over the entire length of the fourth transmembrane segment (TM4) by crosslinking of substituted cysteines. Cysteine 163-172 superoxide dismutase 1 Homo sapiens 19-28 16081415-5 2005 Furthermore, although SIRPalpha (Bit/PTPNS-1) is expressed as a monomer, we showed that SIRPbeta1 is expressed on the cell surface as a disulfide-linked homodimer with bond formation mediated by Cys-320 in the membrane-proximal Ig loop. Cysteine 195-198 superoxide dismutase 1 Homo sapiens 153-162 15777089-6 2005 On the basis of these rate constants, we conclude that the thiol oxidase activity of SOD1 stimulates carbonate anion radical (CO3*-) formation in the presence of HCO3- and that the CO3*- formed in the SOD1/Cys/ HCO3- system is responsible for oxidation and hydroxylation reactions. Cysteine 206-209 superoxide dismutase 1 Homo sapiens 85-89 15777089-6 2005 On the basis of these rate constants, we conclude that the thiol oxidase activity of SOD1 stimulates carbonate anion radical (CO3*-) formation in the presence of HCO3- and that the CO3*- formed in the SOD1/Cys/ HCO3- system is responsible for oxidation and hydroxylation reactions. Cysteine 206-209 superoxide dismutase 1 Homo sapiens 201-205 16202868-3 2005 The direct electrochemistry of the SOD immobilized on the CFME-based electrodes was efficiently realized by electron transfer promoter - cysteine molecules confined on the Au nanoparticles deposited on the CFMEs. Cysteine 137-145 superoxide dismutase 1 Homo sapiens 35-38 15659387-5 2005 Moreover, Cys-146, a cysteine residue of SOD1 that is mutated in familial ALS, is oxidized to cysteic acid in AD and PD brains. Cysteine 10-13 superoxide dismutase 1 Homo sapiens 41-45 15659387-5 2005 Moreover, Cys-146, a cysteine residue of SOD1 that is mutated in familial ALS, is oxidized to cysteic acid in AD and PD brains. Cysteine 10-13 superoxide dismutase 1 Homo sapiens 74-77 15659387-5 2005 Moreover, Cys-146, a cysteine residue of SOD1 that is mutated in familial ALS, is oxidized to cysteic acid in AD and PD brains. Cysteine 21-29 superoxide dismutase 1 Homo sapiens 41-45 15659387-5 2005 Moreover, Cys-146, a cysteine residue of SOD1 that is mutated in familial ALS, is oxidized to cysteic acid in AD and PD brains. Cysteine 21-29 superoxide dismutase 1 Homo sapiens 74-77 15777089-2 2005 Low temperature direct ESR revealed that cysteine (Cys) caused the reduction of copper(II) to copper(I) that was reoxidized by molecular oxygen to copper(II) at the active site of SOD1. Cysteine 41-49 superoxide dismutase 1 Homo sapiens 180-184 15777089-2 2005 Low temperature direct ESR revealed that cysteine (Cys) caused the reduction of copper(II) to copper(I) that was reoxidized by molecular oxygen to copper(II) at the active site of SOD1. Cysteine 51-54 superoxide dismutase 1 Homo sapiens 180-184 15777089-3 2005 The addition of HCO3- to aerobic incubations containing SOD1, Cys, and DTPA in phosphate buffer enhanced the peroxidase activity of SOD1, as measured by hydroxylation of cyclic nitrone spin traps, dichlorodihydrofluorescein oxidation to dichlorofluorescein, and oxidation of tyrosine to dityrosine. Cysteine 62-65 superoxide dismutase 1 Homo sapiens 132-136 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. Cysteine 155-158 superoxide dismutase 1 Homo sapiens 39-43 15777089-5 2005 Using a competitive kinetic method, rate constants for the reaction between the oxidant formed in the SOD1/Cys/HCO3- system and selected inhibitors were measured. Cysteine 107-110 superoxide dismutase 1 Homo sapiens 102-106 16909016-9 2005 For example, WTL SOD1 mutants are more susceptible than wild-type SOD1 to reduction of the intrasubunit disulfide bond between Cys-57 and Cys-146 at physiological pH and temperature. Cysteine 138-141 superoxide dismutase 1 Homo sapiens 17-21 16909016-9 2005 For example, WTL SOD1 mutants are more susceptible than wild-type SOD1 to reduction of the intrasubunit disulfide bond between Cys-57 and Cys-146 at physiological pH and temperature. Cysteine 138-141 superoxide dismutase 1 Homo sapiens 66-70 16909016-9 2005 For example, WTL SOD1 mutants are more susceptible than wild-type SOD1 to reduction of the intrasubunit disulfide bond between Cys-57 and Cys-146 at physiological pH and temperature. Cysteine 127-130 superoxide dismutase 1 Homo sapiens 66-70 15485869-7 2004 The Cys-57 --> Ser mutant of SOD1, a protein incapable of forming the intrasubunit disulfide bond, sediments as a monomer in the absence of metal ions and as a dimer when metals are bound. Cysteine 4-7 superoxide dismutase 1 Homo sapiens 32-36 12038771-1 2002 A third-generation biosensor for superoxide anion (O2-) was developed by immobilizing superoxide dismutase (SOD) on a self-assembled monolayer of cysteine on gold electrode; i.e., a SOD/cysteine-modified gold electrode (SOD/Cys/Au) was fabricated. Cysteine 146-154 superoxide dismutase 1 Homo sapiens 86-106 15096637-10 2004 It will be of interest to study the role of cysteine 111 in the oxidative damage and aggregation of toxic SOD mutants. Cysteine 44-52 superoxide dismutase 1 Homo sapiens 106-109 15096637-6 2004 The reaction of SOD with sodium sulfide, which can react with cysteine to form a persulfide group, and with potassium cyanide, which can selectively remove persulfide bonds, confirmed the addition of a persulfide group at cysteine 111. Cysteine 62-70 superoxide dismutase 1 Homo sapiens 16-19 15096637-6 2004 The reaction of SOD with sodium sulfide, which can react with cysteine to form a persulfide group, and with potassium cyanide, which can selectively remove persulfide bonds, confirmed the addition of a persulfide group at cysteine 111. Cysteine 222-230 superoxide dismutase 1 Homo sapiens 16-19 15096637-9 2004 Thus, these results suggest that cysteine 111 can have a biochemical and biophysical impact on SOD, and suggest that it can interact with copper, potentially mediating the copper-induced oxidative damage of SOD. Cysteine 33-41 superoxide dismutase 1 Homo sapiens 95-98 15096637-9 2004 Thus, these results suggest that cysteine 111 can have a biochemical and biophysical impact on SOD, and suggest that it can interact with copper, potentially mediating the copper-induced oxidative damage of SOD. Cysteine 33-41 superoxide dismutase 1 Homo sapiens 207-210 14623191-8 2003 To further characterize the folding of SOD1, we study the role of cysteine residues in folding and find that non-native disulfide bond formation may significantly alter SOD1 folding dynamics and aggregation propensity. Cysteine 66-74 superoxide dismutase 1 Homo sapiens 39-43 12963370-7 2003 These results support free-cysteine-independent aggregation of FALS mutant SOD as an integral part of FALS pathology. Cysteine 27-35 superoxide dismutase 1 Homo sapiens 75-78 12038771-1 2002 A third-generation biosensor for superoxide anion (O2-) was developed by immobilizing superoxide dismutase (SOD) on a self-assembled monolayer of cysteine on gold electrode; i.e., a SOD/cysteine-modified gold electrode (SOD/Cys/Au) was fabricated. Cysteine 146-154 superoxide dismutase 1 Homo sapiens 108-111 12038771-1 2002 A third-generation biosensor for superoxide anion (O2-) was developed by immobilizing superoxide dismutase (SOD) on a self-assembled monolayer of cysteine on gold electrode; i.e., a SOD/cysteine-modified gold electrode (SOD/Cys/Au) was fabricated. Cysteine 186-194 superoxide dismutase 1 Homo sapiens 86-106 12038771-1 2002 A third-generation biosensor for superoxide anion (O2-) was developed by immobilizing superoxide dismutase (SOD) on a self-assembled monolayer of cysteine on gold electrode; i.e., a SOD/cysteine-modified gold electrode (SOD/Cys/Au) was fabricated. Cysteine 186-194 superoxide dismutase 1 Homo sapiens 108-111 12038771-1 2002 A third-generation biosensor for superoxide anion (O2-) was developed by immobilizing superoxide dismutase (SOD) on a self-assembled monolayer of cysteine on gold electrode; i.e., a SOD/cysteine-modified gold electrode (SOD/Cys/Au) was fabricated. Cysteine 224-227 superoxide dismutase 1 Homo sapiens 108-111 12038771-2 2002 A rapid and direct electron transfer of SOD was realized at the gold electrode by using the cysteine molecule as an electron-transfer promoter. Cysteine 92-100 superoxide dismutase 1 Homo sapiens 40-43 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. Cysteine 7-10 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. Cysteine 7-10 superoxide dismutase 1 Homo sapiens 148-151 12038771-7 2002 The response mechanism of SOD/Cys/Au to O2- and its sensor characteristics are also presented and discussed. Cysteine 30-33 superoxide dismutase 1 Homo sapiens 26-29 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. Cysteine 130-138 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. Cysteine 130-138 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. Cysteine 130-138 superoxide dismutase 1 Homo sapiens 58-61 11698397-1 2002 The ability of copper,zinc superoxide dismutase (Cu,Zn-SOD) to catalyze autoxidation of cysteine and other thiols was investigated by measuring thiol loss and oxygen consumption. Cysteine 88-96 superoxide dismutase 1 Homo sapiens 55-58 11698397-4 2002 Cysteine and cysteamine were highly reactive: the K(m) for cysteine was 1.4 mm and V(max) (with 40 microg/ml SOD) 35 microm/min; the equivalent values for cysteamine (with 20 microg/ml SOD) were 1.4 mm and 36 microm/min. Cysteine 0-8 superoxide dismutase 1 Homo sapiens 109-112 11698397-4 2002 Cysteine and cysteamine were highly reactive: the K(m) for cysteine was 1.4 mm and V(max) (with 40 microg/ml SOD) 35 microm/min; the equivalent values for cysteamine (with 20 microg/ml SOD) were 1.4 mm and 36 microm/min. Cysteine 0-8 superoxide dismutase 1 Homo sapiens 185-188 11698397-6 2002 SOD-mediated oxidation of cysteine, in the absence of chelating agents, proceeded only after a variable lag phase. Cysteine 26-34 superoxide dismutase 1 Homo sapiens 0-3 11698397-10 2002 SOD-catalyzed oxidation of GSH and homocysteine was enhanced by cysteine through a thiol-disulfide exchange mechanism. Cysteine 39-47 superoxide dismutase 1 Homo sapiens 0-3 10432564-3 1999 It was shown that erythrocyte hemolysate and some studied antioxidants (ascorbate and cysteine) inhibit formation of this substance like SOD. Cysteine 86-94 superoxide dismutase 1 Homo sapiens 137-140 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. Cysteine 72-80 superoxide dismutase 1 Homo sapiens 19-45 7541042-4 1995 We demonstrate CTLA-4 is a homodimer interconnected by one disulfide bond in the extracellular domain at cysteine residue 120. Cysteine 105-113 superoxide dismutase 1 Homo sapiens 27-36 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. Cysteine 265-273 superoxide dismutase 1 Homo sapiens 48-68 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. Cysteine 265-273 superoxide dismutase 1 Homo sapiens 83-86 11694392-0 2001 The electrochemical and spectroelectrochemical behaviors of SOD at cysteine modified gold electrode. Cysteine 67-75 superoxide dismutase 1 Homo sapiens 60-63 11694392-2 2001 A quasi-reversible cyclic voltammogram (CV) of SOD was observed on the cysteine-modified gold wire electrode. Cysteine 71-79 superoxide dismutase 1 Homo sapiens 47-50 11473116-8 2001 These results support a mechanism for copper transfer in which CCS and SOD1 dock via their highly conserved dimer interfaces in a manner that precisely orients the Cys-rich copper donor sites of CCS and the His-rich acceptor sites of SOD1 to form a copper-bridged intermediate. Cysteine 164-167 superoxide dismutase 1 Homo sapiens 71-75 11473116-8 2001 These results support a mechanism for copper transfer in which CCS and SOD1 dock via their highly conserved dimer interfaces in a manner that precisely orients the Cys-rich copper donor sites of CCS and the His-rich acceptor sites of SOD1 to form a copper-bridged intermediate. Cysteine 164-167 superoxide dismutase 1 Homo sapiens 234-238 12945268-1 2001 In author"s laboratory, it has been demonstrated with electrochemical techniques that L-cysteine can be used as an effective electron transfer promoter to accelerate the electron transfer process of Cu/Zn superoxide dismutase on gold electrode. Cysteine 86-96 superoxide dismutase 1 Homo sapiens 199-225 9570722-1 1998 CuZn superoxide dismutase (SOD) secretion was detected in media of [35S]cysteine-labeled human neuroblastoma SK-N-BE cells precipitated with antihuman CuZn SOD antibodies. Cysteine 72-80 superoxide dismutase 1 Homo sapiens 0-25 9570722-1 1998 CuZn superoxide dismutase (SOD) secretion was detected in media of [35S]cysteine-labeled human neuroblastoma SK-N-BE cells precipitated with antihuman CuZn SOD antibodies. Cysteine 72-80 superoxide dismutase 1 Homo sapiens 27-30 7556154-2 1995 The bridging His63 residue in human Cu, Zn superoxide dismutase, which binds both metals, has been replaced by a Cys residue. Cysteine 113-116 superoxide dismutase 1 Homo sapiens 36-63 8035664-3 1994 Oxidation of CYS by HX-XO was equally inhibited by superoxide dismutase (SOD) and catalase (CAT), and that of BSA by HX-XO was inhibited weakly by SOD and strongly by CAT. Cysteine 13-16 superoxide dismutase 1 Homo sapiens 51-71 8035664-3 1994 Oxidation of CYS by HX-XO was equally inhibited by superoxide dismutase (SOD) and catalase (CAT), and that of BSA by HX-XO was inhibited weakly by SOD and strongly by CAT. Cysteine 13-16 superoxide dismutase 1 Homo sapiens 73-76 8035664-3 1994 Oxidation of CYS by HX-XO was equally inhibited by superoxide dismutase (SOD) and catalase (CAT), and that of BSA by HX-XO was inhibited weakly by SOD and strongly by CAT. Cysteine 13-16 superoxide dismutase 1 Homo sapiens 147-150 1665488-0 1991 Conjugates of superoxide dismutase with the Fc fragment of immunoglobulin G. We constructed conjugates of superoxide dismutase (SOD) and the Fc fragment of human immunoglobulin G. The lysyl residues of bovine erythrocyte Cu,Zn-SOD were covalently linked with cysteine residues of the Fc fragment using N-succinimidyl 4-(N-maleimido)-butylate as a crosslinking agent. Cysteine 259-267 superoxide dismutase 1 Homo sapiens 14-34 1665488-0 1991 Conjugates of superoxide dismutase with the Fc fragment of immunoglobulin G. We constructed conjugates of superoxide dismutase (SOD) and the Fc fragment of human immunoglobulin G. The lysyl residues of bovine erythrocyte Cu,Zn-SOD were covalently linked with cysteine residues of the Fc fragment using N-succinimidyl 4-(N-maleimido)-butylate as a crosslinking agent. Cysteine 259-267 superoxide dismutase 1 Homo sapiens 106-126 1665488-0 1991 Conjugates of superoxide dismutase with the Fc fragment of immunoglobulin G. We constructed conjugates of superoxide dismutase (SOD) and the Fc fragment of human immunoglobulin G. The lysyl residues of bovine erythrocyte Cu,Zn-SOD were covalently linked with cysteine residues of the Fc fragment using N-succinimidyl 4-(N-maleimido)-butylate as a crosslinking agent. Cysteine 259-267 superoxide dismutase 1 Homo sapiens 128-131 1958215-1 1991 Human CuZn superoxide dismutase (HSOD) has two free cysteines: a buried cysteine (Cys6) located in a beta-strand, and a solvent accessible cysteine (Cys111) located in a loop region. Cysteine 52-61 superoxide dismutase 1 Homo sapiens 6-31 1958215-1 1991 Human CuZn superoxide dismutase (HSOD) has two free cysteines: a buried cysteine (Cys6) located in a beta-strand, and a solvent accessible cysteine (Cys111) located in a loop region. Cysteine 52-60 superoxide dismutase 1 Homo sapiens 6-31 1958215-1 1991 Human CuZn superoxide dismutase (HSOD) has two free cysteines: a buried cysteine (Cys6) located in a beta-strand, and a solvent accessible cysteine (Cys111) located in a loop region. Cysteine 72-80 superoxide dismutase 1 Homo sapiens 6-31