PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 24152914-6 2013 When Cu,Zn-SOD that has been exposed to acrolein was subsequently analyzed by amino acid analysis, serine, histidine, arginine, threonine and lysine residues were particularly sensitive. Histidine 107-116 superoxide dismutase 1 Homo sapiens 11-14 24369116-4 2014 Our results show considerable differences in H43R compared to WT and W32F mutated SOD1, such as increasing distances between the critical residues results in open conformation at the active site, strong fluctuations in the important loops (Zinc and electrostatic loops) and weakening of important hydrogen bonds especially between N (His 43/Arg 43) and carbonyl oxygen (His 120) in agreement with the experimental report. Histidine 334-337 superoxide dismutase 1 Homo sapiens 82-86 24369116-4 2014 Our results show considerable differences in H43R compared to WT and W32F mutated SOD1, such as increasing distances between the critical residues results in open conformation at the active site, strong fluctuations in the important loops (Zinc and electrostatic loops) and weakening of important hydrogen bonds especially between N (His 43/Arg 43) and carbonyl oxygen (His 120) in agreement with the experimental report. Histidine 370-373 superoxide dismutase 1 Homo sapiens 82-86 16792821-3 2006 We also purified histidine-tagged SOD without an HIV-1 Tat and Tat-GFP as control proteins. Histidine 17-26 superoxide dismutase 1 Homo sapiens 34-37 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. Histidine 161-170 superoxide dismutase 1 Homo sapiens 104-108 18365046-1 2003 His-Val-His and His-Val-Gly-Asp are two naturally occurring peptide sequences, present at the active site of Cu,Zn-superoxide dismutase (Cu,Zn-SOD). Histidine 0-3 superoxide dismutase 1 Homo sapiens 109-135 15123612-7 2004 Both proton ((1)H) and nitrogen ((14)N) ENDOR studies of bSOD1 and hSOD1 in the presence of H(2)O(2) revealed a change in the geometry of His-46 (or His-44) and His-48 (or His-46) coordinated to Cu(II) at the active site of WT hSOD1 and bSOD1, respectively. Histidine 138-141 superoxide dismutase 1 Homo sapiens 67-72 15123612-7 2004 Both proton ((1)H) and nitrogen ((14)N) ENDOR studies of bSOD1 and hSOD1 in the presence of H(2)O(2) revealed a change in the geometry of His-46 (or His-44) and His-48 (or His-46) coordinated to Cu(II) at the active site of WT hSOD1 and bSOD1, respectively. Histidine 138-141 superoxide dismutase 1 Homo sapiens 227-232 15123612-7 2004 Both proton ((1)H) and nitrogen ((14)N) ENDOR studies of bSOD1 and hSOD1 in the presence of H(2)O(2) revealed a change in the geometry of His-46 (or His-44) and His-48 (or His-46) coordinated to Cu(II) at the active site of WT hSOD1 and bSOD1, respectively. Histidine 149-152 superoxide dismutase 1 Homo sapiens 67-72 15123612-7 2004 Both proton ((1)H) and nitrogen ((14)N) ENDOR studies of bSOD1 and hSOD1 in the presence of H(2)O(2) revealed a change in the geometry of His-46 (or His-44) and His-48 (or His-46) coordinated to Cu(II) at the active site of WT hSOD1 and bSOD1, respectively. Histidine 149-152 superoxide dismutase 1 Homo sapiens 67-72 15123612-7 2004 Both proton ((1)H) and nitrogen ((14)N) ENDOR studies of bSOD1 and hSOD1 in the presence of H(2)O(2) revealed a change in the geometry of His-46 (or His-44) and His-48 (or His-46) coordinated to Cu(II) at the active site of WT hSOD1 and bSOD1, respectively. Histidine 149-152 superoxide dismutase 1 Homo sapiens 67-72 15469714-7 2004 When Cu,Zn-SOD that had been exposed to catecholamines was subsequently analyzed by an amino acid analysis, the glycine and histidine residues were particularly sensitive. Histidine 124-133 superoxide dismutase 1 Homo sapiens 11-14 14658402-1 2003 We report the clinical and neuropathological features of a Japanese family with familial amyotrophic lateral sclerosis (FALS), whose members have an amino acid substitution of histidine by arginine in Cu/Zn superoxide dismutase. Histidine 176-185 superoxide dismutase 1 Homo sapiens 201-227 15096035-1 2004 Cu-Zn superoxide dismutase (SOD) contains a conserved, metal-free His residue at an opening of the backbone beta-barrel in addition to six Cu- and/or Zn-bound His residues in the active site. Histidine 66-69 superoxide dismutase 1 Homo sapiens 28-31 15096035-1 2004 Cu-Zn superoxide dismutase (SOD) contains a conserved, metal-free His residue at an opening of the backbone beta-barrel in addition to six Cu- and/or Zn-bound His residues in the active site. Histidine 159-162 superoxide dismutase 1 Homo sapiens 28-31 15096035-2 2004 We examined the protonation and hydrogen bonding state of the metal-free His residue (His41) in bovine SOD by UV Raman spectroscopy. Histidine 73-76 superoxide dismutase 1 Homo sapiens 103-106 18365046-0 2003 Interaction of Cu(II)with His-Val-Gly-Asp and of Zn(II) with His-Val-His, two peptides at the active site of Cu,Zn-superoxide dismutase. Histidine 26-29 superoxide dismutase 1 Homo sapiens 109-135 18365046-0 2003 Interaction of Cu(II)with His-Val-Gly-Asp and of Zn(II) with His-Val-His, two peptides at the active site of Cu,Zn-superoxide dismutase. Histidine 61-64 superoxide dismutase 1 Homo sapiens 109-135 18365046-0 2003 Interaction of Cu(II)with His-Val-Gly-Asp and of Zn(II) with His-Val-His, two peptides at the active site of Cu,Zn-superoxide dismutase. Histidine 61-64 superoxide dismutase 1 Homo sapiens 109-135 18365046-1 2003 His-Val-His and His-Val-Gly-Asp are two naturally occurring peptide sequences, present at the active site of Cu,Zn-superoxide dismutase (Cu,Zn-SOD). Histidine 0-3 superoxide dismutase 1 Homo sapiens 137-146 8194601-2 1994 The hyperfine couplings of the remote nitrogens of histidine ligands are determined for the first time by an X-band ESEEM spectroscopy study of 15N-substituted superoxide dismutase (SOD). Histidine 51-60 superoxide dismutase 1 Homo sapiens 160-180 12356748-5 2002 Oxidation of select histidine residues that bind metals in the active site mediates SOD1 aggregation. Histidine 20-29 superoxide dismutase 1 Homo sapiens 84-88 12127151-2 2002 To test the hypothesis that the toxicity of mutant SOD1 originates in Cu(2+)-mediated formation of toxic radicals, we generated transgenic mice that express human SOD1 that encodes disease-linked mutations at two of the four histidine residues that are crucial for the coordinated binding of copper (H46R/H48Q). Histidine 225-234 superoxide dismutase 1 Homo sapiens 163-167 27406670-5 1996 A change in tyrosine at the 32 position in the heavy chain and histidine at position 27 of the light chain of the NQ11.7.22-Fv fragment results in a profound reduction in SOD-like activity. Histidine 63-72 superoxide dismutase 1 Homo sapiens 171-174 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. Histidine 207-210 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. Histidine 207-210 superoxide dismutase 1 Homo sapiens 234-238 11551383-0 2001 Interaction of Cu(2+) with His-Val-His and of Zn(2+) with His-Val-Gly-Asp, two peptides surrounding metal ions in Cu,Zn-superoxide dismutase enzyme. Histidine 27-30 superoxide dismutase 1 Homo sapiens 114-140 11551383-1 2001 His-Val-His and His-Val-Gly-Asp are two naturally occurring peptide sequences, present at the active site of Cu,Zn-superoxide dismutase (Cu,Zn-SOD). Histidine 0-3 superoxide dismutase 1 Homo sapiens 109-135 11551383-1 2001 His-Val-His and His-Val-Gly-Asp are two naturally occurring peptide sequences, present at the active site of Cu,Zn-superoxide dismutase (Cu,Zn-SOD). Histidine 0-3 superoxide dismutase 1 Homo sapiens 137-146 9409355-3 1997 We detected a point mutation at codon 48 of the Cu/Zn superoxide dismutase gene (SOD1) leading to a substitution of histidine by glutamine in the copper-binding domain. Histidine 116-125 superoxide dismutase 1 Homo sapiens 48-74 9409355-3 1997 We detected a point mutation at codon 48 of the Cu/Zn superoxide dismutase gene (SOD1) leading to a substitution of histidine by glutamine in the copper-binding domain. Histidine 116-125 superoxide dismutase 1 Homo sapiens 81-85 8194601-2 1994 The hyperfine couplings of the remote nitrogens of histidine ligands are determined for the first time by an X-band ESEEM spectroscopy study of 15N-substituted superoxide dismutase (SOD). Histidine 51-60 superoxide dismutase 1 Homo sapiens 182-185 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. Histidine 117-120 superoxide dismutase 1 Homo sapiens 44-48 2368186-7 1990 Such metal-chelating agents as histidine and organic acids increase the SOD activity in gastric juice. Histidine 31-40 superoxide dismutase 1 Homo sapiens 72-75 2166134-6 1990 The analysis has shown that the histidine hydrogens involved in metal binding at the enzyme active site are the same in both native and PEG-modified SOD. Histidine 32-41 superoxide dismutase 1 Homo sapiens 149-152 32212239-7 2020 This tight regulation of charge by SOD1 is attributed to the protonation of the bridging histidine upon copper reduction, yielding redox centers that are isoelectric at both oxidation states. Histidine 89-98 superoxide dismutase 1 Homo sapiens 35-39 30284207-2 2019 A bacterial expression system was used to produce human recombinant manganese SOD with a His-tag on the C-end of the protein for better purification. Histidine 89-92 superoxide dismutase 1 Homo sapiens 78-81 26791423-5 2016 His residues constructing the Cu(2+)-binding site in denatured apo-H43R were experimentally assigned by absorption and fluorescence-based assays of SOD1 mutants, in which each of the seven His residues in H43R SOD1 is replaced with Ala. Histidine 0-3 superoxide dismutase 1 Homo sapiens 148-152 26791423-5 2016 His residues constructing the Cu(2+)-binding site in denatured apo-H43R were experimentally assigned by absorption and fluorescence-based assays of SOD1 mutants, in which each of the seven His residues in H43R SOD1 is replaced with Ala. Histidine 0-3 superoxide dismutase 1 Homo sapiens 210-214