PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 16910776-4 2006 To examine this question, we used site-directed mutagenesis to produce a mutant form of human MnSOD that has a leucine at amino acid 26 in the active site rather than the usual histidine. Histidine 177-186 superoxide dismutase 2 Homo sapiens 94-99 23461587-4 2013 The major differences between the QM/MM optimized active sites of WT MnSOD and Mn(Fe)SOD are a smaller (His)N-Mn-N(His) equatorial angle and a longer (Gln146(69))NH O(sol) H-bond distance in the metal-substituted protein. Histidine 104-107 superoxide dismutase 2 Homo sapiens 69-74 23461587-4 2013 The major differences between the QM/MM optimized active sites of WT MnSOD and Mn(Fe)SOD are a smaller (His)N-Mn-N(His) equatorial angle and a longer (Gln146(69))NH O(sol) H-bond distance in the metal-substituted protein. Histidine 104-107 superoxide dismutase 2 Homo sapiens 71-74 10488113-1 1999 Histidine 30 in human manganese superoxide dismutase (MnSOD) is located at a site partially exposed to solvent with its side chain participating in a hydrogen-bonded network that includes the active-site residues Tyr(166) and Tyr(34) and extends to the manganese-bound solvent molecule. Histidine 0-9 superoxide dismutase 2 Homo sapiens 22-52 11912930-5 2002 The active site of MnSOD is dominated by a hydrogen bond network comprising the manganese-bound aqueous ligand, the side chains of four residues (Gln-143, Tyr-34, His-30, and Tyr-166 from an adjacent subunit), as well as other water molecules. Histidine 163-166 superoxide dismutase 2 Homo sapiens 19-24 15128298-6 2004 The coding sequences were expressed in Escherichia coli as six-histidine tagged recombinant proteins and generated products with molecular masses of 86.1 kDa for HSP and 22.4 kDa for MnSOD. Histidine 63-72 superoxide dismutase 2 Homo sapiens 183-188 12651009-6 2003 The purification of MnSOD was performed by chromatography applying the His-tag technology. Histidine 71-74 superoxide dismutase 2 Homo sapiens 20-25 12627943-0 2003 Catalytic and structural effects of amino acid substitution at histidine 30 in human manganese superoxide dismutase: insertion of valine C gamma into the substrate access channel. Histidine 63-72 superoxide dismutase 2 Homo sapiens 85-115 10488113-1 1999 Histidine 30 in human manganese superoxide dismutase (MnSOD) is located at a site partially exposed to solvent with its side chain participating in a hydrogen-bonded network that includes the active-site residues Tyr(166) and Tyr(34) and extends to the manganese-bound solvent molecule. Histidine 0-9 superoxide dismutase 2 Homo sapiens 54-59 10488113-2 1999 We have replaced His(30) with a series of amino acids and Tyr(166) with Phe in human MnSOD. Histidine 17-20 superoxide dismutase 2 Homo sapiens 85-90 28165386-5 2017 Markedly, oxidative modifications of MNSOD were identified at histidine (H54 and H55), tyrosine (Y58), tryptophan (W147, W149, W205 and W210) and asparagine (N206 and N209) residues additional to methionine. Histidine 62-71 superoxide dismutase 2 Homo sapiens 37-42 9685724-6 1998 Amino acid substitutions at a signal peptide-cleavage site, His-Ser-Leu4 to Pro-Met-Va14, in the mature Mn-SOD prevented the processing of the precursor protein, and thus resulted in the accumulation of the precursor protein within mitochondria, as judged on immunostaining with an anti-Mn-SOD antibody. Histidine 60-63 superoxide dismutase 2 Homo sapiens 104-110 9685724-6 1998 Amino acid substitutions at a signal peptide-cleavage site, His-Ser-Leu4 to Pro-Met-Va14, in the mature Mn-SOD prevented the processing of the precursor protein, and thus resulted in the accumulation of the precursor protein within mitochondria, as judged on immunostaining with an anti-Mn-SOD antibody. Histidine 60-63 superoxide dismutase 2 Homo sapiens 287-293 34021366-1 2021 We have generated a mutant of C. elegans manganese superoxide dismutase at histidine 30 by site-directed mutagenesis. Histidine 75-84 superoxide dismutase 2 Homo sapiens 41-71