PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 10852710-1 2000 Glutamine 143 in human manganese superoxide dismutase (MnSOD) forms a hydrogen bond with the manganese-bound solvent molecule and is investigated by replacement using site-specific mutagenesis. Manganese 23-32 superoxide dismutase 2 Homo sapiens 55-60 10852710-3 2000 Two new water molecules in Q143A MnSOD were situated in positions nearly identical with the Oepsilon1 and Nepsilon2 of the replaced Gln 143 side chain and maintained a hydrogen-bonded network connecting the manganese-bound solvent molecule to other residues in the active site. Manganese 207-216 superoxide dismutase 2 Homo sapiens 33-38 10512624-1 1999 Tryptophan 161 is a highly conserved residue that forms a hydrophobic side of the active site cavity of manganese superoxide dismutase (MnSOD), with its indole ring adjacent to and about 5 A from the manganese. Manganese 104-113 superoxide dismutase 2 Homo sapiens 136-141 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. Manganese 22-31 superoxide dismutase 2 Homo sapiens 54-59 10509755-5 1999 Manganese (Mn) SOD activity was increased when HepG2 cells were treated for 1 day with 0.50 or 0.75 mM clofibric acid. Manganese 0-9 superoxide dismutase 2 Homo sapiens 15-18 10512624-5 1999 The tryptophan in MnSOD is not essential for the half-cycle of catalytic activity involving reduction of the manganese; the mutant W161F MnSOD had k(cat)/K(m) at 2.5 x 10(8) M(-)(1) s(-)(1), reduced only 3-fold compared with wild type. Manganese 109-118 superoxide dismutase 2 Homo sapiens 137-142 9603906-7 1998 This residue is located near manganese and in a substrate O-2 gateway in Mn-SOD. Manganese 29-38 superoxide dismutase 2 Homo sapiens 73-79 10455106-1 1999 The reduction with excess H(2)O(2) of human Mn(III) superoxide dismutase (SOD) and the active-site mutant Y34F Mn(III)SOD was measured by scanning stopped-flow spectrophotometry and revealed the presence of an intermediate in the reduction of the manganese. Manganese 247-256 superoxide dismutase 2 Homo sapiens 74-77 34547605-1 2021 Mononuclear manganese(III) peroxido complexes are candidates for the reaction intermediates in manganese containing proteins, such as manganese superoxide dismutase (Mn-SOD) etc. Manganese 95-104 superoxide dismutase 2 Homo sapiens 134-164 9537988-1 1998 Structural and biochemical characterization of the nonliganding residue glutamine 143 near the manganese of human Mn superoxide dismutase (hMnSOD), a homotetramer of 22 kDa, reveals a functional role for this residue. Manganese 95-104 superoxide dismutase 2 Homo sapiens 114-137 9537988-1 1998 Structural and biochemical characterization of the nonliganding residue glutamine 143 near the manganese of human Mn superoxide dismutase (hMnSOD), a homotetramer of 22 kDa, reveals a functional role for this residue. Manganese 95-104 superoxide dismutase 2 Homo sapiens 139-145 9537988-10 1998 Also, unlike the wild-type Mn(III)SOD, which is electron paramagnetic resonance (EPR) silent, Q143N MnSOD has a complex EPR spectrum with many resonances in the region below 2250 G. We conclude that the Gln 143 --> Asn mutation has increased the reduction potential of manganese to stabilize Mn(II), indicating that Gln 143 has a substantial role in maintaining a reduction potential favorable for the oxidation and reduction cycles in the catalytic disproportionation of superoxide. Manganese 272-281 superoxide dismutase 2 Homo sapiens 100-105 7593237-2 1995 SOD-1 (a copper and zinc containing form of SOD) and SOD-2 (a manganese containing form of the enzyme) activities were both observed to be significantly lower in cell lines derived from fetal skin than in lines established from postnatal skin (ages 17-94 years). Manganese 62-71 superoxide dismutase 2 Homo sapiens 53-58 1582797-2 1992 Biochemical and immunochemical techniques were used to compare levels of copper-zinc- and manganese-containing forms of SOD (CuZn-SOD and Mn-SOD) in human adult and fetal RPE cells. Manganese 90-99 superoxide dismutase 2 Homo sapiens 120-123 1582797-2 1992 Biochemical and immunochemical techniques were used to compare levels of copper-zinc- and manganese-containing forms of SOD (CuZn-SOD and Mn-SOD) in human adult and fetal RPE cells. Manganese 90-99 superoxide dismutase 2 Homo sapiens 130-133 1550052-4 1992 Manganese supplementation resulted in significant increases in lymphocyte MnSOD activity and serum manganese concentrations from baseline values but no changes in urinary manganese excretion or in any indices of iron status. Manganese 0-9 superoxide dismutase 2 Homo sapiens 74-79 1550052-6 1992 This work demonstrated that lymphocyte MnSOD activity can be used with serum manganese concentrations to monitor manganese exposure in humans. Manganese 77-86 superoxide dismutase 2 Homo sapiens 39-44 1550052-6 1992 This work demonstrated that lymphocyte MnSOD activity can be used with serum manganese concentrations to monitor manganese exposure in humans. Manganese 113-122 superoxide dismutase 2 Homo sapiens 39-44 34547605-1 2021 Mononuclear manganese(III) peroxido complexes are candidates for the reaction intermediates in manganese containing proteins, such as manganese superoxide dismutase (Mn-SOD) etc. Manganese 95-104 superoxide dismutase 2 Homo sapiens 166-172 7264869-4 1981 One g-atom each of copper and zinc was contained in the subunit of Cu,Zn-SOD, and one g-atom of manganese was contained in the subunit of Mn-SOD. Manganese 96-105 superoxide dismutase 2 Homo sapiens 138-144 34402900-2 2021 Manganese (Mn) is critical for CL function as it is a cofactor for Mn superoxide dismutase (MnSOD) and enzymes involved in cholesterol synthesis. Manganese 0-9 superoxide dismutase 2 Homo sapiens 67-90 34402900-2 2021 Manganese (Mn) is critical for CL function as it is a cofactor for Mn superoxide dismutase (MnSOD) and enzymes involved in cholesterol synthesis. Manganese 0-9 superoxide dismutase 2 Homo sapiens 92-97 34362891-5 2021 By the Paleoproterozoic, they became genetically capable of using iron, nickel, and manganese as cofactors (FeSOD, NiSOD, and MnSOD respectively). Manganese 84-93 superoxide dismutase 2 Homo sapiens 126-131 33015038-2 2020 Superoxide dismutase (SOD) 2 is a manganese-containing enzyme located in mitochondria that protects cells against oxidative stress by scavenging reactive oxygen species (ROS). Manganese 34-43 superoxide dismutase 2 Homo sapiens 0-28 30536754-5 2019 Moreover, the redox gene encoding the manganese-dependent mitochondrial enzyme, superoxide dismutase (SOD)2, was strongly induced at the mRNA and protein levels by multiple signaling pathways downstream of TLR2, namely JAK-STAT3, JNK MAPK and NF-kappaB. Manganese 38-47 superoxide dismutase 2 Homo sapiens 80-107 31904901-4 2020 Superoxide anions are metabolized by manganese-dependent superoxide dismutase (SOD2) in the mitochondria. Manganese 37-46 superoxide dismutase 2 Homo sapiens 79-83 31086870-0 2019 Manganese influx and expression of ZIP8 is essential in primary myoblasts and contributes to activation of SOD2. Manganese 0-9 superoxide dismutase 2 Homo sapiens 107-111 29936984-2 2018 We previously reported that the macromolecular response of BE cells to this stress was largely regulated by the expression of manganese-dependent mitochondrial superoxide dismutase (MnSOD). Manganese 126-135 superoxide dismutase 2 Homo sapiens 182-187 30279321-0 2018 Redox manipulation of the manganese metal in human manganese superoxide dismutase for neutron diffraction. Manganese 26-35 superoxide dismutase 2 Homo sapiens 51-81 21671088-0 2011 Manganese regulates manganese-containing superoxide dismutase (MnSOD) expression in the primary broiler myocardial cells. Manganese 0-9 superoxide dismutase 2 Homo sapiens 20-61 28100855-9 2016 Manganese, copper and zinc are a part of the group of superoxide dismutase enzymes (MnSOD, Cu/ZnSOD), which catalyse the superoxide anion dismutation into hydrogen peroxide and oxygen. Manganese 0-9 superoxide dismutase 2 Homo sapiens 84-89 27212182-0 2016 The kinetics of the effect of manganese supplementation on SOD2 activity in senescent human fibroblasts. Manganese 30-39 superoxide dismutase 2 Homo sapiens 59-63 26436856-4 2015 Cu(2+) was reduced to Cu(1+), while manganese appears to be released from MnSOD active center. Manganese 36-45 superoxide dismutase 2 Homo sapiens 74-79 29293455-1 2018 Manganese (Mn) is an essential nutrient for intracellular activities; it functions as a cofactor for a variety of enzymes, including arginase, glutamine synthetase (GS), pyruvate carboxylase and Mn superoxide dismutase (Mn-SOD). Manganese 0-9 superoxide dismutase 2 Homo sapiens 195-218 29293455-1 2018 Manganese (Mn) is an essential nutrient for intracellular activities; it functions as a cofactor for a variety of enzymes, including arginase, glutamine synthetase (GS), pyruvate carboxylase and Mn superoxide dismutase (Mn-SOD). Manganese 0-9 superoxide dismutase 2 Homo sapiens 220-226 26857738-0 2016 Manganese elevates manganese superoxide dismutase protein level through protein kinase C and protein tyrosine kinase. Manganese 0-9 superoxide dismutase 2 Homo sapiens 19-49 23566586-3 2013 Among the antioxidant enzymes, the manganese-dependent and mitochondria-specific isoform of SOD (MnSOD) represents the first line of defense against superoxide radicals attack. Manganese 35-44 superoxide dismutase 2 Homo sapiens 59-95 23566586-3 2013 Among the antioxidant enzymes, the manganese-dependent and mitochondria-specific isoform of SOD (MnSOD) represents the first line of defense against superoxide radicals attack. Manganese 35-44 superoxide dismutase 2 Homo sapiens 97-102 23461587-2 2013 On the basis of electronic absorption, circular dichroism (CD), magnetic CD (MCD), and variable-temperature variable-field MCD data obtained for oxidized Mn(Fe)SOD, we propose that the active site of this species is virtually identical to that of wild-type manganese SOD (MnSOD), with both containing a metal ion that resides in a trigonal bipyramidal ligand environment. Manganese 257-266 superoxide dismutase 2 Homo sapiens 160-163 22247543-4 2012 Cellular pools of iron can outcompete manganese for binding to manganese superoxide dismutase, and through Fenton chemistry, iron may counteract the benefits of non-proteinaceous manganese antioxidants. Manganese 38-47 superoxide dismutase 2 Homo sapiens 63-93 21671088-0 2011 Manganese regulates manganese-containing superoxide dismutase (MnSOD) expression in the primary broiler myocardial cells. Manganese 0-9 superoxide dismutase 2 Homo sapiens 63-68 21671088-1 2011 Previous studies showed that dietary manganese can increase the MnSOD mRNA expression in a dose-dependent manner in the heart of broilers. Manganese 37-46 superoxide dismutase 2 Homo sapiens 64-69 21671088-2 2011 In order to explore the specific mechanism of the MnSOD expression induced by manganese, a model of MnSOD expression was developed with primary cultured broiler myocardial cells. Manganese 78-87 superoxide dismutase 2 Homo sapiens 50-55 21671088-6 2011 The results showed that MnSOD mRNA, MnSOD protein, and MnSOD activity were induced by manganese in dose- and time-dependent manner. Manganese 86-95 superoxide dismutase 2 Homo sapiens 24-29 21671088-6 2011 The results showed that MnSOD mRNA, MnSOD protein, and MnSOD activity were induced by manganese in dose- and time-dependent manner. Manganese 86-95 superoxide dismutase 2 Homo sapiens 36-41 21671088-6 2011 The results showed that MnSOD mRNA, MnSOD protein, and MnSOD activity were induced by manganese in dose- and time-dependent manner. Manganese 86-95 superoxide dismutase 2 Homo sapiens 36-41 21671088-7 2011 Manganese regulates MnSOD expression not only at transcriptional level but also at translational and/or posttranslational levels. Manganese 0-9 superoxide dismutase 2 Homo sapiens 20-25 18373354-2 2008 Glu162 in homotetrameric human MnSOD spans a dimeric interface and forms a hydrogen bond with His163 of an adjacent subunit which is a direct ligand of the manganese. Manganese 156-165 superoxide dismutase 2 Homo sapiens 31-36 20617513-3 2011 Here, we report that manganese-enhanced magnetic resonance imaging (MEMRI) represents a promising approach for a more selective mesothelioma imaging by monitoring a high-level expression of manganese-superoxide dismutase (Mn-SOD), which is observed in many MM. Manganese 21-30 superoxide dismutase 2 Homo sapiens 190-220 19636420-1 2009 Manganese and extracellular superoxide dismutases (SOD2 and SOD3) are part of the enzymatic defence against reactive oxygen species, which are involved in the pathogenesis of asbestosis. Manganese 0-9 superoxide dismutase 2 Homo sapiens 51-55 17576015-3 2007 The manganese-containing enzyme, manganese superoxide dismutase (Mn-SOD), is the principal antioxidant enzyme which neutralizes the toxic effects of reactive oxygen species. Manganese 4-13 superoxide dismutase 2 Homo sapiens 65-71 17576015-3 2007 The manganese-containing enzyme, manganese superoxide dismutase (Mn-SOD), is the principal antioxidant enzyme which neutralizes the toxic effects of reactive oxygen species. Manganese 4-13 superoxide dismutase 2 Homo sapiens 33-63 17435022-0 2007 Gene expression of manganese-containing superoxide dismutase as a biomarker of manganese bioavailability for manganese sources in broilers. Manganese 79-88 superoxide dismutase 2 Homo sapiens 19-60 17916951-2 2007 Manganese (Mn), the key component of the Mitochondrial antioxidant (MnSOD), plays a key role in the superoxide uncoupling protein 2 (UCP-2) pathway in inhibiting of glucose-stimulated insulin secretion (GSIS). Manganese 0-9 superoxide dismutase 2 Homo sapiens 68-73 15977906-5 2005 Inhibitor studies with purified recombinant Cu/ ZnSOD and MnSOD, both of which were functionally expressed in Escherichia coli, confirmed that they are copper/zinc and manganese-containing SOD, respectively. Manganese 168-177 superoxide dismutase 2 Homo sapiens 58-63 17165602-4 2006 Manganese plays significant role in the free radical defense system as MnSOD, which protects the endothelial and red blood cells and mitochondria from the damage caused by superoxide radicals. Manganese 0-9 superoxide dismutase 2 Homo sapiens 71-76 11491657-1 2001 Cancer cells are in general low in the enzymatic activities of both manganese-containing (MnSOD) and copper- and zinc-containing superoxide dismutase. Manganese 68-77 superoxide dismutase 2 Homo sapiens 90-95 12127599-2 2002 The manganese-containing form of this enzyme (MnSOD) is the major superoxide scavenger in mitochondria; a weak association between a functional genetic polymorphism (Ala-9Val) in the mitochondrial targeting sequence (MTS) of this enzyme and TD has been reported in a Japanese population. Manganese 4-13 superoxide dismutase 2 Homo sapiens 46-51 12126755-4 2002 SOD2, or Mn-SOD (EC 1.15.1.1), exists as a tetramer and is initially synthesized containing a leader peptide, which targets this manganese-containing enzyme exclusively to the mitochondrial spaces. Manganese 129-138 superoxide dismutase 2 Homo sapiens 0-4 12126755-4 2002 SOD2, or Mn-SOD (EC 1.15.1.1), exists as a tetramer and is initially synthesized containing a leader peptide, which targets this manganese-containing enzyme exclusively to the mitochondrial spaces. Manganese 129-138 superoxide dismutase 2 Homo sapiens 9-15 11801664-8 2002 Like MnSODs of other eukaryotic organisms, A. fumigatus MnSOD forms a homotetramer with the manganese ions coordinated by three histidines, one aspartic acid, and one water molecule. Manganese 92-101 superoxide dismutase 2 Homo sapiens 5-10 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. Manganese 80-89 superoxide dismutase 2 Homo sapiens 19-24 11555836-2 2001 Manganese (Mn)(2+)-dependent superoxide dismutase (SOD-2) is primarily responsible for metabolism of superoxide produced in mitochondria by respiratory chain activity during aerobic metabolism of glucose and other substrates. Manganese 0-9 superoxide dismutase 2 Homo sapiens 51-56 15170341-1 2004 The side chain of Gln143, a conserved residue in manganese superoxide dismutase (MnSOD), forms a hydrogen bond with the manganese-bound solvent and is critical in maintaining catalytic activity. Manganese 49-58 superoxide dismutase 2 Homo sapiens 81-86 11062559-4 2000 A single manganese ion is bound per germin monomer by ligands similar to those of manganese superoxide dismutase (MnSOD). Manganese 9-18 superoxide dismutase 2 Homo sapiens 82-112 11062559-4 2000 A single manganese ion is bound per germin monomer by ligands similar to those of manganese superoxide dismutase (MnSOD). Manganese 9-18 superoxide dismutase 2 Homo sapiens 114-119 10882843-2 2000 In the present study, we investigated the genetic association between a functional polymorphism (Ala-9Val) in the human manganese (Mn) SOD gene and schizophrenia or TD (192 schizophrenics: 39 with TD and 153 without TD; 141 controls). Manganese 120-129 superoxide dismutase 2 Homo sapiens 135-138