PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 33867736-7 2021 Following iron therapy, hematological parameters was improved together with a significant increase in GPx (P = 0.04), SOD (p = 0.002), TAC (P = 0.001) and non-significant reduction in DNA damage in IDA group. Iron 10-14 superoxide dismutase 1 Homo sapiens 118-121 6466333-1 1984 Reaction of H2O2 with iron containing superoxide dismutase (SOD) was studied by absorption spectroscopy, activity measurement and amino acid analysis. Iron 22-26 superoxide dismutase 1 Homo sapiens 38-58 6466333-1 1984 Reaction of H2O2 with iron containing superoxide dismutase (SOD) was studied by absorption spectroscopy, activity measurement and amino acid analysis. Iron 22-26 superoxide dismutase 1 Homo sapiens 60-63 6171347-1 1981 Inhibition of bleomycin (BLM)-induced DNA breakage by superoxide dismutase (SOD) has been reported and presumed to be due to its removal of the superoxide free radicals generated by BLM in the presence of iron(II). Iron 205-209 superoxide dismutase 1 Homo sapiens 54-74 6171347-1 1981 Inhibition of bleomycin (BLM)-induced DNA breakage by superoxide dismutase (SOD) has been reported and presumed to be due to its removal of the superoxide free radicals generated by BLM in the presence of iron(II). Iron 205-209 superoxide dismutase 1 Homo sapiens 76-79 2630018-2 1989 It was found that after iron particles were implanted into the vitreous bodies (1) iron concentration in the aqueous humour rose rapidly and significantly (n = 24, P less than 0.01), (2) malondialdehyde (MDA) a degradation metabolite of lipid peroxidation, in the retinas increased significantly (n = 24, P less than 0.05), and (3) superoxide dismutase (SOD) activity decreased (n = 11, P less than 0.05). Iron 24-28 superoxide dismutase 1 Homo sapiens 332-352 2630018-2 1989 It was found that after iron particles were implanted into the vitreous bodies (1) iron concentration in the aqueous humour rose rapidly and significantly (n = 24, P less than 0.01), (2) malondialdehyde (MDA) a degradation metabolite of lipid peroxidation, in the retinas increased significantly (n = 24, P less than 0.05), and (3) superoxide dismutase (SOD) activity decreased (n = 11, P less than 0.05). Iron 24-28 superoxide dismutase 1 Homo sapiens 354-357 2489896-11 1989 3) We observed positive effects on the induction of SOD activity and proliferation by the supplementation of iron, managnese, or both in the metal chlated medium under aerobic condition. Iron 109-113 superoxide dismutase 1 Homo sapiens 52-55 2489896-12 1989 Based on the above results, we found that iron and manganese were essential metals for SOD activity induction. Iron 42-46 superoxide dismutase 1 Homo sapiens 87-90 2843167-3 1988 The hydroxyl-radical formation enhanced by SOD was inhibited by catalase and desferrioxamine, and stimulated by EDTA and diethylenetriaminepenta-acetic acid, suggesting that both hydrogen peroxide and iron ions participate in the reaction. Iron 201-205 superoxide dismutase 1 Homo sapiens 43-46 34022567-11 2021 Several genes of iron metabolism presented a higher expression in DIOS vs MetS: SCL11A2 (a free iron transporter, +76 %, p = 0.04), SOD1 (an antioxidant enzyme, +27 %, p = 0.02), and TFRC (the receptor 1 of transferrin, +59 %, p = 0.003). Iron 17-21 superoxide dismutase 1 Homo sapiens 132-136 30697143-0 2018 The Relevancy of Data Regarding the Metabolism of Iron to Our Understanding of Deregulated Mechanisms in ALS; Hypotheses and Pitfalls. Iron 50-54 superoxide dismutase 1 Homo sapiens 105-108 33683742-8 2021 UL iron significantly reduced glutathione peroxidase (GSH-Px), superoxide dismutase (SOD), catalase (CAT) and total anti-oxidation capacity (T-AOC) in the liver (p < 0.05). Iron 3-7 superoxide dismutase 1 Homo sapiens 63-83 33683742-8 2021 UL iron significantly reduced glutathione peroxidase (GSH-Px), superoxide dismutase (SOD), catalase (CAT) and total anti-oxidation capacity (T-AOC) in the liver (p < 0.05). Iron 3-7 superoxide dismutase 1 Homo sapiens 85-88 32243658-4 2020 The monoatomic and highly dispersed Fe ions in MPGs can both serve as the efficient cross-linkers of gel network, and interestedly also the vital active center of multienzyme mimic of superoxide dismutase (SOD) and peroxidase (POD) activity. Iron 36-38 superoxide dismutase 1 Homo sapiens 184-204 32243658-4 2020 The monoatomic and highly dispersed Fe ions in MPGs can both serve as the efficient cross-linkers of gel network, and interestedly also the vital active center of multienzyme mimic of superoxide dismutase (SOD) and peroxidase (POD) activity. Iron 36-38 superoxide dismutase 1 Homo sapiens 206-209 30513241-0 2019 50-Hz magnetic field impairs the expression of iron-related genes in the in vitro SOD1G93A model of amyotrophic lateral sclerosis. Iron 47-51 superoxide dismutase 1 Homo sapiens 82-86 30513241-4 2019 CONCLUSIONS: 50-Hz MF affects iron homeostasis in the in vitro SOD1G93A ALS model. Iron 30-34 superoxide dismutase 1 Homo sapiens 63-67 31814879-7 2019 The association between dietary iron intake and cellular aging markers and TNFalpha and superoxide dismutase (SOD) was analyzed by Pearson correlation analysis and regression models adjusted by covariates. Iron 32-36 superoxide dismutase 1 Homo sapiens 88-108 31814879-12 2019 Moreover, iron intake was positively associated with TNFalpha in both women and men but positively associated with SOD only in men. Iron 10-14 superoxide dismutase 1 Homo sapiens 115-118 30697143-3 2018 Iron accumulation has been observed in both sporadic and familial forms of ALS, including mouse models. Iron 0-4 superoxide dismutase 1 Homo sapiens 75-78 30697143-4 2018 Therefore, the dysregulation of iron metabolism could play a role in the pathological oxidative stress in ALS. Iron 32-36 superoxide dismutase 1 Homo sapiens 106-109 30697143-6 2018 Reports of accumulation of iron, high serum ferritin, and low serum transferrin levels in ALS patients have encouraged researchers to consider dysregulated iron metabolism as an integral part of ALS pathophysiology. Iron 156-160 superoxide dismutase 1 Homo sapiens 195-198 30697143-9 2018 Furthermore, the iron regulatory pathways, particularly involving hepcidin, have not been thoroughly explored yet within the pathogenesis of iron overload in ALS. Iron 141-145 superoxide dismutase 1 Homo sapiens 158-161 30697143-10 2018 In this sense, it is also essential to explore the relation between iron overload and other ALS-related events, such as neuro-inflammation, protein aggregation, and iron-driven cell death, termed ferroptosis. Iron 68-72 superoxide dismutase 1 Homo sapiens 92-95 30697143-11 2018 In this review, we point out limits of the designs of certain studies that may prevent the understanding of the role of iron in ALS and discuss the relevance of the published data regarding the pathogenic impact of iron metabolism deregulation in this disease and the therapeutics targeting this pathway. Iron 120-124 superoxide dismutase 1 Homo sapiens 128-131 27356602-12 2016 However, it should be considered that overexpression of the SOD1 gene usually leads to increased SOD1 enzymatic activity, a condition which does not occur in human pathology and which may itself change the expression of iron metabolism genes. Iron 220-224 superoxide dismutase 1 Homo sapiens 60-64 30723395-4 2019 The process of misfolding and aggregation of neuronal proteins such as alpha-synuclein, Tau, amyloid beta (Abeta), TDP-43 or SOD1 is a common hallmark of many neurodegenerative disorders and iron has been shown to facilitate protein aggregation. Iron 191-195 superoxide dismutase 1 Homo sapiens 125-129 30465670-1 2018 Atomically dispersed Fe-N4 sites anchored on N-doped porous carbon materials (Fe-SAs/NC) can mimic two antioxidative enzymes of catalase (CAT) and superoxide dismutase (SOD), and therefore serves as a bifunctional single-atom-based enzyme (SAzyme) for scavenging reactive oxygen species (ROS) to remove excess ROS generated during oxidative stress in cells. Iron 21-23 superoxide dismutase 1 Homo sapiens 147-167 30465670-1 2018 Atomically dispersed Fe-N4 sites anchored on N-doped porous carbon materials (Fe-SAs/NC) can mimic two antioxidative enzymes of catalase (CAT) and superoxide dismutase (SOD), and therefore serves as a bifunctional single-atom-based enzyme (SAzyme) for scavenging reactive oxygen species (ROS) to remove excess ROS generated during oxidative stress in cells. Iron 21-23 superoxide dismutase 1 Homo sapiens 169-172 29380557-11 2018 In SH-SY5Y cells stably expressing SOD1 or SOD1 G93A, we observed elevated levels of ferritin L and H and non-haem iron. Iron 115-119 superoxide dismutase 1 Homo sapiens 35-39 29380557-11 2018 In SH-SY5Y cells stably expressing SOD1 or SOD1 G93A, we observed elevated levels of ferritin L and H and non-haem iron. Iron 115-119 superoxide dismutase 1 Homo sapiens 43-47 27026547-4 2016 The results showed that the major component of SOD was chemical SOD due to iron predominate. Iron 75-79 superoxide dismutase 1 Homo sapiens 47-50 27026547-4 2016 The results showed that the major component of SOD was chemical SOD due to iron predominate. Iron 75-79 superoxide dismutase 1 Homo sapiens 64-67 27356602-12 2016 However, it should be considered that overexpression of the SOD1 gene usually leads to increased SOD1 enzymatic activity, a condition which does not occur in human pathology and which may itself change the expression of iron metabolism genes. Iron 220-224 superoxide dismutase 1 Homo sapiens 97-101 26778957-0 2015 Mice Overexpressing Both Non-Mutated Human SOD1 and Mutated SOD1(G93A) Genes: A Competent Experimental Model for Studying Iron Metabolism in Amyotrophic Lateral Sclerosis. Iron 122-126 superoxide dismutase 1 Homo sapiens 60-64 27324098-10 2016 Paradoxically, a superoxide dismutase (SOD) reversed the inhibition of progesterone synthesis only minimally although it strongly inhibited PQ stimulated iron-dependent lipid peroxidation. Iron 154-158 superoxide dismutase 1 Homo sapiens 17-37 27324098-10 2016 Paradoxically, a superoxide dismutase (SOD) reversed the inhibition of progesterone synthesis only minimally although it strongly inhibited PQ stimulated iron-dependent lipid peroxidation. Iron 154-158 superoxide dismutase 1 Homo sapiens 39-42 26778957-4 2015 Of importance, both ALS patients and animals carrying mutated human SOD1 gene show symptoms of oxidative stress and iron metabolism misregulation. Iron 116-120 superoxide dismutase 1 Homo sapiens 68-72 26778957-5 2015 The aim of our study was to characterize changes in iron metabolism in one of the most commonly used models of ALS - transgenic mice overexpressing human mutated SOD1(G93A) gene. Iron 52-56 superoxide dismutase 1 Homo sapiens 162-166 26778957-8 2015 We demonstrate that the overexpression of both SOD1 and SOD1(G93A) genes account for a substantial increase in SOD1 protein levels and activity in selected tissues and that not all the changes in iron metabolism genes expression are specific for the overexpression of the mutated form of SOD1. Iron 196-200 superoxide dismutase 1 Homo sapiens 47-51 26778957-8 2015 We demonstrate that the overexpression of both SOD1 and SOD1(G93A) genes account for a substantial increase in SOD1 protein levels and activity in selected tissues and that not all the changes in iron metabolism genes expression are specific for the overexpression of the mutated form of SOD1. Iron 196-200 superoxide dismutase 1 Homo sapiens 56-60 26778957-8 2015 We demonstrate that the overexpression of both SOD1 and SOD1(G93A) genes account for a substantial increase in SOD1 protein levels and activity in selected tissues and that not all the changes in iron metabolism genes expression are specific for the overexpression of the mutated form of SOD1. Iron 196-200 superoxide dismutase 1 Homo sapiens 56-60 26778957-8 2015 We demonstrate that the overexpression of both SOD1 and SOD1(G93A) genes account for a substantial increase in SOD1 protein levels and activity in selected tissues and that not all the changes in iron metabolism genes expression are specific for the overexpression of the mutated form of SOD1. Iron 196-200 superoxide dismutase 1 Homo sapiens 56-60 25819318-0 2015 DNA interaction, SOD, peroxidase and nuclease activity studies of iron complex having ligand with carboxamido nitrogen donors. Iron 66-70 superoxide dismutase 1 Homo sapiens 17-20 25645023-7 2015 Importantly, assembly of the Fe-S cluster in Pri2 is impaired not only by mutations at the conserved cysteine ligands but also by increased oxidative stress in the sod1Delta mutant lacking the Cu/Zn superoxide dismutase. Iron 29-33 superoxide dismutase 1 Homo sapiens 193-219 23768398-5 2013 The addition of catalase and superoxide dismutase (SOD) prevented the hydroxyl radical driven-degradation of beta-glucan induced by iron(II) or ascorbic acid/iron(II), demonstrating the involvement of both superoxide and hydrogen peroxide in the hydroxyl radical formation. Iron 132-136 superoxide dismutase 1 Homo sapiens 29-49 23768398-6 2013 SOD, which catalyses the dismutation of superoxide into hydrogen peroxide, should have stimulated the formation of radicals, since these radicals are generated from the reaction between hydrogen peroxide and iron(II). Iron 208-212 superoxide dismutase 1 Homo sapiens 0-3 24448401-7 2014 Elevation of SOD1 and increasing trend for iron-storage proteins (FTL, FTH1) may be indicative of an oxidative imbalance that is accompanied by an aberrant iron metabolism. Iron 156-160 superoxide dismutase 1 Homo sapiens 13-17 23768398-5 2013 The addition of catalase and superoxide dismutase (SOD) prevented the hydroxyl radical driven-degradation of beta-glucan induced by iron(II) or ascorbic acid/iron(II), demonstrating the involvement of both superoxide and hydrogen peroxide in the hydroxyl radical formation. Iron 158-162 superoxide dismutase 1 Homo sapiens 51-54 23768398-5 2013 The addition of catalase and superoxide dismutase (SOD) prevented the hydroxyl radical driven-degradation of beta-glucan induced by iron(II) or ascorbic acid/iron(II), demonstrating the involvement of both superoxide and hydrogen peroxide in the hydroxyl radical formation. Iron 132-136 superoxide dismutase 1 Homo sapiens 51-54 23768398-5 2013 The addition of catalase and superoxide dismutase (SOD) prevented the hydroxyl radical driven-degradation of beta-glucan induced by iron(II) or ascorbic acid/iron(II), demonstrating the involvement of both superoxide and hydrogen peroxide in the hydroxyl radical formation. Iron 158-162 superoxide dismutase 1 Homo sapiens 29-49 21345335-3 2011 Iron overloading of mitochondrial fraction resulted in an increase in lipid peroxidation, protein oxidation, and DNA damage, whereas iron overload reduced the glutathione (GSH) concentration, glutathione-S-transferase (GST), glutathione peroxidase (GSHPx), catalase and superoxide dismutase (SOD) activities. Iron 0-4 superoxide dismutase 1 Homo sapiens 270-290 23178912-3 2013 Since enhanced iron levels are discussed to participate in oxidative stress and neuronal death, we analyzed the expression levels of Fe-related mRNAs in a cell culture ALS model with the G93A mutation of SOD1. Iron 133-135 superoxide dismutase 1 Homo sapiens 204-208 23178912-4 2013 We observed an increased total iron content in G93A-SOD1 SH-SY5Y neuroblastoma cells compared to wild-type (WT)-SOD1 cells. Iron 31-35 superoxide dismutase 1 Homo sapiens 52-56 23178912-5 2013 mRNA expression for transferrin receptor 1 (TfR1) and divalent metal transporter 1 was increased in G93A-SOD1 cells, which was in accordance with higher iron uptake. Iron 153-157 superoxide dismutase 1 Homo sapiens 105-109 23178912-7 2013 Expression levels of mitoferrin 1 and 2, frataxin, and iron-sulfur cluster scaffold protein were also significantly increased in G93A-SOD1 cells, suggesting higher mitochondrial iron import and utilization in biosynthetic pathways within the mitochondria. Iron 55-59 superoxide dismutase 1 Homo sapiens 134-138 23178912-7 2013 Expression levels of mitoferrin 1 and 2, frataxin, and iron-sulfur cluster scaffold protein were also significantly increased in G93A-SOD1 cells, suggesting higher mitochondrial iron import and utilization in biosynthetic pathways within the mitochondria. Iron 178-182 superoxide dismutase 1 Homo sapiens 134-138 22954919-6 2012 After the single dialysis, the two iron groups had higher level of serum MDA, MPO and lower level of serum SOD than that of the non-iron supplementation group (P<0.01). Iron 35-39 superoxide dismutase 1 Homo sapiens 107-110 23940258-6 2013 Increased iron incorporation into the FtH homopolymer leads to reduced cellular iron availability, diminished levels of cytosolic catalase, SOD1 protein levels, enhanced ROS production and higher levels of oxidized proteins. Iron 10-14 superoxide dismutase 1 Homo sapiens 140-144 21345335-3 2011 Iron overloading of mitochondrial fraction resulted in an increase in lipid peroxidation, protein oxidation, and DNA damage, whereas iron overload reduced the glutathione (GSH) concentration, glutathione-S-transferase (GST), glutathione peroxidase (GSHPx), catalase and superoxide dismutase (SOD) activities. Iron 0-4 superoxide dismutase 1 Homo sapiens 292-295 21345335-3 2011 Iron overloading of mitochondrial fraction resulted in an increase in lipid peroxidation, protein oxidation, and DNA damage, whereas iron overload reduced the glutathione (GSH) concentration, glutathione-S-transferase (GST), glutathione peroxidase (GSHPx), catalase and superoxide dismutase (SOD) activities. Iron 133-137 superoxide dismutase 1 Homo sapiens 270-290 21345335-3 2011 Iron overloading of mitochondrial fraction resulted in an increase in lipid peroxidation, protein oxidation, and DNA damage, whereas iron overload reduced the glutathione (GSH) concentration, glutathione-S-transferase (GST), glutathione peroxidase (GSHPx), catalase and superoxide dismutase (SOD) activities. Iron 133-137 superoxide dismutase 1 Homo sapiens 292-295 21345335-5 2011 Conversely, naringin supplementation arrested iron-induced depletion in the GSH contents, GSHPx, GST, SOD and catalase activities significantly. Iron 46-50 superoxide dismutase 1 Homo sapiens 102-105 23199069-6 2010 This review will discuss novel pharmacological approaches concerning adjusted therapy for ALS patients: iron-binding brain permeable multimodal compounds, genetic manipulation and cell-based treatment. Iron 104-108 superoxide dismutase 1 Homo sapiens 90-93 20570646-2 2010 The nonacarbon chain streptocyanine 9Cl(NEt(2))(2) was found to be relatively stable in neutral buffered aqueous solutions, to be reduced at a significant rate by superoxide, and addition of iron-dependent superoxide dismutase (Fe-SOD) prevented its bleaching, thus constituting a good candidate as a possible superoxide indicator in a spectrophotometric SOD assay. Iron 191-195 superoxide dismutase 1 Homo sapiens 206-226 20570646-2 2010 The nonacarbon chain streptocyanine 9Cl(NEt(2))(2) was found to be relatively stable in neutral buffered aqueous solutions, to be reduced at a significant rate by superoxide, and addition of iron-dependent superoxide dismutase (Fe-SOD) prevented its bleaching, thus constituting a good candidate as a possible superoxide indicator in a spectrophotometric SOD assay. Iron 191-195 superoxide dismutase 1 Homo sapiens 231-234 20570646-2 2010 The nonacarbon chain streptocyanine 9Cl(NEt(2))(2) was found to be relatively stable in neutral buffered aqueous solutions, to be reduced at a significant rate by superoxide, and addition of iron-dependent superoxide dismutase (Fe-SOD) prevented its bleaching, thus constituting a good candidate as a possible superoxide indicator in a spectrophotometric SOD assay. Iron 191-195 superoxide dismutase 1 Homo sapiens 355-358 21250883-8 2011 Serum ferritin also showed a positive correlation with elevated TBARS and SOD, suggesting that iron overload is involved in the oxidative stress shown in cells. Iron 95-99 superoxide dismutase 1 Homo sapiens 74-77 16680451-2 2006 We have studied the effect of the modulation of SOD1 levels on iron metabolism in a cultured human glial cell line and in a mouse motoneuronal cell line. Iron 63-67 superoxide dismutase 1 Homo sapiens 48-52 19837190-10 2010 Finally we briefly introduce a metal insertion system of SOD, focusing particularly on the iron misincorporation of nSOD, as a part of post-translational modifications. Iron 91-95 superoxide dismutase 1 Homo sapiens 57-60 16828895-2 2006 Various SOD enzymes have been characterized that employ either a copper, manganese, iron or nickel co-factor to carry out the disproportionation of superoxide. Iron 84-88 superoxide dismutase 1 Homo sapiens 8-11 17912757-1 2008 Fe- and Mn-containing superoxide dismutase (sod) enzymes are closely related and similar in both amino acid sequence and structure, but differ in their mode of oligomerization and in their specificity for the Fe or Mn cofactor. Iron 0-2 superoxide dismutase 1 Homo sapiens 22-42 17912757-1 2008 Fe- and Mn-containing superoxide dismutase (sod) enzymes are closely related and similar in both amino acid sequence and structure, but differ in their mode of oligomerization and in their specificity for the Fe or Mn cofactor. Iron 0-2 superoxide dismutase 1 Homo sapiens 44-47 17912757-1 2008 Fe- and Mn-containing superoxide dismutase (sod) enzymes are closely related and similar in both amino acid sequence and structure, but differ in their mode of oligomerization and in their specificity for the Fe or Mn cofactor. Iron 209-211 superoxide dismutase 1 Homo sapiens 22-42 17912757-1 2008 Fe- and Mn-containing superoxide dismutase (sod) enzymes are closely related and similar in both amino acid sequence and structure, but differ in their mode of oligomerization and in their specificity for the Fe or Mn cofactor. Iron 209-211 superoxide dismutase 1 Homo sapiens 44-47 17324120-10 2007 A possible mechanism for the activation of Cn was identified in our studies as the prevention of Fe and Zn losses from the active site of Cn, suggesting a conformation-dependent SOD1-Cn interaction. Iron 97-99 superoxide dismutase 1 Homo sapiens 178-182 16680451-5 2006 We propose that changes in superoxide levels due to alteration of SOD1 activity affect iron metabolism in glial and neuronal cells from higher eukaryotes and that this may be relevant to diseases of the nervous system. Iron 87-91 superoxide dismutase 1 Homo sapiens 66-70 14578853-6 2003 Arachidonic acid (AA) plus iron-induced cell death was partially prevented in both Ad.SOD1- and Ad.SOD2-infected E47 cells. Iron 27-31 superoxide dismutase 1 Homo sapiens 86-90 15313158-10 2004 Iron treatment also reduced various antioxidant enzymes like glutathione peroxidase (GSHPx), catalase, and superoxide dismutase (SOD). Iron 0-4 superoxide dismutase 1 Homo sapiens 107-127 15313158-10 2004 Iron treatment also reduced various antioxidant enzymes like glutathione peroxidase (GSHPx), catalase, and superoxide dismutase (SOD). Iron 0-4 superoxide dismutase 1 Homo sapiens 129-132 16137675-3 2006 Biodegradation of extravasated hemoglobin (exvHb) and deposition of iron in alveoli occurred at 3-56 h post-exposure and was preceded by LKC degranulation and accumulation of MPO, HO-1, and SOD-1 in HLs. Iron 68-72 superoxide dismutase 1 Homo sapiens 190-195 16430211-0 2006 The crucial importance of chemistry in the structure-function link: manipulating hydrogen bonding in iron-containing superoxide dismutase. Iron 101-105 superoxide dismutase 1 Homo sapiens 117-137 16430211-1 2006 Fe-containing superoxide dismutase"s active site Fe is coordinated by a solvent molecule, whose protonation state is coupled to the Fe oxidation state. Iron 0-2 superoxide dismutase 1 Homo sapiens 14-34 16430211-1 2006 Fe-containing superoxide dismutase"s active site Fe is coordinated by a solvent molecule, whose protonation state is coupled to the Fe oxidation state. Iron 49-51 superoxide dismutase 1 Homo sapiens 14-34 16430211-1 2006 Fe-containing superoxide dismutase"s active site Fe is coordinated by a solvent molecule, whose protonation state is coupled to the Fe oxidation state. Iron 49-51 superoxide dismutase 1 Homo sapiens 14-34 16430211-2 2006 Thus, we have proposed that H-bonding between glutamine 69 and this solvent molecule can strongly influence the redox activity of the Fe in superoxide dismutase (SOD). Iron 134-136 superoxide dismutase 1 Homo sapiens 140-160 16430211-2 2006 Thus, we have proposed that H-bonding between glutamine 69 and this solvent molecule can strongly influence the redox activity of the Fe in superoxide dismutase (SOD). Iron 134-136 superoxide dismutase 1 Homo sapiens 162-165 16686997-6 2006 This may due to the enzymatic ability of over-expressed CuZn-superoxide dismutase in Down syndrome to catalyze the formation of H2O2 from O2*-, thereby increasing the availability of substrate H2O2 for the iron-dependent generation of HO* via the Fenton reaction, suggesting that HO* generated from DS-GF may be involved in progressive periodontitis of Down syndrome. Iron 206-210 superoxide dismutase 1 Homo sapiens 56-81 9109411-1 1997 A recombinant truncated form (delta1-102/delta428-452) of the non-heme iron-dependent metalloenzyme human phenylalanine hydroxylase (hPAH, phenylalanine 4-monooxygenase; EC 1.14.16.1) was expressed in E. coli, purified to homogeneity as a homodimer (70 kDa) and crystallized using the hanging drop vapour diffusion method. Iron 71-75 superoxide dismutase 1 Homo sapiens 239-248 11828552-1 2002 AIM: To test whether the activities of erythrocyte superoxide dismutase (SOD) and glutathione peroxidase (GSH-Px) can be affected by oral iron (OI) treatment, parenteral iron (PI) treatment, and parenteral iron treatment with vitamin E supplementation (PIE) in iron deficiency anemia. Iron 138-142 superoxide dismutase 1 Homo sapiens 73-76 11828552-1 2002 AIM: To test whether the activities of erythrocyte superoxide dismutase (SOD) and glutathione peroxidase (GSH-Px) can be affected by oral iron (OI) treatment, parenteral iron (PI) treatment, and parenteral iron treatment with vitamin E supplementation (PIE) in iron deficiency anemia. Iron 170-174 superoxide dismutase 1 Homo sapiens 73-76 11828552-1 2002 AIM: To test whether the activities of erythrocyte superoxide dismutase (SOD) and glutathione peroxidase (GSH-Px) can be affected by oral iron (OI) treatment, parenteral iron (PI) treatment, and parenteral iron treatment with vitamin E supplementation (PIE) in iron deficiency anemia. Iron 170-174 superoxide dismutase 1 Homo sapiens 73-76 11828552-11 2002 CONCLUSION: Oral iron treatment improved the iron deficiency anemia and recovered antioxidant defense system by increasing SOD activity and maintaining GSH-Px activity at normal level. Iron 17-21 superoxide dismutase 1 Homo sapiens 123-126 11053782-4 2000 With electron paramagnetic resonance spectroscopy using N-methyl-D-glucamine dithiocarbamate iron (Fe-MGD), we directly detected NO&z.rad; from purified NOS in the absence of SOD (Xia et al., PNAS 94:12705, 1997). Iron 99-101 superoxide dismutase 1 Homo sapiens 179-182 11410240-2 2001 The SOD activity of 5,10,15,20-tetrakis(4-N-methylpyridyl)]porphine (MPy(4)P) containing Fe, Mn or Cu was measured using a cytochrome c assay by the xanthine/xanthine oxidase system and stopped-flow kinetic analysis. Iron 89-91 superoxide dismutase 1 Homo sapiens 4-7 7673115-9 1995 Although Me2SO, sodium formate, and mannitol had no protective effect, iron chelators, thiourea and urate protected the cells against the SIN-1 plus Cu,Zn-SOD-mediated cytotoxicity. Iron 71-75 superoxide dismutase 1 Homo sapiens 155-158 7998826-3 1994 Iron/hydrogen peroxide-induced DCFH oxidation was inhibited by catalase or by the hydroxyl radical scavenger dimethylsulfoxide; however, superoxide dismutase (SOD) had no effect on DCFH oxidation. Iron 0-4 superoxide dismutase 1 Homo sapiens 159-162 7777104-6 1995 Similarly a decreased SOD activity was observed as compared to group 1 (p < 0.001), indicating its inactivation subsequent to an hyperproduction of reactive oxygen species through iron injection. Iron 183-187 superoxide dismutase 1 Homo sapiens 22-25 1659450-2 1991 We noted that in contrast to results with other hydroxyl radical detection systems, superoxide dismutase (SOD) often increased the amount of hydroxyl radical-derived spin adducts of 5,5-dimethyl-1-pyrroline N-oxide (DMPO) produced by the reaction of hypoxanthine, xanthine oxidase and iron. Iron 285-289 superoxide dismutase 1 Homo sapiens 84-104 1312808-9 1992 In contrast, exogenous SOD did not alter iron release, suggesting that intracellular superoxide anion (O2-) may play an important role in mediating the reduction and release of transferrin-derived iron. Iron 197-201 superoxide dismutase 1 Homo sapiens 23-26 1581527-2 1992 Superoxide dismutase (SOD) increases the rates of iron release with the less filtered smoke extracts, but has no effect on the rate of iron release caused by aqueous extracts of well-filtered gas-phase cigarette smoke. Iron 50-54 superoxide dismutase 1 Homo sapiens 0-20 1581527-2 1992 Superoxide dismutase (SOD) increases the rates of iron release with the less filtered smoke extracts, but has no effect on the rate of iron release caused by aqueous extracts of well-filtered gas-phase cigarette smoke. Iron 50-54 superoxide dismutase 1 Homo sapiens 22-25 8260663-8 1993 The SOD activity of LR strains was irreversibly inhibited 100% by 5 mM H2O2, and exhibited greater sensitivity to NaN3, suggesting the presence of iron in the enzyme. Iron 147-151 superoxide dismutase 1 Homo sapiens 4-7 8260663-10 1993 CONCLUSION: Our data indicate that MAC strains are rich in manganese- or iron-containing SOD, which could contribute to the organism"s resistance to the oxidative burst of activated macrophages. Iron 73-77 superoxide dismutase 1 Homo sapiens 89-92 8117850-0 1993 Cross-linked hemoglobin-superoxide dismutase-catalase scavenges oxygen-derived free radicals and prevents methemoglobin formation and iron release. Iron 134-138 superoxide dismutase 1 Homo sapiens 24-44 8117850-12 1993 Furthermore, the amount of iron released, after incubation with 250 microM H2O2, was 6.8 +/- 1.8 micrograms/dl for PolyHb-SOD-catalase and 76.6 +/- 1.0 micrograms/dl for PolyHb. Iron 27-31 superoxide dismutase 1 Homo sapiens 122-125 8375432-2 1993 Iron-dependent microsomal lipid peroxidation could be initiated by reduced irons coordinated with phosphate moieties in the membranes and significantly inhibited by copper salicylate (hydrophobic and permeable O2-scavenger) and desferrioxamine (a powerful iron-chelating agent), but not by SOD. Iron 0-4 superoxide dismutase 1 Homo sapiens 290-293 1312802-12 1992 If the formation of this complex is prevented by SOD, EDTA, or neocuproine, then OP may complex iron and the net effect may be (like dipyridyl) an inhibition of strand breaks. Iron 96-100 superoxide dismutase 1 Homo sapiens 49-52 1659450-2 1991 We noted that in contrast to results with other hydroxyl radical detection systems, superoxide dismutase (SOD) often increased the amount of hydroxyl radical-derived spin adducts of 5,5-dimethyl-1-pyrroline N-oxide (DMPO) produced by the reaction of hypoxanthine, xanthine oxidase and iron. Iron 285-289 superoxide dismutase 1 Homo sapiens 106-109 2368186-5 1990 The SOD activity in gastric juice can be decreased by adding antacids and Fe ions. Iron 74-76 superoxide dismutase 1 Homo sapiens 4-7 1648368-4 1991 Essentially the same effects were observed in SOD containing either Mn or Fe in the catalytic center. Iron 74-76 superoxide dismutase 1 Homo sapiens 46-49 2026245-2 1991 The monoclonal antibodies able to bind SOD were further screened for their ability to absorb SOD activity using anti-mouse IgG conjugated iron beads as solid supports in magnetic separation. Iron 138-142 superoxide dismutase 1 Homo sapiens 93-96 2127409-2 1990 Iron release was enhanced in the presence of SOD, catalase and under anaerobic conditions. Iron 0-4 superoxide dismutase 1 Homo sapiens 45-48 34266485-2 2021 As iron (Fe) SOD is absent in the human host, this enzyme is a promising molecular target for drug development against trypanosomatids. Iron 3-7 superoxide dismutase 1 Homo sapiens 13-16 34266485-2 2021 As iron (Fe) SOD is absent in the human host, this enzyme is a promising molecular target for drug development against trypanosomatids. Iron 9-11 superoxide dismutase 1 Homo sapiens 13-16