PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 16410455-6 2006 Antioxidant enzymes, especially the three isoforms of superoxide dismutase (SOD), modulate basal levels of superoxide and protect against vasomotor dysfunction. Superoxides 54-64 superoxide dismutase 3 Homo sapiens 76-79 16087389-2 2005 EC-SOD contains a unique heparin-binding domain at its carboxy-terminus that establishes localization to the extracellular matrix where the enzyme scavenges superoxide anion. Superoxides 157-173 superoxide dismutase 3 Homo sapiens 0-6 16469315-1 2006 Human extracellular superoxide dismutase (EC-SOD) is involved in the defence against oxidative stress induced by the superoxide radical. Superoxides 117-135 superoxide dismutase 3 Homo sapiens 6-40 16469315-1 2006 Human extracellular superoxide dismutase (EC-SOD) is involved in the defence against oxidative stress induced by the superoxide radical. Superoxides 117-135 superoxide dismutase 3 Homo sapiens 42-48 15990193-2 2006 Extracellular superoxide dismutase (EC-SOD) is found in the extracellular matrix of tissues and the major scavenger of superoxide radical. Superoxides 119-137 superoxide dismutase 3 Homo sapiens 0-34 15990193-2 2006 Extracellular superoxide dismutase (EC-SOD) is found in the extracellular matrix of tissues and the major scavenger of superoxide radical. Superoxides 119-137 superoxide dismutase 3 Homo sapiens 36-42 16087389-4 2005 In addition to protecting against extracellular oxidative damage, EC-SOD, by scavenging superoxide, preserves nitric oxide bioactivity and facilitates hypoxia-induced gene expression. Superoxides 88-98 superoxide dismutase 3 Homo sapiens 66-72 15862712-5 2005 Extracellular superoxide dismutase (EC-SOD) is the only extracellular scavenger of the superoxide radical. Superoxides 87-105 superoxide dismutase 3 Homo sapiens 0-34 15899505-2 2005 Extracellular SOD (EC-SOD/SOD3) is a major superoxide scavenger and it is located on cell surfaces and primarily in extracellular matrix, and binds heparan sulfates by its carboxyterminal portion. Superoxides 43-53 superoxide dismutase 3 Homo sapiens 14-17 15899505-2 2005 Extracellular SOD (EC-SOD/SOD3) is a major superoxide scavenger and it is located on cell surfaces and primarily in extracellular matrix, and binds heparan sulfates by its carboxyterminal portion. Superoxides 43-53 superoxide dismutase 3 Homo sapiens 19-25 15899505-2 2005 Extracellular SOD (EC-SOD/SOD3) is a major superoxide scavenger and it is located on cell surfaces and primarily in extracellular matrix, and binds heparan sulfates by its carboxyterminal portion. Superoxides 43-53 superoxide dismutase 3 Homo sapiens 26-30 15862712-5 2005 Extracellular superoxide dismutase (EC-SOD) is the only extracellular scavenger of the superoxide radical. Superoxides 87-105 superoxide dismutase 3 Homo sapiens 36-42 15862712-6 2005 The reactivity of superoxide is promiscuous and it is crucial that EC-SOD is positioned at the site of superoxide production to prevent adventitious reactions. Superoxides 18-28 superoxide dismutase 3 Homo sapiens 67-73 15862712-6 2005 The reactivity of superoxide is promiscuous and it is crucial that EC-SOD is positioned at the site of superoxide production to prevent adventitious reactions. Superoxides 103-113 superoxide dismutase 3 Homo sapiens 67-73 11437376-9 2001 In subendothelial space, EC-SOD bound on heparan sulfate might suppress LDL oxidation through reduction of superoxide anion. Superoxides 107-123 superoxide dismutase 3 Homo sapiens 25-31 15375030-6 2005 When EC-SOD was overexpressed in Hep3B cells, we found a significant reduction in Epo gene induction by both CoCl2 (50 microM) and hypoxia (1% O2). Superoxides 143-145 superoxide dismutase 3 Homo sapiens 5-11 14736885-2 2004 EC-SOD participates in the detoxification of reactive oxygen species by catalyzing the dismutation of superoxide radicals. Superoxides 102-112 superoxide dismutase 3 Homo sapiens 0-6 14736885-3 2004 The tissue distribution of the enzyme is particularly important because of the reactive nature of its substrate, and it is likely essential that EC-SOD is positioned at the site of superoxide production to prevent adventitious oxidation. Superoxides 181-191 superoxide dismutase 3 Homo sapiens 145-151 14615576-1 2003 Human extracellular superoxide dismutase (EC-SOD; EC 1.15.1.1) is a scavenger of superoxide anions in the extracellular space. Superoxides 81-98 superoxide dismutase 3 Homo sapiens 6-40 14615576-1 2003 Human extracellular superoxide dismutase (EC-SOD; EC 1.15.1.1) is a scavenger of superoxide anions in the extracellular space. Superoxides 81-98 superoxide dismutase 3 Homo sapiens 42-48 11557552-6 2001 The findings suggest that various physiological and pathological conditions might markedly influence EC-SOD expression, significantly altering the susceptibility of the vascular wall to effects of the superoxide radical. Superoxides 201-219 superoxide dismutase 3 Homo sapiens 101-107 15280800-1 2004 EC-SOD catalyzes the dismutation of superoxide radical to hydrogen peroxide and oxygen in the interstitial spaces of tissues and in extracellular fluids (plasma, lymph, and synovial fluid). Superoxides 36-54 superoxide dismutase 3 Homo sapiens 0-6 15239103-3 2004 The therapeutic efficacy of EC-SOD gene delivery by polycationic liposomes was determined against the toxicity of superoxide anions and hydroxyethyl radicals in HepG2 cells and in a mouse model of acute liver injury caused by D-galactosamine and lipopolysaccharide intoxication. Superoxides 114-131 superoxide dismutase 3 Homo sapiens 28-34 12885586-6 2003 In addition, EC-SOD is likely to play an important role in mediating nitric oxide-induced signaling events, since the reaction of superoxide and nitric oxide can interfere with nitric oxide signaling. Superoxides 130-140 superoxide dismutase 3 Homo sapiens 13-19 11463603-3 2001 The superoxide dismutases (SOD) are the primary enzymatic method to reduce superoxide. Superoxides 4-14 superoxide dismutase 3 Homo sapiens 27-30 9848884-2 1998 Superoxide dismutase (SOD), particularly extracellular SOD (EC-SOD), which accounts for the majority of SOD biological activity, is a major superoxide scavenger. Superoxides 140-150 superoxide dismutase 3 Homo sapiens 41-58 10712391-1 2000 Extracellular superoxide dismutase (EC-SOD) is a major superoxide scavenger and may be important to normal vascular function and cardiovascular health. Superoxides 14-24 superoxide dismutase 3 Homo sapiens 36-42 10329680-1 1999 Extracellular superoxide dismutase (EC-SOD) is the only known extracellular enzyme designed to scavenge the superoxide anion. Superoxides 108-124 superoxide dismutase 3 Homo sapiens 0-34 10329680-1 1999 Extracellular superoxide dismutase (EC-SOD) is the only known extracellular enzyme designed to scavenge the superoxide anion. Superoxides 108-124 superoxide dismutase 3 Homo sapiens 36-42 10720891-1 2000 BACKGROUND: The superoxide anion and other oxygen radicals have been implicated in the progression of chronic renal failure, and are removed by extracellular superoxide dismutase (EC-SOD) in the extracellular space on the surface of the endothelium. Superoxides 16-32 superoxide dismutase 3 Homo sapiens 144-178 10720891-1 2000 BACKGROUND: The superoxide anion and other oxygen radicals have been implicated in the progression of chronic renal failure, and are removed by extracellular superoxide dismutase (EC-SOD) in the extracellular space on the surface of the endothelium. Superoxides 16-32 superoxide dismutase 3 Homo sapiens 180-186 9848884-2 1998 Superoxide dismutase (SOD), particularly extracellular SOD (EC-SOD), which accounts for the majority of SOD biological activity, is a major superoxide scavenger. Superoxides 140-150 superoxide dismutase 3 Homo sapiens 60-66 9501855-12 1998 The large amounts of EC-SOD in the sclera and cornea may be related to the risk for photochemical production of superoxide in these tissues. Superoxides 112-122 superoxide dismutase 3 Homo sapiens 21-27 9699963-11 1998 EC-SOD localization around villous vessels suggests that EC-SOD serves potentially to protect the fetal vasculature from O2-, in both normal and pre-eclamptic pregnancies. Superoxides 121-123 superoxide dismutase 3 Homo sapiens 0-6 9699963-11 1998 EC-SOD localization around villous vessels suggests that EC-SOD serves potentially to protect the fetal vasculature from O2-, in both normal and pre-eclamptic pregnancies. Superoxides 121-123 superoxide dismutase 3 Homo sapiens 57-63 9484979-11 1998 High EC-SOD expression in the arterial wall may be required not only to prevent deleterious effects of superoxide anion but also to preserve NO activity and prevent peroxynitrite formation. Superoxides 103-119 superoxide dismutase 3 Homo sapiens 5-11 8743981-14 1996 The high level of EC SOD in vessels, and its localization between endothelial and smooth muscle cells, suggest that regulation of superoxide may be particularly important in this region, possibly in regulating vascular tone. Superoxides 130-140 superoxide dismutase 3 Homo sapiens 18-24 8015293-1 1994 BACKGROUND: Extracellular superoxide dismutase (EC-SOD) is a principal enzymatic scavenger of the superoxide anion in extracellular spaces. Superoxides 98-114 superoxide dismutase 3 Homo sapiens 12-46 7583586-5 1995 The EC-SOD concentration in the human arterial wall extracellular space is high enough to efficiently suppress the putative pathological effects of the superoxide radical, such as oxidation of LDL and reaction with nitric oxide to form the deleterious peroxynitrite. Superoxides 152-170 superoxide dismutase 3 Homo sapiens 4-10 7583586-8 1995 This wide variation in EC-SOD content suggests that the susceptibility to pathologies induced by superoxide radicals in the vascular wall interstitium should vary widely among species. Superoxides 97-107 superoxide dismutase 3 Homo sapiens 23-29 8015293-1 1994 BACKGROUND: Extracellular superoxide dismutase (EC-SOD) is a principal enzymatic scavenger of the superoxide anion in extracellular spaces. Superoxides 98-114 superoxide dismutase 3 Homo sapiens 48-54 8015293-3 1994 EC-SOD may also be important in regulating intercellular signalling by extracellular superoxide. Superoxides 85-95 superoxide dismutase 3 Homo sapiens 0-6 8379940-9 1993 The findings suggest that the protection level against superoxide radicals provided by EC-SOD in the tissue interstitial space, given the small distribution volume, is not much less prominent than that bestowed on the intracellular space by CuZn-SOD and Mn-SOD. Superoxides 55-65 superoxide dismutase 3 Homo sapiens 87-93 1477980-2 1992 The major protector against superoxide anion in the extracellular space is extracellular-superoxide dismutase (EC-SOD). Superoxides 28-44 superoxide dismutase 3 Homo sapiens 75-109 1477980-2 1992 The major protector against superoxide anion in the extracellular space is extracellular-superoxide dismutase (EC-SOD). Superoxides 28-44 superoxide dismutase 3 Homo sapiens 111-117 35271779-1 2022 Superoxide dismutase 3 (SOD3), one of SOD isozymes, maintains extracellular redox homeostasis through the dismutation reaction of superoxide. Superoxides 130-140 superoxide dismutase 3 Homo sapiens 0-22 1930145-11 1991 Since this phenomenon is increased in diabetes, the cell-surface-associated EC-SOD may be decreased in this disease, increasing the susceptibility of cells to superoxide radicals produced in the extracellular space. Superoxides 159-169 superoxide dismutase 3 Homo sapiens 76-82 33761612-4 2021 Previously, we have observed that the plasma concentration/activity of superoxide dismutase isozymes differs in the context of obesity and/or rs2234694 (SOD1) and rs4880 (SOD2) and that the concentrations of SOD1, SOD2, SOD3 are correlated with each other. Superoxides 71-81 superoxide dismutase 3 Homo sapiens 220-224 33761612-6 2021 In this study, the variability of concentration/activity of superoxide dismutase isozymes in plasma is considered in the context of type 2 diabetes and/or SNPs: rs2234694 (SOD1), rs5746105 (SOD2), rs4880 (SOD2), rs927450 (SOD2), rs8192287 (SOD3). Superoxides 60-70 superoxide dismutase 3 Homo sapiens 240-244 25634994-2 2015 Extracellular superoxide dismutase (EcSOD) is an antioxidant enzyme that catalyzes the dismutation of superoxide in the extracellular environment. Superoxides 14-24 superoxide dismutase 3 Homo sapiens 36-41 25634994-8 2015 Overexpression of EcSOD in PDA cell lines resulted in decreased invasiveness that appeared to be related to reactions of superoxide with nitric oxide. Superoxides 121-131 superoxide dismutase 3 Homo sapiens 18-23 25634994-10 2015 Overexpression of EcSOD or treatment with a superoxide-specific SOD mimic caused significant decreases in PDA cell invasive capacity. Superoxides 44-54 superoxide dismutase 3 Homo sapiens 18-23 25634994-11 2015 CONCLUSIONS: These results support the hypothesis that loss of EcSOD leads to increased reactions of superoxide with nitric oxide, which contributes to the invasive phenotype. Superoxides 101-111 superoxide dismutase 3 Homo sapiens 63-68 34439484-2 2021 Extracellular superoxide dismutase (SOD3) is an enzyme that processes superoxide radicals and has been shown to facilitate vascular endothelial growth factor (VEGF) and nitric oxide (NO) signaling in vascular endothelium. Superoxides 70-80 superoxide dismutase 3 Homo sapiens 36-40 34439467-4 2021 Extracellular superoxide dismutase (EcSOD) is an antioxidant enzyme that catalyzes the dismutation of superoxide anion (O2-) in the extracellular environment. Superoxides 102-118 superoxide dismutase 3 Homo sapiens 0-34 34439467-4 2021 Extracellular superoxide dismutase (EcSOD) is an antioxidant enzyme that catalyzes the dismutation of superoxide anion (O2-) in the extracellular environment. Superoxides 102-118 superoxide dismutase 3 Homo sapiens 36-41 35205334-4 2022 This study aimed to evaluate changes in IL-6 concentration and the concentration/activity of superoxide dismutase isoenzymes (SOD1, SOD2, and SOD3) in the blood of patients with acute pancreatitis (AP) in terms of rs1800795 polymorphism in the IL6 gene. Superoxides 93-103 superoxide dismutase 3 Homo sapiens 142-146 1551878-7 1992 The cytokines influencing the EC-SOD expression are also known to influence superoxide production by leukocytes and other cell types, and the EC-SOD response pattern is roughly compatible with the notion that its function is to protect cells against extracellular superoxide radicals. Superoxides 76-86 superoxide dismutase 3 Homo sapiens 30-36 1551878-7 1992 The cytokines influencing the EC-SOD expression are also known to influence superoxide production by leukocytes and other cell types, and the EC-SOD response pattern is roughly compatible with the notion that its function is to protect cells against extracellular superoxide radicals. Superoxides 264-274 superoxide dismutase 3 Homo sapiens 30-36 1551878-7 1992 The cytokines influencing the EC-SOD expression are also known to influence superoxide production by leukocytes and other cell types, and the EC-SOD response pattern is roughly compatible with the notion that its function is to protect cells against extracellular superoxide radicals. Superoxides 264-274 superoxide dismutase 3 Homo sapiens 142-148 35624792-1 2022 The superoxide dismutase (SOD) family functions as a reactive oxygen species (ROS)-scavenging system by converting superoxide anions into hydrogen peroxide in the cytosol (SOD1), mitochondria (SOD2), and extracellular matrix (SOD3). Superoxides 115-132 superoxide dismutase 3 Homo sapiens 226-230 35360751-2 2022 Activity of extracellular superoxide dismutase (ecSOD), the only extracellular enzyme eliminating superoxide radicals, has been reported to decline in acute exacerbations of COPD (AECOPD). Superoxides 98-108 superoxide dismutase 3 Homo sapiens 12-46 35360751-2 2022 Activity of extracellular superoxide dismutase (ecSOD), the only extracellular enzyme eliminating superoxide radicals, has been reported to decline in acute exacerbations of COPD (AECOPD). Superoxides 98-108 superoxide dismutase 3 Homo sapiens 48-53 35271779-1 2022 Superoxide dismutase 3 (SOD3), one of SOD isozymes, maintains extracellular redox homeostasis through the dismutation reaction of superoxide. Superoxides 130-140 superoxide dismutase 3 Homo sapiens 24-28 33019780-1 2020 This study was aimed at evaluating the changes in the concentration and activity of all superoxide dismutase isoenzymes (SOD1, SOD2, SOD3) in the blood of patients with acute pancreatitis (AP) and healthy subjects, taking into account the extracellular (plasma) and intracellular (erythrocyte lysate) compartment. Superoxides 88-98 superoxide dismutase 3 Homo sapiens 133-137 32128111-8 2020 Along with superoxide scavenging property, SOD3 also displays anti-angiogenic, anti-chemotactic and anti-inflammatory functions in both enzymatic and non-enzymatic manners. Superoxides 11-21 superoxide dismutase 3 Homo sapiens 43-47 32220789-1 2020 Extracellular superoxide dismutase (EcSOD) is the only extracellular scavenger of superoxide anion (O2.-) with unique binding capacity to cell surface and extracellular matrix through its heparin-binding domain. Superoxides 82-98 superoxide dismutase 3 Homo sapiens 0-34 32220789-1 2020 Extracellular superoxide dismutase (EcSOD) is the only extracellular scavenger of superoxide anion (O2.-) with unique binding capacity to cell surface and extracellular matrix through its heparin-binding domain. Superoxides 82-98 superoxide dismutase 3 Homo sapiens 36-41 32220789-1 2020 Extracellular superoxide dismutase (EcSOD) is the only extracellular scavenger of superoxide anion (O2.-) with unique binding capacity to cell surface and extracellular matrix through its heparin-binding domain. Superoxides 100-102 superoxide dismutase 3 Homo sapiens 0-34 32220789-1 2020 Extracellular superoxide dismutase (EcSOD) is the only extracellular scavenger of superoxide anion (O2.-) with unique binding capacity to cell surface and extracellular matrix through its heparin-binding domain. Superoxides 100-102 superoxide dismutase 3 Homo sapiens 36-41 31326693-1 2019 Superoxide dismutase 3 (SOD3) is an extracellular enzyme with the capacity to modulate extracellular redox conditions by catalyzing the dismutation of superoxide to hydrogen peroxide. Superoxides 151-161 superoxide dismutase 3 Homo sapiens 0-22 32600223-3 2020 To limit ROS toxicity, cells use Cu-dependent chaperone proteins, Cu-binding ceruloplasmin, and Cu-modulated enzymes like superoxide dismutases (SOD) like SOD1 and SOD3 to scavenge excess superoxide anion which favours Cu+ reduction, and mitochondrial cytochrome c oxidase, important in aerobic energy production. Superoxides 188-204 superoxide dismutase 3 Homo sapiens 164-168 31326693-1 2019 Superoxide dismutase 3 (SOD3) is an extracellular enzyme with the capacity to modulate extracellular redox conditions by catalyzing the dismutation of superoxide to hydrogen peroxide. Superoxides 151-161 superoxide dismutase 3 Homo sapiens 24-28 30004839-1 2018 Extracellular superoxide dismutase (EC-SOD), one of three mammalian SOD isoforms, is the sole extracellular enzymatic defense against superoxide. Superoxides 14-24 superoxide dismutase 3 Homo sapiens 36-42 30654942-10 2019 Elevated superoxide anions were observed when SOD3 was knocked down. Superoxides 9-26 superoxide dismutase 3 Homo sapiens 46-50 30004839-1 2018 Extracellular superoxide dismutase (EC-SOD), one of three mammalian SOD isoforms, is the sole extracellular enzymatic defense against superoxide. Superoxides 14-24 superoxide dismutase 3 Homo sapiens 39-42 30140407-10 2018 More valuable information could probably be provided about the variety of the diseases caused by superoxide anions toxicities by intervention and application of the non-viral method for expressions of SOD1 and SOD3 enzymes. Superoxides 97-114 superoxide dismutase 3 Homo sapiens 210-214 29029079-1 2017 Extracellular superoxide dismutase (EC-SOD, SOD3) protects tissues against oxidative damage by detoxifying superoxide anions, particularly in the lungs and cardiovascular system. Superoxides 107-124 superoxide dismutase 3 Homo sapiens 0-34 29029079-1 2017 Extracellular superoxide dismutase (EC-SOD, SOD3) protects tissues against oxidative damage by detoxifying superoxide anions, particularly in the lungs and cardiovascular system. Superoxides 107-124 superoxide dismutase 3 Homo sapiens 36-42 29029079-1 2017 Extracellular superoxide dismutase (EC-SOD, SOD3) protects tissues against oxidative damage by detoxifying superoxide anions, particularly in the lungs and cardiovascular system. Superoxides 107-124 superoxide dismutase 3 Homo sapiens 44-48 28751803-1 2017 Extracellular-superoxide dismutase (EC-SOD or SOD3), which catalyzes the dismutation of superoxide anions into hydrogen peroxide, plays a key role in vascular protection against reactive oxygen species (ROS). Superoxides 88-105 superoxide dismutase 3 Homo sapiens 36-42 28751803-1 2017 Extracellular-superoxide dismutase (EC-SOD or SOD3), which catalyzes the dismutation of superoxide anions into hydrogen peroxide, plays a key role in vascular protection against reactive oxygen species (ROS). Superoxides 88-105 superoxide dismutase 3 Homo sapiens 46-50 26912083-3 2016 Antioxidant enzymes, such as extracellular superoxide dismutase (EC-SOD), in the extracellular matrix (ECM) neutralize the toxicity of superoxide. Superoxides 43-53 superoxide dismutase 3 Homo sapiens 65-71 29047081-6 2017 In parallel with these different cellular sites of superoxide production, the three SOD isoforms are also specifically localized to the cytosol (SOD1), mitochondria (SOD2) or extracellular compartment (SOD3). Superoxides 51-61 superoxide dismutase 3 Homo sapiens 202-206 26990420-2 2016 Extracellular-superoxide dismutase (EC-SOD) is mainly produced by vascular smooth muscle cells (VSMCs), is secreted into the extracellular space, and protects cells from the damaging effects of the superoxide anion. Superoxides 198-214 superoxide dismutase 3 Homo sapiens 0-34 26990420-2 2016 Extracellular-superoxide dismutase (EC-SOD) is mainly produced by vascular smooth muscle cells (VSMCs), is secreted into the extracellular space, and protects cells from the damaging effects of the superoxide anion. Superoxides 198-214 superoxide dismutase 3 Homo sapiens 36-42 26901385-1 2016 The extracellular superoxide dismutase (SOD3, EC-SOD) enzyme is a major extracellular scavenger of the superoxide anion, a free radical with the potential to cause oxidative damage. Superoxides 103-119 superoxide dismutase 3 Homo sapiens 40-44 26901385-1 2016 The extracellular superoxide dismutase (SOD3, EC-SOD) enzyme is a major extracellular scavenger of the superoxide anion, a free radical with the potential to cause oxidative damage. Superoxides 103-119 superoxide dismutase 3 Homo sapiens 46-52 27380944-5 2016 Whilst, the exponential rise of O2(.-) is secondary to the focal accumulation of higher order lipid raft-Rac1/2-actin oligomers; O2(.-) mediated inactivation and redistribution of ECSOD, accounts for the minimal concentration of H2O2 that the phagocyte experiences. Superoxides 32-34 superoxide dismutase 3 Homo sapiens 180-185 27380944-5 2016 Whilst, the exponential rise of O2(.-) is secondary to the focal accumulation of higher order lipid raft-Rac1/2-actin oligomers; O2(.-) mediated inactivation and redistribution of ECSOD, accounts for the minimal concentration of H2O2 that the phagocyte experiences. Superoxides 129-131 superoxide dismutase 3 Homo sapiens 180-185 27567024-1 2016 Extracellular superoxide dismutase (EC-SOD or SOD3) protects against various oxidative stress-related diseases by scavenging reactive superoxides in the extracellular space. Superoxides 134-145 superoxide dismutase 3 Homo sapiens 36-42 27567024-1 2016 Extracellular superoxide dismutase (EC-SOD or SOD3) protects against various oxidative stress-related diseases by scavenging reactive superoxides in the extracellular space. Superoxides 134-145 superoxide dismutase 3 Homo sapiens 46-50 24512907-1 2014 Extracellular superoxide dismutase (EC-SOD) is responsible for the dismutation of the superoxide radical produced in the extracellular space and known to be expressed by inflammatory cells, including macrophages and neutrophils. Superoxides 14-24 superoxide dismutase 3 Homo sapiens 36-42 24509158-3 2014 Extracellular superoxide dismutase (EcSOD) inhibits pancreatic cancer cell growth by scavenging nonmitochondrial superoxide. Superoxides 14-24 superoxide dismutase 3 Homo sapiens 36-41 24509158-4 2014 We hypothesized that EcSOD overexpression leads to changes in the O2(-)/H2O2 balance modulating the redox status affecting signal transduction pathways. Superoxides 66-71 superoxide dismutase 3 Homo sapiens 21-26 25906743-1 2015 Extracellular-superoxide dismutase (EC-SOD) is one of the main anti-oxidative enzymes that protect cells against the damaging effects of superoxide. Superoxides 14-24 superoxide dismutase 3 Homo sapiens 36-42 25751262-1 2015 Extracellular superoxide dismutase (SOD3), which catalyzes the dismutation of superoxide anions to hydrogen peroxide at the cell membranes, regulates the cellular growth in a dose-dependent manner. Superoxides 78-95 superoxide dismutase 3 Homo sapiens 36-40 26550576-1 2015 Extracellular superoxide dismutase (SOD3) is a secreted enzyme that uses superoxide anion as a substrate in a dismutase reaction that results in the formation of hydrogen peroxide. Superoxides 73-89 superoxide dismutase 3 Homo sapiens 36-40 24024135-1 2013 Superoxide dismutase (EC-SOD) controls the level of superoxide in the extracellular space by catalyzing the dismutation of superoxide into hydrogen peroxide and molecular oxygen. Superoxides 52-62 superoxide dismutase 3 Homo sapiens 22-28 23318435-11 2014 This study suggests that epigenetic silencing of EcSOD may contribute to mammary tumorigenesis and that restoring the extracellular superoxide scavenging activity could be an effective strategy for breast cancer treatment. Superoxides 132-142 superoxide dismutase 3 Homo sapiens 49-54 23289810-2 2013 Copper-zinc superoxide dismutases, SOD-1 and SOD-3, and manganese superoxide dismutase, SOD-2, are enzymes involved in the protection against oxidative stress and detoxification of superoxide. Superoxides 12-22 superoxide dismutase 3 Homo sapiens 45-50 23329142-1 2013 Extracellular superoxide dismutase (EC-SOD) is the only enzyme that removes superoxide radical in the extracellular space. Superoxides 76-94 superoxide dismutase 3 Homo sapiens 36-42 24024135-9 2013 We speculate that the inactivation of EC-SOD by peroxidase activity plays a role in regulating SOD activity in vivo, as even low levels of superoxide will allow for the peroxidase reaction to occur. Superoxides 139-149 superoxide dismutase 3 Homo sapiens 38-44 24024135-9 2013 We speculate that the inactivation of EC-SOD by peroxidase activity plays a role in regulating SOD activity in vivo, as even low levels of superoxide will allow for the peroxidase reaction to occur. Superoxides 139-149 superoxide dismutase 3 Homo sapiens 41-44 24024135-1 2013 Superoxide dismutase (EC-SOD) controls the level of superoxide in the extracellular space by catalyzing the dismutation of superoxide into hydrogen peroxide and molecular oxygen. Superoxides 123-133 superoxide dismutase 3 Homo sapiens 22-28 22836756-4 2012 We found that miR-21 inhibited the metabolism of superoxide to hydrogen peroxide, produced either by endogenous basal activities or exposure to ionizing radiation (IR), by directing attenuating SOD3 or by an indirect mechanism that limited TNFa production, thereby reducing SOD2 levels. Superoxides 49-59 superoxide dismutase 3 Homo sapiens 194-198 22064654-1 2012 Extracellular superoxide dismutase (EcSOD) is an important superoxide scavenger in the lung in which its loss, sequence variation, or abnormal expression contributes to lung diseases; however, the role of EcSOD in lung cancer has yet to be studied. Superoxides 14-24 superoxide dismutase 3 Homo sapiens 36-41 22313459-2 2012 EC-SOD is also observed in monocytes/macrophages, and its high expression contributes to the suppression of atherosclerosis by scavenging superoxide. Superoxides 138-148 superoxide dismutase 3 Homo sapiens 0-6 22064654-1 2012 Extracellular superoxide dismutase (EcSOD) is an important superoxide scavenger in the lung in which its loss, sequence variation, or abnormal expression contributes to lung diseases; however, the role of EcSOD in lung cancer has yet to be studied. Superoxides 14-24 superoxide dismutase 3 Homo sapiens 205-210 21925591-1 2011 Extracellular superoxide dismutase (EC-SOD) is an antioxidant enzyme that breaks down superoxide anion into oxygen and hydrogen peroxide in extracellular spaces and plays key roles in controlling pulmonary and vascular diseases in response to oxidative stresses. Superoxides 86-102 superoxide dismutase 3 Homo sapiens 0-34 23339859-1 2012 Extracellular superoxide dismutase (SOD3) is a secreted enzyme that regulates levels of extracellular superoxide and protects the extracellular matrix from degradation by reactive species. Superoxides 14-24 superoxide dismutase 3 Homo sapiens 36-40 21925591-1 2011 Extracellular superoxide dismutase (EC-SOD) is an antioxidant enzyme that breaks down superoxide anion into oxygen and hydrogen peroxide in extracellular spaces and plays key roles in controlling pulmonary and vascular diseases in response to oxidative stresses. Superoxides 86-102 superoxide dismutase 3 Homo sapiens 36-42 21621610-1 2011 Extracellular superoxide dismutase (ECSOD) is the major superoxide-scavenging enzyme in the lung. Superoxides 14-24 superoxide dismutase 3 Homo sapiens 36-41 22217996-3 2011 Extracellular superoxide dismutase (SOD3), a copper and zinc superoxide dismutase, which is expressed in selected tissues, is secreted into the extracellular space and catalyzes the dismutation of superoxide radical to hydrogen peroxide and molecular oxygen. Superoxides 197-215 superoxide dismutase 3 Homo sapiens 36-40 20033309-2 2010 We investigated the hypothesis that SOD3, which neutralizes superoxide anions (O2(-)) in the intercellular space of the brain, prevents the inactivation of nitric oxide (NO) and is thus involved in regulating cerebral vascular tone. Superoxides 60-77 superoxide dismutase 3 Homo sapiens 36-40 21804221-2 2011 The increased formation of reactive oxygen species (ROS) is thought to be a key event in the pathogenesis of DR. Extracellular-superoxide dismutase (EC-SOD) is an anti-inflammatory enzyme that is distributed mainly in vascular cells and protects cells from ROS by scavenging superoxide anion. Superoxides 275-291 superoxide dismutase 3 Homo sapiens 113-147 21804221-2 2011 The increased formation of reactive oxygen species (ROS) is thought to be a key event in the pathogenesis of DR. Extracellular-superoxide dismutase (EC-SOD) is an anti-inflammatory enzyme that is distributed mainly in vascular cells and protects cells from ROS by scavenging superoxide anion. Superoxides 275-291 superoxide dismutase 3 Homo sapiens 149-155 21804221-8 2011 It is known that the presence of a high level of EC-SOD throughout the vessel walls might have an important protective role against superoxide in the vascular system. Superoxides 132-142 superoxide dismutase 3 Homo sapiens 49-55 21077177-3 2011 Extracellular-superoxide dismutase (EC-SOD) is a major anti-oxidative enzyme that protects the cells from damaging effects of superoxide. Superoxides 14-24 superoxide dismutase 3 Homo sapiens 36-42 20033309-2 2010 We investigated the hypothesis that SOD3, which neutralizes superoxide anions (O2(-)) in the intercellular space of the brain, prevents the inactivation of nitric oxide (NO) and is thus involved in regulating cerebral vascular tone. Superoxides 79-81 superoxide dismutase 3 Homo sapiens 36-40 20033309-4 2010 In normal conditions, SOD3 was found to minimize O2(-) levels, protecting endogenously produced NO at a sufficient level to maintain cerebral vascular tone and reactivity. Superoxides 49-51 superoxide dismutase 3 Homo sapiens 22-26 20033309-6 2010 SOD3 was found to neutralize superoxide anions produced in the brain during respiration of 100% O2 and to maintain basal NO levels and its vasodilatory potential in normobaric hyperoxia. Superoxides 29-46 superoxide dismutase 3 Homo sapiens 0-4 20033309-6 2010 SOD3 was found to neutralize superoxide anions produced in the brain during respiration of 100% O2 and to maintain basal NO levels and its vasodilatory potential in normobaric hyperoxia. Superoxides 96-98 superoxide dismutase 3 Homo sapiens 0-4 20594416-4 2010 Extracellular-superoxide dismutase (EC-SOD) is an anti-inflammatory enzyme that protects cells from reactive oxygen species (ROS) by scavenging superoxide anion. Superoxides 144-160 superoxide dismutase 3 Homo sapiens 0-34 20594416-4 2010 Extracellular-superoxide dismutase (EC-SOD) is an anti-inflammatory enzyme that protects cells from reactive oxygen species (ROS) by scavenging superoxide anion. Superoxides 144-160 superoxide dismutase 3 Homo sapiens 36-42 19198181-2 2008 We tested the hypothesis that SOD3 regulates the equilibrium between superoxide (O2-) and nitric oxide (NO), thereby controlling vascular tone and cerebrovascular reactivity. Superoxides 69-79 superoxide dismutase 3 Homo sapiens 30-34 18632636-6 2008 Using adenovirus-mediated extracellular superoxide dismutase (EC-SOD) gene transduction to enzymatically decrease O(2)(*-) levels, we showed that in the presence of heparin, adenovirus EC-SOD gene transduction resulted in an increase in the expression of EC-SOD outside the cells with resultant inhibition of cell invasion ability. Superoxides 114-118 superoxide dismutase 3 Homo sapiens 26-60 18726685-1 2008 Extracellular superoxide dismutase (EC-SOD) is the main SOD isoform in the arterial wall contributing to cardiovascular defense against oxidative stress by removing the superoxide anion. Superoxides 169-185 superoxide dismutase 3 Homo sapiens 0-34 18726685-1 2008 Extracellular superoxide dismutase (EC-SOD) is the main SOD isoform in the arterial wall contributing to cardiovascular defense against oxidative stress by removing the superoxide anion. Superoxides 169-185 superoxide dismutase 3 Homo sapiens 36-42 18726685-1 2008 Extracellular superoxide dismutase (EC-SOD) is the main SOD isoform in the arterial wall contributing to cardiovascular defense against oxidative stress by removing the superoxide anion. Superoxides 169-185 superoxide dismutase 3 Homo sapiens 39-42 18971527-2 2008 Extracellular superoxide dismutase (EC-SOD) protects the human body from oxidative stress by converting the toxic superoxide anion (O2-) into less toxic hydrogen peroxide (H2O2). Superoxides 114-130 superoxide dismutase 3 Homo sapiens 0-34 18971527-2 2008 Extracellular superoxide dismutase (EC-SOD) protects the human body from oxidative stress by converting the toxic superoxide anion (O2-) into less toxic hydrogen peroxide (H2O2). Superoxides 114-130 superoxide dismutase 3 Homo sapiens 36-42 18971527-2 2008 Extracellular superoxide dismutase (EC-SOD) protects the human body from oxidative stress by converting the toxic superoxide anion (O2-) into less toxic hydrogen peroxide (H2O2). Superoxides 132-134 superoxide dismutase 3 Homo sapiens 0-34 18971527-2 2008 Extracellular superoxide dismutase (EC-SOD) protects the human body from oxidative stress by converting the toxic superoxide anion (O2-) into less toxic hydrogen peroxide (H2O2). Superoxides 132-134 superoxide dismutase 3 Homo sapiens 36-42 18955813-1 2008 Superoxide dismutase (SOD) removes damaging reactive oxygen species from the cellular environment by catalyzing the dismutation of two superoxide radicals to hydrogen peroxide and oxygen. Superoxides 135-145 superoxide dismutase 3 Homo sapiens 22-25 18298405-1 2008 Superoxide dismutase (SOD) is an enzymatic component of the antioxidant defense system that protects spermatozoa by catalysing the dismutation of superoxide anions to hydrogen peroxide and oxygen. Superoxides 146-163 superoxide dismutase 3 Homo sapiens 22-25 18632636-6 2008 Using adenovirus-mediated extracellular superoxide dismutase (EC-SOD) gene transduction to enzymatically decrease O(2)(*-) levels, we showed that in the presence of heparin, adenovirus EC-SOD gene transduction resulted in an increase in the expression of EC-SOD outside the cells with resultant inhibition of cell invasion ability. Superoxides 114-118 superoxide dismutase 3 Homo sapiens 62-68 18632636-6 2008 Using adenovirus-mediated extracellular superoxide dismutase (EC-SOD) gene transduction to enzymatically decrease O(2)(*-) levels, we showed that in the presence of heparin, adenovirus EC-SOD gene transduction resulted in an increase in the expression of EC-SOD outside the cells with resultant inhibition of cell invasion ability. Superoxides 114-118 superoxide dismutase 3 Homo sapiens 185-191 18632636-6 2008 Using adenovirus-mediated extracellular superoxide dismutase (EC-SOD) gene transduction to enzymatically decrease O(2)(*-) levels, we showed that in the presence of heparin, adenovirus EC-SOD gene transduction resulted in an increase in the expression of EC-SOD outside the cells with resultant inhibition of cell invasion ability. Superoxides 114-118 superoxide dismutase 3 Homo sapiens 185-191 17717013-13 2007 Superoxide was increased in aorta (measured using lucigenin and hydroethidine) after LPS, and levels of superoxide were significantly reduced following ECSOD but not ECSOD(R213G). Superoxides 104-114 superoxide dismutase 3 Homo sapiens 152-157 18385137-1 2008 Human extracellular superoxide dismutase (EC-SOD) is a tetrameric glycoprotein responsible for the removal of superoxide generated in the extracellular space. Superoxides 20-30 superoxide dismutase 3 Homo sapiens 42-48 18203633-2 2008 Extracellular superoxide dismutase (EC-SOD or SOD3) scavenges superoxide is the major catalytic antioxidant in joint fluid and is decreased in OA cartilage. Superoxides 14-24 superoxide dismutase 3 Homo sapiens 36-42 18203633-2 2008 Extracellular superoxide dismutase (EC-SOD or SOD3) scavenges superoxide is the major catalytic antioxidant in joint fluid and is decreased in OA cartilage. Superoxides 14-24 superoxide dismutase 3 Homo sapiens 46-50 17999630-3 2008 The superoxide dismutases (SOD) are a family of enzymes that play a pivotal role protecting tissues from damage by oxidant stress by scavenging superoxide anion, which prevents the formation of other more potent oxidants such as peroxynitrite and hydroxyl radical. Superoxides 144-160 superoxide dismutase 3 Homo sapiens 27-30 17937792-1 2007 BACKGROUND: Human extracellular superoxide dismutase (EC-SOD) is a tetrameric metalloenzyme responsible for the removal of superoxide anions from the extracellular space. Superoxides 123-140 superoxide dismutase 3 Homo sapiens 18-52 17937792-1 2007 BACKGROUND: Human extracellular superoxide dismutase (EC-SOD) is a tetrameric metalloenzyme responsible for the removal of superoxide anions from the extracellular space. Superoxides 123-140 superoxide dismutase 3 Homo sapiens 54-60 18201674-1 2008 Extracellular superoxide dismutase (ecSOD) is the major extracellular scavenger of superoxide (O(2)(.-)) and a main regulator of nitric oxide (NO) bioactivity in the blood vessel wall, heart, lungs, kidney, and placenta. Superoxides 14-24 superoxide dismutase 3 Homo sapiens 36-41 18201674-1 2008 Extracellular superoxide dismutase (ecSOD) is the major extracellular scavenger of superoxide (O(2)(.-)) and a main regulator of nitric oxide (NO) bioactivity in the blood vessel wall, heart, lungs, kidney, and placenta. Superoxides 95-99 superoxide dismutase 3 Homo sapiens 0-34 18201674-1 2008 Extracellular superoxide dismutase (ecSOD) is the major extracellular scavenger of superoxide (O(2)(.-)) and a main regulator of nitric oxide (NO) bioactivity in the blood vessel wall, heart, lungs, kidney, and placenta. Superoxides 95-99 superoxide dismutase 3 Homo sapiens 36-41 17717013-14 2007 Thus, ECSOD reduces superoxide and improves relaxation to acetylcholine in the aorta after LPS, while the ECSOD variant R213G had minimal effect. Superoxides 20-30 superoxide dismutase 3 Homo sapiens 6-11 16584734-1 2007 OBJECTIVE: Extracellular superoxide dismutase (EC-SOD) is the major extracellular scavenger of superoxides, and one of the main regulators of nitric oxide bioactivity in vessel walls. Superoxides 95-106 superoxide dismutase 3 Homo sapiens 11-45 16584734-1 2007 OBJECTIVE: Extracellular superoxide dismutase (EC-SOD) is the major extracellular scavenger of superoxides, and one of the main regulators of nitric oxide bioactivity in vessel walls. Superoxides 95-106 superoxide dismutase 3 Homo sapiens 47-53 17023265-2 2006 Extracellular superoxide dismutase (EC-SOD) is a major superoxide scavenger in human plasma and vascular tissues. Superoxides 14-24 superoxide dismutase 3 Homo sapiens 36-42 17242675-1 2007 PURPOSE: To ameliorate experimental optic neuritis by combining scavenging of superoxide by germ line increases in the extracellular superoxide dismutase (ECSOD) and hydrogen peroxide by viral-mediated gene transfer of the human catalase gene. Superoxides 78-88 superoxide dismutase 3 Homo sapiens 155-160 17242675-5 2007 RESULTS: Combined scavenging of H(2)O(2) and superoxide with ECSOD and catalase suppressed demyelination by 72%, 54% due to catalase, and 19% due to ECSOD. Superoxides 45-55 superoxide dismutase 3 Homo sapiens 61-66 17242675-5 2007 RESULTS: Combined scavenging of H(2)O(2) and superoxide with ECSOD and catalase suppressed demyelination by 72%, 54% due to catalase, and 19% due to ECSOD. Superoxides 45-55 superoxide dismutase 3 Homo sapiens 149-154