PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 24657197-7 2014 In addition, peroxide levels were negatively correlated with relative GPX1- and SOD1-transcript abundances, whereas GPX1 was positively correlated with embryo survival at 24h post-warming. Peroxides 13-21 superoxide dismutase 1 Homo sapiens 80-84 23919400-4 2013 We observed that cysteinylation of cysteine 111 (Cys111) of SOD1 prevents oxidation by peroxide (DOI 10.1021/bi4006122 ). Peroxides 87-95 superoxide dismutase 1 Homo sapiens 60-64 24184207-11 2014 Further studies are needed to define whether SOD-1-dependent superoxide/peroxide balance is relevant for regulation of T cell activation, as well as in the functional cross talk between immune effectors. Peroxides 63-71 superoxide dismutase 1 Homo sapiens 45-50 20079425-6 2010 8-Isoprostane generation was driven by the addition of peroxide and nitric oxide; incubation with permeative PEG-SOD, but not PEG-catalase or impermeative SOD, attenuated hypoxia-induced 8-isoprostane generation. Peroxides 55-63 superoxide dismutase 1 Homo sapiens 113-116 23332757-4 2013 SOD1 binds a C-terminal degron we identified in Yck1p/Yck2p and promotes kinase stability by catalyzing superoxide conversion to peroxide. Peroxides 106-114 superoxide dismutase 1 Homo sapiens 0-4 23927036-5 2013 As much as half of all purified SOD1 protein contained non-native post-translational modifications (PTMs), the most prevalent modifications being cysteinylation and peroxide-related oxidations. Peroxides 165-173 superoxide dismutase 1 Homo sapiens 32-36 23927036-8 2013 To further characterize how cysteinylation may protect SOD1 from oxidation, cysteine-modified SOD1 was prepared in vitro and exposed to peroxide. Peroxides 136-144 superoxide dismutase 1 Homo sapiens 94-98 23927036-9 2013 Cysteinylation conferred nearly complete protection from peroxide-induced oxidation of SOD1. Peroxides 57-65 superoxide dismutase 1 Homo sapiens 87-91 23927036-10 2013 Moreover, SOD1 that has been cysteinylated and peroxide oxidized in vitro comprised a set of PTMs that bear a striking resemblance to the myriad of PTMs observed in SOD1 purified from human tissue. Peroxides 47-55 superoxide dismutase 1 Homo sapiens 10-14 23927036-10 2013 Moreover, SOD1 that has been cysteinylated and peroxide oxidized in vitro comprised a set of PTMs that bear a striking resemblance to the myriad of PTMs observed in SOD1 purified from human tissue. Peroxides 47-55 superoxide dismutase 1 Homo sapiens 165-169 21911079-4 2011 SOD catalyzes the dismutation of O(2)(-) to H(2)O(2), and GPx catalyzes the reduction of H(2)O(2) and other harmful peroxides by glutathione (GSH). Peroxides 116-125 superoxide dismutase 1 Homo sapiens 0-3 17725652-7 2007 SOD serum activity correlated positively with NO(x) serum levels and negatively with peroxide serum levels in healthy controls and in chronic migraine sufferers before and after biofeedback. Peroxides 85-93 superoxide dismutase 1 Homo sapiens 0-3 19815008-7 2010 Gp120-induced Ca(2+) signaling in both neuron types was inhibited by GPx1 or Cu/Zn superoxide dismutase (SOD1), implicating superoxide and peroxide in ligand (gp120)-induced signaling upstream of Ca(2+) release from intracellular stores. Peroxides 85-93 superoxide dismutase 1 Homo sapiens 105-109 19804834-4 2010 Stimulation of intracellular peroxide production by TPA was detected by a DCHF-DA assay, and the addition of superoxide dismutase (SOD) or tempol significantly inhibited TPA-induced migration/invasion and COX-2 protein expression accompanied by a decrease in peroxide production. Peroxides 111-119 superoxide dismutase 1 Homo sapiens 131-134 19432205-6 2008 The age-related alterations in F, SOD, and GR stress responsiveness lead to activation of peroxide oxidation of lipids that may be considered as an important factor of aging damage of erythrocyte functioning and reliability of oxygen transport to tissues under stress conditions. Peroxides 90-98 superoxide dismutase 1 Homo sapiens 34-37 15247047-1 2004 One of the most important antioxidant enzymes is superoxide dismutase (SOD), which catalyzes the dismutation of superoxide radicals to peroxide. Peroxides 51-59 superoxide dismutase 1 Homo sapiens 71-74 17292965-1 2007 It is well known that the wild type Cu,Zn superoxide dismutase (holo SOD) catalyzes the conversion of superoxide anion to peroxide hydrogen and dioxygen. Peroxides 44-52 superoxide dismutase 1 Homo sapiens 69-72 16608305-6 2006 This result supports that the positive guanidinium plays a role in the catalytic mechanism of Cu,Zn-SOD by ensuring that superoxide enters and peroxide leaves rapidly from the coordination sphere of the copper ion. Peroxides 123-131 superoxide dismutase 1 Homo sapiens 100-103 15812313-4 2005 Motoneuron-neuroblastoma hybrid (VSC 4.1) cells expressing mutant SOD1, when treated with copper chloride, showed reduced viability and increased levels of endogenous peroxides. Peroxides 167-176 superoxide dismutase 1 Homo sapiens 66-70 17336361-3 2007 SOD1 converts superoxide to peroxide; GPx1 converts peroxide to water. Peroxides 16-24 superoxide dismutase 1 Homo sapiens 0-4 17336361-3 2007 SOD1 converts superoxide to peroxide; GPx1 converts peroxide to water. Peroxides 28-36 superoxide dismutase 1 Homo sapiens 0-4 2308398-0 1990 Glutathione peroxidase, superoxide dismutase, and catalase inactivation by peroxides and oxygen derived free radicals. Peroxides 75-84 superoxide dismutase 1 Homo sapiens 24-44 8613912-5 1996 Addition of enzymes that metabolize peroxide (catalase or superoxide dismutase [SOD]) also reduced fluorescence by nearly 50%. Peroxides 36-44 superoxide dismutase 1 Homo sapiens 80-83 8932447-1 1996 PURPOSE: Superoxide dismutase (SOD), an antioxidant enzyme, converts peroxide radicals into hydrogen peroxide. Peroxides 11-19 superoxide dismutase 1 Homo sapiens 31-34 8252716-4 1993 This inhibition was reduced by addition of nonionic detergents, which contain organic peroxide inhibitors of SOD, to the fructosamine reagent. Peroxides 86-94 superoxide dismutase 1 Homo sapiens 109-112 11255131-4 2001 Low SOD and catalase activity and high activity of glutathione-dependent enzymes in tumors suggest that glutathione peroxidase and glutathione S-transferase play a major role in peroxide utilization in malignant tumors. Peroxides 178-186 superoxide dismutase 1 Homo sapiens 4-7 1657737-6 1991 Like superoxide dismutase (SOD) and other oxidatively denatured proteins, glutathione peroxidase inactivated by peroxides or free radicals seems to be degraded preferentially by proteases. Peroxides 112-121 superoxide dismutase 1 Homo sapiens 5-25 1657737-6 1991 Like superoxide dismutase (SOD) and other oxidatively denatured proteins, glutathione peroxidase inactivated by peroxides or free radicals seems to be degraded preferentially by proteases. Peroxides 112-121 superoxide dismutase 1 Homo sapiens 27-30 199619-7 1977 Under the influence of inhibited phagosome formation by cytochalasin B, the cells released an increased amount of superoxide and peroxide into the extracellular medium relative to oxygen consumption, and all detectable peroxide release could be inhibited by the addition of ferricytochrome c. Decreased H(2)O(2) production in the presence of this compound could not be ascribed to diminished bacterial binding, decreased oxidase activity, or increased H(2)O(2) catabolism and was reversed by the simultaneous addition of SOD. Peroxides 116-124 superoxide dismutase 1 Homo sapiens 521-524 2722888-1 1989 The interaction between superoxide dismutase (SOD) and peroxide, under anaerobic conditions in the presence of an OH radical scavenger, formate, and an indicator, nitro blue tetrazolium, involves five reactions and an equilibrium: (table; see text) Reaction 3 occurs at a rate that is proportional to both peroxide and enzyme with no kinetic evidence for any intermediate peroxide-enzyme complex. Peroxides 26-34 superoxide dismutase 1 Homo sapiens 46-49 2722888-1 1989 The interaction between superoxide dismutase (SOD) and peroxide, under anaerobic conditions in the presence of an OH radical scavenger, formate, and an indicator, nitro blue tetrazolium, involves five reactions and an equilibrium: (table; see text) Reaction 3 occurs at a rate that is proportional to both peroxide and enzyme with no kinetic evidence for any intermediate peroxide-enzyme complex. Peroxides 55-63 superoxide dismutase 1 Homo sapiens 24-44 2722888-1 1989 The interaction between superoxide dismutase (SOD) and peroxide, under anaerobic conditions in the presence of an OH radical scavenger, formate, and an indicator, nitro blue tetrazolium, involves five reactions and an equilibrium: (table; see text) Reaction 3 occurs at a rate that is proportional to both peroxide and enzyme with no kinetic evidence for any intermediate peroxide-enzyme complex. Peroxides 55-63 superoxide dismutase 1 Homo sapiens 46-49 2722888-1 1989 The interaction between superoxide dismutase (SOD) and peroxide, under anaerobic conditions in the presence of an OH radical scavenger, formate, and an indicator, nitro blue tetrazolium, involves five reactions and an equilibrium: (table; see text) Reaction 3 occurs at a rate that is proportional to both peroxide and enzyme with no kinetic evidence for any intermediate peroxide-enzyme complex. Peroxides 55-63 superoxide dismutase 1 Homo sapiens 24-44 2722888-1 1989 The interaction between superoxide dismutase (SOD) and peroxide, under anaerobic conditions in the presence of an OH radical scavenger, formate, and an indicator, nitro blue tetrazolium, involves five reactions and an equilibrium: (table; see text) Reaction 3 occurs at a rate that is proportional to both peroxide and enzyme with no kinetic evidence for any intermediate peroxide-enzyme complex. Peroxides 55-63 superoxide dismutase 1 Homo sapiens 46-49 34943042-3 2021 Superoxide dismutase (SOD)-1 represents the major physiological intracellular source of peroxides. Peroxides 88-97 superoxide dismutase 1 Homo sapiens 0-28 30328005-6 2019 Molecular dynamics (MD) simulations were consistent with differential access of peroxide versus quencher to SOD1"s interior complicating surface accessibility considerations. Peroxides 80-88 superoxide dismutase 1 Homo sapiens 108-112 31319025-2 2019 Superoxide dismutase (SOD) protects cells from superoxide-triggered apoptosis by converting superoxide to oxygen and peroxide. Peroxides 2-10 superoxide dismutase 1 Homo sapiens 22-25 28171220-7 2016 As the enzyme superoxide dismutase (SOD) is mainly involved in the formation of nitrosative stress (peroxides) we measured the activity, and found significant differences in the placebo and verum group after 3 and 6 month (p=0,050 and p=0,003 respectively). Peroxides 100-109 superoxide dismutase 1 Homo sapiens 14-34 28171220-7 2016 As the enzyme superoxide dismutase (SOD) is mainly involved in the formation of nitrosative stress (peroxides) we measured the activity, and found significant differences in the placebo and verum group after 3 and 6 month (p=0,050 and p=0,003 respectively). Peroxides 100-109 superoxide dismutase 1 Homo sapiens 36-39