Results 21 to 30 of about 346,257 (357)
Catalysis from A to Z, 2020 Proteins that protect cells against elevated levels of superoxide a reactive oxygen species. These antioxidant enzymes catalyze the formation of molecular oxygen and hydrogen peroxide from the superoxide anion.
P. Sears
semanticscholar +1 more source
Superoxide dismutase: an evolutionary puzzle. [PDF]
Proceedings of the National Academy of Sciences, 1985 We have obtained the complete amino acid sequence of copper/zinc-containing superoxide dismutase (SOD, superoxide:superoxide oxidoreductase, EC 1.15.1.1) from Drosophila melanogaster. The sequence of this enzyme is also known for man, horse, cow, and the yeast Saccharomyces cerevisiae. The rate of evolution of this enzyme is far from constant.
Lee, YM, Friedman, DJ, Ayala, FJ
openaire +5 more sources
The landscape of cognitive impairment in superoxide dismutase 1-amyotrophic lateral sclerosis
Neural Regeneration Research, 2023 Although mutations in the superoxide dismutase 1 gene account for only a minority of total amyotrophic lateral sclerosis cases, the discovery of this gene has been crucial for amyotrophic lateral sclerosis research. Since the identification of superoxide
Ilaria Martinelli +6 more
doaj +1 more source
Expression of Extracellular Superoxide Dismutase Protein in Diabetes [PDF]
Archives of Plastic Surgery, 2013 Background Diabetes is characterized by chronic hyperglycemia, which can increase reactive oxygen species (ROS) production by the mitochondrial electron transport chain.
Chul Han Kim
doaj +2 more sources
Reaction of the desulfoferrodoxin from Desulfoarculus baarsii with superoxide anion. Evidence for a superoxide reductase activity [PDF]
The journal of biological chemistry, American Society for
Biochemistry and Molecular Biology, 2000, 275, pp.115-21, 2014 Desulfoferrodoxin is a small protein found in sulfate-reducing bacteria that contains two independent mononuclear iron centers, one ferric and one ferrous. Expression of desulfoferrodoxin from Desulfoarculus baarsii has been reported to functionally complement a superoxide dismutase deficient Escherichia coli strain.
arxiv +1 more source
The Copper Chaperone for Superoxide Dismutase [PDF]
Journal of Biological Chemistry, 1997 Copper is distributed to distinct localizations in the cell through diverse pathways. We demonstrate here that the delivery of copper to copper/zinc superoxide dismutase (SOD1) is mediated through a soluble factor identified as Saccharomyces cerevisiae LYS7 and human CCS (copper chaperone for SOD).
Bernhard Krems +5 more
openaire +3 more sources
ASSOCIATION BETWEEN BLOOD DONATION FREQUENCY, ANTIOXIDANT ENZYMES AND LIPID PEROXIDATION [PDF]
Acta Medica Iranica, 2008 "nIron is a pro-oxidant cofactor that may be linked to atherosclerosis progression. Free iron catalyzes the generation of free radicals and free radicals promote the oxidation of lipids.
M Mehrabani +6 more
doaj +2 more sources
A simple method for clinical assay of superoxide dismutase.
Clinical Chemistry, 1988 This assay for superoxide dismutase (SOD, EC 1.15.1.1) activity involves inhibition of nitroblue tetrazolium reduction, with xanthine-xanthine oxidase used as a superoxide generator.
Yi Sun, L. Oberley, Ying Li
semanticscholar +1 more source
Discovery of superoxide reductase: an historical perspective [PDF]
Journal of Biological Inorganic Chemistry, 2004, 9, pp.119-23, 2014 For more than 30 years, the only enzymatic system known to catalyze the elimination of superoxide was superoxide dismutase, SOD. SOD has been found in almost all organisms living in the presence of oxygen, including some anaerobic bacteria, supporting the notion that superoxide is a key and general component of oxidative stress. Recently, a new concept
arxiv +1 more source
Polymer coated cerium oxide nanoparticles as oxidoreductase-like catalysts [PDF]
ACS Appl. Mater. Interfaces 2020, 12, 37, 42056 - 42066, 2020 Cerium oxide nanoparticles have been shown to mimic oxidoreductase enzymes by catalyzing the decomposition of organic substrates and reactive oxygen species. This mimicry can be found in superoxide radicals and hydrogen peroxides, harmful molecules produced in oxidative stress asso-ciated diseases.
arxiv +1 more source