Extracellular superoxide dismutase in biology and medicine.
By C. Fattman, L. Schaefer, T. Oury. Free Radical Biology & Medicine, 2003
649 citations recorded by the source corpus.
Subfields: Molecular Biology, Nutrition and Dietetics, Physiology
View Paper: https://www.semanticscholar.org/paper/c61f7b99a1176f618b1a24515de379d1f24d63ba
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Citations in the corpus
- Effects of dietary copper sources and levels on performance, copper status, plasma antioxidant activities and relative copper bioavailability in Carassius auratus gibelio (2010, background): “One family of antioxidant enzymes, the superoxide dismutase (SOD), functions to remove damaging reactive oxygen species (ROS) from the cellular environment by catalyzing the dismutation of two superoxide radicals to hydrogen peroxide and oxygen (Fattman et al., 2003; Lin et al., 2008).”
- Regulation of superoxide dismutase genes: implications in disease. (2009, background): “An additional NF-κB site has been identified in the second intron, but its regulatory role in ECSOD expression remains unclear [42].”
- Dietary copper requirements of juvenile grouper, Epinephelus malabaricus (2008, neutral): “One family of antioxidant enzymes, the superoxide dismutase (SOD), function to remove damaging reactive oxygen species (ROS) from the cellular environment by catalyzing the dismutation of two superoxide radicals to hydrogen peroxide and oxygen (Fattman et al., 2003).”
- Superoxide dismutases: Dual roles in controlling ROS damage and regulating ROS signaling (2018, neutral): “High expression of Sod3 was identified in selected tissues, particularly in blood vessels, lung, kidney, and heart (Marklund, 1984; Folz and Crapo, 1994; Strålin et al., 1995; Fattman et al., 2003).”
- Biological Activities of Reactive Oxygen and Nitrogen Species: Oxidative Stress versus Signal Transduction (2015, background): “However, extracellular SOD, which mainly occurs in tissue ([36,37]; reviewed in [38,39]), can also be found in plasma under specific pathological conditions [40] and contribute to the elimination of O2• .”
- Hydrogen Peroxide: A Signaling Messenger (2006, neutral): “The enhanced proliferation rate resulting from NOX1 was inhibited by the overexpression catalase (10), consistent with, but not definitively indicative”
- Superoxide Dismutases: Role in Redox Signaling, Vascular Function, and Diseases (2011, positive): “FUKAI AND USHIO-FUKAI domain, which results in reduced heparan sulfate affinity and higher plasma levels (63, 67).”