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Chemical Compound Review

copper; zinc     copper; zinc

Synonyms: B-124, AC1L4JU8, 81219-95-6, Copper alloy, Cu,Zn (U.S. Bronze B-124)
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Disease relevance of Copper alloy, Cu,Zn (U.S. Bronze B-124)


High impact information on Copper alloy, Cu,Zn (U.S. Bronze B-124)

  • Copper-zinc superoxide dismutase (CuZnSOD, SOD1 protein) is an abundant copper- and zinc-containing protein that is present in the cytosol, nucleus, peroxisomes, and mitochondrial intermembrane space of human cells [1].
  • Copper, zinc superoxide dismutase (SOD) catalyses the very rapid two-step dismutation of the toxic superoxide radical (O-2) to molecular oxygen and hydrogen peroxide through the alternate reduction and oxidation of the active-site copper [6].
  • Copper/zinc superoxide dismutase activity in trisomy 21 by translocation [7].
  • Copper, zinc, and iron in normal and leukemic lymphocytes from children [4].
  • Copper/zinc superoxide dismutase (SOD1) is an abundant intracellular enzyme with an essential role in antioxidant defense [8].

Chemical compound and disease context of Copper alloy, Cu,Zn (U.S. Bronze B-124)

  • Copper-zinc superoxide dismutase activity did not change with heat stress or drug treatment, whereas manganese superoxide dismutase activity was increased in old animals only [9].

Biological context of Copper alloy, Cu,Zn (U.S. Bronze B-124)


Anatomical context of Copper alloy, Cu,Zn (U.S. Bronze B-124)


Associations of Copper alloy, Cu,Zn (U.S. Bronze B-124) with other chemical compounds


Gene context of Copper alloy, Cu,Zn (U.S. Bronze B-124)


Analytical, diagnostic and therapeutic context of Copper alloy, Cu,Zn (U.S. Bronze B-124)


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  3. Copper/zinc superoxide dismutase transgenic brain accumulates hydrogen peroxide after perinatal hypoxia ischemia. Fullerton, H.J., Ditelberg, J.S., Chen, S.F., Sarco, D.P., Chan, P.H., Epstein, C.J., Ferriero, D.M. Ann. Neurol. (1998) [Pubmed]
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  7. Copper/zinc superoxide dismutase activity in trisomy 21 by translocation. Garber, P., Sinet, P.M., Jerome, H., Lejeune, J. Lancet (1979) [Pubmed]
  8. Mechanisms of biosynthesis of mammalian copper/zinc superoxide dismutase. Bartnikas, T.B., Gitlin, J.D. J. Biol. Chem. (2003) [Pubmed]
  9. Thiol supplementation in aged animals alters antioxidant enzyme activity after heat stress. Morrison, J.P., Coleman, M.C., Aunan, E.S., Walsh, S.A., Spitz, D.R., Kregel, K.C. J. Appl. Physiol. (2005) [Pubmed]
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  11. Structure of fully reduced bovine copper zinc superoxide dismutase at 1.15 A. Hough, M.A., Hasnain, S.S. Structure (Camb.) (2003) [Pubmed]
  12. Antioxidant enzyme gene expression in rats with remnant kidney induced chronic renal failure. Van Den Branden, C., Ceyssens, B., De Craemer, D., De Bleser, P., Hellemans, K., Geerts, A., Verbeelen, D. Exp. Nephrol. (2000) [Pubmed]
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  22. Overexpression of copper zinc superoxide dismutase suppresses human glioma cell growth. Zhang, Y., Zhao, W., Zhang, H.J., Domann, F.E., Oberley, L.W. Cancer Res. (2002) [Pubmed]
  23. Developmental changes in murine brain antioxidant enzymes. Khan, J.Y., Black, S.M. Pediatr. Res. (2003) [Pubmed]
  24. Copper/zinc superoxide dismutase attenuates neuronal cell death by preventing extracellular signal-regulated kinase activation after transient focal cerebral ischemia in mice. Noshita, N., Sugawara, T., Hayashi, T., Lewén, A., Omar, G., Chan, P.H. J. Neurosci. (2002) [Pubmed]
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