Loss of in Vitro Metal Ion Binding Specificity in Mutant Copper-Zinc Superoxide Dismutases Associated with Familial Amyotrophic Lateral Sclerosis
Open Access
- 1 January 2000
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 275 (2) , 1007-1014
- https://doi.org/10.1074/jbc.275.2.1007
Abstract
No abstract availableKeywords
This publication has 41 references indexed in Scilit:
- Metal ion reconstitution studies of yeast copper-zinc superoxide dismutase: the "phantom" subunit and the possible role of Lys7pJBIC Journal of Biological Inorganic Chemistry, 1998
- SUPEROXIDE RADICAL AND SUPEROXIDE DISMUTASESAnnual Review of Biochemistry, 1995
- Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosisNature, 1993
- Silver-binding properties of bovine cuprozinc superoxide dismutase and the overall stability of selected metal-ion derivativesJournal of the American Chemical Society, 1990
- Investigation of Cu2Co2SOD and its anion derivatives. Proton NMR and electronic spectraJournal of the American Chemical Society, 1985
- Determination and analysis of the 2 Å structure of copper, zinc superoxide dismutaseJournal of Molecular Biology, 1982
- The pH dependence of metal ion binding to the native zinc site of bovine erythrocuprein (superoxide dismutase)Journal of the American Chemical Society, 1982
- Metal sites of copper-zinc superoxide dismutaseBiochemistry, 1977
- Reversible uncoupling of the copper and cobalt spin systems in cobalt bovine superoxide dismutase at low pHFEBS Letters, 1975
- The superoxide dismutase activity of human erythrocupreinFEBS Letters, 1973