Role of the Dimeric Structure in Cu,Zn Superoxide Dismutase
Open Access
- 1 March 1998
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 273 (10) , 5655-5661
- https://doi.org/10.1074/jbc.273.10.5655
Abstract
No abstract availableKeywords
This publication has 30 references indexed in Scilit:
- The Cu,Zn superoxide dismutase from Escherichia coli retains monomeric structure at high protein concentration. Evidence for altered subunit interaction in all the bacteriocupreinsBiochemical Journal, 1996
- Novel dimeric interface and electrostatic recognition in bacterial Cu,Zn superoxide dismutaseProceedings of the National Academy of Sciences, 1996
- Cloning and analysis of sodC, encoding the copper-zinc superoxide dismutase of Escherichia coliJournal of Bacteriology, 1996
- Bacterial [Cu,Zn]-superoxide dismutase: phylogenetically distinct from the eukaryotic enzyme, and not so rare after all!Microbiology, 1995
- Conserved Patterns in the Cu,Zn Superoxide Dismutase FamilyJournal of Molecular Biology, 1994
- Evolutionary conservativeness of electric field in the Cu,Zn superoxide dismutase active site: Evidence for co-ordinated mutation of charged amino acid residuesJournal of Molecular Biology, 1992
- Evolution of CuZn superoxide dismutase and the Greek Key β‐barrel structural motifProteins-Structure Function and Bioinformatics, 1989
- Aspects of the Structure, Function, and Applications of Superoxide DismutasCritical Reviews in Biochemistry, 1987
- Bovine Erythrocyte Superoxide DismutaseJournal of Biological Chemistry, 1974
- On the Stability of Bovine Superoxide DismutaseJournal of Biological Chemistry, 1973