Structural and biophysical properties of metal-free pathogenic SOD1 mutants A4V and G93A
Authors:
- Svetlana V. AntonyukSASvetlana V. Antonyuk
- Alexander B. TaylorATAlexander B. Taylor
- Stephen P. HollowaySHStephen P. Holloway
- P. John HartPHP. John Hart
- 1 December 2009
- journal article
- research article
- Published by Elsevier in Archives of Biochemistry and Biophysics
- Vol. 492 (1-2) , 40-47
Abstract
No abstract availableKeywords
This publication has 63 references indexed in Scilit:
- Functional features cause misfolding of the ALS-provoking enzyme SOD1Proceedings of the National Academy of Sciences, 2009
- Role of mutant SOD1 disulfide oxidation and aggregation in the pathogenesis of familial ALSProceedings of the National Academy of Sciences, 2009
- Structural and Biophysical Properties of the Pathogenic SOD1 Variant H46R/H48QBiochemistry, 2009
- Structures of the G85R Variant of SOD1 in Familial Amyotrophic Lateral SclerosisJournal of Biological Chemistry, 2008
- Biological effects of CCS in the absence of SOD1 enzyme activation: implications for disease in a mouse model for ALSHuman Molecular Genetics, 2008
- Soluble misfolded subfractions of mutant superoxide dismutase-1s are enriched in spinal cords throughout life in murine ALS modelsProceedings of the National Academy of Sciences, 2007
- Overexpression of CCS in G93A-SOD1 mice leads to accelerated neurological deficits with severe mitochondrial pathologyProceedings of the National Academy of Sciences, 2007
- Posttranslational Modifications in Cu,Zn-Superoxide Dismutase and Mutations Associated with Amyotrophic Lateral SclerosisAntioxidants & Redox Signaling, 2006
- [20] Processing of X-ray diffraction data collected in oscillation mode1997
- Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosisNature, 1993