Oxidation versus aggregation — how do SOD1 mutants cause ALS?
- 1 December 2000
- journal article
- editorial
- Published by Springer Nature in Nature Medicine
- Vol. 6 (12), 1320-1321
- https://doi.org/10.1038/82122
Abstract
No abstract availableThis publication has 10 references indexed in Scilit:
- Formation of high molecular weight complexes of mutant Cu,Zn-superoxide dismutase in a mouse model for familial amyotrophic lateral sclerosisProceedings of the National Academy of Sciences, 2000
- Toxicity of ALS-Linked SOD1 MutantsScience, 2000
- Copper chaperone for superoxide dismutase is essential to activate mammalian Cu/Zn superoxide dismutaseProceedings of the National Academy of Sciences, 2000
- Induction of Nitric Oxide -- Dependent Apoptosis in Motor Neurons by Zinc-Deficient Superoxide DismutaseScience, 1999
- From Charcot to SOD1Neuron, 1999
- Up‐Regulation of Protein Chaperones Preserves Viability of Cells Expressing Toxic Cu/Zn‐Superoxide Dismutase Mutants Associated with Amyotrophic Lateral SclerosisJournal of Neurochemistry, 1999
- Aggregation and Motor Neuron Toxicity of an ALS-Linked SOD1 Mutant Independent from Wild-Type SOD1Science, 1998
- The Copper Chaperone for Superoxide DismutaseJournal of Biological Chemistry, 1997
- Aggregation of Mutant Cu/Zn Superoxide Dismutase Proteins in a Culture Model of ALSJournal of Neuropathology and Experimental Neurology, 1997
- Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosisNature, 1993