Non-native Soluble Oligomers of Cu/Zn Superoxide Dismutase (SOD1) Contain a Conformational Epitope Linked to Cytotoxicity in Amyotrophic Lateral Sclerosis (ALS)
Author:
Affiliation:
1. Department of Biochemistry and Biophysics, 120 Mason Farm Road, CB# 7260, University of North Carolina, Chapel Hill, North Carolina, United States 27599
Funder
National Institutes of Health
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi500158w
Reference41 articles.
1. FALS mutations in Cu, Zn superoxide dismutase destabilize the dimer and increase dimer dissociation propensity: A large-scale thermodynamic analysis
2. Protein Aggregation and Protein Instability Govern Familial Amyotrophic Lateral Sclerosis Patient Survival
3. High Molecular Weight Complexes of Mutant Superoxide Dismutase 1: Age-Dependent and Tissue-Specific Accumulation
4. Soluble misfolded subfractions of mutant superoxide dismutase-1s are enriched in spinal cords throughout life in murine ALS models
5. ALS-linked mutant SOD1 induces ER stress- and ASK1-dependent motor neuron death by targeting Derlin-1
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