Gibbs Energy of Superoxide Dismutase Heterodimerization Accounts for Variable Survival in Amyotrophic Lateral Sclerosis
Author:
Affiliation:
1. Department of Chemistry and Biochemistry, Baylor University, Waco, Texas 76798-7348, United States
Funder
Division of Chemistry
Welch Foundation
U.S. Department of Defense
Publisher
American Chemical Society (ACS)
Subject
Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis
Link
https://pubs.acs.org/doi/pdf/10.1021/jacs.6b01742
Reference56 articles.
1. Autosomal recessive adult-onset amyotrophic lateral sclerosis associated with homozygosity for Asp90Ala CuZn-superoxide dismutase mutation: A clinical and genealogical study of 36 patients
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4. An examination of wild-type SOD1 in modulating the toxicity and aggregation of ALS-associated mutant SOD1
5. Heterodimer formation of wild-type and amyotrophic lateral sclerosis-causing mutant Cu/Zn-superoxide dismutase induces toxicity independent of protein aggregation
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