Mutations in the Cu-Zn superoxide dismutase 1 gene SOD1 can cause familial amyotrophic lateral sclerosis (fALS) in a process that involves dissociation of the SOD1 dimer; this study shows that a novel cyclic thiosulfinate cross-linker has favorable drug-like properties and can stabilize the SOD1 dimer in vivo, with therapeutic implications for fALS
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In your coverage, please use this URL to provide access to the freely available paper in PLOS Biology : http://journals.plos.org/plosbiology/article?id=10.1371/journal.pbio.3002462
Author Countries : United States, Australia, United Kingdom
Funding: This work was supported by the National Institute of Neurological Disorders and Stroke of National Institute of Health (R01NS065263 to J.N.A.), the ALS Association (18-IIA-420 to J.N.A., M.J.O., and R.M.), Johnston Rducational Ventures (#685162 to J.N.A.), and the National Science Foundation (#MCB-1517290, CHE-1905214 to M.J.O.). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.
PLOS Biology
Evaluating protein cross-linking as a therapeutic strategy to stabilize SOD1 variants in a mouse model of familial ALS
Competing interests: The authors have declared that no competing interests exist.