image: Potential ALS therapeutic S-XL6 turns toxic Cu/Zn-superoxide dismutase monomers into stable dimers.
Credit: Ella Maru Studio (CC-BY 4.0, https://creativecommons.org/licenses/by/4.0/)
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.
Journal
PLOS Biology
Article Title
Evaluating protein cross-linking as a therapeutic strategy to stabilize SOD1 variants in a mouse model of familial ALS
COI Statement
Competing interests: The authors have declared that no competing interests exist.