Article
Evaluating protein cross-linking as a therapeutic strategy to stabilize SOD1 variants in a mouse model of familial ALS.
PLoS biology - 1 Jan 2024
Hossain Md Amin, Sarin Richa, Donnelly Daniel P, Miller Brandon C, Weiss Alexandra, McAlary Luke, Antonyuk Svetlana V, Salisbury Joseph P, Amin Jakal, Conway Jeremy B, Watson Samantha S, Winters Jenifer N, Xu Yu, Alam Novera, Brahme Rutali R, Shahbazian Haneyeh, Sivasankar Durgalakshmi, Padmakumar Swathi, Sattarova Aziza, Ponmudiyan Aparna C, Gawde Tanvi, Verrill David E, Yang Wensheng, Kannapadi Sunanda, Plant Leigh D, Auclair Jared R, Makowski Lee, Petsko Gregory A, Ringe Dagmar, Agar Nathalie Y R, Greenblatt David J, Ondrechen Mary Jo, Chen Yunqiu, Yerbury Justin J, Manetsch Roman, Hasnain S Samar, Brown Robert H, Agar Jeffrey N
Abstract excerpt
Mutations in the gene encoding Cu-Zn superoxide dismutase 1 (SOD1) cause a subset of familial amyotrophic lateral sclerosis (fALS) cases. A shared effect of these mutations is that SOD1, which is normally a stable dimer, dissociates into toxic monomers that seed toxic aggregates. Considerable research effort has been devoted to developing compounds that stabilize the dimer of fALS SOD1 variants, but...
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