Evaluating protein cross-linking as a therapeutic strategy to stabilize SOD1 variants in a mouse model of familial ALS

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.