Superoxide dismutase 1 (misfolded form) (SOD1 (misfolded SOD1))

Misfolded superoxide dismutase 1 refers specifically to SOD1 protein that has lost its native structure due to genetic mutations or post-translational modifications such as metal ion loss or abnormal oxidation, resulting in protein destabilization, exposure of normally buried epitopes, and formation of toxic aggregates. These misfolded forms acquire aberrant interactions and cytotoxic functions that contribute directly to the pathogenesis of amyotrophic lateral sclerosis (ALS), both familial (mutant SOD1) and, in some cases, sporadic disease (post-translationally modified wild-type SOD1). Misfolded SOD1 destabilizes cellular proteostasis, induces oxidative stress, and promotes neurodegeneration by forming intracellular filaments and activating microglia toxic responses. It is considered a validated molecular therapeutic target in ALS, with ongoing research focused on inhibitors, antibodies, or molecular chaperones to prevent misfolding, aggregation, and toxicity.

Other names

misfolded SOD1mutant SOD1aberrant SOD1SOD1 protein (mutant/misfolded)Cu/Zn superoxide dismutase 1 (misfolded)SOD1 A4V (as a pathogenic mutation)oxidized SOD1SOD1 aggregates

Inhibition of misfolded SOD1 aggregation, stabilization of native conformation, obscuration/neutralization of pathogenic epitopes, post-translational modification repair, proteostasis modulation.