Article
Disulfide bond mediates aggregation, toxicity, and ubiquitylation of familial amyotrophic lateral sclerosis-linked mutant SOD1.
The Journal of biological chemistry - 21 Sept 2007
Niwa Jun-ichi, Yamada Shin-ichi, Ishigaki Shinsuke, Sone Jun, Takahashi Miho, Katsuno Masahisa, Tanaka Fumiaki, Doyu Manabu, Sobue Gen
Abstract excerpt
Mutations in the Cu/Zn-superoxide dismutase (SOD1) gene cause familial amyotrophic lateral sclerosis (ALS) through the gain of a toxic function; however, the nature of this toxic function remains largely unknown. Ubiquitylated aggregates of mutant SOD1 proteins in affected brain lesions are pathological hallmarks of the disease and are suggested to be involved in several proposed mechanisms of motor neuron death....
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