Implications of fALS Mutations on Sod1 Function and Oligomerization in Cell Models
Sign Up to like & getrecommendations! Published in 2017 at "Molecular Neurobiology"
DOI: 10.1007/s12035-017-0755-4
Abstract: Among the familial forms of amyotrophic lateral sclerosis (fALS), 20% are associated with the Cu,Zn-superoxide dismutase (Sod1). fALS is characterized by the accumulation of aggregated proteins and the increase in oxidative stress markers. Here, we… read more here.
Keywords: fals sod1; sod1; sod1 mutants; fals mutations ... See more keywords
Reduced thermodynamic stability as prerequisite for aggregation of SOD1 mutants: a path through the reduction in intramolecular disulfide bonds
Sign Up to like & getrecommendations! Published in 2020 at "Journal of the Iranian Chemical Society"
DOI: 10.1007/s13738-020-01911-4
Abstract: Amyotrophic lateral sclerosis is a fatal, devastating, rapidly progressive, adult onset neurodegenerative disease, which is involved in the formation of proteinaceous virulent aggregates from superoxide dismutase 1 (SOD1) as a Cu/Zn metalloenzyme in motor neurons.… read more here.
Keywords: reduction; aggregation; sod1; sod1 mutants ... See more keywords
Structural Properties and Interaction Partners of Familial ALS-Associated SOD1 Mutants
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DOI: 10.3389/fneur.2019.00527
Abstract: Amyotrophic lateral sclerosis (ALS) is the most common motor neuron degenerative disease in adults and has also been proven to be a type of conformational disease associated with protein misfolding and dysfunction. To date, more… read more here.
Keywords: structural properties; interaction partners; sod1 mutants; partners familial ... See more keywords