Title : Nucleation and kinetics of SOD1 aggregation in human cells for ALS1.

Pub. Date : 2020 Mar

PMID : 32056106






5 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 Aberrant structural formations of Cu/Zn superoxide dismutase enzyme (SOD1) are the probable mechanism by which circumscribed mutations in the SOD1 gene cause familial amyotrophic lateral sclerosis (ALS1). Superoxides superoxide dismutase 1 Homo sapiens
2 Aberrant structural formations of Cu/Zn superoxide dismutase enzyme (SOD1) are the probable mechanism by which circumscribed mutations in the SOD1 gene cause familial amyotrophic lateral sclerosis (ALS1). Superoxides superoxide dismutase 1 Homo sapiens
3 Aberrant structural formations of Cu/Zn superoxide dismutase enzyme (SOD1) are the probable mechanism by which circumscribed mutations in the SOD1 gene cause familial amyotrophic lateral sclerosis (ALS1). Superoxides superoxide dismutase 1 Homo sapiens
4 Superoxide exposure via paraquat initiated the formation of SOD1 trimers in untransfected SH-SY5Y cells and increased the aggregation propensity of G85R in HEK293FT. Superoxides superoxide dismutase 1 Homo sapiens
5 These data show the kinetic formation of aberrant SOD1 subsets implicated in ALS1 and indicate that superoxide substrate may initiate its radical polymerization. Superoxides superoxide dismutase 1 Homo sapiens