Ontology highlight
ABSTRACT:
SUBMITTER: Furukawa Y
PROVIDER: S-EPMC4759189 | biostudies-literature | 2016 Feb
REPOSITORIES: biostudies-literature
Furukawa Yoshiaki Y Anzai Itsuki I Akiyama Shuji S Imai Mizue M Cruz Fatima Joy C FJ Saio Tomohide T Nagasawa Kenichi K Nomura Takao T Ishimori Koichiro K
The Journal of biological chemistry 20151222 8
Misfolding of Cu,Zn-superoxide dismutase (SOD1) is a pathological change in the familial form of amyotrophic lateral sclerosis caused by mutations in the SOD1 gene. SOD1 is an enzyme that matures through the binding of copper and zinc ions and the formation of an intramolecular disulfide bond. Pathogenic mutations are proposed to retard the post-translational maturation, decrease the structural stability, and hence trigger the misfolding of SOD1 proteins. Despite this, a misfolded and potentiall ...[more]