Ontology highlight
ABSTRACT:
SUBMITTER: Moen RJ
PROVIDER: S-EPMC4272649 | biostudies-literature | 2014 Oct
REPOSITORIES: biostudies-literature
Moen Rebecca J RJ Cornea Sinziana S Oseid Daniel E DE Binder Benjamin P BP Klein Jennifer C JC Thomas David D DD
Biochemical and biophysical research communications 20140926 3
We have examined the chemical and functional reversibility of oxidative modification in myosin. Redox regulation has emerged as a crucial modulator of protein function, with particular relevance to aging. We previously identified a single methionine residue in Dictyostelium discoideum (Dicty) myosin II (M394, near the myosin cardiomyopathy loop in the actin-binding interface) that is functionally sensitive to oxidation. We now show that oxidation of M394 is reversible by methionine sulfoxide red ...[more]