Ontology highlight
ABSTRACT:
OTHER RELATED OMICS DATASETS IN: PRJNA31257PRJNA176729
SUBMITTER: Sharat Vayttaden
PROVIDER: MODEL4780784080 | BioModels | 2005-01-01
REPOSITORIES: BioModels
Items per page: 1 - 5 of 11 |
The Journal of biological chemistry 19990701 29
Phosphorylation of neuronal nitric-oxide synthase (nNOS) by Ca2+/calmodulin (CaM)-dependent protein kinases (CaM kinases) including CaM kinase Ialpha (CaM-K Ialpha), CaM kinase IIalpha (CaM-K IIalpha), and CaM kinase IV (CaM-K IV), was studied. It was found that purified recombinant nNOS was phosphorylated by CaM-K Ialpha, CaM-K IIalpha, and CaM-K IV at Ser847 in vitro. Replacement of Ser847 with Ala (S847A) prevented phosphorylation by CaM kinases. Phosphorylated recombinant wild-type nNOS at S ...[more]