Ontology highlight
ABSTRACT:
SUBMITTER: Salerno JC
PROVIDER: S-EPMC4166121 | biostudies-literature | 2014 Sep
REPOSITORIES: biostudies-literature
Salerno John C JC Ghosh Dipak K DK Razdan Raj R Helms Katy A KA Brown Christopher C CC McMurry Jonathan L JL Rye Emily A EA Chrestensen Carol A CA
Bioscience reports 20140917 5
eNOS (endothelial nitric oxide synthase) contains a MAPK (mitogen-activated protein kinase)-binding site associated with a major eNOS control element. Purified ERK (extracellular-signal-regulated kinase) phosphorylates eNOS with a stoichiometry of 2-3 phosphates per eNOS monomer. Phosphorylation decreases NO synthesis and cytochrome c reductase activity. Three sites of phosphorylation were detected by MS. All sites matched the SP and TP MAPK (mitogen-activated protein kinase) phosphorylation mot ...[more]