Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Endothelial NO synthase phosphorylated at SER635 produces NO without requiring intracellular calcium increase.

Free radical biology & medicine - 1 Oct 2003

Boo Yong Chool, Sorescu George P, Bauer Philip M, Fulton David, Kemp Bruce E, Harrison David G, Sessa William C, Jo Hanjoong

Abstract excerpt

Shear stress stimulates NO production involving the Ca2+-independent mechanisms in endothelial cells. We have shown that exposure of bovine aortic endothelial cells (BAEC) to shear stress stimulates phosphorylation of eNOS at S635 and S1179 by the protein kinase A- (PKA-) dependent mechanisms. We examined whether phosphorylation of S635 of eNOS induced by PKA stimulates NO production in a calcium-independent...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Aorta, Thoracic
Share to Cyclic AMP-Dependent Protein Kinases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Endothelium, Vascular

Share to Intracellular Fluid

Share to Nitric Oxide

Share to Nitric Oxide Synthase

Share to Nitric Oxide Synthase Type III

Share to Phosphoserine

Source

Identifiers

PMID: 14583337
DOI: 10.1016/s0891-5849(03)00397-6

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Endothelial NO synthase phosphorylated at SER635 produces NO without requiring intracellular calcium increase.PMID 14583337Read ↗

Serine 1179 Phosphorylation of Endothelial Nitric Oxide Synthase Increases Superoxide Generation and Alters Cofactor Regulation.Semantic proximity Read ↗

Inhibition of MEK/ERK1/2 signalling alters endothelial nitric oxide synthase activity in an agonist-dependent manner.Semantic proximity Read ↗

The N-terminal portion of autoinhibitory element modulates human endothelial nitric-oxide synthase activity through coordinated controls of phosphorylation at Thr495 and Ser1177.Semantic proximity Read ↗

AMP-activated protein kinase functionally phosphorylates endothelial nitric oxide synthase Ser633.Semantic proximity Read ↗

Role of eNOS phosphorylation at Ser-116 in regulation of eNOS activity in endothelial cells.Semantic proximity Read ↗

Functional reconstitution of endothelial nitric oxide synthase reveals the importance of serine 1179 in endothelium-dependent vasomotion.Semantic proximity Read ↗

Biochemical consequences of the NOS3 Glu298Asp variation in human endothelium: altered caveolar localization and impaired response to shear.Semantic proximity Read ↗

The phosphorylation state of eNOS modulates vascular reactivity and outcome of cerebral ischemia in vivo.Semantic proximity Read ↗

Gab1, SHP2, and protein kinase A are crucial for the activation of the endothelial NO synthase by fluid shear stress.Semantic proximity Read ↗

eNOS phosphorylation on serine 1176 affects insulin sensitivity and adiposity.Semantic proximity Read ↗

Regulation of endothelium-derived nitric oxide production by the protein kinase Akt.Semantic proximity Read ↗

Hyperglycemia inhibits endothelial nitric oxide synthase activity by posttranslational modification at the Akt site.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.