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

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

PloS one - 1 Jan 2015

Peng Hu, Zhuang Yugang, Harbeck Mark C, He Donghong, Xie Lishi, Chen Weiguo

Abstract excerpt

Endothelial nitric oxide synthase (eNOS) is responsible for maintaining systemic blood pressure, vascular remodeling and angiogenesis. In addition to producing NO, eNOS can also generate superoxide (O2-.) in the absence of the cofactor tetrahydrobiopterin (BH4). Previous studies have shown that bovine eNOS serine 1179 (Serine 1177/human) phosphorylation critically modulates NO synthesis. However, the effect of...

Read the complete abstract on PubMed

Topics

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

Share to Biopterins
Share to Calmodulin
Share to Citrulline

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Electron Spin Resonance Spectroscopy

Share to Endothelium, Vascular

Share to Nitric Oxide Synthase Type III

Share to Superoxides

Source

Open in PubMed Open full text

Identifiers

PMID: 26560496
DOI: 10.1371/journal.pone.0142854
PMCID: PMC4641627

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Serine 1179 Phosphorylation of Endothelial Nitric Oxide Synthase Increases Superoxide Generation and Alters Cofactor Regulation.PMID 26560496Read ↗

The Characteristics and Regulatory Mechanisms of Superoxide Generation from eNOS Reductase Domain.Semantic proximity Read ↗

Endothelial NO synthase phosphorylated at SER635 produces NO without requiring intracellular calcium increase.Semantic proximity Read ↗

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

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

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

A pivotal role for tryptophan 447 in enzymatic coupling of human endothelial nitric oxide synthase (eNOS): effects on tetrahydrobiopterin-dependent catalysis and eNOS dimerization.Semantic proximity Read ↗

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

Enhanced electron flux and reduced calmodulin dissociation may explain "calcium-independent" eNOS activation by phosphorylation.Semantic proximity Read ↗

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

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

Molecular modeling and simulation of the human eNOS reductase domain, an enzyme involved in the release of vascular nitric oxide.Semantic proximity Read ↗

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