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

Mutation of N-myristoylation site converts endothelial cell nitric oxide synthase from a membrane to a cytosolic protein.

Circulation research - 1 Apr 1993

Sessa W C, Barber C M, Lynch K R

Abstract excerpt

Endothelial cell nitric oxide synthase (ECNOS) is a membrane-associated enzyme that generates endothelium-derived relaxing factor/nitric oxide (EDRF/NO) from L-arginine. We have suggested, from the cloning of the bovine ECNOS cDNA, that the presence of an N-myristoylation consensus sequence may impart its membrane localization since cytosolic forms of NOS do not contain such domains. To test the hypothesis that...

Read the complete abstract on PubMed

Topics

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

Share to Base Sequence
Share to Cell Membrane
Share to Cytosol

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Endothelium, Vascular

Share to Molecular Probes

Share to Molecular Sequence Data

Share to Mutation

Share to Tissue Distribution

Source

Identifiers

PMID: 7680289
DOI: 10.1161/01.res.72.4.921

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mutation of N-myristoylation site converts endothelial cell nitric oxide synthase from a membrane to a cytosolic protein.PMID 7680289Read ↗

Myristoylation of endothelial cell nitric oxide synthase is important for extracellular release of nitric oxide.Semantic proximity Read ↗

N-terminal palmitoylation within the appropriate amino acid environment conveys on NOS2 the ability to progress along the intracellular sorting pathways.Semantic proximity Read ↗

Palmitoylation of inducible nitric-oxide synthase at Cys-3 is required for proper intracellular traffic and nitric oxide synthesis.Semantic proximity Read ↗

S-nitrosylation inhibits pannexin 1 channel function.Semantic proximity Read ↗

Subcellular targeting and agonist-induced site-specific phosphorylation of endothelial nitric-oxide synthase.Semantic proximity Read ↗

S-glutathionylation uncouples eNOS and regulates its cellular and vascular function.Semantic proximity Read ↗

Dual acylation of PDE2A splice variant 3: targeting to synaptic membranes.Semantic proximity Read ↗

Nitric Oxide and Posttranslational Modification of the Vascular ProteomeSemantic proximity Read ↗

Nitric oxide synthase (NOS2) mutation in Dahl/Rapp rats decreases enzyme stability.Semantic proximity Read ↗

Argininosuccinate Synthetase is Reversibly Inactivated by S-Nitrosylation in Vitro and in VivoSemantic proximity Read ↗

Cysteine-674 of the sarco/endoplasmic reticulum calcium ATPase is required for the inhibition of cell migration by nitric oxide.Semantic proximity Read ↗

Targeting of a G alpha subunit (Gi1 alpha) and c-Src tyrosine kinase to caveolae membranes: clarifying the role of N-myristoylation.Semantic proximity Read ↗

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