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

Characterization of a novel posttranslational modification in neuronal nitric oxide synthase by small ubiquitin-related modifier-1.

Biochimica et biophysica acta - 1 Jul 2011

Watanabe Masatomo, Itoh Kouichi

Abstract excerpt

The multifaceted functions of nitric oxide (NO) in the CNS are defined by the activity of neuronal NO synathase (nNOS). The activities of nNOS are modulated by posttranslational modifications, such as phosphorylation and ubiquitination, but whether it is modified by small ubiquitin-related modifier (SUMO) remains unknown. The aim of this study was to elucidate whether nNOS is posttranslationally modified by SUMO...

Read the complete abstract on PubMed

Topics

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

Share to Cysteine Endopeptidases
Share to Endopeptidases
Share to Nitric Oxide Synthase Type I

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization

Share to SUMO-1 Protein

Share to Sumoylation

Share to Ubiquitin-Conjugating Enzyme UBC9

Share to Ubiquitin-Conjugating Enzymes

Source

Identifiers

PMID: 21545853
DOI: 10.1016/j.bbapap.2011.04.006

Genes

SENP1
SENP2

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Characterization of a novel posttranslational modification in neuronal nitric oxide synthase by small ubiquitin-related modifier-1.PMID 21545853Read ↗

Nitric oxide destabilizes Pias3 and regulates sumoylation.Semantic proximity Read ↗

RNF4—A Paradigm for SUMOylation‐Mediated UbiquitinationSemantic proximity Read ↗

SUMO proteomics to decipher the SUMO‐modified proteome regulated by various diseasesSemantic proximity Read ↗

Progress of small ubiquitin-related modifiers in kidney diseasesSemantic proximity Read ↗

The post-translational modification, SUMOylation, and cancer (Review)Semantic proximity Read ↗

SUMO : A new perspective to decipher fibrosisSemantic proximity Read ↗

SUMOylation as a Therapeutic Target for Myocardial InfarctionSemantic proximity Read ↗

SUMO--a post-translational modification with therapeutic potential?Semantic proximity Read ↗

Enhanced SUMOylation and SENP-1 protein levels following oxygen and glucose deprivation in neurones.Semantic proximity Read ↗

Ubiquitous regulation of cerebrovascular diseases by ubiquitin‐modifying enzymesSemantic proximity Read ↗

Progress in the Discovery of Small Molecule Modulators of DeSUMOylationSemantic proximity Read ↗

Post-translational modification by SUMOSemantic proximity Read ↗

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