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

Regulation of multimers via truncated isoforms: a novel mechanism to control nitric-oxide signaling.

Genes & development - 1 Aug 2004

Stasiv Yuri, Kuzin Boris, Regulski Michael, Tully Tim, Enikolopov Grigori

Abstract excerpt

Nitric oxide (NO) is an essential regulator of Drosophila development and physiology. We describe a novel mode of regulation of NO synthase (NOS) function that uses endogenously produced truncated protein isoforms of Drosophila NOS (DNOS). These isoforms inhibit NOS enzymatic activity in vitro and in vivo, reflecting their ability to form complexes with the full-length DNOS protein (DNOS1). Truncated isoforms...

Read the complete abstract on PubMed

Topics

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

Share to Bromodeoxyuridine
Share to Eye
Share to Free Radical Scavengers

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Nitric Oxide

Share to Nitric Oxide Synthase

Share to Retinoblastoma Protein

Share to S Phase

Source

Open in PubMed Open full text

Identifiers

PMID: 15256486
DOI: 10.1101/gad.298004
PMCID: PMC517402

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

Regulation of multimers via truncated isoforms: a novel mechanism to control nitric-oxide signaling.PMID 15256486Read ↗

iNOS is not responsible for nitrosylation of RyR1 in mdx mice with truncated dystrophinSemantic proximity Read ↗

RNA diversity has profound effects on the translation of neuronal nitric oxide synthase.Semantic proximity Read ↗

Structural diversity of neuronal nitric oxide synthase mRNA in the nervous system.Semantic proximity Read ↗

Nitric oxide-mediated posttranslational modifications control neurotransmitter release by modulating complexin farnesylation and enhancing its clamping ability.Semantic proximity Read ↗

mdx muscle pathology is independent of nNOS perturbationSemantic proximity Read ↗

S-sulfenylation-mediated inhibition of the GSNOR1 activity regulates ovule development in Arabidopsis.Semantic proximity Read ↗

S-Nitrosylation of the epidermal growth factor receptor: a regulatory mechanism of receptor tyrosine kinase activity.Semantic proximity Read ↗

Nitric oxide repression of Nanog promotes mouse embryonic stem cell differentiation.Semantic proximity Read ↗

Versatile regulation of neuronal nitric oxide synthase by specific regions of its C-terminal tail.Semantic proximity Read ↗

Bacterial Nitric-oxide Synthases Operate without a Dedicated Redox PartnerSemantic proximity Read ↗

Use of chimeric forms of neuronal nitric-oxide synthase as dominant negative mutants.Semantic proximity Read ↗

Identification of a plant nitric oxide synthase gene involved in hormonal signaling.Semantic proximity Read ↗

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