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

The extracellular A-loop of dual oxidases affects the specificity of reactive oxygen species release.

The Journal of biological chemistry - 6 Mar 2015

Ueyama Takehiko, Sakuma Megumi, Ninoyu Yuzuru, Hamada Takeshi, Dupuy Corinne, Geiszt Miklós, Leto Thomas L, Saito Naoaki

Abstract excerpt

NADPH oxidase (Nox) family proteins produce superoxide (O2 (⨪)) directly by transferring an electron to molecular oxygen. Dual oxidases (Duoxes) also produce an O2 (⨪) intermediate, although the final species secreted by mature Duoxes is H2O2, suggesting that intramolecular O2 (⨪) dismutation or...

Read the complete abstract on PubMed

Topics

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

Share to Dual Oxidases
Share to Glycosylation
Share to Hydrogen Peroxide

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to NADPH Oxidases

Share to Oxygen

Share to Reactive Oxygen Species

Share to Superoxides

Share to Thyroid Hormones

Source

Open in PubMed Open full text

Identifiers

PMID: 25586178
DOI: 10.1074/jbc.M114.592717
PMCID: PMC4358283

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-25586178-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The extracellular A-loop of dual oxidases affects the specificity of reactive oxygen species release.PMID 25586178Read ↗

Conserved cysteine residues provide a protein-protein interaction surface in dual oxidase (DUOX) proteins.Semantic proximity Read ↗

Molecular evolution of the reactive oxygen-generating NADPH oxidase (Nox/Duox) family of enzymesSemantic proximity Read ↗

Nox Enzymes and New Thinking on Reactive Oxygen: A Double-Edged Sword RevisitedSemantic proximity Read ↗

Conformation of the N-Terminal Ectodomain Elicits Different Effects on DUOX Function: A Potential Impact on Congenital Hypothyroidism Caused by a H2O2 Production Defect.Semantic proximity Read ↗

Roles of DUOX-Mediated Hydrogen Peroxide in Metabolism, Host Defense, and SignalingSemantic proximity Read ↗

NOX5: from basic biology to signaling and disease.Semantic proximity Read ↗

The E-loop is involved in hydrogen peroxide formation by the NADPH oxidase Nox4.Semantic proximity Read ↗

NADPH oxidase 4 function as a hydrogen peroxide sensor.Semantic proximity Read ↗

The Nox Family of NAD(P)H Oxidases: Host Defense and BeyondSemantic proximity Read ↗

Dual oxidase-2 has an intrinsic Ca2+-dependent H2O2-generating activity.Semantic proximity Read ↗

Crucial role of two potential cytosolic regions of Nox2, 191TSSTKTIRRS200 and 484DESQANHFAVHHDEEKD500, on NADPH oxidase activation.Semantic proximity Read ↗

Tetraspanin is required for generation of reactive oxygen species by the dual oxidase system in Caenorhabditis elegans.Semantic proximity Read ↗

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