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Article

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

The Journal of biological chemistry - 8 Mar 2013

Meitzler Jennifer L, Hinde Sara, Bánfi Botond, Nauseef William M, Ortiz de Montellano Paul R

Abstract excerpt

Intramolecular disulfide bond formation is promoted in oxidizing extracellular and endoplasmic reticulum compartments and often contributes to protein stability and function. DUOX1 and DUOX2 are distinguished from other members of the NOX protein family by the presence of a unique extracellular N-terminal region. These peroxidase-like domains lack the conserved cysteines that confer structural stability to...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 23362256
DOI: 10.1074/jbc.M112.414797
PMCID: PMC3591624

Genes

DUOX1
DUOX2
DUOXA1

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.

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Conserved cysteine residues provide a protein-protein interaction surface in dual oxidase (DUOX) proteins.PMID 23362256Read ↗

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