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Article

Identification of a conserved Rac-binding site on NADPH oxidases supports a direct GTPase regulatory mechanism.

The Journal of biological chemistry - 9 May 2008

Kao Yu-Ya, Gianni Davide, Bohl Benjamin, Taylor Ross M, Bokoch Gary M

Abstract excerpt

The NADPH oxidases (Noxs) are a family of superoxide-generating enzymes implicated in a variety of biological processes. Full activity of Nox1, -2, and -3 requires the action of a Rac GTPase. A direct regulatory interaction of Rac with Nox2 has been proposed as part of a two-step mechanism for regulating electron transfer during superoxide formation. Using truncation analysis of Rac binding to the cytoplasmic...

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Identifiers

PMID: 18347018
DOI: 10.1074/jbc.M801010200
PMCID: PMC2442356

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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.

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