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Review
. 2008 Jun 20;283(25):16961-5.
doi: 10.1074/jbc.R700045200. Epub 2008 Apr 17.

Biological roles for the NOX family NADPH oxidases

William M Nauseef  1
Affiliations
Review

Biological roles for the NOX family NADPH oxidases

William M Nauseef. J Biol Chem. .
No abstract available

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Figures

FIGURE 1.
FIGURE 1.
Assembly and activation of the phagocyte NADPH oxidase. In resting phagocytes, heterodimeric gp91phox-p22phox resides in the membrane, whereas the complex of p47phox-p67phox-p40phox is cytosolic. Agonist-triggered phosphorylation of the autoinhibitory domain of p47phox (series of small boxes) releases a conformational restriction, making interactive protein motifs, including the PX domain, Src homology 3 regions (SH3), and proline-rich regions (PRR), in p47phox accessible to associate at the membrane and to mediate oxidase assembly. See text for additional details.
FIGURE 2.
FIGURE 2.
Structural organization of NOX protein family members. There are four different formats for the structural organization of members of the NOX protein family depending on the nature of their activity (constitutive versus agonist-dependent), the requirement of p22phox, dependence on cytosolic cofactors, the presence of EF-hands, and dependence on calcium. Duox alone has an additional transmembrane domain with an extracellular domain with limited sequence homology to animal peroxidases (PRX).
See this image and copyright information in PMC

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