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Bridging the divide or deepening it?

Edgar Pick

Science (New York, N.Y.)

|July 15, 2006

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No abstract available in PubMed .

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Bridging the divide or deepening it?

Related Concept Videos

The molecular basis of Rac-GTP action-promoting binding of p67<sup>phox</sup> to Nox2 by disengaging the β hairpin from downstream residues.

p67<sup>phox</sup> -derived self-assembled peptides prevent Nox2 NADPH oxidase activation by an auto-inhibitory mechanism.

p67<sup>phox</sup> binds to a newly identified site in Nox2 following the disengagement of an intramolecular bond-Canaan sighted?

Cell-Free NADPH Oxidase Activation Assays: A Triumph of Reductionism.

Using Synthetic Peptides for Exploring Protein-Protein Interactions in the Assembly of the NADPH Oxidase Complex.

Binding of p67<sup>phox</sup> to Nox2 is stabilized by disulfide bonds between cysteines in the <sup>369</sup> Cys-Gly-Cys<sup>371</sup> triad in Nox2 and in p67<sup>phox</sup>.

Related Experiment Videos

Bridging the divide or deepening it?

Related Concept Videos

Related Articles

The molecular basis of Rac-GTP action-promoting binding of p67<sup>phox</sup> to Nox2 by disengaging the β hairpin from downstream residues.

p67<sup>phox</sup> -derived self-assembled peptides prevent Nox2 NADPH oxidase activation by an auto-inhibitory mechanism.

p67<sup>phox</sup> binds to a newly identified site in Nox2 following the disengagement of an intramolecular bond-Canaan sighted?

Cell-Free NADPH Oxidase Activation Assays: A Triumph of Reductionism.

Using Synthetic Peptides for Exploring Protein-Protein Interactions in the Assembly of the NADPH Oxidase Complex.

Binding of p67<sup>phox</sup> to Nox2 is stabilized by disulfide bonds between cysteines in the <sup>369</sup> Cys-Gly-Cys<sup>371</sup> triad in Nox2 and in p67<sup>phox</sup>.