Structural organization of the neutrophil NADPH oxidase: phosphorylation and translocation during priming and activation

@article{Sheppard2005StructuralOO,
  title={Structural organization of the neutrophil NADPH oxidase: phosphorylation and translocation during priming and activation},
  author={Forest R. Sheppard and Marguerite R. Kelher and Ernest E. Moore and Nathan J. D. McLaughlin and Anirban Banerjee and Christopher C Silliman},
  journal={Journal of Leukocyte Biology},
  year={2005},
  volume={78}
}
The reduced nicotinamide adenine dinucleotide phosphate (NADPH) oxidase is part of the microbicidal arsenal used by human polymorphonuclear neutrophils (PMNs) to eradicate invading pathogens. The production of a superoxide anion (O2–) into the phagolysosome is the precursor for the generation of more potent products, such as hydrogen peroxide and hypochlorite. However, this production of O2– is dependent on translocation of the oxidase subunits, including gp91phox, p22phox, p47phox, p67phox… 

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