We are analyzing https://link.springer.com/article/10.1007/s00418-004-0679-8.

Title:
Assembly of the phagocyte NADPH oxidase | Histochemistry and Cell Biology
Description:
Stimulated phagocytes undergo a burst in respiration whereby molecular oxygen is converted to superoxide anion through the action of an NADPH-dependent oxidase. The multicomponent phagocyte oxidase is unassembled and inactive in resting cells but assembles at the plasma or phagosomal membrane upon phagocyte activation. Oxidase components include flavocytochrome b558, an integral membrane heterodimer comprised of gp91phox and p22phox, and three cytosolic proteins, p47phox, p67phox, and Rac1 or Rac2, depending on the species and phagocytic cell. In a sense, the phagocyte oxidase is spatially regulated, with critical elements segregated in the membrane and cytosol but ready to undergo nearly immediate assembly and activation in response to stimulation. To achieve such spatial regulation, the individual components in the resting phagocyte adopt conformations that mask potentially interactive structural domains that might mediate productive intermolecular associations and oxidase assembly. In response to stimulation, post-translational modifications of the oxidase components release these constraints and thereby render potential interfaces accessible and interactive, resulting in translocation of the cytosolic elements to the membrane where the functional oxidase is assembled and active. This review summarizes data on the structural features of the phagocyte oxidase components and on the agonist-dependent conformational rearrangements that contribute to oxidase assembly and activation.
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Keywords {🔍}

google, scholar, pubmed, cas, oxidase, article, nadph, pphox, biol, activation, chem, human, neutrophil, rac, phagocyte, cell, disease, nauseef, cytosolic, granulomatous, assembly, protein, neutrophils, chronic, biochem, domain, cytochrome, translocation, complex, membrane, activity, sci, blood, sumimoto, interaction, curnutte, system, burst, components, proteins, respiratory, flavocytochrome, regulation, cellfree, proc, clin, jesaitis, domains, phosphorylation, natl,

Topics {✒️}

neutrophil-activating peptide 1/interleukin 8 receptors month download article/chapter arachidonate-activatable superoxide-generating system tpr-mediated protein–protein interactions rac/rho gtp-binding proteins gdp/gtp exchange proteins phagocyte nadph-oxidase flavocytochrome b558 trisulfopyrenyl-wheat germ agglutinin small gtp-binding protein hematopoietic-specifc rho gtpase c-terminally truncated forms cytokine-mediated bax deficiency superoxide-generating nadph oxidase superoxide-producing phagocyte oxidase agonist-dependent conformational rearrangements allen l-ah active n-terminal region human neutrophil flavocytochrome b558 johnston rb jr gene encoding gp91-phox nadph-dependent superoxide production flavocytochrome b-245 b-chain anionic amphiphile-independent activation cytosolic proteins p47-phox chronic granulomatous disease full article pdf p67-phox requires interaction nadph oxidase subunits neutrophil-activating peptide 2 p40-p47-p67phox complex c-terminal end protein–protein interactions privacy choices/manage cookies p67phox-p47phox fusion protein neutrophil respiratory oxidase autosomal recessive forms fatal granulomatous disease respiratory burst oxidase neutrophil nadph oxidase cell biology aims phagocyte nadph oxidase secretion-incompetent variant van berkel wjh respiratory burst enzyme membrane recombinant proteins nadph-dependent oxidase cell-free system dominant negative mutation nadph oxidase complex nadph oxidase assembly

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         description:Stimulated phagocytes undergo a burst in respiration whereby molecular oxygen is converted to superoxide anion through the action of an NADPH-dependent oxidase. The multicomponent phagocyte oxidase is unassembled and inactive in resting cells but assembles at the plasma or phagosomal membrane upon phagocyte activation. Oxidase components include flavocytochrome b558, an integral membrane heterodimer comprised of gp91phox and p22phox, and three cytosolic proteins, p47phox, p67phox, and Rac1 or Rac2, depending on the species and phagocytic cell. In a sense, the phagocyte oxidase is spatially regulated, with critical elements segregated in the membrane and cytosol but ready to undergo nearly immediate assembly and activation in response to stimulation. To achieve such spatial regulation, the individual components in the resting phagocyte adopt conformations that mask potentially interactive structural domains that might mediate productive intermolecular associations and oxidase assembly. In response to stimulation, post-translational modifications of the oxidase components release these constraints and thereby render potential interfaces accessible and interactive, resulting in translocation of the cytosolic elements to the membrane where the functional oxidase is assembled and active. This review summarizes data on the structural features of the phagocyte oxidase components and on the agonist-dependent conformational rearrangements that contribute to oxidase assembly and activation.
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            Oxidase assembly
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            Biochemistry
            Developmental Biology
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      headline:Assembly of the phagocyte NADPH oxidase
      description:Stimulated phagocytes undergo a burst in respiration whereby molecular oxygen is converted to superoxide anion through the action of an NADPH-dependent oxidase. The multicomponent phagocyte oxidase is unassembled and inactive in resting cells but assembles at the plasma or phagosomal membrane upon phagocyte activation. Oxidase components include flavocytochrome b558, an integral membrane heterodimer comprised of gp91phox and p22phox, and three cytosolic proteins, p47phox, p67phox, and Rac1 or Rac2, depending on the species and phagocytic cell. In a sense, the phagocyte oxidase is spatially regulated, with critical elements segregated in the membrane and cytosol but ready to undergo nearly immediate assembly and activation in response to stimulation. To achieve such spatial regulation, the individual components in the resting phagocyte adopt conformations that mask potentially interactive structural domains that might mediate productive intermolecular associations and oxidase assembly. In response to stimulation, post-translational modifications of the oxidase components release these constraints and thereby render potential interfaces accessible and interactive, resulting in translocation of the cytosolic elements to the membrane where the functional oxidase is assembled and active. This review summarizes data on the structural features of the phagocyte oxidase components and on the agonist-dependent conformational rearrangements that contribute to oxidase assembly and activation.
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         Respiratory burst
         Neutrophils
         Phagocytes
         Oxidase assembly
         Biomedicine
         general
         Cell Biology
         Biochemistry
         Developmental Biology
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