1989
DOI: 10.1073/pnas.86.18.7195
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Cloning of the cDNA and functional expression of the 47-kilodalton cytosolic component of human neutrophil respiratory burst oxidase.

Abstract: 9563Correction. In the article "Cloning of the cDNA and functional expression of the 47-kilodalton cytosolic component of human neutrophil respiratory burst oxidase"

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Cited by 287 publications
(145 citation statements)
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References 38 publications
(38 reference statements)
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“…The oxidase subunit p47 phox contains several serine residues clustered within the carboxyl terminus that form potential protein kinase C phosphorylation sites (29). Native p47 phox is a highly basic protein that undergoes stepwise charge shifts with successive phosphorylation events (29,30).…”
Section: Discussionmentioning
confidence: 99%
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“…The oxidase subunit p47 phox contains several serine residues clustered within the carboxyl terminus that form potential protein kinase C phosphorylation sites (29). Native p47 phox is a highly basic protein that undergoes stepwise charge shifts with successive phosphorylation events (29,30).…”
Section: Discussionmentioning
confidence: 99%
“…Native p47 phox is a highly basic protein that undergoes stepwise charge shifts with successive phosphorylation events (29,30). In neutrophils, p47 phox phosphorylation is thought to be a prerequisite for its interaction with p22 phox and the formation of a functional oxidase complex (15,16).…”
Section: Discussionmentioning
confidence: 99%
“…The ORF of human p47 phox cDNA (17,18) was inserted into the MFGS retrovirus vector (Cell Genesys, Foster City, CA) (8-10). MFGS-p47 phox plasmid was transfected into the amphotropic envelope packaging line -CRIP, and a vector-producing clone was selected (8)(9)(10).…”
mentioning
confidence: 99%
“…Cloning of the various components of the oxidase demonstrated that they contain SH3 domains and proline-rich regions that can interact with each other and are important in the assembly of the catalytically active oxidase at the plasma membrane (25)(26)(27). It was suggested that part of the activation process involves changes in the conformation of the various components, revealing new binding sites.…”
Section: Discussionmentioning
confidence: 99%
“…Phosphorylation or detergents such as SDS could provide the means for such conformation changes (28). Since (17,29,30). However, using various methodologies, several groups showed that PKC, cAMP protein kinase (PKA), the mitogen-activated protein kinases p38MAPK and ERK2, and the p21-activated kinases (PAKs) could phosphorylate p47Phox in vitro (10,(31)(32)(33).…”
Section: Discussionmentioning
confidence: 99%