| http://purl.uniprot.org/citations/7938008 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/7938008 | http://www.w3.org/2000/01/rdf-schema#comment | "The NADPH oxidase responsible for generation of superoxide anion and related microbicidal oxidants by phagocytes is assembled from at least five distinct proteins. Two are cytosolic components (p47-phox and p67-phox) that contain Src homology 3 (SH3) domains and associate with a transmembrane cytochrome b558 upon activation. We show here that the SH3 domains of p47-phox bind to proline-rich sequences in p47-phox itself and the p22-phox subunit of cytochrome b558. Binding of the p47-phox SH3 domains to p22-phox was abolished by a mutation in one proline-rich sequence (Pro156-->Gln) noted in a distinct form of chronic granulomatous disease and was inhibited by a short proline-rich synthetic peptide corresponding to residues 149-162 of p22-phox. Expression of mutated p22-phox did not restore oxidase activity to p22-phox-deficient B cells and did not enable p22-phox-dependent translocation of p47-phox to membranes in phorbol ester-stimulated cells. We also show that the cytosolic oxidase components associate with one another through the C-terminal SH3 domain of p67-phox and a proline-rich C-terminal sequence in p47-phox. These SH3 target sites conform to consensus features deduced from SH3 binding sites in other systems. We propose a model in which the oxidase complex assembles through a mechanism involving SH3 domains of both cytosolic proteins and cognate proline-rich targets in other oxidase components."xsd:string |
| http://purl.uniprot.org/citations/7938008 | http://purl.org/dc/terms/identifier | "doi:10.1073/pnas.91.22.10650"xsd:string |
| http://purl.uniprot.org/citations/7938008 | http://purl.uniprot.org/core/author | "Leto T.L."xsd:string |
| http://purl.uniprot.org/citations/7938008 | http://purl.uniprot.org/core/author | "Adams A.G."xsd:string |
| http://purl.uniprot.org/citations/7938008 | http://purl.uniprot.org/core/author | "de Mendez I."xsd:string |
| http://purl.uniprot.org/citations/7938008 | http://purl.uniprot.org/core/date | "1994"xsd:gYear |
| http://purl.uniprot.org/citations/7938008 | http://purl.uniprot.org/core/name | "Proc Natl Acad Sci U S A"xsd:string |
| http://purl.uniprot.org/citations/7938008 | http://purl.uniprot.org/core/pages | "10650-10654"xsd:string |
| http://purl.uniprot.org/citations/7938008 | http://purl.uniprot.org/core/title | "Assembly of the phagocyte NADPH oxidase: binding of Src homology 3 domains to proline-rich targets."xsd:string |
| http://purl.uniprot.org/citations/7938008 | http://purl.uniprot.org/core/volume | "91"xsd:string |
| http://purl.uniprot.org/citations/7938008 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/7938008 |
| http://purl.uniprot.org/citations/7938008 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/7938008 |
| http://purl.uniprot.org/uniprot/P13498#attribution-A29D99D4C3C56216E3B13E85A83300DE | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/7938008 |
| http://purl.uniprot.org/uniprot/P13498#attribution-E20CDF21CF69BD9CD1DC928F4C077894 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/7938008 |
| http://purl.uniprot.org/uniprot/P14598#attribution-689C98EB8FD717E653DCE4AE3944A41E | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/7938008 |
| http://purl.uniprot.org/uniprot/P14598#attribution-A29D99D4C3C56216E3B13E85A83300DE | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/7938008 |
| http://purl.uniprot.org/uniprot/P19878#attribution-689C98EB8FD717E653DCE4AE3944A41E | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/7938008 |