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http://purl.uniprot.org/citations/11884510http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11884510http://www.w3.org/2000/01/rdf-schema#comment"The PX domain, which until recently was an orphan domain, has emerged as the latest member of the phosphoinositide-binding module superfamily. Structural studies have revealed that it has a novel fold and identified key residues that interact with the bound phosphoinositide, enabling some prediction of phosphoinositide-binding specificity. Specificity for PtdIns(3)P appears to be the most common, and several proteins containing PX domains localise to PtdIns(3)P-rich endosomal and vacuolar structures through their PX domains: these include the yeast t-SNARE Vam7p, mammalian sorting nexins (involved in membrane trafficking events) and the Ser/Thr kinase CISK, which is implicated in cell survival. Additionally, phosphoinositide binding to the PX domains of p40(phox) and p47(phox) appears to play a critical role in the active assembly of the neutrophil oxidase complex."xsd:string
http://purl.uniprot.org/citations/11884510http://purl.org/dc/terms/identifier"doi:10.1242/jcs.115.6.1099"xsd:string
http://purl.uniprot.org/citations/11884510http://purl.uniprot.org/core/author"Andrews S."xsd:string
http://purl.uniprot.org/citations/11884510http://purl.uniprot.org/core/author"Hawkins P.T."xsd:string
http://purl.uniprot.org/citations/11884510http://purl.uniprot.org/core/author"Stephens L.R."xsd:string
http://purl.uniprot.org/citations/11884510http://purl.uniprot.org/core/author"Ellson C.D."xsd:string
http://purl.uniprot.org/citations/11884510http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/11884510http://purl.uniprot.org/core/name"J Cell Sci"xsd:string
http://purl.uniprot.org/citations/11884510http://purl.uniprot.org/core/pages"1099-1105"xsd:string
http://purl.uniprot.org/citations/11884510http://purl.uniprot.org/core/title"The PX domain: a new phosphoinositide-binding module."xsd:string
http://purl.uniprot.org/citations/11884510http://purl.uniprot.org/core/volume"115"xsd:string
http://purl.uniprot.org/citations/11884510http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11884510
http://purl.uniprot.org/citations/11884510http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/11884510
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http://purl.uniprot.org/uniprot/#_Q01846-mappedCitation-11884510http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/11884510
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http://purl.uniprot.org/uniprot/#_Q07528-mappedCitation-11884510http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/11884510
http://purl.uniprot.org/uniprot/#_P29366-mappedCitation-11884510http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/11884510
http://purl.uniprot.org/uniprot/#_P32873-mappedCitation-11884510http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/11884510
http://purl.uniprot.org/uniprot/#_P32912-mappedCitation-11884510http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/11884510
http://purl.uniprot.org/uniprot/#_P32913-mappedCitation-11884510http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/11884510
http://purl.uniprot.org/uniprot/#_P36126-mappedCitation-11884510http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/11884510