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http://purl.uniprot.org/citations/22817985http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/22817985http://www.w3.org/2000/01/rdf-schema#comment"The Helicobacter pylori type IV secretion effector CagA is a major bacterial virulence determinant and critical for gastric carcinogenesis. Upon delivery into gastric epithelial cells, CagA localizes to the inner face of the plasma membrane, where it acts as a pathogenic scaffold/hub that promiscuously recruits host proteins to potentiate oncogenic signaling. We find that CagA comprises a structured N-terminal region and an intrinsically disordered C-terminal region that directs versatile protein interactions. X-ray crystallographic analysis of the N-terminal CagA fragment (residues 1-876) revealed that the region has a structure comprised of three discrete domains. Domain I constitutes a mobile CagA N terminus, while Domain II tethers CagA to the plasma membrane by interacting with membrane phosphatidylserine. Domain III interacts intramolecularly with the intrinsically disordered C-terminal region, and this interaction potentiates the pathogenic scaffold/hub function of CagA. The present work provides a tertiary-structural basis for the pathophysiological/oncogenic action of H. pylori CagA."xsd:string
http://purl.uniprot.org/citations/22817985http://purl.org/dc/terms/identifier"doi:10.1016/j.chom.2012.05.010"xsd:string
http://purl.uniprot.org/citations/22817985http://purl.uniprot.org/core/author"Hayashi T."xsd:string
http://purl.uniprot.org/citations/22817985http://purl.uniprot.org/core/author"Inagaki F."xsd:string
http://purl.uniprot.org/citations/22817985http://purl.uniprot.org/core/author"Senda T."xsd:string
http://purl.uniprot.org/citations/22817985http://purl.uniprot.org/core/author"Shimizu T."xsd:string
http://purl.uniprot.org/citations/22817985http://purl.uniprot.org/core/author"Senda M."xsd:string
http://purl.uniprot.org/citations/22817985http://purl.uniprot.org/core/author"Noda N.N."xsd:string
http://purl.uniprot.org/citations/22817985http://purl.uniprot.org/core/author"Kumeta H."xsd:string
http://purl.uniprot.org/citations/22817985http://purl.uniprot.org/core/author"Morohashi H."xsd:string
http://purl.uniprot.org/citations/22817985http://purl.uniprot.org/core/author"Hatakeyama M."xsd:string
http://purl.uniprot.org/citations/22817985http://purl.uniprot.org/core/author"Higashi H."xsd:string
http://purl.uniprot.org/citations/22817985http://purl.uniprot.org/core/author"Venugopalan N."xsd:string
http://purl.uniprot.org/citations/22817985http://purl.uniprot.org/core/author"Horio M."xsd:string
http://purl.uniprot.org/citations/22817985http://purl.uniprot.org/core/author"Kashiba Y."xsd:string
http://purl.uniprot.org/citations/22817985http://purl.uniprot.org/core/author"Nagase L."xsd:string
http://purl.uniprot.org/citations/22817985http://purl.uniprot.org/core/author"Sasaya D."xsd:string
http://purl.uniprot.org/citations/22817985http://purl.uniprot.org/core/date"2012"xsd:gYear
http://purl.uniprot.org/citations/22817985http://purl.uniprot.org/core/name"Cell Host Microbe"xsd:string
http://purl.uniprot.org/citations/22817985http://purl.uniprot.org/core/pages"20-33"xsd:string
http://purl.uniprot.org/citations/22817985http://purl.uniprot.org/core/title"Tertiary structure-function analysis reveals the pathogenic signaling potentiation mechanism of Helicobacter pylori oncogenic effector CagA."xsd:string
http://purl.uniprot.org/citations/22817985http://purl.uniprot.org/core/volume"12"xsd:string
http://purl.uniprot.org/citations/22817985http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/22817985
http://purl.uniprot.org/citations/22817985http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/22817985