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http://purl.uniprot.org/citations/11081636http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11081636http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11081636http://www.w3.org/2000/01/rdf-schema#comment"The Listeria monocytogenes surface protein InlB promotes bacterial entry into mammalian cells. Here, we identify a cellular surface receptor required for InlB-mediated entry. Treatment of mammalian cells with InlB protein or infection with L. monocytogenes induces rapid tyrosine phosphorylation of Met, a receptor tyrosine kinase (RTK) for which the only known ligand is Hepatocyte Growth Factor (HGF). Like HGF, InlB binds to the extracellular domain of Met and induces "scattering" of epithelial cells. Experiments with Met-positive and Met-deficient cell lines demonstrate that Met is required for InlB-dependent entry of L. monocytogenes. InlB is a novel Met agonist that induces bacterial entry through exploitation of a host RTK pathway."xsd:string
http://purl.uniprot.org/citations/11081636http://purl.org/dc/terms/identifier"doi:10.1016/s0092-8674(00)00141-0"xsd:string
http://purl.uniprot.org/citations/11081636http://purl.org/dc/terms/identifier"doi:10.1016/s0092-8674(00)00141-0"xsd:string
http://purl.uniprot.org/citations/11081636http://purl.uniprot.org/core/author"Shen Y."xsd:string
http://purl.uniprot.org/citations/11081636http://purl.uniprot.org/core/author"Shen Y."xsd:string
http://purl.uniprot.org/citations/11081636http://purl.uniprot.org/core/author"Park M."xsd:string
http://purl.uniprot.org/citations/11081636http://purl.uniprot.org/core/author"Park M."xsd:string
http://purl.uniprot.org/citations/11081636http://purl.uniprot.org/core/author"Ireton K."xsd:string
http://purl.uniprot.org/citations/11081636http://purl.uniprot.org/core/author"Ireton K."xsd:string
http://purl.uniprot.org/citations/11081636http://purl.uniprot.org/core/author"Naujokas M."xsd:string
http://purl.uniprot.org/citations/11081636http://purl.uniprot.org/core/author"Naujokas M."xsd:string
http://purl.uniprot.org/citations/11081636http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/11081636http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/11081636http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/11081636http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/11081636http://purl.uniprot.org/core/pages"501-510"xsd:string
http://purl.uniprot.org/citations/11081636http://purl.uniprot.org/core/pages"501-510"xsd:string
http://purl.uniprot.org/citations/11081636http://purl.uniprot.org/core/title"InIB-dependent internalization of Listeria is mediated by the Met receptor tyrosine kinase."xsd:string
http://purl.uniprot.org/citations/11081636http://purl.uniprot.org/core/title"InIB-dependent internalization of Listeria is mediated by the Met receptor tyrosine kinase."xsd:string
http://purl.uniprot.org/citations/11081636http://purl.uniprot.org/core/volume"103"xsd:string
http://purl.uniprot.org/citations/11081636http://purl.uniprot.org/core/volume"103"xsd:string
http://purl.uniprot.org/citations/11081636http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11081636
http://purl.uniprot.org/citations/11081636http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11081636