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http://purl.uniprot.org/citations/21235237http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21235237http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21235237http://www.w3.org/2000/01/rdf-schema#comment"Bacterial pathogens secrete effectors into their hosts that subvert host defenses and redirect host processes. EspG is a type three secretion effector with a disputed function that is found in enteropathogenic Escherichia coli. Here we show that EspG is structurally similar to VirA, a Shigella virulence factor; EspG has a large, conserved pocket on its surface; EspG binds directly to the amino-terminal inhibitory domain of human p21-activated kinase (PAK); and mutations to conserved residues in the surface pocket disrupt the interaction with PAK."xsd:string
http://purl.uniprot.org/citations/21235237http://purl.org/dc/terms/identifier"doi:10.1021/bi1020138"xsd:string
http://purl.uniprot.org/citations/21235237http://purl.org/dc/terms/identifier"doi:10.1021/bi1020138"xsd:string
http://purl.uniprot.org/citations/21235237http://purl.uniprot.org/core/author"Spiller B.W."xsd:string
http://purl.uniprot.org/citations/21235237http://purl.uniprot.org/core/author"Spiller B.W."xsd:string
http://purl.uniprot.org/citations/21235237http://purl.uniprot.org/core/author"Germane K.L."xsd:string
http://purl.uniprot.org/citations/21235237http://purl.uniprot.org/core/author"Germane K.L."xsd:string
http://purl.uniprot.org/citations/21235237http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/21235237http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/21235237http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/21235237http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/21235237http://purl.uniprot.org/core/pages"917-919"xsd:string
http://purl.uniprot.org/citations/21235237http://purl.uniprot.org/core/pages"917-919"xsd:string
http://purl.uniprot.org/citations/21235237http://purl.uniprot.org/core/title"Structural and functional studies indicate that the EPEC effector, EspG, directly binds p21-activated kinase."xsd:string
http://purl.uniprot.org/citations/21235237http://purl.uniprot.org/core/title"Structural and functional studies indicate that the EPEC effector, EspG, directly binds p21-activated kinase."xsd:string
http://purl.uniprot.org/citations/21235237http://purl.uniprot.org/core/volume"50"xsd:string
http://purl.uniprot.org/citations/21235237http://purl.uniprot.org/core/volume"50"xsd:string
http://purl.uniprot.org/citations/21235237http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/21235237
http://purl.uniprot.org/citations/21235237http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/21235237
http://purl.uniprot.org/citations/21235237http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/21235237
http://purl.uniprot.org/citations/21235237http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/21235237
http://purl.uniprot.org/uniprot/B7UMC8http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/21235237
http://purl.uniprot.org/uniprot/#_B7UMC8-citation-21235237http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/21235237