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http://purl.uniprot.org/citations/17196820http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17196820http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17196820http://www.w3.org/2000/01/rdf-schema#comment"The double-stranded (ds) RNA-activated protein kinase, PKR, has a key role in the innate immunity response to viral infection in higher eukaryotes. PKR contains an N-terminal dsRNA-binding domain and a C-terminal kinase domain. In the prevalent autoinhibition model for PKR activation, dsRNA binding induces a conformational change that leads to the release of the dsRNA-binding domain from the kinase, thus relieving the inhibition of the latent enzyme. Structural and biophysical data now favor a model whereby dsRNA principally functions to induce dimerization of PKR via the kinase domain. This dimerization model has implications for other PKR regulatory mechanisms and represents a new structural paradigm for control of protein kinase activity."xsd:string
http://purl.uniprot.org/citations/17196820http://purl.org/dc/terms/identifier"doi:10.1016/j.tibs.2006.12.003"xsd:string
http://purl.uniprot.org/citations/17196820http://purl.org/dc/terms/identifier"doi:10.1016/j.tibs.2006.12.003"xsd:string
http://purl.uniprot.org/citations/17196820http://purl.uniprot.org/core/author"Cole J.L."xsd:string
http://purl.uniprot.org/citations/17196820http://purl.uniprot.org/core/author"Cole J.L."xsd:string
http://purl.uniprot.org/citations/17196820http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17196820http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17196820http://purl.uniprot.org/core/name"Trends Biochem. Sci."xsd:string
http://purl.uniprot.org/citations/17196820http://purl.uniprot.org/core/name"Trends Biochem. Sci."xsd:string
http://purl.uniprot.org/citations/17196820http://purl.uniprot.org/core/pages"57-62"xsd:string
http://purl.uniprot.org/citations/17196820http://purl.uniprot.org/core/pages"57-62"xsd:string
http://purl.uniprot.org/citations/17196820http://purl.uniprot.org/core/title"Activation of PKR: an open and shut case?"xsd:string
http://purl.uniprot.org/citations/17196820http://purl.uniprot.org/core/title"Activation of PKR: an open and shut case?"xsd:string
http://purl.uniprot.org/citations/17196820http://purl.uniprot.org/core/volume"32"xsd:string
http://purl.uniprot.org/citations/17196820http://purl.uniprot.org/core/volume"32"xsd:string
http://purl.uniprot.org/citations/17196820http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17196820
http://purl.uniprot.org/citations/17196820http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17196820
http://purl.uniprot.org/citations/17196820http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/17196820
http://purl.uniprot.org/citations/17196820http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/17196820
http://purl.uniprot.org/uniprot/P19525http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/17196820
http://purl.uniprot.org/uniprot/#_P19525-citation-17196820http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17196820
http://purl.uniprot.org/uniprot/#_P11142-mappedCitation-17196820http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17196820
http://purl.uniprot.org/uniprot/#_Q15633-mappedCitation-17196820http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17196820