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http://purl.uniprot.org/citations/10195894http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10195894http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10195894http://www.w3.org/2000/01/rdf-schema#comment"IkappaB [inhibitor of nuclear factor kappaB (NF-kappaB)] kinase (IKK) phosphorylates IkappaB inhibitory proteins, causing their degradation and activation of transcription factor NF-kappaB, a master activator of inflammatory responses. IKK is composed of three subunits-IKKalpha and IKKbeta, which are highly similar protein kinases, and IKKgamma, a regulatory subunit. In mammalian cells, phosphorylation of two sites at the activation loop of IKKbeta was essential for activation of IKK by tumor necrosis factor and interleukin-1. Elimination of equivalent sites in IKKalpha, however, did not interfere with IKK activation. Thus, IKKbeta, not IKKalpha, is the target for proinflammatory stimuli. Once activated, IKKbeta autophosphorylated at a carboxyl-terminal serine cluster. Such phosphorylation decreased IKK activity and may prevent prolonged activation of the inflammatory response."xsd:string
http://purl.uniprot.org/citations/10195894http://purl.org/dc/terms/identifier"doi:10.1126/science.284.5412.309"xsd:string
http://purl.uniprot.org/citations/10195894http://purl.org/dc/terms/identifier"doi:10.1126/science.284.5412.309"xsd:string
http://purl.uniprot.org/citations/10195894http://purl.uniprot.org/core/author"Chen Y."xsd:string
http://purl.uniprot.org/citations/10195894http://purl.uniprot.org/core/author"Chen Y."xsd:string
http://purl.uniprot.org/citations/10195894http://purl.uniprot.org/core/author"Karin M."xsd:string
http://purl.uniprot.org/citations/10195894http://purl.uniprot.org/core/author"Karin M."xsd:string
http://purl.uniprot.org/citations/10195894http://purl.uniprot.org/core/author"Hayakawa M."xsd:string
http://purl.uniprot.org/citations/10195894http://purl.uniprot.org/core/author"Hayakawa M."xsd:string
http://purl.uniprot.org/citations/10195894http://purl.uniprot.org/core/author"Delhase M."xsd:string
http://purl.uniprot.org/citations/10195894http://purl.uniprot.org/core/author"Delhase M."xsd:string
http://purl.uniprot.org/citations/10195894http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10195894http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10195894http://purl.uniprot.org/core/name"Science"xsd:string
http://purl.uniprot.org/citations/10195894http://purl.uniprot.org/core/name"Science"xsd:string
http://purl.uniprot.org/citations/10195894http://purl.uniprot.org/core/pages"309-313"xsd:string
http://purl.uniprot.org/citations/10195894http://purl.uniprot.org/core/pages"309-313"xsd:string
http://purl.uniprot.org/citations/10195894http://purl.uniprot.org/core/title"Positive and negative regulation of IkappaB kinase activity through IKKbeta subunit phosphorylation."xsd:string
http://purl.uniprot.org/citations/10195894http://purl.uniprot.org/core/title"Positive and negative regulation of IkappaB kinase activity through IKKbeta subunit phosphorylation."xsd:string
http://purl.uniprot.org/citations/10195894http://purl.uniprot.org/core/volume"284"xsd:string
http://purl.uniprot.org/citations/10195894http://purl.uniprot.org/core/volume"284"xsd:string
http://purl.uniprot.org/citations/10195894http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10195894
http://purl.uniprot.org/citations/10195894http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10195894