http://purl.uniprot.org/citations/10195894 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/10195894 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/10195894 | http://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/10195894 | http://purl.org/dc/terms/identifier | "doi:10.1126/science.284.5412.309"xsd:string |
http://purl.uniprot.org/citations/10195894 | http://purl.org/dc/terms/identifier | "doi:10.1126/science.284.5412.309"xsd:string |
http://purl.uniprot.org/citations/10195894 | http://purl.uniprot.org/core/author | "Chen Y."xsd:string |
http://purl.uniprot.org/citations/10195894 | http://purl.uniprot.org/core/author | "Chen Y."xsd:string |
http://purl.uniprot.org/citations/10195894 | http://purl.uniprot.org/core/author | "Karin M."xsd:string |
http://purl.uniprot.org/citations/10195894 | http://purl.uniprot.org/core/author | "Karin M."xsd:string |
http://purl.uniprot.org/citations/10195894 | http://purl.uniprot.org/core/author | "Hayakawa M."xsd:string |
http://purl.uniprot.org/citations/10195894 | http://purl.uniprot.org/core/author | "Hayakawa M."xsd:string |
http://purl.uniprot.org/citations/10195894 | http://purl.uniprot.org/core/author | "Delhase M."xsd:string |
http://purl.uniprot.org/citations/10195894 | http://purl.uniprot.org/core/author | "Delhase M."xsd:string |
http://purl.uniprot.org/citations/10195894 | http://purl.uniprot.org/core/date | "1999"xsd:gYear |
http://purl.uniprot.org/citations/10195894 | http://purl.uniprot.org/core/date | "1999"xsd:gYear |
http://purl.uniprot.org/citations/10195894 | http://purl.uniprot.org/core/name | "Science"xsd:string |
http://purl.uniprot.org/citations/10195894 | http://purl.uniprot.org/core/name | "Science"xsd:string |
http://purl.uniprot.org/citations/10195894 | http://purl.uniprot.org/core/pages | "309-313"xsd:string |
http://purl.uniprot.org/citations/10195894 | http://purl.uniprot.org/core/pages | "309-313"xsd:string |
http://purl.uniprot.org/citations/10195894 | http://purl.uniprot.org/core/title | "Positive and negative regulation of IkappaB kinase activity through IKKbeta subunit phosphorylation."xsd:string |
http://purl.uniprot.org/citations/10195894 | http://purl.uniprot.org/core/title | "Positive and negative regulation of IkappaB kinase activity through IKKbeta subunit phosphorylation."xsd:string |
http://purl.uniprot.org/citations/10195894 | http://purl.uniprot.org/core/volume | "284"xsd:string |
http://purl.uniprot.org/citations/10195894 | http://purl.uniprot.org/core/volume | "284"xsd:string |
http://purl.uniprot.org/citations/10195894 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/10195894 |
http://purl.uniprot.org/citations/10195894 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/10195894 |