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http://purl.uniprot.org/citations/9520446http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9520446http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9520446http://www.w3.org/2000/01/rdf-schema#comment"Activation of the transcription factor NF-kappaB by inflammatory cytokines involves the successive action of NF-kappaB-inducing kinase (NIK) and two IkappaB kinases, IKK-alpha and IKK-beta. Here we show that NIK preferentially phosphorylates IKK-alpha over IKK-beta, leading to the activation of IKK-alpha kinase activity. This phosphorylation of IKK-alpha occurs specifically on Ser-176 in the activation loop between kinase subdomains VII and VIII. A mutant form of IKK-alpha containing alanine at residue 176 cannot be phosphorylated or activated by NIK and acts as a dominant negative inhibitor of interleukin 1- and tumor necrosis factor-induced NF-kappaB activation. Conversely, a mutant form of IKK-alpha containing glutamic acid at residue 176 is constitutively active. Thus, the phosphorylation of IKK-alpha on Ser-176 by NIK may be required for cytokine-mediated NF-kappaB activation."xsd:string
http://purl.uniprot.org/citations/9520446http://purl.org/dc/terms/identifier"doi:10.1073/pnas.95.7.3792"xsd:string
http://purl.uniprot.org/citations/9520446http://purl.org/dc/terms/identifier"doi:10.1073/pnas.95.7.3792"xsd:string
http://purl.uniprot.org/citations/9520446http://purl.uniprot.org/core/author"Cao Z."xsd:string
http://purl.uniprot.org/citations/9520446http://purl.uniprot.org/core/author"Cao Z."xsd:string
http://purl.uniprot.org/citations/9520446http://purl.uniprot.org/core/author"Ling L."xsd:string
http://purl.uniprot.org/citations/9520446http://purl.uniprot.org/core/author"Ling L."xsd:string
http://purl.uniprot.org/citations/9520446http://purl.uniprot.org/core/author"Goeddel D.V."xsd:string
http://purl.uniprot.org/citations/9520446http://purl.uniprot.org/core/author"Goeddel D.V."xsd:string
http://purl.uniprot.org/citations/9520446http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9520446http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9520446http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/9520446http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/9520446http://purl.uniprot.org/core/pages"3792-3797"xsd:string
http://purl.uniprot.org/citations/9520446http://purl.uniprot.org/core/pages"3792-3797"xsd:string
http://purl.uniprot.org/citations/9520446http://purl.uniprot.org/core/title"NF-kappaB-inducing kinase activates IKK-alpha by phosphorylation of Ser-176."xsd:string
http://purl.uniprot.org/citations/9520446http://purl.uniprot.org/core/title"NF-kappaB-inducing kinase activates IKK-alpha by phosphorylation of Ser-176."xsd:string
http://purl.uniprot.org/citations/9520446http://purl.uniprot.org/core/volume"95"xsd:string
http://purl.uniprot.org/citations/9520446http://purl.uniprot.org/core/volume"95"xsd:string
http://purl.uniprot.org/citations/9520446http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9520446
http://purl.uniprot.org/citations/9520446http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9520446
http://purl.uniprot.org/citations/9520446http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/9520446
http://purl.uniprot.org/citations/9520446http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/9520446