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http://purl.uniprot.org/citations/8816457http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8816457http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8816457http://www.w3.org/2000/01/rdf-schema#comment"Stimulation with inducers that cause persistent activation of NF-kappa B results in the degradation of the NF-kappa B inhibitors, I kappa B alpha and I kappa B beta. Despite the rapid resynthesis and accumulation of I kappa B alpha, NF-kappa B remains induced under these conditions. We now report that I kappa B beta is also resynthesized in stimulated cells and appears as an unphosphorylated protein. The unphosphorylated I kappa B beta forms a stable complex with NF-kappa B in the cytosol; however, this binding fails to mask the nuclear localization signal and DNA binding domain on NF-kappa B, and the I kappa B beta-NF-kappa B complex enters the nucleus. It appears therefore that during prolonged stimulation, I kappa B beta functions as a chaperone for NF-kappa B by protecting it from I kappa B alpha and allowing it to be transported to the nucleus."xsd:string
http://purl.uniprot.org/citations/8816457http://purl.org/dc/terms/identifier"doi:10.1128/mcb.16.10.5444"xsd:string
http://purl.uniprot.org/citations/8816457http://purl.org/dc/terms/identifier"doi:10.1128/mcb.16.10.5444"xsd:string
http://purl.uniprot.org/citations/8816457http://purl.uniprot.org/core/author"Ghosh S."xsd:string
http://purl.uniprot.org/citations/8816457http://purl.uniprot.org/core/author"Ghosh S."xsd:string
http://purl.uniprot.org/citations/8816457http://purl.uniprot.org/core/author"Douglas I."xsd:string
http://purl.uniprot.org/citations/8816457http://purl.uniprot.org/core/author"Douglas I."xsd:string
http://purl.uniprot.org/citations/8816457http://purl.uniprot.org/core/author"Phillips R.J."xsd:string
http://purl.uniprot.org/citations/8816457http://purl.uniprot.org/core/author"Phillips R.J."xsd:string
http://purl.uniprot.org/citations/8816457http://purl.uniprot.org/core/author"Suyang H."xsd:string
http://purl.uniprot.org/citations/8816457http://purl.uniprot.org/core/author"Suyang H."xsd:string
http://purl.uniprot.org/citations/8816457http://purl.uniprot.org/core/date"1996"xsd:gYear
http://purl.uniprot.org/citations/8816457http://purl.uniprot.org/core/date"1996"xsd:gYear
http://purl.uniprot.org/citations/8816457http://purl.uniprot.org/core/name"Mol. Cell. Biol."xsd:string
http://purl.uniprot.org/citations/8816457http://purl.uniprot.org/core/name"Mol. Cell. Biol."xsd:string
http://purl.uniprot.org/citations/8816457http://purl.uniprot.org/core/pages"5444-5449"xsd:string
http://purl.uniprot.org/citations/8816457http://purl.uniprot.org/core/pages"5444-5449"xsd:string
http://purl.uniprot.org/citations/8816457http://purl.uniprot.org/core/title"Role of unphosphorylated, newly synthesized IkappaB beta in persistent activation of NF-kappaB."xsd:string
http://purl.uniprot.org/citations/8816457http://purl.uniprot.org/core/title"Role of unphosphorylated, newly synthesized IkappaB beta in persistent activation of NF-kappaB."xsd:string
http://purl.uniprot.org/citations/8816457http://purl.uniprot.org/core/volume"16"xsd:string
http://purl.uniprot.org/citations/8816457http://purl.uniprot.org/core/volume"16"xsd:string
http://purl.uniprot.org/citations/8816457http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8816457
http://purl.uniprot.org/citations/8816457http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8816457