http://purl.uniprot.org/citations/15226358 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/15226358 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/15226358 | http://www.w3.org/2000/01/rdf-schema#comment | "Transcription factors of the nuclear factor (NF)-kappaB/Rel family translocate into the nucleus upon degradation of the IkappaBs. Postinduction repression of NF-kappaB activity depends on NF-kappaB-regulated resynthesis of IkappaBalpha, which dissociates NF-kappaB from DNA and exports it to the cytosol. We found that after activation, p65/RelA is degraded by the proteasome in the nucleus and in a DNA binding-dependent manner. If proteasome activity is blocked, NF-kappaB is not promptly removed from some target genes in spite of IkappaBalpha resynthesis and sustained transcription occurs. These results indicate that proteasomal degradation of p65/RelA does not merely regulate its stability and abundance, but also actively promotes transcriptional termination."xsd:string |
http://purl.uniprot.org/citations/15226358 | http://purl.org/dc/terms/identifier | "doi:10.1084/jem.20040196"xsd:string |
http://purl.uniprot.org/citations/15226358 | http://purl.org/dc/terms/identifier | "doi:10.1084/jem.20040196"xsd:string |
http://purl.uniprot.org/citations/15226358 | http://purl.uniprot.org/core/author | "Saccani S."xsd:string |
http://purl.uniprot.org/citations/15226358 | http://purl.uniprot.org/core/author | "Saccani S."xsd:string |
http://purl.uniprot.org/citations/15226358 | http://purl.uniprot.org/core/author | "Marazzi I."xsd:string |
http://purl.uniprot.org/citations/15226358 | http://purl.uniprot.org/core/author | "Marazzi I."xsd:string |
http://purl.uniprot.org/citations/15226358 | http://purl.uniprot.org/core/author | "Natoli G."xsd:string |
http://purl.uniprot.org/citations/15226358 | http://purl.uniprot.org/core/author | "Natoli G."xsd:string |
http://purl.uniprot.org/citations/15226358 | http://purl.uniprot.org/core/author | "Beg A.A."xsd:string |
http://purl.uniprot.org/citations/15226358 | http://purl.uniprot.org/core/author | "Beg A.A."xsd:string |
http://purl.uniprot.org/citations/15226358 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
http://purl.uniprot.org/citations/15226358 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
http://purl.uniprot.org/citations/15226358 | http://purl.uniprot.org/core/name | "J. Exp. Med."xsd:string |
http://purl.uniprot.org/citations/15226358 | http://purl.uniprot.org/core/name | "J. Exp. Med."xsd:string |
http://purl.uniprot.org/citations/15226358 | http://purl.uniprot.org/core/pages | "107-113"xsd:string |
http://purl.uniprot.org/citations/15226358 | http://purl.uniprot.org/core/pages | "107-113"xsd:string |
http://purl.uniprot.org/citations/15226358 | http://purl.uniprot.org/core/title | "Degradation of promoter-bound p65/RelA is essential for the prompt termination of the nuclear factor kappaB response."xsd:string |
http://purl.uniprot.org/citations/15226358 | http://purl.uniprot.org/core/title | "Degradation of promoter-bound p65/RelA is essential for the prompt termination of the nuclear factor kappaB response."xsd:string |
http://purl.uniprot.org/citations/15226358 | http://purl.uniprot.org/core/volume | "200"xsd:string |
http://purl.uniprot.org/citations/15226358 | http://purl.uniprot.org/core/volume | "200"xsd:string |
http://purl.uniprot.org/citations/15226358 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/15226358 |
http://purl.uniprot.org/citations/15226358 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/15226358 |