PubMed:10224130 JSONTXT

{"project":"sentences","denotations":[{"id":"T1","span":{"begin":0,"end":140},"obj":"Sentence"},{"id":"T2","span":{"begin":141,"end":277},"obj":"Sentence"},{"id":"T3","span":{"begin":278,"end":386},"obj":"Sentence"},{"id":"T4","span":{"begin":387,"end":567},"obj":"Sentence"},{"id":"T5","span":{"begin":568,"end":730},"obj":"Sentence"},{"id":"T6","span":{"begin":731,"end":899},"obj":"Sentence"},{"id":"T7","span":{"begin":900,"end":1049},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Regulation of NF-kappaB RelA phosphorylation and transcriptional activity by p21(ras) and protein kinase Czeta in primary endothelial cells.\nThe activity of the transcription factor NF-kappaB is thought to be regulated mainly through cytoplasmic retention by IkappaB molecules. Here we present evidence of a second mechanism of regulation acting on NF-kappaB after release from IkappaB. In endothelial cells this mechanism involves phosphorylation of the RelA subunit of NF-kappaB through a pathway involving activation of protein kinase Czeta (PKCzeta) and p21(ras). We show that transcriptional activity of RelA is dependent on phosphorylation of the N-terminal Rel homology domain but not the C-terminal transactivation domain. Inhibition of phosphorylation by dominant negative mutants of PKCzeta or p21(ras) results in loss of RelA transcriptional activity without interfering with DNA binding. Raf/MEK, small GTPases, phosphatidylinositol 3-kinase, and stress-activated protein kinase pathways are not involved in this mechanism of regulation."}

{"project":"bionlp-st-pc-2013-training","denotations":[{"id":"T1","span":{"begin":14,"end":23},"obj":"Complex"},{"id":"T2","span":{"begin":24,"end":28},"obj":"Gene_or_gene_product"},{"id":"T3","span":{"begin":77,"end":80},"obj":"Gene_or_gene_product"},{"id":"T4","span":{"begin":81,"end":84},"obj":"Gene_or_gene_product"},{"id":"T5","span":{"begin":90,"end":110},"obj":"Gene_or_gene_product"},{"id":"T6","span":{"begin":182,"end":191},"obj":"Complex"},{"id":"T7","span":{"begin":234,"end":245},"obj":"Cellular_component"},{"id":"T8","span":{"begin":259,"end":266},"obj":"Gene_or_gene_product"},{"id":"T9","span":{"begin":349,"end":358},"obj":"Complex"},{"id":"T10","span":{"begin":378,"end":385},"obj":"Gene_or_gene_product"},{"id":"T11","span":{"begin":455,"end":459},"obj":"Gene_or_gene_product"},{"id":"T12","span":{"begin":471,"end":480},"obj":"Complex"},{"id":"T13","span":{"begin":523,"end":543},"obj":"Gene_or_gene_product"},{"id":"T14","span":{"begin":545,"end":552},"obj":"Gene_or_gene_product"},{"id":"T15","span":{"begin":558,"end":561},"obj":"Gene_or_gene_product"},{"id":"T16","span":{"begin":562,"end":565},"obj":"Gene_or_gene_product"},{"id":"T17","span":{"begin":609,"end":613},"obj":"Gene_or_gene_product"},{"id":"T18","span":{"begin":664,"end":667},"obj":"Gene_or_gene_product"},{"id":"T19","span":{"begin":793,"end":800},"obj":"Gene_or_gene_product"},{"id":"T20","span":{"begin":804,"end":807},"obj":"Gene_or_gene_product"},{"id":"T21","span":{"begin":808,"end":811},"obj":"Gene_or_gene_product"},{"id":"T22","span":{"begin":832,"end":836},"obj":"Gene_or_gene_product"},{"id":"T23","span":{"begin":900,"end":903},"obj":"Gene_or_gene_product"},{"id":"T24","span":{"begin":904,"end":907},"obj":"Gene_or_gene_product"},{"id":"T25","span":{"begin":924,"end":953},"obj":"Gene_or_gene_product"},{"id":"T26","span":{"begin":959,"end":990},"obj":"Gene_or_gene_product"}],"text":"Regulation of NF-kappaB RelA phosphorylation and transcriptional activity by p21(ras) and protein kinase Czeta in primary endothelial cells.\nThe activity of the transcription factor NF-kappaB is thought to be regulated mainly through cytoplasmic retention by IkappaB molecules. Here we present evidence of a second mechanism of regulation acting on NF-kappaB after release from IkappaB. In endothelial cells this mechanism involves phosphorylation of the RelA subunit of NF-kappaB through a pathway involving activation of protein kinase Czeta (PKCzeta) and p21(ras). We show that transcriptional activity of RelA is dependent on phosphorylation of the N-terminal Rel homology domain but not the C-terminal transactivation domain. Inhibition of phosphorylation by dominant negative mutants of PKCzeta or p21(ras) results in loss of RelA transcriptional activity without interfering with DNA binding. Raf/MEK, small GTPases, phosphatidylinositol 3-kinase, and stress-activated protein kinase pathways are not involved in this mechanism of regulation."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":122,"end":139},"obj":"Body_part"},{"id":"T2","span":{"begin":234,"end":245},"obj":"Body_part"},{"id":"T3","span":{"begin":390,"end":407},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL_0000115"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/GO_0005737"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/CL_0000115"}],"text":"Regulation of NF-kappaB RelA phosphorylation and transcriptional activity by p21(ras) and protein kinase Czeta in primary endothelial cells.\nThe activity of the transcription factor NF-kappaB is thought to be regulated mainly through cytoplasmic retention by IkappaB molecules. Here we present evidence of a second mechanism of regulation acting on NF-kappaB after release from IkappaB. In endothelial cells this mechanism involves phosphorylation of the RelA subunit of NF-kappaB through a pathway involving activation of protein kinase Czeta (PKCzeta) and p21(ras). We show that transcriptional activity of RelA is dependent on phosphorylation of the N-terminal Rel homology domain but not the C-terminal transactivation domain. Inhibition of phosphorylation by dominant negative mutants of PKCzeta or p21(ras) results in loss of RelA transcriptional activity without interfering with DNA binding. Raf/MEK, small GTPases, phosphatidylinositol 3-kinase, and stress-activated protein kinase pathways are not involved in this mechanism of regulation."}

{"project":"CL-cell","denotations":[{"id":"T1","span":{"begin":122,"end":139},"obj":"Cell"},{"id":"T2","span":{"begin":390,"end":407},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0000115"},{"id":"A2","pred":"cl_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL:0000115"}],"text":"Regulation of NF-kappaB RelA phosphorylation and transcriptional activity by p21(ras) and protein kinase Czeta in primary endothelial cells.\nThe activity of the transcription factor NF-kappaB is thought to be regulated mainly through cytoplasmic retention by IkappaB molecules. Here we present evidence of a second mechanism of regulation acting on NF-kappaB after release from IkappaB. In endothelial cells this mechanism involves phosphorylation of the RelA subunit of NF-kappaB through a pathway involving activation of protein kinase Czeta (PKCzeta) and p21(ras). We show that transcriptional activity of RelA is dependent on phosphorylation of the N-terminal Rel homology domain but not the C-terminal transactivation domain. Inhibition of phosphorylation by dominant negative mutants of PKCzeta or p21(ras) results in loss of RelA transcriptional activity without interfering with DNA binding. Raf/MEK, small GTPases, phosphatidylinositol 3-kinase, and stress-activated protein kinase pathways are not involved in this mechanism of regulation."}