Id |
Subject |
Object |
Predicate |
Lexical cue |
T1 |
0-140 |
Sentence |
denotes |
Regulation of NF-kappaB RelA phosphorylation and transcriptional activity by p21(ras) and protein kinase Czeta in primary endothelial cells. |
T2 |
141-277 |
Sentence |
denotes |
The activity of the transcription factor NF-kappaB is thought to be regulated mainly through cytoplasmic retention by IkappaB molecules. |
T3 |
278-386 |
Sentence |
denotes |
Here we present evidence of a second mechanism of regulation acting on NF-kappaB after release from IkappaB. |
T4 |
387-567 |
Sentence |
denotes |
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). |
T5 |
568-730 |
Sentence |
denotes |
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. |
T6 |
731-899 |
Sentence |
denotes |
Inhibition of phosphorylation by dominant negative mutants of PKCzeta or p21(ras) results in loss of RelA transcriptional activity without interfering with DNA binding. |
T7 |
900-1049 |
Sentence |
denotes |
Raf/MEK, small GTPases, phosphatidylinositol 3-kinase, and stress-activated protein kinase pathways are not involved in this mechanism of regulation. |