Pub. Date : 2003 Jun 1
PMID : 12759443
7 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | IKK beta plays an essential role in the phosphorylation of RelA/p65 on serine 536 induced by lipopolysaccharide. | Serine | v-rel reticuloendotheliosis viral oncogene homolog A (avian) | Mus musculus |
| 2 | IKK beta plays an essential role in the phosphorylation of RelA/p65 on serine 536 induced by lipopolysaccharide. | Serine | v-rel reticuloendotheliosis viral oncogene homolog A (avian) | Mus musculus |
| 3 | Here, we reported that LPS induced the phosphorylation of the p65 trans-activation domain on serine 536 in monocytes/macrophages. | Serine | v-rel reticuloendotheliosis viral oncogene homolog A (avian) | Mus musculus |
| 4 | Using mouse embryonic fibroblasts lacking either IKK alpha or IKK beta, we found that IKK beta played an essential role in LPS-induced p65 phosphorylation on serine 536, while IKK alpha was partially required for the p65 phosphorylation. | Serine | v-rel reticuloendotheliosis viral oncogene homolog A (avian) | Mus musculus |
| 5 | The LPS-induced p65 phosphorylation on serine 536 was independent of the phosphatidylinositol 3"-kinase/Akt signaling pathway. | Serine | v-rel reticuloendotheliosis viral oncogene homolog A (avian) | Mus musculus |
| 6 | Furthermore, we found that the phosphorylation on serine 536 increased the p65 transcription activity. | Serine | v-rel reticuloendotheliosis viral oncogene homolog A (avian) | Mus musculus |
| 7 | In summary, our results demonstrate that IKK beta plays an essential role in the LPS-induced p65 phosphorylation on serine 536, which may represent a mechanism to regulate the NF-kappa B transcription activity by LPS. | Serine | v-rel reticuloendotheliosis viral oncogene homolog A (avian) | Mus musculus |