Histone deacetylase inhibitors synergize p300 autoacetylation that regulates its transactivation activity and complex formation.

@article{Stiehl2007HistoneDI,
  title={Histone deacetylase inhibitors synergize p300 autoacetylation that regulates its transactivation activity and complex formation.},
  author={D. Stiehl and Brian D. Fath and Dongming Liang and Yubao Jiang and Nianli Sang},
  journal={Cancer research},
  year={2007},
  volume={67 5},
  pages={
          2256-2264
        }
}
p300/cyclic AMP-responsive element binding protein-binding protein (CBP) are general coactivators for multiple transcription factors involved in various cellular processes. Several highly conserved domains of p300/CBP serve as interacting sites for transcription factors and regulatory proteins. Particularly, the intrinsic histone acetyltransferase (HAT) activity and transactivation domains (TAD) play essential roles for their coactivating function. Autoacetylation of p300/CBP is commonly… CONTINUE READING
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