Transcription factor TAFII250 phosphorylates the acidic domain of Mdm2 through recruitment of protein kinase CK2
โ Scribed by Nerea Allende-Vega; Lynsey McKenzie; David Meek
- Publisher
- Springer
- Year
- 2008
- Tongue
- English
- Weight
- 311 KB
- Volume
- 316
- Category
- Article
- ISSN
- 0300-8177
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## Abstract We have investigated the role of phosphorylation by vertebrate protein kinase CK2 on the activity of the General Transcription Factors TFIIA, TFIIE, TFIIF, and RNAPII. The largest subunits of TFIIA, TFIIE, and TFIIF were phosphorylated by CK2 holoenzyme. Also, RNA polymerase II was phos
## Abstract The antioxidantโactivated transcription factor nuclear factor erythroid 2โrelated factor 2 (Nrf2) regulates the induction of cytoprotective genes against chemical toxicity and oxidative injuries. The role of phosphorylation in Nrf2 activation has been suggested but remains elusive. We r