Modulation of protein kinase FA/GSK-3a by tyrosine phosphorylation in A431 cells was investigated. Kinase F A / G S K -~~ was found to exist in a highly tyrosine-phosphorylated/activated state in resting cells but could become tyrosine-dephosphorylated and inactivated down to less than 30% of contro
β¦ LIBER β¦
Dephosphorylation and inactivation of Akt/PKB is counteracted by protein kinase CK2 in HEK 293T cells
β Scribed by Giovanni Di Maira; Francesca Brustolon; Lorenzo A. Pinna; Maria Ruzzene
- Publisher
- Springer
- Year
- 2009
- Tongue
- English
- Weight
- 492 KB
- Volume
- 66
- Category
- Article
- ISSN
- 1420-682X
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## Abstract Bradykinin (BK) and angiotensin II (AngII) often have opposite roles in cardiovascular diseases. Our aim here was to construct hybrid receptors which bind AngII but signal as BK. Various sequences of the intracellular face of the AngII type I receptor, AT1R, were replaced with correspon