KESTREL: a powerful method for identifying the physiological substrates of protein kinases
Author:
Affiliation:
1. MRC Protein Phosphorylation Unit, MSI/WTB Complex, Dow Street, Dundee DD1 5EH, U.K.
2. Kinasource Ltd, MSI/WTB Complex, Dow Street, Dundee DD1 5EH, U.K.
Abstract
Publisher
Portland Press Ltd.
Subject
Cell Biology,Molecular Biology,Biochemistry
Link
https://portlandpress.com/biochemj/article-pdf/393/1/1/641016/bj3930001.pdf
Reference30 articles.
1. A novel method to identify protein kinase substrates: eEF2 kinase is phosphorylated and inhibited by SAPK4/p38δ;Knebel;EMBO J.,2001
2. Activation of serum- and glucocorticoid-regulated protein kinase by agonists that activate phosphatidylinositide 3-kinase is mediated by 3-phosphoinositide-dependent protein kinase-1 (PDK1) and PDK2;Kobayashi;Biochem. J.,1999
3. Serum and glucocorticoid-inducible kinase (SGK) is a target of the PI 3-kinase-stimulated signaling pathway;Park;EMBO J.,1999
4. Protein kinase SGK mediates survival signals by phosphorylating the forkhead transcription factor FKHRL1 (FOXO3a);Brunet;Mol. Cell. Biol.,2001
5. In vivo role of the PIF-binding docking site of PDK1 defined by knock-in mutation;Collins;EMBO J.,2003
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