Mechanism of Phosphorylation of Protein Kinase B/Akt by a Constitutively Active 3-Phosphoinositide-dependent Protein Kinase-1
Open Access
- 1 December 2000
- journal article
- Published by Elsevier BV in Journal of Biological Chemistry
- Vol. 275 (51), 40400-40406
- https://doi.org/10.1074/jbc.m003937200
Abstract
No abstract availableKeywords
This publication has 30 references indexed in Scilit:
- Sphingosine Is a Novel Activator of 3-Phosphoinositide-dependent Kinase 1Journal of Biological Chemistry, 2000
- Ceramide Inhibits Protein Kinase B/Akt by Promoting Dephosphorylation of Serine 473Journal of Biological Chemistry, 2000
- Inhibition of PKB/Akt1 by C2-Ceramide Involves Activation of Ceramide-Activated Protein Phosphatase in PC12 CellsMolecular and Cellular Neuroscience, 2000
- Primary Structure, Tissue Distribution, and Expression of Mouse Phosphoinositide-dependent Protein Kinase-1, a Protein Kinase That Phosphorylates and Activates Protein Kinase CζPublished by Elsevier BV ,1999
- Intracellular signalling: PDK1 – a kinase at the hub of thingsCurrent Biology, 1999
- Regulation of Protein Kinase BJournal of Receptors and Signal Transduction, 1999
- Inhibition of Akt Kinase by Cell-permeable Ceramide and Its Implications for Ceramide-induced ApoptosisPublished by Elsevier BV ,1998
- Characterization of a 3-phosphoinositide-dependent protein kinase which phosphorylates and activates protein kinase BαCurrent Biology, 1997
- Akt, a Pleckstrin Homology Domain Containing Kinase, Is Activated Primarily by PhosphorylationJournal of Biological Chemistry, 1996
- [19] Rapid and efficient site-specific mutagenesis without phenotypic selectionMethods in enzymology, 1987