C. Peter Downes

TL;DR: In this paper, a protein kinase that phosphorylates PKB α at Thr308 and increases its activity over 30-fold was found to play a key role in mediating the activation of PKB by insulin and growth factors.

TL;DR: The results argue that the low malignant potential of tumors arising from TSC1-2 dysfunction may be explained by the failure of TSC mutant cells to activate PI3K and its downstream effectors.

TL;DR: It is shown that oxidants, including those produced by cells, can activate downstream signalling via the inactivation of PTEN, and may have significant implications for the many cellular processes in which PtdIns(3,4,5)P3 and oxidants are produced concurrently.

TL;DR: Mice lacking the p110δ catalytic subunit of phosphatidylinositol 3-kinase have reduced numbers of B1 and marginal zone B cells, reduced levels of serum immunoglobulins, respond poorly to immunization with type II thymus-independent antigen, and are defective in their primary and secondary responses to thymUS-dependent antigen.

TL;DR: PDK1 and PDK2 might be the same enzyme, the substrate specificity and activity of PDK1 being regulated through its interaction with another protein(s), and PRK2 is a probable substrate for PDK 1.