Activation of Akt, or protein kinase B, is frequently observed in human cancers.

Both agents lowered protein kinase B activity, but this was not mediated by inhibiting phosphoinositide 3-kinase.

We found a high level of protein kinase B (AKT) phosphorylation after 6 h of cold exposure.

The Akt ( protein kinase B) kinase is a key player in transduction of antiapoptotic and proliferative signals in T cells.

A lower level of phosphorylated protein kinase B was observed in PFKFB3-knockdown endothelial cells, which was accompanied by a decrease in intracellular lactate.

Expression of insulin-signaling molecules such as insulin receptor, protein kinase B, and glucose transporter-4 were decreased in male JYD mice compared with female mice.

In vitro studies suggest that the proapoptotic function of forkhead protein FKHR is probably inactivated by means of phosphorylation through the protein kinase B pathway.

The levels of P13K and protein kinase B (AKT) and its phosphorylation as well as the expression of IL-6 were analyzed.

Numerous published reports indicated that protein kinase B (Akt) and glucose transporter 4 (GLUT4) play crucial roles in ameliorating IR and diabetic symptoms.