Thomas A. Leonard

The paper demonstrates that protein kinases can undergo intramolecular autophosphorylation using single-molecule reaction chambers, challenging the conventional view of intermolecular activation.

This study identifies how PIP3 activates an ancestral Tec kinase by displacing its PH domain from an inhibitory interaction with its kinase domain.

This study identifies MAST1 and 14-3-3 as regulators of Tau phosphorylation in the developing cortex through interactions and phosphorylation events.

This study identifies dimerization-dependent cis-autophosphorylation as the mechanism activating UPR and ISR kinases, showing it is necessary and sufficient for PERK activation.

This study reveals that PHLPP2 is a pseudophosphatase with no catalytic activity, challenges its role as a tumor suppressor, and identifies its non-catalytic functions in Akt signaling.