Anton M. Bennett

The paper investigates how structural changes in the 4-5 loop of MKP5 affect its catalytic activity and shows that mutations in this loop and adjacent regions disrupt enzyme function.

This study investigates the allosteric regulation of MKP5 by identifying the role of residue Y435 in maintaining the structural integrity of the allosteric pocket and its interaction with p38 MAPK and JNK.

This study introduces Opto-OGT, an optogenetic tool to control O-GlcNAc modification, showing its ability to modulate mTORC and AKT signaling in response to light.

This study shows MKP-5 promotes TGF-β signaling via JNK-dependent pathway by affecting SMAD2 phosphorylation and fibrogenic gene activation.