R. Manjula

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 investigates the interaction between TULP3 and SIRT1/SIRT2 using biochemical methods, finding that both TULP3 domains are required for binding but TULP3 is not a deacetylation substrate for SIRT1.