Deep Chatterjee

This paper determines the crystal structures of DFCP1's ATPase domain with ADP and ATP analogues, revealing structural elements that regulate ATP hydrolysis and omegasome dynamics.

The paper identifies novel kinase:Rab pairs and characterizes substrate recognition determinants for Rab phosphorylation by kinases like LRRK2.

Hybrid type-II inhibitors RN277 and RN341 target inactive LRRK2 with far fewer kinase off-targets than Rebastinib, preserve S935 phosphorylation, and rescue kinesin motility in vitro.

The paper repurposes a benzoxazepinone scaffold originally designed for RIPK1 inhibition to develop a novel type-III LIMK1/2 inhibitor with high selectivity.

This study develops a high-affinity DARPin that binds to LRRK2's WD40 domain, improving structural analysis and revealing its role in disrupting LRRK2 filaments and Rab8A phosphorylation.

This study presents cryo-EM structures of LRRK2 bound to type-I and type-II inhibitors, revealing conformational changes and providing a basis for inhibitor design.