Ronald T. Hay

The paper develops a photocrosslinking activity-based probe to study interactions between ubiquitin and RING E3 ligases, confirming existing structures and evaluating new models.

This study identifies SUMOylation of HAdV E2A/DBP as a mechanism to inhibit p53 activity and apoptosis, revealing a novel pathway for viral oncogenic potential.

The paper solves cryo-EM structures of a degrader-mediated complex to reveal structural insights into target protein ubiquitination mechanisms.

The paper identifies TOPORS as a SUMO-targeted ubiquitin ligase (STUbL) essential for SUMO-dependent DNA-protein crosslink repair and stress responses, showing its cooperative function with RNF4.