Shitao Zou

This study reveals how UBE3C reprograms the proteasome to degrade ultra-stable protein folds by bypassing USP14 and enhancing substrate unfolding.

The paper determines cryo-EM structures of UBE3B and UBE3C in complex with calmodulin, showing how calcium signaling controls their higher-order assembly and activity.

This paper identifies rapaprotin as a 26S proteasome assembly inhibitor that is activated by PREP to induce apoptosis and synergizes with proteasome inhibitors in cancer cells.

This study uses cryo-EM and genetic engineering to show how USP14 non-catalytically regulates proteasome activity through salt-dependent allosteric changes.