Di Wu

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

The paper develops a kinetic model to describe USP14-regulated substrate degradation in the 26S proteasome, showing that USP14 reduces degradation rates and depends on substrate and ATP concentrations.

This study develops a reaction-diffusion model to quantify proteasome-associated liquid-liquid phase separation and its bidirectional impact on degradation efficiency.