Ken C. Dong

The paper identifies two proteasomal mechanisms that target proteins with exposed cysteines, revealing their role in quality control and linking them to human diseases.

This study identifies the mechanism by which antizyme mediates ubiquitin-independent degradation of yODC by the 26S proteasome through structural and biochemical analysis.

The paper identifies a novel ubiquitin-binding groove on the yeast 26S proteasome using photo-crosslinking mass spectrometry.

The paper solves high-resolution structures of TXNL1 bound to the human 26S proteasome, revealing conformation-specific binding and new insights into ATP hydrolysis and substrate translocation mechanisms.

This study shows Rpn11 acts as an allosteric ubiquitin sensor in the proteasome, enhancing substrate degradation by stabilizing the proteasome's engagement state.

This paper identifies how Nub1 traps unfolded FAT10 for ubiquitin-independent degradation by the 26S proteasome through a novel mechanism involving structural dynamics and proteasomal engagement.

The paper identifies PITHD1 as an endogenous inhibitor of the 26S proteasome in dormant cells, revealing a triple-lock mechanism that prevents protein degradation during cellular dormancy.