Hyun-Seo Kang

This study identifies how DNA and ubiquitin relieve autoinhibition in SPRTN, enabling its protease activity through conformational changes.

This study shows that ubiquitin activates SPRTN protease to degrade DNA-protein crosslinks, maintaining genome stability and preventing disease.

This study shows that PURA syndrome mutations disrupt PURA's structure and P-body association, explaining full penetrance of the disease.

The paper identifies a splicing mechanism in human short introns involving RBM17 and SAP30BP, showing their interaction promotes splicing through a UHM-ULM binding and recruitment to phosphorylated SF3B1.

The paper identifies SPF45/RBM17 as essential for splicing a subset of human short introns, showing it competes with U2AF65 for binding to SF3B1, while U2AF is not required for this process.