Moritz Hunkeler

This study uses high-throughput chemistry to discover chemical inducers of proximity by modifying pre-existing ligands and screening for degrader activity.

This study identifies the structural basis of VCP-VCPIP1-p47 complex formation and demonstrates the role of VCPID in enhancing DUB activity and Golgi reassembly.

The paper shows that structural ubiquitin contributes to K48 linkage-specificity in Tom1 through a non-canonical binding site identified via cryo-EM.

This paper identifies HUWE1 as a ubiquitin ligase that enhances ubiquitin modifications on proteins and aggregates, promoting their degradation via proteasome and autophagy pathways.

This study identifies HAPSTR1 as a HUWE1 substrate that facilitates its nuclear localization, thereby regulating stress signaling pathways and cell proliferation.

The paper presents cryo-EM structures of BIRC6-client complexes to elucidate the mechanism of Smac-mediated caspase release and BIRC6 function in apoptosis regulation.

The paper presents the cryo-EM structure of HUWE1, revealing its modular architecture and its role in degrading cell-fate decision factors.