Björn Udo Klink

This study presents the cryo-EM structure of the RalGAP tumor suppressor complex, revealing its tetrameric architecture and providing insights into its function and relevance in cancer.

This paper reveals the molecular mechanism of α-latrotoxin action by determining its high-resolution structures and showing conformational changes during pore formation.

The paper reports cryoEM structures of the Pex1/Pex6 ATPase complex from yeast, revealing how it translocates substrates through conformational changes and mechanical force propagation.

The paper provides the first structural characterization of the yeast peroxisomal docking complex Pex14p/Pex17p, revealing its subunit organization and potential role in import pore formation.

The paper presents a high-resolution cryo-EM structure of a human BBSome core subcomplex, revealing its open conformation and interactions with cargo and membrane components.