G. Hagelueken

This study identifies nanobodies that inhibit GSDMD pore formation without affecting caspase cleavage, providing structural insights and potential drug design frameworks.

The paper demonstrates conformational coupling between the TRAP transporter HiSiaQM and its substrate binding protein HiSiaP using disulfide engineering and single-molecule TIRF microscopy.

This study identifies an isoleucine residue in RIG-I that prevents recognition of 5p-RNA, thereby maintaining immune tolerance to mitochondrial RNA.

The paper reports the crystal structure of CRISPR-Lon, a protein that activates by binding cA4 and cleaves CRISPR-T to release a nuclease-like fragment.

This paper presents the first cryo-EM structure of TRAP transporter membrane domains and identifies structural features that enable monomeric elevator architecture.

The paper determines the directionality of PYD filament growth by showing ASC elongates exclusively on the B-end of NLRP3 filaments, enabling a transition from NLRP3 nucleation to ASC elongation.

The paper determines the cryo-EM structure of NLRP3 bound to CRID3, revealing how the inhibitor stabilizes the protein and provides insights for drug development.

This study investigates the conformational changes in the sialic acid TRAP transporter SBP VcSiaP upon substrate binding, showing that substrate induces closure and provides structural insights for inhibitor development.