Felix Schöpf

This study determines the structural basis of Fusobacterium nucleatum adhesin Fap2 interactions with Gal-GalNAc and TIGIT, revealing binding mechanisms and structural details.

This study identifies oligophosphorylation as a new phosphorylation mode, showing NME1 can catalyze its own oligophosphorylation using ATP, with implications for phosphoregulation.

This study presents the first structural description of the fusobacterial TAA CbpF and its interaction with CEACAM1, revealing a novel binding mode and potential targets for drug design in CRC.