Daniel Roderer

The paper investigates the binding of scorpion toxin CTX to the MthK channel using cryo-EM, NMR, and MD simulations to explain toxin affinity and subtype tolerance.

This study uses cryo-EM and solid-state NMR to determine the structure and dynamics of MscL from E. coli, revealing lipid-protein interactions that drive mechanosensitive gating.

This study characterizes how full-length recombinant Bcl-xL monomers inhibit apoptosis through direct and indirect mechanisms using in vitro and organelle assays.

The paper identifies how spatial N-glycan rearrangements on α5β1 integrin nucleate galectin-3 oligomers, determining endocytic fate and retrograde trafficking.

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.

This study investigates the multi-state kinetics of Tc toxin prepore-to-pore transition, identifying intermediate states and transition times under various conditions.

The paper models the structure and mechanism of the CPE-claudin-4 pore complex, revealing its hexameric architecture and cation selectivity.

This study identifies two glycans, heparins/heparan sulfates and Lewis antigens, as receptors for Tc toxins, revealing a two-step adhesion mechanism involving glycan binding to toxin subunits.

The paper determines the structure of a Tc holotoxin pore and elucidates its translocation mechanism through conformational changes and lipid interactions.

The paper presents high-resolution structures of five TcA toxins from different bacteria, revealing conserved architecture and a common mechanism of action despite previous suggestions of variability.