Benjamin Bardiaux

The paper investigates the structural basis of endopilus assembly, stability, and functional specificity in bacterial type II secretion systems using comparative analysis of two pathogens.

The paper introduces NEF, a standard for NMR data exchange, and demonstrates its application in structure determination, metabolomics, and ligand screening.

This paper identifies small molecules that inhibit the SARS-CoV-2 E protein interaction with ZO-1 PDZ2 using X-ray crystallography, HTRF screening, and docking simulations, with one compound showing antiviral activity.

This study shows that acylation stabilizes the native fold of CyaA and facilitates its membrane orientation, revealing how post-translational modification drives toxin activity.

The paper develops a standardized system for validating biomolecular structures against NMR restraints using NEF and NMR-STAR formats, implemented in the wwPDB OneDep system.

The paper introduces a graph-based method to build atomic protein models from cryo-EM density maps using residue co-evolution data to improve segmentation and sequence assignment.