Benoı̂t Roux

This study determines the structural changes in a Type II ABC importer's substrate-binding protein in different nucleotide states, revealing how ATP binding and hydrolysis regulate its conformation and interaction with the transporter.

This study determines the structure of Kv channels bound to 4AP, showing it binds the closed state and enters via membrane-facing fenestrations, explaining its inhibitory mechanism.

The paper determines the cryo-EM structure of a Shaker K+ channel mutant and shows that voltage sensing domain activation induces a dynamic shift in the linker population equilibrium rather than directly pulling the gate open.

This paper designs and tests covalent kinase activity probes using computational methods and shows they target multiple kinases in live cells with distinct kinetics and conformations.

This paper develops a kinetic model to analyze covalent inhibitors by accounting for intermediate states, showing how transient conformations affect inhibitor potency and dissociation rates.

This study investigates the C-type inactivation mechanism in a Kv-like KcsA mutant, finding that the E71V mutation leads to a different structural conformation compared to wild-type KcsA.