Francisco Bezanilla

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 investigates the molecular mechanism of fast sodium channel inactivation using fluorescence spectroscopy and electrophysiology, proposing an alternative 'lock and key' model.

The paper reveals the closed state structure of the Shaker K+ channel by uncoupling voltage sensor domains, showing a novel 'roll and turn' movement of S6 helices and a noncanonical selectivity filter state.

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 study shows that a single mutation can drastically alter the temperature response of Kv channels by modifying their electromechanical coupling.