Eduardo Perozo

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 identifies how NS1619 binds to BK channels and stabilizes their open conformation through structural and dynamic analysis.

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 reveals how prestin translates membrane tension into charge and motor movement during sound-evoked vibrations through structural analysis and complementary experiments.

This study uses cryo-EM to examine BK channel structures with locked voltage sensor states, revealing how voltage and calcium binding interact to control channel gating.

The paper determines structures of conductive and non-conductive HERG selectivity filters and identifies a mechanism for rapid inactivation kinetics.

This study determines the cryo-EM structures of Prestin in multiple states, revealing its mechanism of area expansion and anion-binding site competition with salicylate.