Gustavo F. Contreras

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.

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.

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.