Edward Mendez-Otalvaro

The paper identifies affinity hotspots in the modulator pocket of the K2P channel TREK1 by analyzing chemical substitutions and their effects on binding and gating.

The paper identifies the down-to-up state transition as the primary activation pathway for TREK K2P channels, showing it does not involve lipid occlusion of the pore.

The paper presents a cryoEM structure of the human THIK-1 K2P K+ channel, revealing structural features and regulatory mechanisms involving lipids and anaesthetics.

This study uses molecular dynamics simulations to investigate how two activators affect TREK1 channel gating by modulating hydrogen bond networks and carbonyl flipping in the selectivity filter.