Stephen J. Tucker

This study identifies the binding site of CVN293 on THIK-1 K2P channel and reveals its allosteric inhibition mechanism through cryoEM structures and functional validation.

The paper identifies equivalent gain-of-function variants in KCNK3 and KCNK9 that cause distinct channelopathies and investigates their functional effects on homomeric and heteromeric TASK channels.

This study identifies the molecular mechanisms of GqPCR-mediated inhibition of TASK-1 and TASK-3 K2P channels and links their dysfunction to disease.

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

The paper shows that electronic polarization is essential for accurately simulating Cl- permeation through the hBest1 channel and resolving ion-like densities in cryo-EM structures.

This study presents cryoEM structures of TASK-1 and TASK-3 channels, revealing structural insights into their gating mechanism and pH sensitivity, and how mutations disrupt function in disease.

The paper identifies nanobodies that selectively modulate TREK-2 channel activity and reveals their binding mechanisms through structural analysis.

The paper identifies de novo gain-of-function mutations in KCNK3 causing a developmental disorder with sleep apnea by disrupting X-gating of TASK-1 channels.

This paper reveals the structure of TASK-1 channels, identifying a unique lower X-gate that traps inhibitors in the vestibule, explaining their slow washout and pharmacological properties.

The paper reports cryo-EM and crystal structures of GABAA receptors with ligands, revealing the molecular basis of BZD modulation.