Marcus Schewe

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 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.

This study uses molecular dynamics to analyze TREK-2 channel conformational changes, linking them to disease mechanisms and drug discovery.

This paper reveals the atomistic mechanism of voltage gating in TREK K2P channels through molecular dynamics simulations and electrophysiology, showing how SF conformational flexibility and water influx regulate ion permeation.

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.

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.

This paper identifies a lower cytoplasmic gate in TALK-2 channels and demonstrates bidirectional coupling between this gate and the selectivity filter gate, showing that ion occupancy and stimuli can influence both gates.

The paper reveals the atomistic mechanism of long-range coupling between the cytosolic sensor domain and the selectivity filter in TREK K2P channels, showing how conformational changes and phosphorylation regulate channel activity.

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.