Bert L. de Groot

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.

This study investigates how lipid interactions influence BK channel conductivity and activation, proposing a multi-modal mechanism involving lipid entry reduction and structural stabilization.

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 investigates the gating mechanism of MthK channels using mutants, revealing hydrophobic and lipid-mediated processes that drive channel closure.

This study shows sodium ions regulate GPCR activation by altering allosteric coupling networks and hydration patterns in the dopamine D2 receptor.

This study identifies a calcium-mediated gating mechanism in the MthK potassium channel using solid-state NMR and MD simulations, revealing how Ca2+ blocks outward K+ flow while allowing inward flow.

This paper shows that anle138b binds to a cavity in lipidic Aβ fibrils and reduces fibril formation by 75%, suggesting a potential therapeutic mechanism for Alzheimer's disease.

This paper improves molecular dynamics simulations of potassium channels by incorporating polarization effects, achieving accurate predictions of conductance, ion occupancy, voltage response, and selectivity.

The paper evaluates structure-based methods to predict how kinase mutations affect inhibitor binding, finding they accurately classify mutations as resistant or sensitizing.

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.

The paper presents six atomic structures of α-synuclein fibrils in the presence of phospholipids, revealing how phospholipids influence fibril morphology and lipid interactions.