David L. Stokes

This study uses cryo-EM to capture high-resolution structures of the KdpFABC potassium pump in E. coli during active transport, revealing lipid interactions and functional roles in potassium movement.

This study investigates K+ transport through the inter-subunit tunnel of KdpFABC using simulations and experiments, finding that the tunnel is mostly water-filled with a single K+ binding site and a high energy barrier.

The paper investigates the conduction pathway of potassium through the E. coli KdpFABC pump using cryo-EM and biochemical assays, revealing a tunnel for K+ transport and a low-affinity release site in KdpB.

This study identifies PIN-FORMED auxin transporters as mediators of phenoxyacetic acid herbicide transport and characterizes their molecular mechanism using Cryo-EM structures.