John B. Cowgill

This paper reports cryo-EM structures of human α5β3 GABAARs with modulators, revealing activation mechanisms and differential responses to GABA and etomidate.

This study presents cryo-EM structures of human rho1 GABAA receptors bound to antagonist and agonist drugs, revealing distinct binding poses and conformational changes that explain their pharmacological effects.

The paper characterizes the inhibitory mechanisms of two neuroactive steroids at the human {rho}1 GABAA receptor using cryo-EM, electrophysiology, and molecular dynamics simulations.

The paper identifies how the HCN voltage sensor can drive pore opening in either direction, revealing a common principle in voltage-gated ion channels.