W. Dylan Hale

The paper identifies 70 extracellular proteins interacting with AMPARs during synaptic plasticity, showing OBCAM and NTM regulate AMPAR mobility.

This study investigates the structural features of GluA4 AMPA receptors, revealing their unique architecture and conformational plasticity that influence ion channel function and disease relevance.

The paper determines the structure of the TARP subunit γ2 using cryo-EM and identifies structural motifs that differentiate TARPs from claudins and explain subfamily variations.

This study reveals how negative allosteric modulators inhibit AMPA receptors by disrupting glutamate binding and outcompeting positive modulators, offering insights for therapeutic design.

This study engineers novel adhesion molecules that drive synapse formation in cultured neurons by combining domains from bacterial proteins and synaptic cell-adhesion molecules.