Edward C. Twomey

This study determines the structure of human GluD1 and elucidates its ligand-gating mechanism using cryoEM and electrophysiology.

The paper identifies dopamine as a direct agonist of GluDs, showing G-protein regulation of their activity and implications for neurological diseases.

This study determines the cryo-EM structure of PCDH15, revealing its right-handed double-helix dimer architecture essential for mechanotransduction.

This study identifies PSA as an inhibitory auxiliary subunit of VRACs, showing its regulatory role is independent of aminopeptidase activity.

This study shows memantine inhibits calcium-permeable AMPA receptors, revealing a new mechanism distinct from NMDA receptors and suggesting therapeutic potential for neurological disorders.

This study identifies ion permeation pathways in AMPARs using cryo-EM and MD simulations, showing how mutations affect ion flow and susceptibility to blockage.

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.

This study shows that glutamate gating of AMPA receptors is temperature sensitive and distinct from PAM-induced gating, revealing conserved structural motifs and desensitization mechanisms.

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.