David M. Thal

The paper presents cryo-EM structures of the delta opioid receptor with PAMs, identifies a novel allosteric site, and describes a mechanism for enhanced binding and activation.

This paper reports the cryo-EM structure of the M4 mAChR bound to MK-97 and acetylcholine, revealing how MK-97's binding mode improves PAM activity through distributed interactions.

This paper presents cryo-EM structures of PORCN with inhibitors, revealing a conserved water-mediated binding mechanism for rational drug design.

The paper presents cryo-EM structures of the human A3 adenosine receptor in three functional states, revealing a unique activation mechanism and a cryptic binding pocket.

The paper presents a cryo-EM structure of the M5 mAChR with a novel allosteric binding site identified through mutagenesis, pharmacology, and simulations.

This paper demonstrates that a standard 120-keV TEM with a direct electron detector can achieve high-resolution cryo-EM reconstructions of various proteins.

This study determines the structure of the human P2X1 receptor in different ligand-bound states and identifies key residues involved in ligand binding and selectivity.

This study shows positive allosteric modulators stabilize the GPCR-G protein ternary complex, enhancing signaling when nucleotides are present.