Dehua Yang

The paper develops a computational framework to predict small molecule GLP-1R agonists, identifying chemically distinct candidates with varying efficacy.

This study presents cryo-EM structures of hURAT1 bound with anti-gout drugs and uric acid, revealing transport mechanisms and drug inhibition.

This study reveals the molecular mechanism by which GLP-1(9-36) and the allosteric modulator LSN3318839 enhance GLP-1R signaling through distinct structural interactions.

The paper identifies a conserved carbohydrate-recognition motif in purinergic receptors and demonstrates its role in activating GPCRs through sugar nucleotide binding.

The paper reports cryo-EM structures of RXFP4-Gi complexes with INSL5 and agonists, revealing a unique peptide-binding mechanism and subtype selectivity determinants.

This paper reports cryo-EM structures of small molecule GLP-1R agonists Boc5 and WB4-24, revealing a novel binding pocket and mechanism for peptidomimetic agonism.

This study reports the cryo-EM structure of the human VIP2R bound to PACAP27 and Gs, revealing a unique N-terminal helix conformation that stabilizes the ligand-receptor interface.

The paper investigates how splice variants of GIPR modulate cAMP and β-arrestin signaling independently of ligand binding.

The paper identifies a splice variant of the GHRHR receptor that mediates constitutive signal bias towards β-arrestin recruitment, impacting downstream signaling pathways in prostate cancer cells.

The paper reports high-resolution structures of MC4R with agonists and reveals insights into ligand recognition and activation mechanisms.

This study determines cryo-EM structures of dual and triple agonists bound to GIPR, GLP-1R, and GCGR to elucidate their superior efficacy over monoagonists in glucose homeostasis.

The paper reports the cryo-EM structure of the human GIPR complexed with GIP and a Gs heterotrimer, revealing how GIP is recognized and activates the receptor.

The paper reports cryo-EM structures of GLP-1R with ago-allosteric modulators, revealing their mechanism of action and providing insights for therapeutic design.

The paper identifies a universal activation mechanism for class A GPCRs by analyzing high-resolution structures, linking ligand binding to G protein coupling through TM6 movement.