H. Eric Xu

This study fine-tunes an intracellular allosteric pocket of NTSR1 to program GPCR signaling bias, revealing how ligand modifications alter transducer coupling and downstream signaling.

This study shows β-arrestin1 directly binds Gαs to sustain endosomal GPCR signaling by stabilizing Gs in a signaling-competent state.

The paper identifies TAAR1 agonists with antipsychotic-like effects through computational screening and experimental validation, showing improved potency and reduced side effects in a schizophrenia model.

The paper defines the molecular mechanism of graded activation of the dopamine D1 receptor and shows how ligand efficacy is encoded through an activation pathway.

This study determines the cryo-EM structures of OXGR1 bound to metabolites, revealing conserved mechanisms for metabolite recognition and receptor activation.

The paper presents cryo-EM structures of EP2 and EP4 receptors with antagonists, revealing structural differences that explain selectivity and binding modes.

The paper identifies multiple allosteric sites on the D1 dopamine receptor that allow synergistic enhancement of GPCR signaling through combined positive allosteric modulators.

This study reveals the molecular mechanism of pH sensing and activation in GPR4 through cryo-EM structures, showing proton-driven conformational changes and lipid modulation.

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

The paper presents cryo-EM structures of the human taurine transporter, identifies taurine-binding sites, and shows that enhanced taurine uptake reduces cellular senescence in biliary epithelial cells.

The paper solves the cryo-EM structure of CCR1-Gi complex in pre-coupled state, revealing molecular mechanism of GPCR-G protein activation and highlighting conserved pre-coupling in chemokine receptors.

This study presents cryo-EM structures of MCH-activated MCHR1 and MCHR2 with G-proteins, revealing ligand recognition mechanisms and activation pathways.

The paper presents cryo-EM structures of endothelin receptors bound to ligands, revealing their recognition mode and activation mechanism.

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

The paper reports the structures of TSHR activated by TSH and an autoantibody, revealing a universal activation mechanism and the role of cholesterol in TSHR localization.

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 reports the structures of galanin bound to its receptors and G proteins, revealing the molecular basis for allosteric agonism and G protein subtype selectivity.

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 cryo-EM structures of LHCGR in different activation states, revealing a push and pull mechanism of receptor activation and the role of an allosteric agonist.

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 reports the structures of D1R-Gs complex bound to dopamine and LY3154207, revealing mechanisms of dopamine recognition and allosteric modulation for drug discovery.

The paper discovers suramin as a potent inhibitor of SARS-CoV-2 RNA polymerase and provides its structural mechanism for repurposing in treating COVID-19.

This study reports the structure of SARS-CoV-2 RdRp with and without Remdesivir, showing how the drug inhibits viral RNA replication by terminating chain elongation.