Xinheng He

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.

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 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 determines the cryo-EM structure of QRFPR bound to 26RFa, revealing the recognition mechanism and aiding drug design for obesity and diabetes.

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

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

AI2BMD efficiently simulates large biomolecules with ab initio accuracy, outperforming DFT in speed while maintaining chemical accuracy for dynamics and free energy calculations.

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

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.

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 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.