Xiangyu Liu

The paper reports cryo-EM structures of melanocortin receptors bound to endogenous inverse agonists, revealing mechanisms of inverse agonism and subtype selectivity.

The paper presents a cryo-EM structure of the dopamine D2 receptor bound to a non-basic ligand, revealing structural dynamics and binding energy landscapes that explain subtype selectivity.

This paper introduces a de novo design strategy called 'click fusion' to create stable GPCR fusion proteins, enabling structural studies via cryo-EM.

This study determines the structure of mouse BOCT1 and reveals its function as an independent iron transporter using cryo-EM and functional assays.

The paper stabilizes GPCRs in specific conformations using a fusion protein and screens nanobodies to identify conformation-specific binders.

This paper identifies atazanavir as a pan-positive allosteric modulator that activates multiple Family A GPCRs and sustains G protein signaling through non-canonical mechanisms.

This study determines the structure of a GPCR-G protein-β-arrestin complex stabilized by an allosteric modulator, showing a novel binding mode that allows coexistence with G protein signaling.