Lihua Zhao

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

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

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 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.

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.