Ka Young Chung

This paper identifies naturally-encoded signaling bias at C5aR1 and C5aR2 receptors through structural and functional analyses, revealing molecular mechanisms underlying biased signaling in GPCRs.

This study identifies an arginine switch mechanism that drives the stepwise activation of β-arrestin through conformational changes induced by GPCR interactions.

This study investigates how ETB couples to different G proteins, finding that it interacts with Gi and Gq but not Gs, with specific regions influencing these interactions.

The paper characterizes the conformational changes in the Gαs protein upon GTP binding and identifies a novel regulator, MAGE D2, using a Bayesian integrative modeling approach.