Jue Chen

The paper systematically identifies effector functions of pathogen ORFs across multiple pathways, revealing new roles for known effectors and uncharacterized proteins.

This study uses single-molecule magnetic tweezers to analyze CFTR folding defects and shows pharmacological correctors reshape the folding energy landscape by catalyzing transitions.

This study reports cryo-EM structures of TAP in multiple functional states, revealing how nucleotide-dependent conformational changes drive peptide transport and release.

This study reports cryo-EM structures of TAP inhibited by four viral proteins, revealing a common mechanism to block antigen presentation.

This study determines the cryo-EM structures of MRP2 in three conformational states, revealing its transport mechanism and substrate recognition.

This study presents cryo-EM structures of PKA-C bound to CFTR, revealing mechanisms of phosphorylation and reversible activation through catalytic interactions and conformational flexibility.

This paper determines the structure of CFTR bound to CFTRinh-172 using cryo-EM, revealing its dual role as a pore blocker and gating modulator.

This study identifies the structure of the CFTR selectivity filter, revealing a chloride-binding site that defines ion selectivity and conductance.

The paper identifies novel CFTR modulators using molecular docking, electrophysiology, cryo-EM, and medicinal chemistry, discovering potentiators and inhibitors with mid-nanomolar activity.