Show‐Ling Shyng

This study uses cryoEM to reveal MgATP/MgADP-dependent conformational changes and IDR organization in vascular KATP channels.

The paper identifies seven new SUR1 mutations in HI patients that impair KATP channel trafficking and function, showing varied responses to pharmacochaperone rescue.

The paper identifies a novel KATP channel pharmacochaperone, Aekatperone, using AI screening and cryoEM, showing reversible inhibition and functional recovery of trafficking mutants.

This study reveals how pharmacochaperones stabilize KATP channels by binding to SUR1 and supporting Kir6.2 N-terminus insertion, enabling mutant channel assembly.