D. H. Brotherton

The paper shows that mutating K125 in Cx26 to glutamate mimics CO2 regulation, causing gap junctions to remain closed, and reveals structural changes in Cx26 that explain this regulation.

This study determines the crystal structure of a BASS transporter in complex with pantoate, revealing how substrate binding is coupled to sodium ion binding and transport through conformational changes.

The paper solves the crystal structure of CodB, a cytosine transporter, and compares it to Mhp1 to elucidate substrate transport mechanisms in the NCS1 family.

This study shows CO2 directly affects Connexin26 gap junctions by inducing conformational changes that regulate channel gating.