R. B. Stockbridge

This study examines how bacterial SMR transporters handle metformin metabolites, showing they efficiently export guanylurea and providing insights into their function and potential role in microbial adaptation.

The paper develops a method to overexpress, purify, and reconstitute the lysine transporter Ypq1 in yeast vacuoles, demonstrating its pH-gated transport function and lysine-dependent stability.

This study investigates the dimerization mechanism of the inverted-topology fluoride channel Fluc, showing that membrane forces drive assembly while Na+ binding activates the channel.

The paper determines crystal structures of EmrE, a bacterial SMR transporter, in complex with various substrates, revealing structural flexibility in the binding site.

This study identifies fluoride binding sites and anion recognition mechanisms in Fluc family channels using structural and electrophysiological methods.