R. Dutzler

This study investigates whether CALHM2 and CALHM4 form heteromers and characterizes their structural properties.

The paper determines the structure of human SLC26A6 and identifies it as a coupled chloride-bicarbonate exchanger, revealing structural differences that explain its anion selectivity and coupling mechanism compared to SLC26A9.

The paper investigates the structural and functional properties of a plant NRAMP-related aluminum transporter from Setaria italica, showing its ability to transport divalent and trivalent metal ions and its unique binding site for Al3+ and Ga3+.

This study presents cryo-EM structures of ferroportin bound to vamifeport and nanobodies, revealing conformational changes and the inhibitor's binding site.

This study determines the structure of a heteromeric LRRC8A/C channel, revealing its unique organization and activation mechanism.

The paper characterizes a magnesium transporter from the SLC11/NRAMP family in prokaryotes, showing it transports Mg2+ and Mn2+ without H+ coupling and reveals its structural features.

The paper presents cryo-EM structures of XKR9, a lipid scramblase, showing its monomeric architecture and activation mechanism via caspase cleavage.

The paper investigates CALHM channels in the human placenta, identifying their expression patterns and structural differences, and links these to functional properties and lipid distribution.

This study uses cryo-EM to reveal the stepwise activation mechanism of nhTMEM16, showing how Ca2+-binding induces conformational changes that facilitate lipid scrambling.

This study presents cryo-EM structures of TMEM16F in different states and shows how its function as a lipid scramblase and ion channel relates to conformational changes.