R. Dutzler

Structural features of heteromeric channels composed of CALHM2 and CALHM4 paralogs

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

Structural and functional properties of the transporter SLC26A6 reveal mechanism of coupled anion exchange

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.

Structural and functional properties of a plant NRAMP related aluminum transporter

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+.

Structures of ferroportin in complex with its specific inhibitor vamifeport

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

Structure of a volume-regulated heteromeric LRRC8A/C channel

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

Structural and functional properties of a magnesium transporter of the SLC11/NRAMP family

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.

Cryo-EM structures of the Caspase activated protein XKR9 involved in apoptotic lipid scrambling

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

Cryo-EM structures and functional properties of CALHM channels of the human placenta

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.

Stepwise activation mechanism of the scramblase nhTMEM16 revealed by cryo-EM

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

Cryo-EM structures and functional characterization of the lipid scramblase TMEM16F

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.