A combined systematic alanine scanning and molecular modelling approach reveals the molecular basis for an allosteric inhibition mechanism of K⁺-flux gating in K_2P channels.

Structural and functional studies of a potassium ion channel that is opened and closed by different ligands have revealed a novel gating mechanism.

Cations are essential cofactors in the ATP activation mechanism of the KtrAB cation channel and appear to be cofactors of many other nucleotide-dependent RCK domains.

Calcium release from the endoplasmic reticulum through the IP₃ receptor ion channel is strongly regulated by a calcium-binding protein in the lumen of the endoplasmic reticulum.

A cryo-electron microscopy study of the human CLC-1 chloride ion channel reveals the structural basis of why some CLC proteins function as passive chloride channels whereas others function as an active proton-chloride antiporters.

Nramp-family transporters adapt a common fold to a novel mechanism in which the spatial and temporal separation of like-charge transition metal and proton co-substrates circumvents the expected electrostatic repulsion.

Mathematical analyses explore the impact of co-substrate cycling on the dynamics of cellular metabolism, and demonstrate that these dynamics can limit cellular fluxes and that co-substrate pool dynamics can be regulated to regulate fluxes.

Visualization of the real-time conformational transitions of the human voltage-gated proton channel hHv1 provided novel insights into how voltage and pH gradients modify the dynamic behaviors of channel structures to control proton flow across membrane.

An unbiased model for the self-organisation of the Golgi apparatus displays either anterograde vesicular transport or cisternal maturation depending on ratios of budding, fusion and biochemical conversion rates.

The role of lysosomal Ca²⁺ flux associated with K⁺ efflux, a well-known event in inflammasome activation in metabolic inflammation and inflammasome activation, has been presented.