The X-ray structure of the PaNhaP provides a unique view of substrate-ion binding and release in electroneutral sodium/proton antiporters.

The inward-open and outward-open structures of MjNhaP1 explain the mechanism of electroneutral sodium-proton antiport across the cell membrane.

Sodium ions but not protons induce defined helix movements in a sodium/proton antiporter and suggest a mechanism for Na + binding and transport.

The manner in which protons control the conformational behaviour of mammalian peptide transporters is revealed through state-of-the-art molecular dynamics simulations supported by cell-based assays.

Proton channels are present in reef-building corals and constitute important molecular players that should help understand calcification and the response of these organisms to ocean acidification.

A viral heliorhodopsin from Emiliania huxleyi virus 202 (V2HeR3) is a light-activated proton transporter, which has the potential to depolarize the host cells by light, possibly to overcome the host defense mechanisms or to prevent superinfection.

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.

The autophagy protein ATG2A tethers membranes and transfers lipids between them, suggesting that autophagosome membranes grow upon the acquisition of lipids from the ER through the ATG2A bridge.

The primary respiratory defect seen in aged cardiomyocytes is an elevated proton leak mediated by ANT1, and this is prevented by treatment with SS-31 (elamipretide).

Crystal structures provide structural rationales for the transport stoichiometry of the gastric proton pump, which suffices the energy requirement for the generation of a million-fold proton gradient across the membrane.