The structure of the membrane-integrated components of a unique substrate decarboxylation-driven primary-active sodium pump provides insights into its transport mechanism.

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

Dysfunction and overexpression of ENaC-mediated sodium influx exacerbates activation of NLRP3-inflammasome mediated inflammation in cells with CF-associated mutations and is modulated by inhibition of these amiloride-sensitive sodium (Na⁺) channels.

In potassium-dependent NTPases, insertion of the activating potassium ion into the active site leads to rotation of the gamma-phosphate yielding a near-eclipsed, catalytically productive conformation of the triphosphate chain.

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

Sodium ions control the rates of both substrate binding and dissociation of an archaeal homologue of glutamate transporters in a manner that minimizes binding intermediates and maximizes transport efficiency.

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

Transient Ca elevations of cytoplasmic calcium in cardiac myocytes profoundly activate cardiac Na/K pump activity in parallel with physical-chemical changes of the sarcolemma but without involvement of conventional signaling mechanisms.

After summarizing over 2,400 articles in plain language, the eLife Features team shares what it has learnt about writing and editing for a broad audience.

The way that bacteria grow—either floating in liquid or attached to a surface—affects their ability to evolve antimicrobial resistance and our ability to treat infections.