Computational models of gating processes in an ion channel show how stability shifts upon ligand-binding and mutations are reproduced, which highlights mechanistic details and proposes a new role for symmetry in gating.

A combination of molecular dynamics simulations and electron cryomicroscopy characterizes interactions of a pentameric ligand-gated ion channel with 25 lipid molecules, specifically in a functional state in which they were not previously observed.

Development of nanobodies against a model pentameric ligand-gated ion channel demonstrates they can be functionally active as negative or positive allosteric modulators and offers opportunities for future drug development.

The amino terminus of acid-sensing ion channel 1a forms a reentrant 'loop' that frames the lower pore and harbors a conserved 'His-Gly' motif implicated in gating and ion selectivity mechanisms.

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.

Mambalgin1 binds to the thumb domain of human ASIC1a channel and inhibits the channel through hindering the proton-induced transitions from the resting closed state to the active and/or desensitized state.

Polyunsaturated fatty acids enhance desensitization in pentameric ligand-gated ion channels.

Single-particle cryo-EM and electrophysiology studies of the chloride channel TMEM16A reveals the structural basis for anion conduction and uncover its relationship to lipid scramblases of the same family.

Phosphatidylglycerol binding at multiple sites stabilizes the open state relative to the desensitized state of a pentameric ligand-gated ion channel.

Three residues work together as a valve-like mechanism to control desensitization from pre-open and open states in the ion channels ASIC1a, ASIC2a, and ASIC3.