Research into light-gated ion channels called channelrhodospins laid the foundations for the development of optogenetics, a technique that has gone on to revolutionize neuroscience.

Structural and functional analysis of a recently discovered non-canonical potassium channel family reveals a unique selectivity filter that is exposed to permeating ions only in the conductive state.

High-speed atomic force microscopy reveals that the open state of the divalent ion channel CorA is highly dynamic and defined by the fast exchange between conformations.

The TRPV1, TRPV2 and TRPV3 channels are gated on the cytosolic side of the pore, whereas structural changes in the ion selectivity filter associated with activation don't control cation access.

The gating polarity of a voltage-gated ion channel is primarily determined by turn propensity of residues at a critical position in the middle of the S4 voltage-sensing helix.

TMEM16F shifts its ion selectivity in response to change of intracellular Ca²⁺, membrane potential and ionic strength.

The molecular identity of the temperature-sensitive ion channel of human sperm that ensures depolarization is TRPV4.

Electrophysiological experiments, Ca²⁺ imaging, and behavioral studies in mice identify the TRPM3 ion channel as a novel target of G-protein βγ subunits.

Optogenetic tools enable sophisticated measurements of a voltage-gated sodium channel implicated in pain, as well as high-throughput screening of candidate channel blockers.

Efflux of xenobiotic fluoride from microorganisms occurs through a novel family of ion channels with stringent selectivity for fluoride ion and dual-topology molecular architecture.