Loss of potassium channel activity from fast-spiking interneurons increases their excitability leading to unexpectedly increased fast excitatory transmission and seizure susceptibility.

Serotonin neurons in chronically isolated mice become less responsive to excitatory stimulation, but inhibiting a distinctive calcium-activated potassium channel can restore both neuronal activity and behavior.

Highly temperature-sensitive behavior of voltage-gated potassium channels provides a mechanistic model for how heat-activated TRP channels serve as temperature and pain sensors.

Potassium ions enter and leave human sperm cells via a calcium-dependent ion channel that is also pH-independent.

The mammalian potassium channel KCa3.1, which is important for T- and B-cell activation, is inhibited by cytoplasmic copper, mediated by a histidine residue (His358) that is phosphorylated to activate the channel.

Type 1 potassium channels alter their composition and localisation to suppress hyper-excitability and neuropathic pain of injured sensory neurons.

Expression of the isolated voltage sensing domain significantly alters its structural conformation as well as its gating kinetics, indicating the importance of studying the biological assembly in its entirety.

Single-particle cryo-electron microscopy reveals the first subnanometer structure of ATP-sensitive potassium (K_ATP) channels, which provides insight into the structural mechanisms of channel assembly and gating.

The pseudokinase protein SCYL1 is an evolutionarily conserved enhancer of Slo2 potassium channel activity.

The structure of a voltage-activated potassium channel in lipid nanodiscs solved using cryo-electron microscopy is similar to previous X-ray structures, and provides insights into the mechanism of C-type inactivation.