Structure modeling, site-directed mutagenesis, and current recordings revealed the mechanism by which stabilization of voltage sensors in the resting and activated states determines the gating properties of the Ca_V1.1 calcium channel.

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.

Charybdotoxin, a toxin produced by scorpions, blocks a K⁺ channel by binding in a lock-and-key fashion to the mouth of the channel and presenting a lysine amino group, which serves as a K⁺ mimic in the selectivity filter.

The intermediate state conformation of the human KCNQ1 potassium channel voltage sensor domain was determined, validated, and shown to be conductive under physiological conditions.

Phosphatidic acid influences the gating of voltage-gated K+ channels through a non-specific surface charge mechanism and through a specific interaction between a voltage sensor arginine and the primary phosphate head group on the cytoplasmic membrane leaflet.

LRRK2 G2019S knock-in mice are a genetically faithful model that recapitulates the slow disease progression of familial PD, with initial alterations to behaviour and neurotransmission providing early pathophysiological targets for neuroprotective interventions.

Tricyclic antidepressants activate lysosomal two-pore Na⁺ channels in a voltage-dependent manner.

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.

ArcLight, a popular optogenetic reporter of voltage, is studied at both single-molecule and macroscopic levels, which leads to new mechanistic understanding and to the rational design of a faster reporter.

Aminoglycosides are a class of antibiotics that can kill Escherichia coli by building up internal voltage through disrupting the normal consumption of ATP.