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

Conformational motions elicited by antagonists, partial agonists, and agonists in serotonin-gated ion channels 5-HT_3AR progressively spread from the extracellular to the transmembrane domain.

A fluorometric analysis under voltage clamp shows the presence of a converged electric field in P2X2 channel with no canonical voltage-sensor and identifies the structural determinants for the voltage-dependent gating.

A powerful new fluorescence approach elucidates the structural mechanism for a specialized ion channel behavior important for cardiac and neuronal excitability.

Because voltage-gated KCNQ2 channels are central to physiological and pathophysiological events, understanding how disease-causing mutations in different channel regions disrupt function will help future development of mutation-specific antiepileptic therapies.

Fatty acid analogues are interesting prototype compounds that may inspire the development of future I_Ks channel activators to treat patients with long QT syndrome caused by diverse arrhythmia-causing mutations in the I_Ks channel.

Transmembrane protein 266 contains a functional S1-S4 voltage-sensing domain that is regulated by extracellular Zn²⁺ ions.

Allosteric modulation of BK channels, vital for the physiology of nerve, muscle and endocrine cells, is determined by direct coupling between gating ring RCK1 domains and the voltage sensor function.

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.

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.