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.

Contrary to a generally accepted principle, the pore properties of KCNQ1 channels depend on the states of voltage-sensing domains activation; KCNE1 alters the voltage-sensing domains-pore coupling to modulate KCNQ1 channel properties.

Experimental measurement of the trajectory of gating charge surrogates during voltage activation and deactivation in a voltage sensor.

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.

Tuning the strength of inter- and intra-subunit hydrogen bonds can control potassium flux across biological membranes.

Interactions between the voltage sensor and intracellular domains modulate voltage-dependent gating and calmodulin inhibition in the voltage-gated potassium channel Eag1.

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.

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.

Melanopsin phototransduction targets distinct complements of transduction channels across intrinsically photosensitive retinal ganglion cell subtypes and does not require hyperpolarization-activated cyclic nucleotide-gated channels.

High-speed calcium imaging from the axon initial segment shows that sodium channels are in part permeable to calcium ions.