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.

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

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.

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

Analysis of iconic and gating currents of wild type and mutated BK channels reveals a strong inhibition of this channel by extracellular acidification and elucidates the underlying mechanism that is potentially applicable to other voltage-dependent cation channels.

A combined systematic alanine scanning and molecular modelling approach reveals the molecular basis for an allosteric inhibition mechanism of K⁺-flux gating in K_2P channels.

Gating currents analysis at different Ca²⁺ concentrations of BK channels reveals a strong allosteric coupling between Ca²⁺- and voltage-sensing modules via equivalent contributions exerted by the RCK1 and RCK2 Ca²⁺-sites.

NG2 glial cells respond to synaptic input with calcium signals in the absence of action potentials and process synaptic depolarizations with somatic and dendritic voltage gated channels.

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