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

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.

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

Structural and functional analysis of a recently discovered non-canonical potassium channel family reveals a unique selectivity filter that is exposed to permeating ions only in the conductive state.

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 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.

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.

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

Changing substituents on the aromatic rings of polyunsaturated fatty acid analogues tailors their activation effect on the I_Ks channel and thus their therapeutic potential for long QT syndrome.