A structure of a pancreatic ATP-sensitive potassium channel complex at 3.63Å resolution obtained by cryo-electron microscopy reveals how a commonly used anti-diabetic drug interacts with and inhibits the channel to stimulate insulin secretion.

Simultaneous measurements of ligand binding and channel currents are used to understand gating of the ATP-sensitive K⁺ channel.

A combined FRET- and electrophysiology-based approach is used to study ATP/ADP ADP binding to the stimulatory nucleotide binding site of ATP-sensitive K+ channels and investigate their activation mechanism.

The functional interaction of Na⁺ and K_ATP channels at the intercalated disk of cardiomyocytes depends on Ankyrin G and is clinically relevant since K_ATP channel mutations affect Na⁺ channel expression.

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.

Altered activity of ATP-sensitive K⁺ channels underlies the metabolic seizure resistance produced by genetic manipulation of the BAD protein in mice.

Structural, computational and functional approaches reveal the role of an extended acidic chamber near the nucleotide binding site in activation of P2X3 receptor channels by divalent-bound ATP.

Diverse K_ATP channel inhibitors occupy a common binding pocket and stabilize an interaction between Kir6.2 and SUR1 to allosterically control gating and promote the assembly and trafficking of nascent channels.

The gating mechanism of trimeric ATP-gated P2X receptors has been explored using photo-switchable cross-linkers, via a versatile strategy that could be applied to other membrane proteins.

Purified Pannexin 1 channels activated by caspase cleavage in proteoliposomes reconstitute a permeation pathway for intercellular signaling molecules important in inflammation and cell clearance.