Mapping the ion permeation pathway within the internal pore of ATP-activated P2X receptor channels.

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.

Structural insights into the orthosteric inhibition and subtype specificity of P2X receptors by classical P2X antagonists facilitate the rational design of novel competitive antagonists for P2X receptors.

Comparision of current and fluorescent kinetics from P2X7 receptor mutants labeled with the fluorescent amino acid ANAP suggests that the characteristic P2X7 current facilitation involves changes in channel gating rather than interactions or conformational changes of its intracellular ballast domain.

Crystal structures of a mammalian P2X7 receptor and structure-based functional studies reveal a novel drug-binding site and subtype-specific conformational rearrangements required for channel opening.

Functional reconstitution of a mammalian P2X7 receptor uncovers an intrinsic and lipid-dependent dye-permeable membrane pore.

A novel BAC transgenic mouse model reveals glial restriction of P2X7 expression in the central and peripheral nervous systems.

Keratinocytes are critical for normal innocuous and noxious touch through their mechanically evoked ATP release and subsequent signaling to P2X4 channels on sensory neurons.

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.

A murine model of sepsis shows that the purinergic P2X7 receptor controls the release of CD14 in extracellular vesicles playing a key role in cytokine production, bacterial clearance, and survival.