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.

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

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

Purinergic signaling controls mammalian sperm transport.

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.

CO₂/H⁺-dependent purinergic signaling by astrocytes provides specialized control of vascular tone in a brainstem respiratory center in a manner that contributes to respiratory behavior.

Genetic and biochemical analyses demonstrate that cell-surface lectin receptors can potentially function as extracellular NAD⁺-binding receptors and provide direct evidence for extracellular NAD⁺ being a bona fide endogenous signaling molecule in plants.

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.

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.