The structure of a pannexin 1 uncovers the extracellular loops of pannexin 1 as important structural motifs for ion selectivity and channel inhibition.

Endothelial pannexin 1-P2Y2 purinergic receptor-TRPV4 channel signaling, facilitated by caveolin-1, is a novel pathway for lowering pulmonary arterial pressure.

Cleavage of pannexin-1 channel by caspases facilitates the loss of intracellular ATP level and attenuates glycolytic metabolism of apoptotic cells.

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

A comprehensive analysis questioned the prevailing views of Src-mediated hPANX1 phosphorylation at Tyr199 and Tyr309.

The structure of pannexin 1, a channel protein with a large pore, has been determined for the first time.

Mutated NLRP3 forms cryo-sensitive aggregates that induce inflammasome assembly distinct from the canonical NLRP3 inflammasome.

Apoptotic cells release molecules to recruit macrophages, but do not cause inflammation because they also secrete AMP that functions as a ‘calm down’ signal.

An in silico analysis of gap junction proteins supports the hypothesis that connexins replaced the primordial innexins in chordate gap junctions due to an evolutionary bottleneck.

The innexin protein UNC-7, a homologue of vertebrate pannexins, plays a specific, gap junction-independent role in C. elegans mechanosensation.