The amino terminus of acid-sensing ion channel 1a forms a reentrant 'loop' that frames the lower pore and harbors a conserved 'His-Gly' motif implicated in gating and ion selectivity mechanisms.

Mambalgin1 binds to the thumb domain of human ASIC1a channel and inhibits the channel through hindering the proton-induced transitions from the resting closed state to the active and/or desensitized state.

Three residues work together as a valve-like mechanism to control desensitization from pre-open and open states in the ion channels ASIC1a, ASIC2a, and ASIC3.

The rotation of the β11-12 linker is a crucial control point for acid-sensing ion channel gating and motion of this linker is required for the channel to desensitize.

Two acid-sensing members of the degenerin/epithelial sodium channel family play distinct roles in controlling different aspects of rhythmic proton and calcium oscillations in the nematode intestine.

The cytosolic elements of the acid-sensing ion channel move toward the plasma membrane when the channel is exposed to acidic conditions.

Expression patterns and biophysical properties of acid-sensing ion channels in numerous bilaterian animals offer insight into the deployment of ion channels by the evolving nervous system in complex animals.

A novel FRET approach suggests that the intracellular termini of acid-sensing ion channel 1a do not form a complex at rest requiring a new hypothesis for ASIC1a involvement in stroke.

A peptide toxin with therapeutic potential in stroke and pain induces multiple long-lasting conformational changes in acid-sensing ion channels and affects how the channels respond to endogenous ligands.

Sodium selectivity of acid-sensing ion channels is mediated by negatively charged side chains and not by a size-exclusion mechanism.