Development of specific and high-affinity nanobodies to probe the structure of human acid sensing ion channel-1a and as binding modifiers of the toxins PcTx and MitTx1.

Mouse brain neurons response to transcranial ultrasound at the energy level of 5 mW/cm² and repeated stimulations lead to neurogenesis while ASIC1a is required both in vitro and in vivo as one of the mechanoreceptors.

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.

An interaction between the ion channel ASIC1a and the protein RIP1 is responsible for neuronal death caused by tissue acidosis.

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.

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.

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

The tarantula toxins psalmotoxin and guangxitoxin have a similar concave surface for interacting with α-helices in voltage-gated and acid-sensing ion channels.

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.

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.