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.

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.

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

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

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 voltage-sensing mechanism of a subfamily of potassium channels is modulated in unconventional ways by an amino acid transporter.

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

L-amino acids are agonists of calcium-sensing receptor, and act jointly with calcium and phosphate ions to control receptor function.

Receptor recognition of antimicrobial peptides is important for Salmonellae to survive inside macrophages and cause disease.