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Electrophysiological and computational techniques provide a structural basis for understanding the conformational changes that are required to activate Hv1 proton channels.

PIP₂ inhibits the proton-activated chloride (PAC) channel by selectively stabilizing its desensitized state.

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.

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.

Asp234 is deprotonated in the ground state and forms the proton transfer pathway that proceeds from the Schiff base toward Glu68 in the intermediate state of the anion channelrhodopsin GtACR1.

Analysis of conformational changes indicates that activation of acid-sensing ion channels involves protonation of diverse extracellular sites and interaction of interdomain loops with the upper ends of transmembrane helices.

Single-molecule F₁F_O studies show mutation-dependent pKa changes of both F_O half-channels, and proton translocation-dependent 11° ATP synthase-direction sub-steps, which support a Grotthuss proton transfer-dependent two-step F_O torque generating mechanism.

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 X-ray structure of the PaNhaP provides a unique view of substrate-ion binding and release in electroneutral sodium/proton antiporters.

Mitochondrial Cx43 hemichannels regulate ATP generation by mediating K+, H+, and ATP transfer across the mitochondrial inner membrane and the interaction with mitochondrial ATP synthase, contributing to maintenance of mitochondrial redox and cell protection under oxidative stress.