The gating polarity of a voltage-gated ion channel is primarily determined by turn propensity of residues at a critical position in the middle of the S4 voltage-sensing helix.

Intracellular NASPM, unlike the widely used spermine, fully blocks outward currents through calcium-permeable AMPA-type glutamate receptors, enabling an improved functional readout for this physiologically important receptor subtype in neurons.

Ion conduction in the calcium-activated chloride channel TMEM16A is directly regulated by calcium, which binds to a site close to the pore thereby shaping the electrostatics at its intracellular entrance.

When artificial networks modeled on a Drosophila neuron are tasked with discriminating objects on collision course from other visual scenes, their optimized solutions reproduce many functional features of the original loom-selective neuron.

Outward calcium ion currents desensitize the human PKD2-L1 ion channel via a mechanism that is independent of cytosolic motifs.

A combination of high-resolution structure determination, electrophysiology, and MD simulations reveal fundamental insight into the molecular function of voltage-gated chloride channels.

The cryo-EM structure and functional characterization of the chloride-selective ion transporter Slc26a9 defines its oligomeric architecture and transport mechanism.

The molecular identity of the temperature-sensitive ion channel of human sperm that ensures depolarization is TRPV4.

Building on previous work (Huang et al., 2016), we show that translational control by p-eIF2α is a defense mechanism that prevents persistent cocaine-induced synaptic synaptic potentiation underlying compulsive drug seeking.

Whole endosome recording shows that chloride interacts with vesicular glutamate transporters as both allosteric activator and permeant ion, and although the mode of permeation differs, chloride and glutamate use a related conduction pathway.