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.

A comprehensive functional analysis of mitochondrial Ca²⁺ uniporter (MCU) demonstrates that the auxiliary MICU subunits potentiate Ca²⁺ transport via MCU.