Expression of the appropriate repertoire of membrane channels, essential for activity of flight-promoting central dopaminergic neurons of Drosophila, requires store-operated Ca²⁺ entry during late pupal development and early adults.

The spider venom peptide Pn3a recognizes a pharmacophore unique to Ca_V3.3 amongst T-type calcium channels, underscoring its potential as a novel molecular tool for the study of Ca_V3.3-mediated currents in native cells.

Chromosomal instability of cancer can be quantitatively measured by phylogenetic analysis of 200 tumor cells while using evolutionary principles to account for cellular selection.

A peptide toxin with therapeutic potential in stroke and pain induces multiple long-lasting conformational changes in acid-sensing ion channels and affects how the channels respond to endogenous ligands.

HiLITR is a molecular reporter of protein localization that enables straightforward, large-scale, fluorescence-activated cell sorting-based discovery of genes that regulate complex cellular processes, such as mitochondrial and ER tail-anchored protein trafficking.

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 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.

The TRPV1, TRPV2 and TRPV3 channels are gated on the cytosolic side of the pore, whereas structural changes in the ion selectivity filter associated with activation don't control cation access.

A facile method is implemented to modify membrane proteins with biophysical reporters using cysteine-independent approaches in live cells.

Charybdotoxin, a toxin produced by scorpions, blocks a K⁺ channel by binding in a lock-and-key fashion to the mouth of the channel and presenting a lysine amino group, which serves as a K⁺ mimic in the selectivity filter.