The activation and membrane localization of the broadly-tuned noxious chemosensory cation channel TRPA1 are regulated by direct interactions with cholesterol via CRAC motifs in transmembane segments 2 and 4.

A pain-relaying ion channel on a hypersensitive population of sensory neurons can instead elicit sensations of itch in both fish and mice when directly activated, providing a novel model of itch transduction.

Joint sequence, structure, and phylogenetic analyses identify highly conserved features in transmembrane domains of transient receptor potential (TRP) ion channel proteins that offer a novel explanation for how TRPs could integrate stimuli into cellular signals.

Electron-donating nucleophilic compounds activate TRPA1 ion channels in fruit flies and mosquitoes, but not humans, making TRPA1 a promising target for insect repellants.

Acute hypoxia activates TRPA1 channels in cerebral artery endothelial cells to activate an early adaptive response to reduce tissue ischemic damage through vasodilation.

In response to tissue damage, reactive oxygen species can be sensed by cation channels TRPA1/RyR to cause increases of cytosolic Ca²⁺ in intestinal stem cells, activating Ras/MAPK activity and stimulating stem cell proliferation in Drosophila.

Single-molecule measurement of conformational dynamics using a genetically encoded fluorescent probe suggests that the selectivity filter region of TRPV1 channels undergoes dynamic motion during agonist activation.

Fruit flies can taste and avoid food contaminated with a bacterial toxin using the same channel protein that functions in humans as sensor of noxious chemical stimuli.

An atomic model of the 3744-residue Tra1 protein reveals multiple transcription activator binding sites, its integration within the SAGA chromatin coactivator complex, and a striking similarity to DNA-repair factor DNA-PKcs.

Cytosolic and organellar Hsp90s from higher eukaryotes have evolved a variable, and environmentally responsive N-terminal extension to regulate their activity.