For channel aficionados, this is a familiar story, so what is different about the TRPA1 structure? Paulsen and colleagues find that around 80% of TRPA1's mass is outside the channel's core ...

TRPA1 receptor proteins form pores called ion channels in sensory nerve cell membranes. These channels, normally closed, open in response to certain chemical signals, which allows ions to pass into ...

Though scientific knowledge of TRPA1’s roles in detecting sensations, both positive and negative, has been developing for at least a decade now, the April 2015 discovery of its structure represents a ...

So the researchers decided to give it a try on TRPA1, and it worked. "The big advance here is that we can actually see the structure of the molecule — we can see the atoms in the molecule ...

TRPA1 receptor proteins form pores called ion channels in sensory nerve cell membranes. These channels, normally closed, open in response to certain chemical signals, which allows ions to pass into ...

Proposed model for how acetic acid might activate the ion channel TRPA1. A new study in the Journal of General Physiology identifies TRPA1 as the sensor in animals responsible for identifying weak ...

Transient Receptor Potential Ankyrin 1 (TRPA1) is a non-selective cation channel that is expressed in a subset of nociceptive afferent sensory nerves. When activated, TRPA1 can evoke nociceptive ...

“The days of just getting one structure and publishing a paper are over. Now we have the technology to tell complex, interesting stories about the molecular machines that make our cells function.” In ...

9,951,046 covering the company’s novel, small molecule modulators of TRPA1 as well as compositions and methods for treating pain that include the compounds. The patent has a term extending to ...

In humans, TRPA1 is activated by allyl isothiocyanate ... They also have pits but theirs are spread across their snouts, are simpler in structure and have fewer nerve connections.