A painful trp can be a bonding experience.
The receptive field of the TRPA1 nociceptor is remarkably expansive when compared to other chemodetectors such as odorant receptors. The identification of a unique mechanism utilized by TRPA1 helps clarify how this protein can efficiently alert the cell to an array of reactive chemical agents, regardless of their structure.
Peterlin
Zita
Z
Department of Biological Sciences, Columbia University, New York, NY 10027, USA.
Chesler
Alexander
A
Firestein
Stuart
S
D000818:Animals; D017487:Ankyrins; D015220:Calcium Channels / Q000737:chemistry* / Q000502:physiology*; D006801:Humans; D009619:Nociceptors / Q000502:physiology*; D009812:Odorants; D010146:Pain / Q000503:physiopathology; D051381:Rats; D018035:Receptors, Odorant / Q000737:chemistry* / Q000502:physiology*; D013268:Stimulation, Chemical; D000074025:TRPA1 Cation Channel; D050052:TRPC Cation Channels
D017487:Ankyrins; D015220:Calcium Channels; D018035:Receptors, Odorant; D000074025:TRPA1 Cation Channel; D050052:TRPC Cation Channels; C480976:Trpa1 protein, rat