title: A painful trp can be a bonding experience.
abstract: 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.
authors.affiliation: Department of Biological Sciences, Columbia University, New York, NY 10027, USA.
authors.forename: Zita
authors.initials: Z
authors.lastname: Peterlin
authors.forename: Alexander
authors.initials: A
authors.lastname: Chesler
authors.forename: Stuart
authors.initials: S
authors.lastname: Firestein
mesh_terms: 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
chemical_list: D017487:Ankyrins; D015220:Calcium Channels; D018035:Receptors, Odorant; D000074025:TRPA1 Cation Channel; D050052:TRPC Cation Channels; C480976:Trpa1 protein, rat