Evidence map›Paper›PMID 26387779›Full record

ReviewBioEssays : news and reviews in molecular, cellular and developmental biology2015

How the TRPA1 receptor transmits painful stimuli: Inner workings revealed by electron cryomicroscopy.

Monique S J Brewster, Rachelle Gaudet

Open access · greenAbstract readReview
In one paragraph

Review in BioEssays : news and reviews in molecular, cellular and developmental biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.2field-weighted citation impact, top 14% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

19 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Review
  6. Peripheral Ion Channel Genes Screening in Painful Small Fiber Neuropathy.International journal of molecular sciences · 2022
    Article
  7. Structural Pharmacology of TRP Channels.Journal of molecular biology · 2021
    Review
  8. Article
  9. TRPA1 gene variants hurting our feelings.Pflugers Archiv : European journal of physiology · 2020
    Review
  10. Review
  11. Terpenoids Commonly Found inCannabis and cannabinoid research · 2020
    Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Monique S J BrewsterMolecular and Cellular Biology, Harvard University, Cambridge, MA, USA.
Rachelle GaudetMolecular and Cellular Biology, Harvard University, Cambridge, MA, USA.
Harvard University · US

Funding

Y-FAMILY POLYMERASES AND CO-FACTORS IN TRANSLESION REPLICATIONP41RR015301 · NCRR · CORNELL UNIVERSITY ITHACA · PI DONG, ZIGANG · 2001 to 2011
$28.2M
Structure and Function of TRPV Ion ChannelsR01GM081340 · NIGMS · HARVARD UNIVERSITY · PI GAUDET, RACHELLE · 2008 to 2012
$1.6M
Structure and Biochemistry of TRPA1:a noxious chemical and temperature sensorF31GM109741 · NIGMS · HARVARD UNIVERSITY · PI BREWSTER, MONIQUE SELINA JENNIFER · 2014 to 2015
$56k
NCRR NIH HHS P41 RR015301NIGMS NIH HHS 5-F31-GM-109741NIGMS NIH HHS F31 GM109741NIGMS NIH HHS R01 GM081340
6 · The paper itself

Abstract

A new high-resolution structure of a pain-sensing ion channel, TRPA1, provides a molecular scaffold to understand channel function. Unexpected structural features include a TRP-domain helix similar to TRPV1, a novel ligand-binding site, and an unusual C-terminal coiled coil stabilized by inositol hexakisphosphate (IP6). TRP-domain helices, which structurally act as a nexus for communication between the channel gates and its other domains, may thus be a feature conserved across the entire TRP family and, possibly, other allosterically-gated channels. Similarly, the TRPA1 antagonist-binding site could also represent a druggable location in other ion channels. Combined with known TRPA1 functional properties, the structural role for IP6 leads us to propose that polyphosphate unbinding could act as a molecular kill switch for TRPA1 inactivation. Finally, although packing of the TRPA1 membrane-proximal region hints at a mechanism for electrophile sensing, the details of how TRPA1 responds to noxious reactive electrophiles and temperature await future studies.

Indexed as

Binding SitesCalcium ChannelsCryoelectron MicroscopyHumansNerve Tissue ProteinsPainPhytic AcidProtein BindingProtein Structure, TertiaryTransient Receptor Potential ChannelsTRPA1 Cation ChannelCalcium ChannelsNerve Tissue ProteinsPhytic AcidTransient Receptor Potential ChannelsTRPA1 Cation ChannelTRPA1 protein, humanallosteric gatingankyrin repeatscoiled coilelectron cryomicroscopypolyphosphatestransient receptor potential ion channelsTRP domain

Identifiers

PMID26387779
PMCPMC4862669
OpenAlexW1917163647

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.