Evidence map›Paper›PMID 24305161›Full record

ArticleNature2013

TRPV1 structures in distinct conformations reveal activation mechanisms.

Erhu Cao, Maofu Liao, Yifan Cheng, David Julius

Abstract read
In one paragraph

Article in Nature, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 588 papers.

0numbers the graph read from it
0cells of the map it votes in
588citing papers in PubMed
–field-weighted citation impact
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

588 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Review
  8. Article
  9. Temperature and intrinsic CaNature structural & molecular biology · 2026
    Article
  10. TRPV1 antagonism occurs through diverse structural mechanisms.bioRxiv : the preprint server for biology · 2026
    Article
  11. The journal of physical chemistry. B · 2026
    Article
  12. Article
  13. Article
  14. Article
  15. Journal of Zhejiang University. Science. B · 2026
    Review
  16. Article
  17. Article
  18. A Historical Outline of Fluorescence Spectroscopy in Ion Channel Research.Advances in experimental medicine and biology · 2026
    Review
  19. Article
  20. Review

528 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors.

Erhu Cao1] Department of Physiology, University of California, San Francisco, California 94158-2517, USA [2].
Maofu Liao
Yifan Cheng
David Julius

Funding

Structures and gating mechanisms of TRP ion channelsR01GM098672 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI CHENG, YIFAN · 2011 to 2018
$2.6M
Molecular Mechanisms of Receptor and Channel FunctionR01NS047723 · NINDS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI JULIUS, DAVID · 2012 to 2016
$2.2M
Exploiting toxins to probe sensory signalingR01NS065071 · NINDS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI JULIUS, DAVID · 2009 to 2012
$1.3M
GPU Computing Enabled Linux Computer ClusterS10RR026814 · NCRR · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI CHENG, YIFAN · 2010 to 2010
$228k
NCRR NIH HHS S10 RR026814NCRR NIH HHS S10RR026814NIGMS NIH HHS R01 GM098672NIGMS NIH HHS R01GM098672NINDS NIH HHS R01 NS047723NINDS NIH HHS R01NS047723NINDS NIH HHS R01 NS065071NINDS NIH HHS R01NS065071
6 · The paper itself

Abstract

Transient receptor potential (TRP) channels are polymodal signal detectors that respond to a wide range of physical and chemical stimuli. Elucidating how these channels integrate and convert physiological signals into channel opening is essential to understanding how they regulate cell excitability under normal and pathophysiological conditions. Here we exploit pharmacological probes (a peptide toxin and small vanilloid agonists) to determine structures of two activated states of the capsaicin receptor, TRPV1. A domain (consisting of transmembrane segments 1-4) that moves during activation of voltage-gated channels remains stationary in TRPV1, highlighting differences in gating mechanisms for these structurally related channel superfamilies. TRPV1 opening is associated with major structural rearrangements in the outer pore, including the pore helix and selectivity filter, as well as pronounced dilation of a hydrophobic constriction at the lower gate, suggesting a dual gating mechanism. Allosteric coupling between upper and lower gates may account for rich physiological modulation exhibited by TRPV1 and other TRP channels.

Indexed as

Models, MolecularAnimalsMutationProtein Structure, TertiaryRatsTRPV Cation ChannelsTrpv1 protein, ratTRPV Cation Channels

Identifiers

PMID24305161
PMCPMC4023639

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.