Evidence map›Paper›PMID 24305160›Full record

ArticleNature2013

Structure of the TRPV1 ion channel determined by electron cryo-microscopy.

Maofu Liao, Erhu Cao, David Julius, Yifan Cheng

Open access · bronzeAbstract 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 920 papers.

0numbers the graph read from it
0cells of the map it votes in
920citing papers in PubMed
81.9field-weighted citation impact, top 1% 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

920 citing papers in PubMed, 1,710 citations in OpenAlex.

  1. Trial
  2. Review
  3. An Extracellular Pore‑Targeting Peptide Defines a Designable Allosteric Site in TRPV2.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  4. Article
  5. Review
  6. eLife · 2026
    Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. Supercritical COPharmaceutics · 2026
    Article
  17. Article
  18. Review
  19. Article
  20. A novel role for TRPV1 in macrophage giant cell formation.bioRxiv : the preprint server for biology · 2026
    Article

860 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 at 1 institution in 1 country.

Maofu Liao1] Keck Advanced Microscopy Laboratory, Department of Biochemistry and Biophysics, University of California, San Francisco, California 94158-2517, USA [2].
Erhu Cao
David Julius
Yifan Cheng
University of California, San Francisco · US

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 sensors for a wide range of cellular and environmental signals, but elucidating how these channels respond to physical and chemical stimuli has been hampered by a lack of detailed structural information. Here we exploit advances in electron cryo-microscopy to determine the structure of a mammalian TRP channel, TRPV1, at 3.4 Å resolution, breaking the side-chain resolution barrier for membrane proteins without crystallization. Like voltage-gated channels, TRPV1 exhibits four-fold symmetry around a central ion pathway formed by transmembrane segments 5-6 (S5-S6) and the intervening pore loop, which is flanked by S1-S4 voltage-sensor-like domains. TRPV1 has a wide extracellular 'mouth' with a short selectivity filter. The conserved 'TRP domain' interacts with the S4-S5 linker, consistent with its contribution to allosteric modulation. Subunit organization is facilitated by interactions among cytoplasmic domains, including amino-terminal ankyrin repeats. These observations provide a structural blueprint for understanding unique aspects of TRP channel function.

Indexed as

Cryoelectron MicroscopyModels, MolecularAnimalsAnkyrin RepeatHEK293 CellsHumansProtein Structure, TertiaryRatsTRPV Cation ChannelsTrpv1 protein, ratTRPV Cation Channels

Identifiers

PMID24305160
PMCPMC4078027
OpenAlexW2164659462

What OpenQuestion holds

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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.