Evidence map›Paper›PMID 29279388›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2018

Heat activation is intrinsic to the pore domain of TRPV1.

Feng Zhang, Andres Jara-Oseguera, Tsg-Hui Chang, Chanhyung Bae, Sonya M Hanson, Kenton J Swartz

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
4.3field-weighted citation impact, top 5% 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

59 citing papers in PubMed, 86 citations in OpenAlex.

  1. Article
  2. Article
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  4. Review
  5. Journal of Zhejiang University. Science. B · 2026
    Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Protein dynamics underlies strong temperature dependence of heat receptors.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  13. Article
  14. Article
  15. Article
  16. Dilation of ion selectivity filters in cation channels.Trends in biochemical sciences · 2024
    Review
  17. Review
  18. Article
  19. A suicidal mechanism for the exquisite temperature sensitivity of TRPV1.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  20. Review
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

6 authors at 2 institutions in 1 country.

Feng ZhangMolecular Physiology and Biophysics Section, Porter Neuroscience Research Center, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892.
Andres Jara-OsegueraMolecular Physiology and Biophysics Section, Porter Neuroscience Research Center, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892.
Tsg-Hui ChangMolecular Physiology and Biophysics Section, Porter Neuroscience Research Center, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892.
Chanhyung BaeMolecular Physiology and Biophysics Section, Porter Neuroscience Research Center, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892.
Sonya M HansonMolecular Physiology and Biophysics Section, Porter Neuroscience Research Center, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892.
Kenton J SwartzMolecular Physiology and Biophysics Section, Porter Neuroscience Research Center, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892 Kenton.Swartz@nih.gov.
National Institutes of Health · USNational Institute of Neurological Disorders and Stroke · US

Funding

Gating mechanisms and pharmacology of voltage-activated ion channelsZIANS002945 · NINDS · NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE · PI SWARTZ, KENTON · 2009 to 2025
$44.2M
PROBING THE STRUCTURE AND FUNCTION OF POTASSIUM AND CALCIUM CHANNELSZ01NS002945 · NINDS · NEUROLOGICAL DISORDERS AND STROKE · PI SWARTZ, KENTON J · 1997 to 2008
$1.9M
Mechanisms of TRPV1 channel gating and modulation by temperature and vanilloidsR00NS101053 · NINDS · UNIVERSITY OF TEXAS AT AUSTIN · PI JARA OSEGUERA, ANDRES · 2021 to 2023
$745k
Intramural NIH HHS Z01 NS002945NINDS NIH HHS K99 NS101053NINDS NIH HHS R00 NS101053
6 · The paper itself

Abstract

The TRPV1 channel is a sensitive detector of pain-producing stimuli, including noxious heat, acid, inflammatory mediators, and vanilloid compounds. Although binding sites for some activators have been identified, the location of the temperature sensor remains elusive. Using available structures of TRPV1 and voltage-activated potassium channels, we engineered chimeras wherein transmembrane regions of TRPV1 were transplanted into the Shaker Kv channel. Here we show that transplanting the pore domain of TRPV1 into Shaker gives rise to functional channels that can be activated by a TRPV1-selective tarantula toxin that binds to the outer pore of the channel. This pore-domain chimera is permeable to Na

Indexed as

Amino Acid SequenceAnimalsBinding SitesGene Expression RegulationHEK293 CellsHumansMiceModels, MolecularProtein ConformationProtein DomainsRatsRecombinant Fusion ProteinsShaker Superfamily of Potassium ChannelsTRPV Cation ChannelsRecombinant Fusion ProteinsShaker Superfamily of Potassium ChannelsTrpv1 protein, ratTRPV Cation ChannelscapsaicinDkTxtarantula toxinthermosensingtransient receptor potential

Identifiers

PMID29279388
PMCPMC5777071
OpenAlexW2781164311

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.