Evidence map›Paper›PMID 28154143›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

Single-residue molecular switch for high-temperature dependence of vanilloid receptor TRPV3.

Beiying Liu, Feng Qin

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
3.2field-weighted citation impact, top 9% 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

41 citing papers in PubMed, 83 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. TRPV3 in skin thermosensation and temperature responses.The journal of physiological sciences : JPS · 2025
    Review
  9. Review
  10. Protein dynamics underlies strong temperature dependence of heat receptors.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  11. Review
  12. Article
  13. Article
  14. iScience · 2024
    Article
  15. Review
  16. Article
  17. Article
  18. 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
  19. Article
  20. 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.

Beiying LiuDepartment of Physiology and Biophysical Sciences, State University of New York, Buffalo, NY 14214.
Feng QinDepartment of Physiology and Biophysical Sciences, State University of New York, Buffalo, NY 14214 qin@buffalo.edu.
University at Buffalo, State University of New York · US

Funding

Temperature-Dependent Gating of Vanilloid ReceptorsR01GM104521 · NIGMS · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI QIN, FENG · 2013 to 2016
$1.3M
NIGMS NIH HHS R01 GM104521
6 · The paper itself

Abstract

Thermal transient receptor potential (TRP) channels, a group of ion channels from the transient receptor potential family, play important functions in pain and thermal sensation. These channels are directly activated by temperature and possess strong temperature dependence. Furthermore, their temperature sensitivity can be highly dynamic and use-dependent. For example, the vanilloid receptor transient receptor potential 3 (TRPV3), which has been implicated as a warmth detector, becomes responsive to warm temperatures only after intensive stimulation. Upon initial activation, the channel exhibits a high-temperature threshold in the noxious temperature range above 50 °C. This use dependence of heat sensitivity thus provides a mechanism for sensitization of thermal channels. However, how the channels acquire the use dependence remains unknown. Here, by comparative studies of chimeric channels between use-dependent and use-independent homologs, we have determined the molecular basis that underlies the use dependence of temperature sensitivity of TRPV3. Remarkably, the restoration of a single residue that is apparently missing in the use-dependent homologs could largely eliminate the use dependence of heat sensitivity of TRPV3. The location of the region suggests a mechanism of temperature-dependent gating of thermal TRP channels involving an intracellular region assembled around the TRP domain.

Indexed as

Hot TemperatureAmino AcidsAnimalsHEK293 CellsHumansIon Channel GatingMembrane PotentialsMiceMutationPatch-Clamp TechniquesTemperatureTRPV Cation ChannelsAmino AcidsTRPV3 protein, humanTRPV Cation ChannelshyperalgesiahysteresisthermoreceptorTRP channeluse dependence

Identifiers

PMID28154143
PMCPMC5321025
OpenAlexW2583210520

What OpenQuestion holds

Textmetadata
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.