Evidence map›Paper›PMID 20858418›Full record

ArticleBiophysical journal2010

Kinetic and energetic analysis of thermally activated TRPV1 channels.

Jing Yao, Beiying Liu, Feng Qin

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.

0numbers the graph read from it
0cells of the map it votes in
71citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

71 citing papers in PubMed, 127 citations in OpenAlex.

  1. Article
  2. Article
  3. Journal of Zhejiang University. Science. B · 2026
    Review
  4. Article
  5. Article
  6. Structural basis of the inhibition of TRPV1 by analgesic sesquiterpenes.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Protein dynamics underlies strong temperature dependence of heat receptors.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  8. iScience · 2024
    Article
  9. 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
  10. Article
  11. Implications of a temperature-dependent heat capacity for temperature-gated ion channels.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  12. Article
  13. Cannabidiol sensitizes TRPV2 channels to activation by 2-APB.bioRxiv : the preprint server for biology · 2023
    Article
  14. Article
  15. A journey from molecule to physiology andFrontiers in pharmacology · 2023
    Review
  16. Review
  17. Dual amplification strategy turns TRPM2 channels into supersensitive central heat detectors.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  18. Article
  19. Article
  20. Article

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

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

3 authors at 1 institution in 1 country.

Jing YaoDepartment of Physiology and Biophysical Sciences, State University of New York, Buffalo, New York, USA.
Beiying Liu
Feng Qin
University at Buffalo, State University of New York · US

Funding

Mechanisms of Heat Activation and Multimodal Functions of VR1 Receptor ChannelsR01GM065994 · NIGMS · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI QIN, FENG · 2002 to 2010
$2.4M
NIGMS NIH HHS R01 GM065994NIGMS NIH HHS R01-GM65994
6 · The paper itself

Abstract

Thermal TRP channels are important for thermal sensation and nociception, but their gating mechanisms have remained elusive. With optically generated submillisecond temperature steps from 22°C to >60°C, we have directly measured the activation and deactivation kinetics of TRPV1 channels, and from the measurements we determined the energetics of thermal gating. We show that activation by temperature follows single exponential time courses. It occurs in a few milliseconds and is significantly faster than activation by agonists. The gating has characteristics of a melting process involving large compensatory enthalpy (>100 kcal/mol) and entropy changes with little free energy change. The reaction path is asymmetrical with temperature mainly driving the opening while the closing has nominal but negative temperature dependence (i.e., sensitivity to cold). Both voltage and agonists alter the slope of the temperature-dependent gating curve as well as shifting the midpoint. However, compared to the energetic effect of temperature on gating, the effect of voltage is small. Our data on the interdependence between voltage and direct temperature responses are not fit to a model involving independent stimuli but instead support a temperature-sensing mechanism that is coupled to charge movement or agonist binding.

Indexed as

Ion Channel GatingTemperatureAnimalsElectric ConductivityHEK293 CellsHot TemperatureHumansKineticsRatsThermodynamicsTRPV Cation ChannelsTrpv1 protein, ratTRPV Cation Channels

Identifiers

PMID20858418
PMCPMC2941006
OpenAlexW1965985711

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.