Evidence map›Paper›PMID 21878524›Full record

ArticleThe Journal of physiology2011

Ligand stoichiometry of the cold- and menthol-activated channel TRPM8.

Annelies Janssens, Thomas Voets

Open access · greenAbstract read
In one paragraph

Article in The Journal of physiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
1.6field-weighted citation impact, top 21% 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

32 citing papers in PubMed, 41 citations in OpenAlex.

  1. Symmetry-driven gating of TRPM8 by PIPNature communications · 2026
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  3. Deep mutational scan of the pore of the cold-sensing TRPM8 channel.bioRxiv : the preprint server for biology · 2026
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  12. Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2019
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Annelies JanssensLaboratory of Ion Channel Research and TRP Research Platform Leuven, KU Leuven, Herestraat 49 bus 802, B-3000 Leuven, Belgium.
Thomas Voets
KU Leuven · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Temperature-sensitive transient receptor potential (TRP) channels play a key role in somatosensation, not only as primary thermosensors but also as chemosensors for various compounds that evoke a thermal sensation. The fundamental mechanisms whereby TRP channels translate ligand binding into opening of the ion conducting pore are, however, poorly understood, and the actual number of ligands that bind to these channels is fully unknown. Here, we investigated the ligand stoichiometry of the cold sensor and menthol receptor TRPM8. Based on a detailed biophysical analysis of tandem constructs of wild-type and menthol-insensitive TRPM8 subunits, we now provide direct evidence that each channel has four independent and energetically equivalent menthol interaction sites. These results suggest a fundamentally different ligand stoichiometry in TRP channels, in comparison with other major families of ligand-gated ion channels.

Indexed as

Cold TemperatureBinding SitesCalciumCell Line, TumorHumansLigandsMembrane PotentialsMentholMutationPatch-Clamp TechniquesTRPM Cation ChannelsCalciumLigandsMentholTRPM8 protein, humanTRPM Cation Channels

Identifiers

PMID21878524
PMCPMC3224877
OpenAlexW1959838017

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.