Evidence map›Paper›PMID 37857704›Full record

ArticleCommunications biology2023

Structure of human TRPM8 channel.

Sergii Palchevskyi, Mariusz Czarnocki-Cieciura, Giulio Vistoli, Silvia Gervasoni, Elżbieta Nowak, Andrea R Beccari, Marcin Nowotny, Carmine Talarico

Open access · goldAbstract read
In one paragraph

Article in Communications biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
7.7field-weighted citation impact, top 2% 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

24 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
  2. Symmetry-driven gating of TRPM8 by PIPNature communications · 2026
    Article
  3. Article
  4. Article
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  8. Article
  9. Review
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  14. Article
  15. Article
  16. The structural basis of cold sensitivity.bioRxiv : the preprint server for biology · 2025
    Article
  17. Article
  18. Article
  19. Calcium channels as pharmacological targets for cancer therapy.Clinical and experimental medicine · 2025
    Review
  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

8 authors at 4 institutions in 3 countries.

Sergii Palchevskyi *Laboratory of Protein Structure, International Institute of Molecular and Cell Biology in Warsaw, 02-109, Warsaw, Poland.
Mariusz Czarnocki-Cieciura *Laboratory of Protein Structure, International Institute of Molecular and Cell Biology in Warsaw, 02-109, Warsaw, Poland.ORCID http://orcid.org/0000-0001-5582-2851
Giulio VistoliDipartimento di Scienze Farmaceutiche, Università degli Studi di Milano, Via Mangiagalli, 25, I-20133, Milano, Italy.
Silvia GervasoniDipartimento di Scienze Farmaceutiche, Università degli Studi di Milano, Via Mangiagalli, 25, I-20133, Milano, Italy.ORCID http://orcid.org/0000-0002-5731-3396
Elżbieta NowakLaboratory of Protein Structure, International Institute of Molecular and Cell Biology in Warsaw, 02-109, Warsaw, Poland.
Andrea R BeccariDompé Farmaceutici SpA, EXSCALATE, Via Tommaso De Amicis, 95, I-80131, Napoli, Italy.
Marcin NowotnyLaboratory of Protein Structure, International Institute of Molecular and Cell Biology in Warsaw, 02-109, Warsaw, Poland. mnowotny@iimcb.gov.pl.ORCID http://orcid.org/0000-0001-8632-0977
Carmine TalaricoDompé Farmaceutici SpA, EXSCALATE, Via Tommaso De Amicis, 95, I-80131, Napoli, Italy. carmine.talarico@dompe.com.ORCID http://orcid.org/0000-0003-4789-0955
International Institute of Molecular and Cell Biology · PLDompé (Italy) · ITUniversity of Cagliari · ITUniversity of Milan · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

TRPM8 is a non-selective cation channel permeable to both monovalent and divalent cations that is activated by multiple factors, such as temperature, voltage, pressure, and changes in osmolality. It is a therapeutic target for anticancer drug development, and its modulators can be utilized for several pathological conditions. Here, we present a cryo-electron microscopy structure of a human TRPM8 channel in the closed state that was solved at 2.7 Å resolution. Our structure comprises the most complete model of the N-terminal pre-melastatin homology region. We also visualized several lipids that are bound by the protein and modeled how the human channel interacts with icilin. Analyses of pore helices in available TRPM structures showed that all these structures can be grouped into different closed, desensitized and open state conformations based on the register of the pore helix S6 which positions particular amino acid residues at the channel constriction.

Indexed as

TRPM Cation ChannelsCryoelectron MicroscopyHumansMembrane ProteinsTemperatureMembrane ProteinsTRPM8 protein, humanTRPM Cation Channels

Identifiers

PMID37857704
PMCPMC10587237
OpenAlexW4387782156

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.