Evidence map›Paper›PMID 29217583›Full record

ArticleScience (New York, N.Y.)2018

Structure of the cold- and menthol-sensing ion channel TRPM8.

Ying Yin, Mengyu Wu, Lejla Zubcevic, William F Borschel, Gabriel C Lander, Seok-Yong Lee

Abstract read
In one paragraph

Article in Science (New York, N.Y.), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 193 papers.

0numbers the graph read from it
0cells of the map it votes in
193citing papers in PubMed
22.5field-weighted citation impact, top 1% 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

193 citing papers in PubMed, 303 citations in OpenAlex.

  1. Article
  2. Article
  3. Symmetry-driven gating of TRPM8 by PIPNature communications · 2026
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133 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

6 authors at 2 institutions in 1 country.

Ying YinDepartment of Biochemistry, Duke University School of Medicine, Durham, NC 27710, USA.ORCID 0000-0002-4128-8616
Mengyu WuDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.ORCID 0000-0002-2248-9383
Lejla ZubcevicDepartment of Biochemistry, Duke University School of Medicine, Durham, NC 27710, USA.ORCID 0000-0002-1884-9235
William F BorschelDepartment of Biochemistry, Duke University School of Medicine, Durham, NC 27710, USA.ORCID 0000-0003-4064-9026
Gabriel C LanderDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.ORCID 0000-0003-4921-1135
Seok-Yong LeeDepartment of Biochemistry, Duke University School of Medicine, Durham, NC 27710, USA.ORCID 0000-0002-0662-9921
Duke University · USScripps Research Institute · US

Funding

Structure, function, and pharmacology of neuronal membrane transport proteinsR35NS097241 · NINDS · DUKE UNIVERSITY · PI LEE, SEOK-YONG · 2016 to 2023
$6.1M
Molecular basis of axonal transport described by high-resolution 3D imagingDP2EB020402 · NIBIB · SCRIPPS RESEARCH INSTITUTE, THE · PI LANDER, GABRIEL C · 2014 to 2014
$2.8M
COMPUTING AND DATA STORAGE CLUSTER FOR ELECTRON MICROSCOPYS10OD021634 · OD · SCRIPPS RESEARCH INSTITUTE, THE · PI LANDER, GABRIEL C · 2016 to 2016
$531k
NIBIB NIH HHS DP2 EB020402NIH HHS S10 OD021634NINDS NIH HHS R35 NS097241
6 · The paper itself

Abstract

Transient receptor potential melastatin (TRPM) cation channels are polymodal sensors that are involved in a variety of physiological processes. Within the TRPM family, member 8 (TRPM8) is the primary cold and menthol sensor in humans. We determined the cryo-electron microscopy structure of the full-length TRPM8 from the collared flycatcher at an overall resolution of ~4.1 ångstroms. Our TRPM8 structure reveals a three-layered architecture. The amino-terminal domain with a fold distinct among known TRP structures, together with the carboxyl-terminal region, forms a large two-layered cytosolic ring that extensively interacts with the transmembrane channel layer. The structure suggests that the menthol-binding site is located within the voltage-sensor-like domain and thus provides a structural glimpse of the design principle of the molecular transducer for cold and menthol sensation.

Indexed as

AnimalsAvian ProteinsBinding SitesCold TemperatureCryoelectron MicroscopyImage Processing, Computer-AssistedMentholModels, MolecularPasseriformesProtein DomainsProtein FoldingProtein Structure, SecondaryProtein SubunitsTRPM Cation ChannelsAvian ProteinsMentholProtein SubunitsTRPM Cation Channels

Identifiers

PMID29217583
PMCPMC5810135
OpenAlexW2775387645

What OpenQuestion holds

Textmetadata
LicenceTDM
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.