Evidence map›Paper›PMID 34239124›Full record

ArticleNature structural & molecular biology2021

Structural mechanism of heat-induced opening of a temperature-sensitive TRP channel.

Kirill D Nadezhdin, Arthur Neuberger, Yuri A Trofimov, Nikolay A Krylov, Viktor Sinica, Nikita Kupko, Viktorie Vlachova, Eleonora Zakharian, Roman G Efremov, Alexander I Sobolevsky

Abstract read
In one paragraph

Article in Nature structural & molecular biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 101 papers.

0numbers the graph read from it
0cells of the map it votes in
101citing papers in PubMed
–field-weighted citation impact
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

101 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Review
  14. Review
  15. Bioorganic studies on the nyctinastic leaf-movement of plants.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2026
    Review
  16. Article
  17. Review
  18. Article
  19. Article
  20. Examining the thermotropic properties of large circularized nanodiscs.Biochimica et biophysica acta. Biomembranes · 2025
    Article

41 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

10 authors.

Kirill D Nadezhdin *Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY, USA.
Arthur Neuberger *Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY, USA.ORCID http://orcid.org/0000-0002-7744-6559
Yuri A TrofimovShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia.
Nikolay A KrylovShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia.ORCID http://orcid.org/0000-0002-4520-0351
Viktor SinicaDepartment of Cellular Neurophysiology, Institute of Physiology Czech Academy of Sciences, Prague, Czech Republic.
Nikita KupkoDepartment of Biochemistry and Molecular Biophysics, Columbia University, New York, NY, USA.ORCID http://orcid.org/0000-0002-6438-7326
Viktorie VlachovaDepartment of Cellular Neurophysiology, Institute of Physiology Czech Academy of Sciences, Prague, Czech Republic.ORCID http://orcid.org/0000-0002-8621-0935
Eleonora ZakharianDepartment of Cancer Biology & Pharmacology, University of Illinois College of Medicine, Peoria, IL, USA.
Roman G EfremovShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia.
Alexander I SobolevskyDepartment of Biochemistry and Molecular Biophysics, Columbia University, New York, NY, USA. as4005@cumc.columbia.edu.ORCID http://orcid.org/0000-0001-5181-8644

Funding

Pacific Northwest Center for Cryo-EM - Screening supplementU24GM129547 · NIGMS · OREGON HEALTH & SCIENCE UNIVERSITY · PI EVANS, JAMES E, GOUAUX, JAMES E · 2018 to 2023
$54.8M
NCCAT: National Center for CryoEM Access and Training- Supplement for Windows 10 and FFIU24GM129539 · NIGMS · NEW YORK STRUCTURAL BIOLOGY CENTER · PI DE MARCO, ALEX, KIEFT, JEFFREY S · 2018 to 2023
$53.9M
Structure and Function of AMPA subtype ionotropic glutamate receptorsR01NS083660 · NINDS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI KURNIKOVA, MARIA G, SOBOLEVSKY, ALEXANDER · 2013 to 2022
$4.3M
Structure and function of Transient Receptor Potential ChannelsR01CA206573 · NCI · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI Alexander Sobolevsky · 2017 to 2026
$3.8M
Single-Particle Cryo-EM Characterization of AMPA Receptor Functional StatesR01NS107253 · NINDS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI Alexander Sobolevsky · 2018 to 2026
$3.5M
Structural and functional principles of activation and regulation of the transient receptor potential channel TRPV3.R01AR078814 · NIAMS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI Alexander Sobolevsky · 2022 to 2026
$2.8M
NCI NIH HHS R01 CA206573NIAMS NIH HHS R01 AR078814NIGMS NIH HHS U24 GM129539NIGMS NIH HHS U24 GM129547NINDS NIH HHS R01 NS083660NINDS NIH HHS R01 NS107253
6 · The paper itself

Abstract

Numerous physiological functions rely on distinguishing temperature through temperature-sensitive transient receptor potential channels (thermo-TRPs). Although the function of thermo-TRPs has been studied extensively, structural determination of their heat- and cold-activated states has remained a challenge. Here, we present cryo-EM structures of the nanodisc-reconstituted wild-type mouse TRPV3 in three distinct conformations: closed, heat-activated sensitized and open states. The heat-induced transformations of TRPV3 are accompanied by changes in the secondary structure of the S2-S3 linker and the N and C termini and represent a conformational wave that links these parts of the protein to a lipid occupying the vanilloid binding site. State-dependent differences in the behavior of bound lipids suggest their active role in thermo-TRP temperature-dependent gating. Our structural data, supported by physiological recordings and molecular dynamics simulations, provide an insight for understanding the molecular mechanism of temperature sensing.

Indexed as

AnimalsCell LineCold TemperatureCryoelectron MicroscopyHEK293 CellsHot TemperatureHumansIon Channel GatingLipidsMiceProtein BindingProtein ConformationThermodynamicsThermosensingTRPV Cation ChannelsLipidsTrpv3 protein, mouseTRPV Cation Channels

Identifiers

PMID34239124
PMCPMC8283911

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.