Evidence map›Paper›PMID 26779611›Full record

ArticleNature structural & molecular biology2016

Cryo-electron microscopy structure of the TRPV2 ion channel.

Lejla Zubcevic, Mark A Herzik, Ben C Chung, Zhirui Liu, Gabriel C Lander, Seok-Yong Lee

Abstract read
In one paragraph

Article in Nature structural & molecular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 156 papers.

0numbers the graph read from it
0cells of the map it votes in
156citing papers in PubMed
34.6field-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

156 citing papers in PubMed, 283 citations in OpenAlex.

  1. An Extracellular Pore‑Targeting Peptide Defines a Designable Allosteric Site in TRPV2.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  2. Article
  3. Article
  4. The journal of physical chemistry. B · 2026
    Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Structural Pharmacology of TRPV4 Antagonists.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Article
  13. Wound Repair and CaCells · 2024
    Review
  14. Article
  15. Structure of human TRPM8 channel.Communications biology · 2023
    Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Vascular mechanotransduction.Physiological reviews · 2023
    Review

96 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 3 institutions in 1 country.

Lejla Zubcevic *Department of Biochemistry, Duke University Medical Center, Durham, North Carolina, USA.
Mark A Herzik *Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, California, USA.
Ben C ChungDepartment of Biochemistry, Duke University Medical Center, Durham, North Carolina, USA.
Zhirui LiuDepartment of Biochemistry, Duke University Medical Center, Durham, North Carolina, USA.
Gabriel C LanderDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, California, USA.
Seok-Yong LeeDepartment of Biochemistry, Duke University Medical Center, Durham, North Carolina, USA.
Duke Medical Center · USDuke University Hospital · USScripps Research Institute · US

Funding

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
Pharmacology and biophysics of the voltage-gated sodium channel Nav1.7: a therapeDP2OD008380 · OD · DUKE UNIVERSITY · PI LEE, SEOK-YONG · 2011 to 2011
$2.4M
NCCDPHP CDC HHS DP2EB020402NIBIB NIH HHS DP2 EB020402NIGMS NIH HHS R01GM100894NIH HHS DP2 OD008380NIH HHS DP2OD008380
6 · The paper itself

Abstract

Transient receptor potential vanilloid (TRPV) cation channels are polymodal sensors involved in a variety of physiological processes. TRPV2, a member of the TRPV family, is regulated by temperature, by ligands, such as probenecid and cannabinoids, and by lipids. TRPV2 has been implicated in many biological functions, including somatosensation, osmosensation and innate immunity. Here we present the atomic model of rabbit TRPV2 in its putative desensitized state, as determined by cryo-EM at a nominal resolution of ∼4 Å. In the TRPV2 structure, the transmembrane segment 6 (S6), which is involved in gate opening, adopts a conformation different from the one observed in TRPV1. Structural comparisons of TRPV1 and TRPV2 indicate that a rotation of the ankyrin-repeat domain is coupled to pore opening via the TRP domain, and this pore opening can be modulated by rearrangements in the secondary structure of S6.

Indexed as

AnimalsAnkyrin RepeatCryoelectron MicroscopyModels, MolecularProtein ConformationRabbitsTRPV Cation ChannelsTRPV Cation Channels

Identifiers

PMID26779611
PMCPMC4876856
OpenAlexW2301186499

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.