Evidence map›Paper›PMID 18490661›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2008

Structure of TRPV1 channel revealed by electron cryomicroscopy.

Vera Y Moiseenkova-Bell, Lia A Stanciu, Irina I Serysheva, Ben J Tobe, Theodore G Wensel

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 116 papers.

0numbers the graph read from it
0cells of the map it votes in
116citing papers in PubMed
7.5field-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

116 citing papers in PubMed, 216 citations in OpenAlex.

  1. Review
  2. Journal of Zhejiang University. Science. B · 2026
    Review
  3. Review
  4. Review
  5. Review
  6. Article
  7. Review
  8. Structural mechanism of TRPV5 inhibition by econazole.Structure (London, England : 1993) · 2024
    Article
  9. Review
  10. Article
  11. Review
  12. Review
  13. Review
  14. Article
  15. The Utility ofInternational journal of environmental research and public health · 2022
    Review
  16. Article
  17. Role of mechanosensitive channels/receptors in atherosclerosis.American journal of physiology. Cell physiology · 2022
    Review
  18. Article
  19. Article
  20. Review

56 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

5 authors at 2 institutions in 1 country.

Vera Y Moiseenkova-BellVerna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX 77030, USA.
Lia A Stanciu
Irina I Serysheva
Ben J Tobe
Theodore G Wensel
Baylor College of Medicine · USPurdue University West Lafayette · US

Funding

ZERNIKE PHASE PLATE CRYOEM IN OKAZAKIP41RR002250 · NCRR · UNIVERSITY OF ARIZONA · PI CHIU, WAH · 1985 to 2011
$22.1M
Trasnducin Interactions with Photoreceptor MembranesR01EY007981 · NEI · BAYLOR COLLEGE OF MEDICINE · PI WENSEL, THEODORE G · 1989 to 2016
$6.1M
Structure-Function Studies Of IP3R ChannelsR01GM072804 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI SERYSHEVA, IRINA I · 2005 to 2023
$4.8M
Training in Pharmacoinformatics(RMI)R90DK071505 · NIDDK · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI STANCEL, GEORGE M. · 2004 to 2008
$1.4M
NCRR NIH HHS P41 RR002250NCRR NIH HHS P41-RR02250NEI NIH HHS R01 EY007981NEI NIH HHS R01-EY07981NIDDK NIH HHS R90 DK071505NIDDK NIH HHS T90-DK071505NIGMS NIH HHS P01-GM99116NIGMS NIH HHS R01 GM072804NIGMS NIH HHS R01-GM072804
6 · The paper itself

Abstract

The transient receptor potential (TRP) family of ion channels participate in many signaling pathways. TRPV1 functions as a molecular integrator of noxious stimuli, including heat, low pH, and chemical ligands. Here, we report the 3D structure of full-length rat TRPV1 channel expressed in the yeast Saccharomyces cerevisiae and purified by immunoaffinity chromatography. We demonstrate that the recombinant purified TRPV1 channel retains its structural and functional integrity and is suitable for structural analysis. The 19-A structure of TRPV1 determined by using single-particle electron cryomicroscopy exhibits fourfold symmetry and comprises two distinct regions: a large open basket-like domain, likely corresponding to the cytoplasmic N- and C-terminal portions, and a more compact domain, corresponding to the transmembrane portion. The assignment of transmembrane and cytoplasmic regions was supported by fitting crystal structures of the structurally homologous Kv1.2 channel and isolated TRPV1 ankyrin repeats into the TRPV1 structure.

Indexed as

AnimalsAnkyrin RepeatCell MembraneCryoelectron MicroscopyCrystallographyCytoplasmImaging, Three-DimensionalKv1.2 Potassium ChannelProtein ConformationRatsRecombinant ProteinsSaccharomyces cerevisiaeTRPV Cation ChannelsKv1.2 Potassium ChannelRecombinant ProteinsTrpv1 protein, ratTRPV Cation Channels

Identifiers

PMID18490661
PMCPMC2396679
OpenAlexW2077225258

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.