Evidence map›Paper›PMID 21908607›Full record

ArticleThe Journal of biological chemistry2011

Molecular architecture and subunit organization of TRPA1 ion channel revealed by electron microscopy.

Teresa L Cvetkov, Kevin W Huynh, Matthew R Cohen, Vera Y Moiseenkova-Bell

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
7.5field-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

63 citing papers in PubMed, 125 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Review
  5. Article
  6. Review
  7. Review
  8. Review
  9. Review
  10. TRPA1 as a therapeutic target for nociceptive pain.Expert opinion on therapeutic targets · 2020
    Review
  11. TRPA1 gene variants hurting our feelings.Pflugers Archiv : European journal of physiology · 2020
    Review
  12. Review
  13. Article
  14. Review
  15. Review
  16. Biological Applications at the Cutting Edge of Cryo-Electron Microscopy.Microscopy and microanalysis : the official journal of Microscopy Society of America, Microbeam Analysis Society, Microscopical Society of Canada · 2018
    Review
  17. Article
  18. Review
  19. Mechanistic link between diesel exhaust particles and respiratory reflexes.The Journal of allergy and clinical immunology · 2018
    Article
  20. Dawning of a new era in TRP channel structural biology by cryo-electron microscopy.Pflugers Archiv : European journal of physiology · 2018
    Review

3 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

4 authors at 1 institution in 1 country.

Teresa L CvetkovDepartment of Pharmacology, School of Medicine, Case Western Reserve University, Cleveland, Ohio 44106.
Kevin W HuynhDepartment of Pharmacology, School of Medicine, Case Western Reserve University, Cleveland, Ohio 44106.
Matthew R CohenDepartment of Pharmacology, School of Medicine, Case Western Reserve University, Cleveland, Ohio 44106.
Vera Y Moiseenkova-BellDepartment of Pharmacology, School of Medicine, Case Western Reserve University, Cleveland, Ohio 44106. Electronic address: vxm102@case.edu.
Case Western Reserve University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Transient receptor potential ankyrin 1 (TRPA1) is a non-selective ion channel, which is expressed in nociceptor sensory neurons and transduces chemical, inflammatory, and neuropathic pain signals. Numerous non-reactive compounds and electrophilic compounds, such as endogenous inflammatory mediators and exogenous pungent chemicals, can activate TRPA1. Here we report a 16-Å resolution structure of purified, functional, amphipol-stabilized TRPA1 analyzed by single-particle EM. Molecular models of the N and C termini of the channel were generated using the I-TASSER protein structure prediction server and docked into the EM density to provide insight into the TRPA1 subunit organization. This structural analysis suggests a location for critical N-terminal cysteine residues involved in electrophilic activation at the interface between neighboring subunits. Our results indicate that covalent modifications within this pocket may alter interactions between subunits and promote conformational changes that lead to channel activation.

Indexed as

AnimalsCalciumChromatography, GelCircular DichroismInflammationLigandsMiceMicroscopy, ElectronModels, MolecularMolecular ConformationProtein ConformationProtein Structure, TertiarySaccharomyces cerevisiaeStructure-Activity RelationshipTransient Receptor Potential ChannelsTRPA1 Cation ChannelCalciumLigandsTransient Receptor Potential ChannelsTRPA1 Cation ChannelTrpa1 protein, mouse

Identifiers

PMID21908607
PMCPMC3207480
OpenAlexW1974426088

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.