Evidence map›Paper›PMID 20975702›Full record

ArticleNature communications2010

Pore-opening mechanism in trimeric P2X receptor channels.

Mufeng Li, Toshimitsu Kawate, Shai D Silberberg, Kenton J Swartz

Abstract read
In one paragraph

Article in Nature communications, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.

0numbers the graph read from it
0cells of the map it votes in
68citing 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

68 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Dilation of ion selectivity filters in cation channels.Trends in biochemical sciences · 2024
    Review
  6. Vascular mechanotransduction.Physiological reviews · 2023
    Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Identification of a distinct desensitisation gate in the ATP-gated P2X2 receptor.Biochemical and biophysical research communications · 2020
    Article
  14. Hearing loss mutations alter the functional properties of human P2X2 receptor channels through distinct mechanisms.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  15. Article
  16. Druggable negative allosteric site of P2X3 receptors.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  17. The crosstalk between autonomic nervous system and blood vessels.International journal of physiology, pathophysiology and pharmacology · 2018
    Review
  18. Article
  19. Article
  20. Article

8 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.

Mufeng LiMolecular Physiology and Biophysics Section, Porter Neuroscience Research Center, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, Maryland 20892, USA. Mufeng_Li@nih.gov
Toshimitsu Kawate
Shai D Silberberg
Kenton J Swartz

Funding

Intramural NIH HHS
6 · The paper itself

Abstract

The opening of ion channels in response to ligand binding, voltage or membrane stretch underlies electrical and chemical signalling throughout biology. Two structural classes of pore-opening mechanisms have been established, including bending of pore-lining helices in the case of tetrameric cation channels, or tilting of such helices in mechanosensitive channels. In this paper, we explore how the structure of the pore changes during opening in P2X receptors by measuring the modification of introduced cysteine residues in transmembrane helices by thiol-reactive reagents, and by engineering metal bridges. Our results are consistent with the X-ray structure of the closed state, and demonstrate that expansion of the gate region in the external pore is accompanied by a significant narrowing of the inner pore, indicating that pore-forming helices straighten on ATP binding to open the channel. This unique pore-opening mechanism has fundamental implications for the role of subunit interfaces in the gating mechanism of P2X receptors and points to a role of the internal pore in ion permeation.

Indexed as

AnimalsElectrophysiologyHEK293 CellsHumansProtein Structure, SecondaryProtein Structure, TertiaryRatsReceptors, Purinergic P2XTransfectionZebrafish ProteinsReceptors, Purinergic P2XZebrafish Proteins

Identifiers

PMID20975702
PMCPMC2982178

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.