Evidence map›Paper›PMID 18587390›Full record

ArticleNature neuroscience2008

Gating the pore of P2X receptor channels.

Mufeng Li, Tsg-Hui Chang, Shai D Silberberg, Kenton J Swartz

Open access · greenAbstract read
In one paragraph

Article in Nature neuroscience, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.

0numbers the graph read from it
0cells of the map it votes in
74citing papers in PubMed
7.8field-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

74 citing papers in PubMed, 111 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Dilation of ion selectivity filters in cation channels.Trends in biochemical sciences · 2024
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Identification of a distinct desensitisation gate in the ATP-gated P2X2 receptor.Biochemical and biophysical research communications · 2020
    Article
  12. Article
  13. 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
  14. Article
  15. Article
  16. Review
  17. Article
  18. On the permeation of large organic cations through the pore of ATP-gated P2X receptors.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  19. Localization of the gate and selectivity filter of the full-length P2X7 receptor.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  20. Conductance of P2X4 purinergic receptor is determined by conformational equilibrium in the transmembrane region.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article

14 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 2 institutions in 1 country.

Mufeng LiMolecular Physiology and Biophysics Section, Porter Neuroscience Research Center, US National Institute of Neurological Disorders and Stroke, US National Institutes of Health, 35 Convent Drive, MSC 3701, Bethesda, Maryland 20892, USA.
Tsg-Hui Chang
Shai D Silberberg
Kenton J Swartz
National Institutes of Health · USNational Institute of Neurological Disorders and Stroke · US

Funding

Gating mechanisms and pharmacology of P2X receptor channelsZIANS003018 · NINDS · NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE · PI SWARTZ, KENTON · 2009 to 2025
$13.8M
Gating mechanisms and pharmacology of P2X receptor channelsZ01NS003018 · NINDS · NEUROLOGICAL DISORDERS AND STROKE · PI SWARTZ, KENTON · 2007 to 2008
$996k
Intramural NIH HHS ZIA NS003018
6 · The paper itself

Abstract

Three families of ligand-activated ion channels mediate synaptic communication between excitable cells in mammals. For pentameric channels related to nicotinic acetylcholine receptors and tetrameric channels such as glutamate receptors, the pore-forming and gate regions have been studied extensively. In contrast, little is known about the structure of trimeric P2X receptor channels, a family of channels that are activated by ATP and are important in neuronal signaling, pain transmission and inflammation. To identify the pore-forming and gate regions in P2X receptor channels, we introduced cysteine residues throughout the two transmembrane (TM) segments and studied their accessibility to thiol-reactive compounds and ions. Our results show that TM2 lines the central ion-conduction pore, TM1 is positioned peripheral to TM2 and the flow of ions is minimized in the closed state by a gate formed by the external region of TM2.

Indexed as

Amino Acid SubstitutionAnimalsCadmium CompoundsCell LineCell MembraneCysteineHumansIon Channel GatingKidneyMesylatesModels, BiologicalMutagenesis, Site-DirectedPatch-Clamp TechniquesProtein Structure, TertiaryRatsReceptors, Purinergic P2(2-(trimethylammonium)ethyl)methanethiosulfonateCadmium CompoundsCysteineMesylatesP2RX2 protein, humanReceptors, Purinergic P2Receptors, Purinergic P2X2Silver Nitrate

Identifiers

PMID18587390
PMCPMC2629452
OpenAlexW1968920700

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.