Evidence map›Paper›PMID 29632192›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2018

Crystal structures of a pentameric ion channel gated by alkaline pH show a widely open pore and identify a cavity for modulation.

Haidai Hu, Ákos Nemecz, Catherine Van Renterghem, Zaineb Fourati, Ludovic Sauguet, Pierre-Jean Corringer, Marc Delarue

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

16 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. Extracellular KNature communications · 2026
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  8. Review
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  11. Probing solution structure of the pentameric ligand-gated ion channel GLIC by small-angle neutron scattering.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  12. Article
  13. Article
  14. Structural basis for allosteric transitions of a multidomain pentameric ligand-gated ion channel.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  15. Modulation of theeLife · 2020
    Article
  16. Electrostatics, proton sensor, and networks governing the gating transition in GLIC, a proton-gated pentameric ion channel.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
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

7 authors at 2 institutions in 1 country.

Haidai HuUnité Dynamique Structurale des Macromolécules, Institut Pasteur, UMR 3528, CNRS, 75015 Paris, France.
Ákos NemeczUnité Récepteurs-canaux, Institut Pasteur, UMR 3571, CNRS, 75015 Paris, France.
Catherine Van RenterghemUnité Récepteurs-canaux, Institut Pasteur, UMR 3571, CNRS, 75015 Paris, France.
Zaineb FouratiUnité Dynamique Structurale des Macromolécules, Institut Pasteur, UMR 3528, CNRS, 75015 Paris, France.
Ludovic SauguetUnité Dynamique Structurale des Macromolécules, Institut Pasteur, UMR 3528, CNRS, 75015 Paris, France.
Pierre-Jean CorringerUnité Récepteurs-canaux, Institut Pasteur, UMR 3571, CNRS, 75015 Paris, France.
Marc DelarueUnité Dynamique Structurale des Macromolécules, Institut Pasteur, UMR 3528, CNRS, 75015 Paris, France; marc.delarue@pasteur.fr.
Centre National de la Recherche Scientifique · FRInstitut Pasteur · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Pentameric ligand-gated ion channels (pLGICs) constitute a widespread class of ion channels, present in archaea, bacteria, and eukaryotes. Upon binding of their agonists in the extracellular domain, the transmembrane pore opens, allowing ions to go through, via a gating mechanism that can be modulated by a number of drugs. Even though high-resolution structural information on pLGICs has increased in a spectacular way in recent years, both in bacterial and in eukaryotic systems, the structure of the open channel conformation of some intensively studied receptors whose structures are known in a nonactive (closed) form, such as

Indexed as

Allosteric RegulationBacterial ProteinsCrystallography, X-RayGammaproteobacteriaHydrogen-Ion ConcentrationLigand-Gated Ion ChannelsQuaternary Ammonium CompoundsBacterial ProteinsLigand-Gated Ion ChannelsQuaternary Ammonium Compoundstetramethylammoniumcrystallographydruggable cavityelectrophysiologyligand-gated ion channelstructural biology

Identifiers

PMID29632192
PMCPMC5924894
OpenAlexW2797635870

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.