Evidence map›Paper›PMID 26282895›Full record

ArticleNature communications2015

Stoichiometry for α-bungarotoxin block of α7 acetylcholine receptors.

Corrie J B daCosta, Chris R Free, Steven M Sine

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

30 citing papers in PubMed, 48 citations in OpenAlex.

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  6. Cell signaling and epigenetic regulation of nicotine-induced carcinogenesis.Environmental pollution (Barking, Essex : 1987) · 2024
    Review
  7. Aberrant evoked calcium signaling and nAChR cluster morphology in aFrontiers in cell and developmental biology · 2024
    Article
  8. Article
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  10. Article
  11. Article
  12. eLife · 2022
    Article
  13. Article
  14. Article
  15. A single historical substitution drives an increase in acetylcholine receptor complexity.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Molecular function of the novel α7β2 nicotinic receptor.Cellular and molecular life sciences : CMLS · 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

3 authors at 1 institution in 1 country.

Corrie J B daCostaDepartment of Physiology and Biomedical Engineering, Mayo Clinic College of Medicine, 200 First Street SW, Rochester, Minnesota 55905, USA.
Chris R FreeDepartment of Physiology and Biomedical Engineering, Mayo Clinic College of Medicine, 200 First Street SW, Rochester, Minnesota 55905, USA.
Steven M Sine1] Department of Physiology and Biomedical Engineering, Mayo Clinic College of Medicine, 200 First Street SW, Rochester, Minnesota 55905, USA [2] Department of Neurology, Mayo Clinic College of Medicine, 200 First Street SW, Rochester, Minnesota 55905, USA.
Mayo Clinic · US

Funding

STRUCTURE/FUNCTION OF THE ACETYLCHOLINE RECEPTORR01NS031744 · NINDS · MAYO CLINIC ROCHESTER · PI SINE, STEVEN M · 1992 to 2023
$7.3M
Structure and Function of the Acetylcholine ReceptorR37NS031744 · NINDS · MAYO CLINIC ROCHESTER · PI SINE, STEVEN M · 2001 to 2007
$4.1M
NINDS NIH HHS NS031744NINDS NIH HHS R01 NS031744NINDS NIH HHS R37 NS031744
6 · The paper itself

Abstract

α-Bungarotoxin (α-Btx) binds to the five agonist binding sites on the homopentameric α7-acetylcholine receptor, yet the number of bound α-Btx molecules required to prevent agonist-induced channel opening remains unknown. To determine the stoichiometry for α-Btx blockade, we generate receptors comprised of wild-type and α-Btx-resistant subunits, tag one of the subunit types with conductance mutations to report subunit stoichiometry, and following incubation with α-Btx, monitor opening of individual receptor channels with defined subunit stoichiometry. We find that a single α-Btx-sensitive subunit confers nearly maximal suppression of channel opening, despite four binding sites remaining unoccupied by α-Btx and accessible to the agonist. Given structural evidence that α-Btx locks the agonist binding site in an inactive conformation, we conclude that the dominant mechanism of antagonism is non-competitive, originating from conformational arrest of the binding sites, and that the five α7 subunits are interdependent and maintain conformational symmetry in the open channel state.

Indexed as

alpha7 Nicotinic Acetylcholine ReceptorBinding SitesBungarotoxinsGene Expression RegulationHEK293 CellsHumansIodine RadioisotopesKineticsModels, MolecularMutagenesis, Site-DirectedMutationProtein BindingProtein Conformationalpha7 Nicotinic Acetylcholine ReceptorBungarotoxinsIodine Radioisotopes

Identifiers

PMID26282895
PMCPMC4544739
OpenAlexW2406380726

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.