Evidence map›Paper›PMID 32275860›Full record

ArticleNeuron2020

Structure of the Native Muscle-type Nicotinic Receptor and Inhibition by Snake Venom Toxins.

Md Mahfuzur Rahman, Jinfeng Teng, Brady T Worrell, Colleen M Noviello, Myeongseon Lee, Arthur Karlin, Michael H B Stowell, Ryan E Hibbs

Open access · bronzeAbstract read
In one paragraph

Article in Neuron, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 111 papers.

0numbers the graph read from it
0cells of the map it votes in
111citing papers in PubMed
11.2field-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

111 citing papers in PubMed, 202 citations in OpenAlex.

  1. Longitudinal dynamics and clinical significance of acetylcholine receptor blocking antibodies in myasthenia gravis.Neurological sciences : official journal of the Italian Neurological Society and of the Italian Society of Clinical Neurophysiology · 2026
    Article
  2. Review
  3. Review
  4. Precise mapping of a snake venom phospholipase AToxicon : official journal of the International Society on Toxinology · 2025
    Article
  5. Article
  6. Article
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  12. Review
  13. Gating mechanism of the human α1β GlyR by glycine.Structure (London, England : 1993) · 2024
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Influence of lipid bilayer on the structure of the muscle-type nicotinic acetylcholine receptor.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  20. Ion transport in muscle acetylcholine receptor maintained by conserved salt bridges between the pore and lipid membrane.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article

51 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 3 institutions in 1 country.

Md Mahfuzur RahmanDepartment of Neuroscience, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.
Jinfeng TengDepartment of Neuroscience, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.
Brady T WorrellDepartment of Molecular, Cellular & Developmental Biology, University of Colorado, Boulder, CO 80309, USA.
Colleen M NovielloDepartment of Neuroscience, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.
Myeongseon LeeDepartment of Molecular, Cellular & Developmental Biology, University of Colorado, Boulder, CO 80309, USA.
Arthur KarlinCenter for Molecular Recognition & Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA.
Michael H B StowellDepartment of Molecular, Cellular & Developmental Biology, University of Colorado, Boulder, CO 80309, USA. Electronic address: stowellm@colorado.edu.
Ryan E HibbsDepartment of Neuroscience, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA. Electronic address: ryan.hibbs@utsouthwestern.edu.
The University of Texas Southwestern Medical Center · USUniversity of Colorado Boulder · USColumbia University · US

Funding

Pacific Northwest Center for Cryo-EM - Screening supplementU24GM129547 · NIGMS · OREGON HEALTH & SCIENCE UNIVERSITY · PI EVANS, JAMES E, GOUAUX, JAMES E · 2018 to 2023
$54.8M
Identifying exosome-mediated cargo transport machinery in Alzheimer's diseaseRF1AG061829 · NIA · UNIVERSITY OF COLORADO · PI SHEN, JINGSHI, STOWELL, MICHAEL H. B. · 2018 to 2018
$2.7M
Structural studies of heteromeric nicotinic acetylcholine receptors - Diversity SupplementR01DA042072 · NIDA · UT SOUTHWESTERN MEDICAL CENTER · PI HIBBS, RYAN E · 2016 to 2020
$2.0M
3D Structure and mechanism of the alpha7 nicotinic acetylcholine receptorR01NS095899 · NINDS · UT SOUTHWESTERN MEDICAL CENTER · PI HIBBS, RYAN E · 2016 to 2020
$1.8M
Structural biology of the alpha4beta2 nicotinic acetylcholine receptorR33DA037492 · NIDA · UT SOUTHWESTERN MEDICAL CENTER · PI HIBBS, RYAN E · 2017 to 2018
$802k
Structural biology of the alpha4beta2 nicotinic acetylcholine receptorR21DA037492 · NIDA · UT SOUTHWESTERN MEDICAL CENTER · PI HIBBS, RYAN E · 2014 to 2015
$368k
NIA NIH HHS RF1 AG061829NIDA NIH HHS R01 DA042072NIDA NIH HHS R21 DA037492NIDA NIH HHS R33 DA037492NIGMS NIH HHS U24 GM129547NINDS NIH HHS R01 NS095899
6 · The paper itself

Abstract

The nicotinic acetylcholine receptor, a pentameric ligand-gated ion channel, converts the free energy of binding of the neurotransmitter acetylcholine into opening of its central pore. Here we present the first high-resolution structure of the receptor type found in muscle-endplate membrane and in the muscle-derived electric tissues of fish. The native receptor was purified from Torpedo electric tissue and functionally reconstituted in lipids optimal for cryo-electron microscopy. The receptor was stabilized in a closed state by the binding of α-bungarotoxin. The structure reveals the binding of a toxin molecule at each of two subunit interfaces in a manner that would block the binding of acetylcholine. It also reveals a closed gate in the ion-conducting pore, formed by hydrophobic amino acid side chains, located ∼60 Å from the toxin binding sites. The structure provides a framework for understanding gating in ligand-gated channels and how mutations in the acetylcholine receptor cause congenital myasthenic syndromes.

Indexed as

AnimalsBinding SitesBungarotoxinsCarbacholCryoelectron MicroscopyElectric OrganMolecular ConformationNicotinic AgonistsNicotinic AntagonistsPatch-Clamp TechniquesProtein ConformationReceptors, NicotinicTorpedoBungarotoxinsCarbacholNicotinic AgonistsNicotinic AntagonistsReceptors, Nicotinicacetylcholine receptorcryo-EMCys-loop receptorion channel structureligand-gated ion channelmembrane proteinnicotinic receptorTorpedotoxinα-bungarotoxin

Identifiers

PMID32275860
PMCPMC8867384
OpenAlexW3015593286

What OpenQuestion holds

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LicenceTDM
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.