Evidence map›Paper›PMID 22811427›Full record

ReviewPhysiological reviews2012

End-plate acetylcholine receptor: structure, mechanism, pharmacology, and disease.

Steven M Sine

Abstract readReview
In one paragraph

Review in Physiological reviews, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed, 1 pooled it
4.6field-weighted citation impact, top 4% 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

61 citing papers in PubMed, 1 synthesis or guideline pooled it, 134 citations in OpenAlex.

  1. Pooled it
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  18. Review
  19. 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
  20. Article

1 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

1 author at 1 institution in 1 country.

Steven M SineDepartment of Physiology and Biomedical Engineering, Mayo Clinic College of Medicine, Rochester, Minnesota 55905, USA. sine@mayo.edu
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 NS-31744NINDS NIH HHS R01 NS031744NINDS NIH HHS R37 NS031744
6 · The paper itself

Abstract

The synapse is a localized neurohumoral contact between a neuron and an effector cell and may be considered the quantum of fast intercellular communication. Analogously, the postsynaptic neurotransmitter receptor may be considered the quantum of fast chemical to electrical transduction. Our understanding of postsynaptic receptors began to develop about a hundred years ago with the demonstration that electrical stimulation of the vagus nerve released acetylcholine and slowed the heart beat. During the past 50 years, advances in understanding postsynaptic receptors increased at a rapid pace, owing largely to studies of the acetylcholine receptor (AChR) at the motor endplate. The endplate AChR belongs to a large superfamily of neurotransmitter receptors, called Cys-loop receptors, and has served as an exemplar receptor for probing fundamental structures and mechanisms that underlie fast synaptic transmission in the central and peripheral nervous systems. Recent studies provide an increasingly detailed picture of the structure of the AChR and the symphony of molecular motions that underpin its remarkably fast and efficient chemoelectrical transduction.

Indexed as

Synaptic TransmissionAcetylcholineAction PotentialsAnimalsHumansModels, MolecularMotor EndplateMutationMyasthenia GravisProtein ConformationReceptors, CholinergicStructure-Activity RelationshipAcetylcholineReceptors, Cholinergic

Identifiers

PMID22811427
PMCPMC3489064
OpenAlexW2128505545

What OpenQuestion holds

Textmetadata
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.