Evidence map›Paper›PMID 24297903›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Stoichiometry for activation of neuronal α7 nicotinic receptors.

Natalia Andersen, Jeremías Corradi, Steven M Sine, Cecilia Bouzat

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
–field-weighted citation impact
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

54 citing papers in PubMed.

  1. Trial
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Nicotine: From Discovery to Biological Effects.International journal of molecular sciences · 2023
    Review
  9. Article
  10. Article
  11. Review
  12. Cannabidiol as a modulator of α7 nicotinic receptors.Cellular and molecular life sciences : CMLS · 2022
    Article
  13. Article
  14. Review
  15. Article
  16. Review
  17. Review
  18. Therapeutic Targeting ofPharmacological reviews · 2021
    Review
  19. Article
  20. 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
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.

Natalia AndersenInstituto de Investigaciones Bioquímicas, Universidad Nacional del Sur-Consejo Nacional de Investigaciones Científicas y Técnicas, 8000 Bahía Blanca, Argentina.
Jeremías Corradi
Steven M Sine
Cecilia Bouzat

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
Allosteric Coupling in Homomeric Cys-loop ReceptorsR01NS053521 · NINDS · MAYO CLINIC ROCHESTER · PI SINE, STEVEN M · 2006 to 2009
$1.3M
NINDS NIH HHS NS031744NINDS NIH HHS R01 NS031744NINDS NIH HHS R01 NS053521NINDS NIH HHS R37 NS031744
6 · The paper itself

Abstract

Neuronal α7 nicotinic receptors elicit rapid cation influx in response to acetylcholine (ACh) or its hydrolysis product choline. They contribute to cognition, synaptic plasticity, and neuroprotection and have been implicated in neurodegenerative and neuropsychiatric disorders. α7, however, often localizes distal to sites of nerve-released ACh and binds ACh with low affinity, and thus elicits its biological response with low agonist occupancy. To assess the function of α7 when ACh occupies fewer than five of its identical binding sites, we measured the open-channel lifetime of individual receptors in which four of the five ACh binding sites were disabled. To improve the time resolution of the inherently brief α7 channel openings, background mutations or a potentiator was used to increase open duration. We find that, in receptors with only one intact binding site, the open-channel lifetime is indistinguishable from receptors with five intact binding sites, counter to expectations from prototypical neurotransmitter-gated ion channels where the open-channel lifetime increases with the number of binding sites occupied by agonist. Replacing the membrane-embedded domain of α7 by that of the related 5-HT3A receptor increases the number of sites that need to be occupied to achieve the maximal open-channel lifetime, thus revealing a unique interdependence between the detector and actuator domains of these receptors. The distinctive ability of a single occupancy to elicit a full biological response adapts α7 to volume transmission, a prevalent mechanism of ACh-mediated signaling in the nervous system and nonneuronal cells.

Indexed as

Acetylcholinealpha7 Nicotinic Acetylcholine ReceptorBinding SitesHEK293 CellsHumansMutationProtein Structure, TertiaryReceptors, Serotonin, 5-HT3Signal TransductionAcetylcholinealpha7 Nicotinic Acetylcholine ReceptorReceptors, Serotonin, 5-HT3agonist binding sitechannel gatingCys-loop receptorspatch-clampα7 nicotinic receptor

Identifiers

PMID24297903
PMCPMC3870720

What OpenQuestion holds

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Read underepoch 390

Registered trials

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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.