Evidence map›Paper›PMID 29313059›Full record

ArticleCellular and molecular life sciences : CMLS2018

Molecular function of the novel α7β2 nicotinic receptor.

Beatriz E Nielsen, Teresa Minguez, Isabel Bermudez, Cecilia Bouzat

Open access · bronzeAbstract read
In one paragraph

Article in Cellular and molecular life sciences : CMLS, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

17 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Analogs of α-conotoxin PnIC selectively inhibit α7β2- over α7-only subtype nicotinic acetylcholine receptors via a novel allosteric mechanism.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2024
    Article
  3. Review
  4. Cannabidiol as a modulator of α7 nicotinic receptors.Cellular and molecular life sciences : CMLS · 2022
    Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Implications of Oligomeric Amyloid-Beta (oAβThe Journal of neuroscience : the official journal of the Society for Neuroscience · 2021
    Article
  10. Review
  11. Article
  12. Article
  13. A New Antagonist ofFrontiers in neuroscience · 2020
    Article
  14. Article
  15. Complex Control of Striatal Neurotransmission by Nicotinic Acetylcholine Receptors via Excitatory Inputs onto Medium Spiny Neurons.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2018
    Article
  16. Article
  17. 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 at 2 institutions in 2 countries.

Beatriz E NielsenInstituto de Investigaciones Bioquímicas de Bahía Blanca, Departamento de Biología, Bioquímica y Farmacia, Universidad Nacional del Sur-Consejo Nacional de Investigaciones Científicas y Técnicas (UNS-CONICET), 8000, Bahía Blanca, Argentina.ORCID http://orcid.org/0000-0001-9927-3639
Teresa MinguezDepartment of Medical and Biological Sciences, Oxford Brookes University, Oxford, OX3 0BP, UK.
Isabel BermudezDepartment of Medical and Biological Sciences, Oxford Brookes University, Oxford, OX3 0BP, UK.
Cecilia BouzatInstituto de Investigaciones Bioquímicas de Bahía Blanca, Departamento de Biología, Bioquímica y Farmacia, Universidad Nacional del Sur-Consejo Nacional de Investigaciones Científicas y Técnicas (UNS-CONICET), 8000, Bahía Blanca, Argentina. inbouzat@criba.edu.ar.ORCID http://orcid.org/0000-0003-0388-6129
Consejo Nacional de Investigaciones Científicas y Técnicas · AROxford Brookes University · GB

Funding

Agencia Nacional de Promoción Científica y Tecnológica PICT 2013 393Agencia Nacional de Promoción Científica y Tecnológica PICT 2015 0941
6 · The paper itself

Abstract

The α7 nicotinic receptor is a promising drug target for neurological and inflammatory disorders. Although it is the homomeric member of the family, a novel α7β2 heteromeric receptor has been discovered. To decipher the functional contribution of the β2 subunit, we generated heteromeric receptors with fixed stoichiometry by two different approaches comprising concatenated and unlinked subunits. Receptors containing up to three β2 subunits are functional. As the number of β2 subunits increases in the pentameric arrangement, the durations of channel openings and activation episodes increase progressively probably due to decreased desensitization. The prolonged activation episodes conform the kinetic signature of α7β2 and may have an impact on neuronal excitability. For activation of α7β2 receptors, an α7/α7 binding-site interface is required, thus indicating that the three β2 subunits are located consecutively in the pentameric arrangement. α7-positive allosteric modulators (PAMs) are emerging as novel therapeutic drugs. The presence of β2 in the pentamer affects neither type II PAM potentiation nor activation by an allosteric agonist whereas it impairs type I PAM potentiation. This first single-channel study provides fundamental basis required to decipher the role and function of the novel α7β2 receptor and opens doors to develop selective therapeutic drugs.

Indexed as

alpha7 Nicotinic Acetylcholine ReceptorAnimalsBinding SitesCell LineHEK293 CellsHumansOocytesProtein SubunitsXenopusalpha7 Nicotinic Acetylcholine ReceptorProtein SubunitsCys-loop receptorsNicotinic receptorPatch-clampSingle-channel recordings

Identifiers

PMID29313059
PMCPMC11105712
OpenAlexW2783862467

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.