Evidence map›Paper›PMID 25721789›Full record

ArticleBrain research2015

Allosteric modulation of the glycine receptor activated by agonists differing in efficacy.

Nicole-Marie M Farley, S John Mihic

Open access · greenAbstract read
In one paragraph

Article in Brain research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.7field-weighted citation impact, top 35% 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

3 citing papers in PubMed, 6 citations in OpenAlex.

  1. Interactions between Zinc and Allosteric Modulators of the Glycine Receptor.The Journal of pharmacology and experimental therapeutics · 2017
    Article
  2. Review
  3. 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

2 authors at 1 institution in 1 country.

Nicole-Marie M FarleyDepartment of Neuroscience, Division of Pharmacology and Toxicology, Waggoner Center for Alcohol & Addiction Research, Institutes for Neuroscience and Cell & Molecular Biology, University of Texas at Austin, Austin, TX 78712, USA.
S John MihicDepartment of Neuroscience, Division of Pharmacology and Toxicology, Waggoner Center for Alcohol & Addiction Research, Institutes for Neuroscience and Cell & Molecular Biology, University of Texas at Austin, Austin, TX 78712, USA. Electronic address: mihic@austin.utexas.edu.
The University of Texas at Austin · US

Funding

Novel molecular and cellular approaches for alcoholism medication developmentP01AA020683 · NIAAA · UNIVERSITY OF TEXAS AT AUSTIN · PI MIHIC, S JOHN · 2012 to 2016
$3.3M
NIAAA NIH HHS P01 AA020683NIAAA NIH HHS P01AA020683
6 · The paper itself

Abstract

The glycine receptor (GlyR) is the predominant inhibitory neurotransmitter receptor in the brainstem and spinal cord but is also found in higher brain regions. GlyR function is affected by a variety of allosteric modulators including drugs of abuse, such as ethanol and inhalants and the ubiquitous divalent cation zinc. Two-electrode voltage-clamp experiments were conducted on Xenopus laevis oocytes expressing wild-type α1 homomeric glycine receptors to compare the degree of enhancement produced by zinc on GlyR activated by two agonists (glycine vs. taurine) that vary markedly in their efficacies. Zinc potentiation of both glycine- and taurine-evoked currents was the same at the concentrations of agonists that produced the same currents, corresponding to 6% of the maximal effect of glycine compared to 23% of the maximal effect of taurine. Similar results were seen with 50 and 200 mM ethanol. A direct comparison of agonist concentration-response curves showed that zinc enhancement was greater, overall, for taurine-activated than glycine-activated receptors. In addition, zinc only enhanced taurine- but not glycine-activated GlyR when agonists were applied at saturating concentrations. These data suggest that zinc affects taurine affinity, as well as the probability of channel opening at sub-maximal taurine concentrations, and that the magnitude of allosteric modulation at the GlyR depends on the efficacy of the agonist tested. This has implications for mutagenesis studies in which changes in the degree of allosteric modulation observed may result from mutation-induced changes in agonist efficacy.

Indexed as

Allosteric RegulationAnimalsDose-Response Relationship, DrugGlycineReceptors, GlycineTaurineXenopus laevisZincGlycineReceptors, GlycineTaurineZincAllosteric modulationElectrophysiologyEthanolGlycine receptorXenopus oocytesZinc

Identifiers

PMID25721789
PMCPMC4398968
OpenAlexW2005517159

What OpenQuestion holds

Textmetadata
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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.