Evidence map›Paper›PMID 27401877›Full record

ReviewMolecular pharmacology2016

Structure and Pharmacologic Modulation of Inhibitory Glycine Receptors.

Carlos F Burgos, Gonzalo E Yévenes, Luis G Aguayo

Open access · bronzeAbstract readReview
In one paragraph

Review in Molecular pharmacology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed, 1 pooled it
4.4field-weighted citation impact, top 5% 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

37 citing papers in PubMed, 1 synthesis or guideline pooled it, 82 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Extracellular KNature communications · 2026
    Article
  5. Article
  6. Asymmetric gating of a homopentameric ion channel GLIC revealed by cryo-EM.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. The Concise Guide to PHARMACOLOGY 2023/24: Ion channels.British journal of pharmacology · 2023
    Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Review
  17. Review
  18. Review
  19. Article
  20. Review
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

3 authors at 1 institution in 1 country.

Carlos F BurgosLaboratory of Neurophysiology (C.F.B., L.G.A.), and Laboratory of Neuropharmacology (G.E.Y.), Department of Physiology, University of Concepción, Concepción, Chile.
Gonzalo E YévenesLaboratory of Neurophysiology (C.F.B., L.G.A.), and Laboratory of Neuropharmacology (G.E.Y.), Department of Physiology, University of Concepción, Concepción, Chile.
Luis G AguayoLaboratory of Neurophysiology (C.F.B., L.G.A.), and Laboratory of Neuropharmacology (G.E.Y.), Department of Physiology, University of Concepción, Concepción, Chile laguayo@udec.cl.
University of Concepción · CL

Funding

Potentiation of Glycine Receptors by EthanolR01AA015150 · NIAAA · UNIVERSITY OF CONCEPCION · PI AGUAYO, LUIS GERARDO · 2004 to 2010
$1.1M
NIAAA NIH HHS R01 AA015150
6 · The paper itself

Abstract

Glycine receptors (GlyR) are inhibitory Cys-loop ion channels that contribute to the control of excitability along the central nervous system (CNS). GlyR are found in the spinal cord and brain stem, and more recently they were reported in higher regions of the CNS such as the hippocampus and nucleus accumbens. GlyR are involved in motor coordination, respiratory rhythms, pain transmission, and sensory processing, and they are targets for relevant physiologic and pharmacologic modulators. Several studies with protein crystallography and cryoelectron microscopy have shed light on the residues and mechanisms associated with the activation, blockade, and regulation of pentameric Cys-loop ion channels at the atomic level. Initial studies conducted on the extracellular domain of acetylcholine receptors, ion channels from prokaryote homologs-Erwinia chrysanthemi ligand-gated ion channel (ELIC), Gloeobacter violaceus ligand-gated ion channel (GLIC)-and crystallized eukaryotic receptors made it possible to define the overall structure and topology of the Cys-loop receptors. For example, the determination of pentameric GlyR structures bound to glycine and strychnine have contributed to visualizing the structural changes implicated in the transition between the open and closed states of the Cys-loop receptors. In this review, we summarize how the new information obtained in functional, mutagenesis, and structural studies have contributed to a better understanding of the function and regulation of GlyR.

Indexed as

AnimalsBinding SitesHumansIon Channel GatingModels, MolecularProtein Structure, SecondaryReceptors, GlycineReceptors, Glycine

Identifiers

PMID27401877
PMCPMC4998662
OpenAlexW2473367284

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.