Evidence map›Paper›PMID 32719334›Full record

ArticleNature communications2020

Mechanisms of activation and desensitization of full-length glycine receptor in lipid nanodiscs.

Arvind Kumar, Sandip Basak, Shanlin Rao, Yvonne Gicheru, Megan L Mayer, Mark S P Sansom, Sudha Chakrapani

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
74citing papers in PubMed, 1 pooled it
8.0field-weighted citation impact, top 1% 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

74 citing papers in PubMed, 1 synthesis or guideline pooled it, 117 citations in OpenAlex.

  1. Cys-loop receptors on cannabinoids: All high?Frontiers in physiology · 2022
    Pooled it
  2. Article
  3. Review
  4. Review
  5. Human GlyRα2 pore dynamics in gating and inhibition.Structure (London, England : 1993) · 2026
    Article
  6. Article
  7. Extracellular KNature communications · 2026
    Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Examining the thermotropic properties of large circularized nanodiscs.Biochimica et biophysica acta. Biomembranes · 2025
    Article
  13. Article
  14. Article
  15. 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
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

14 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

7 authors at 3 institutions in 2 countries.

Arvind KumarDepartment of Physiology and Biophysics, Case Western Reserve University, Cleveland, OH, 44106-4970, USA.ORCID http://orcid.org/0000-0002-8421-8669
Sandip BasakDepartment of Physiology and Biophysics, Case Western Reserve University, Cleveland, OH, 44106-4970, USA.ORCID http://orcid.org/0000-0003-4018-8020
Shanlin RaoDepartment of Biochemistry, University of Oxford, Oxford, OX1 3QU, UK.
Yvonne GicheruDepartment of Physiology and Biophysics, Case Western Reserve University, Cleveland, OH, 44106-4970, USA.
Megan L MayerDivision of CryoEM and Bioimaging, SSRL, SLAC National Accelerator Laboratory, Stanford University, Menlo Park, CA, 94025, USA.
Mark S P SansomDepartment of Biochemistry, University of Oxford, Oxford, OX1 3QU, UK.ORCID http://orcid.org/0000-0001-6360-7959
Sudha ChakrapaniDepartment of Physiology and Biophysics, Case Western Reserve University, Cleveland, OH, 44106-4970, USA. Sudha.chakrapani@case.edu.
Case Western Reserve University · USUniversity of Oxford · GBSLAC National Accelerator Laboratory · US

Funding

3 D ELECTRON MICROSCOPY OF MACROMOLECULES (5P41RR002250-27)P41GM103832 · NIGMS · STANFORD UNIVERSITY · PI CHIU, WAH · 2012 to 2019
$15.1M
Structure and Function of Pentameric Ligand-Gated Ion ChannelsR35GM134896 · NIGMS · CASE WESTERN RESERVE UNIVERSITY · PI Sudha Chakrapani · 2020 to 2026
$4.7M
Acquisition of a 300 kV Electron Microscope for Structural BiologyS10OD021600 · OD · STANFORD UNIVERSITY · PI CHIU, WAH · 2016 to 2016
$2.0M
MOLECULAR MECHANISMS OF DESENSITIZATION AND DRUG MODULATION IN LIGAND-GATED ION CHANNELSR01GM108921 · NIGMS · CASE WESTERN RESERVE UNIVERSITY · PI CHAKRAPANI, SUDHA · 2014 to 2018
$1.9M
STRUCTURE, FUNCTION, AND MODULATION OF SERORTONIN (3A) RECEPTORSR01GM131216 · NIGMS · CASE WESTERN RESERVE UNIVERSITY · PI CHAKRAPANI, SUDHA · 2019 to 2019
$442k
NIGMS NIH HHS P41 GM103832NIGMS NIH HHS R01 GM108921NIGMS NIH HHS R01 GM131216NIGMS NIH HHS R35 GM134896NIH HHS S10 OD021600
6 · The paper itself

Abstract

Glycinergic synapses play a central role in motor control and pain processing in the central nervous system. Glycine receptors (GlyRs) are key players in mediating fast inhibitory neurotransmission at these synapses. While previous high-resolution structures have provided insights into the molecular architecture of GlyR, several mechanistic questions pertaining to channel function are still unanswered. Here, we present Cryo-EM structures of the full-length GlyR protein complex reconstituted into lipid nanodiscs that are captured in the unliganded (closed), glycine-bound (open and desensitized), and allosteric modulator-bound conformations. A comparison of these states reveals global conformational changes underlying GlyR channel gating and modulation. The functional state assignments were validated by molecular dynamics simulations, and the observed permeation events are in agreement with the anion selectivity and conductance of GlyR. These studies provide the structural basis for gating, ion selectivity, and single-channel conductance properties of GlyR in a lipid environment.

Indexed as

Ion Channel GatingAllosteric RegulationAnimalsBinding SitesGlycineLipidsMolecular Dynamics SimulationNanoparticlesNeurotransmitter AgentsProtein ConformationReceptors, GlycineXenopusZebrafish Proteinsglra1 protein, zebrafishGlycineLipidsNeurotransmitter AgentsReceptors, GlycineZebrafish Proteins

Identifiers

PMID32719334
PMCPMC7385131
OpenAlexW3045228316

What OpenQuestion holds

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LicenceCC BY
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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.