Evidence map›Paper›PMID 22000510›Full record

ReviewStructure (London, England : 1993)2011

Emerging models of glutamate receptor ion channel structure and function.

Mark L Mayer

Open access · bronzeAbstract readReview
In one paragraph

Review in Structure (London, England : 1993), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
4.5field-weighted citation impact, top 4% 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

48 citing papers in PubMed, 74 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. NMDA receptor channel gating control by the pre-M1 helix.The Journal of general physiology · 2020
    Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Pharmacological Strategies for Manipulating Plant CaInternational journal of molecular sciences · 2018
    Review
  10. Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Functional Evaluation of a De NovoMolecular pharmacology · 2017
    Article
  16. Article
  17. Article
  18. Structural rearrangement of the intracellular domains during AMPA receptor activation.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  19. Article
  20. 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

1 author at 1 institution in 1 country.

Mark L MayerLaboratory of Cellular and Molecular Neurophysiology, Porter Neuroscience Research Center, NICHD, NIH, DHHS, Bethesda, MD 20892, USA. mayerm@mail.nih.gov
National Institutes of Health · US

Funding

Structure And Function Of Neurotransmitter Receptor Ion ChannelsZIAHD000707 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI MAYER, MARK L · 2009 to 2015
$9.5M
Intramural NIH HHS ZIA HD000707
6 · The paper itself

Abstract

Excitatory synaptic transmission in the brain is mediated by ligand-gated ion channels (iGluRs) activated by glutamate. Distinct from other neurotransmitter receptors, the extracellular domains of iGluRs are loosely packed assemblies with two clearly distinct layers, each of which has both local and global 2-fold axes of symmetry. By contrast, the iGluR transmembrane segments have 4-fold symmetry and share a conserved pore loop architecture found in tetrameric voltage-gated ion channels. The striking layered architecture of iGluRs revealed by the 3.6 Å resolution structure of an AMPA receptor homotetramer likely arose from gene fusion events that occurred early in evolution. Although this modular design has greatly facilitated biophysical and structural studies on individual iGluR domains, and suggested conserved mechanisms for iGluR gating, recent work is beginning to reveal unanticipated diversity in the structure, allosteric regulation, and assembly of iGluR subtypes.

Indexed as

Ion Channel GatingModels, MolecularAnimalsBinding SitesBiophysical PhenomenaCrystallography, X-RayExcitatory Amino Acid AgonistsGlutamic AcidLigandsMembrane ProteinsMutationProtein ConformationProtein MultimerizationRatsReceptors, Ionotropic GlutamateStructure-Activity RelationshipExcitatory Amino Acid AgonistsGlutamic AcidLigandsMembrane ProteinsReceptors, Ionotropic GlutamateXenopus Proteins

Identifiers

PMID22000510
PMCPMC3197216
OpenAlexW2103009824

What OpenQuestion holds

Textmetadata
LicenceTDM
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.