Evidence map›Paper›PMID 29887499›Full record

ArticleStructure (London, England : 1993)2018

Glutamate and Glycine Binding to the NMDA Receptor.

Alvin Yu, Albert Y Lau

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

36 citing papers in PubMed, 61 citations in OpenAlex.

  1. Voltage-sensor conformational microenvironments encode isoform-selective ion channel activation.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Review
  3. Primary cilia and neural computation.Journal of biomedical science · 2026
    Review
  4. Article
  5. Article
  6. Review
  7. A conifer metabolite corrects episodic ataxia type 1 by voltage sensor-mediated ligand activation of Kv1.1.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. Structural insights into NMDA receptor pharmacology.Biochemical Society transactions · 2023
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Effects of glycine on metabolic syndrome components: a review.Journal of endocrinological investigation · 2022
    Review
  19. Review
  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

2 authors at 1 institution in 1 country.

Alvin YuProgram in Molecular Biophysics, Johns Hopkins University, Baltimore, MD 21218, USA; Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
Albert Y LauProgram in Molecular Biophysics, Johns Hopkins University, Baltimore, MD 21218, USA; Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA. Electronic address: alau@jhmi.edu.
Johns Hopkins University · US

Funding

PROGRAM IN MOLECULAR BIOPHYSICST32GM008403 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI BARRICK, DOUGLAS E. · 1990 to 2019
$13.5M
Breakthrough Molecular Dynamics Research via an Anton2 SupercomputerR01GM116961 · NIGMS · CARNEGIE-MELLON UNIVERSITY · PI BLOOD, PHILIP D. · 2016 to 2023
$3.0M
Structural dynamics and function of the glutamate receptor ligand-binding domainR01GM094495 · NIGMS · UNIVERSITY OF CHICAGO · PI LAU, ALBERT Y · 2010 to 2013
$1.0M
NIGMS NIH HHS R01 GM094495NIGMS NIH HHS R01 GM116961NIGMS NIH HHS T32 GM008403
6 · The paper itself

Abstract

At central nervous system synapses, agonist binding to postsynaptic ionotropic glutamate receptors (iGluRs) results in signaling between neurons. N-Methyl-D-aspartic acid (NMDA) receptors are a unique family of iGluRs that activate in response to the concurrent binding of glutamate and glycine. Here, we investigate the process of agonist binding to the GluN2A (glutamate binding) and GluN1 (glycine binding) NMDA receptor subtypes using long-timescale unbiased molecular dynamics simulations. We find that positively charged residues on the surface of the GluN2A ligand-binding domain (LBD) assist glutamate binding via a "guided-diffusion" mechanism, similar in fashion to glutamate binding to the GluA2 LBD of AMPA receptors. Glutamate can also bind in an inverted orientation. Glycine, on the other hand, binds to the GluN1 LBD via an "unguided-diffusion" mechanism, whereby glycine finds its binding site primarily by random thermal fluctuations. Free energy calculations quantify the glutamate- and glycine-binding processes.

Indexed as

AnimalsBinding SitesCrystallography, X-RayGlutamic AcidGlycineHumansMolecular Dynamics SimulationProtein BindingProtein DomainsProtein Structure, TertiaryReceptors, N-Methyl-D-AspartateGlutamic AcidGlycineReceptors, N-Methyl-D-Aspartatefree energy calculationsglutamate receptorsligand bindingmolecular dynamics simulationsNMDA receptors

Identifiers

PMID29887499
PMCPMC6031449
OpenAlexW2806876216

What OpenQuestion holds

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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.