Evidence map›Paper›PMID 29681798›Full record

ArticleFrontiers in molecular neuroscience2018

The LILI Motif of M3-S2 Linkers Is a Component of the NMDA Receptor Channel Gate.

Marek Ladislav, Jiri Cerny, Jan Krusek, Martin Horak, Ales Balik, Ladislav Vyklicky

Open access · goldAbstract read
In one paragraph

Article in Frontiers in molecular neuroscience, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

22 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
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  4. Characterization of Mice Carrying a Neurodevelopmental Disease-Associated GluN2B(L825V) Variant.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2024
    Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. PYTHIA: Deep Learning Approach for Local Protein Conformation Prediction.International journal of molecular sciences · 2021
    Article
  10. Palmitoylation Controls NMDA Receptor Function and Steroid Sensitivity.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2021
    Article
  11. Article
  12. Cross-subunit interactions that stabilize open states mediate gating in NMDA receptors.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  13. Review
  14. Article
  15. Site of Action of Brain Neurosteroid Pregnenolone Sulfate at the N-Methyl-D-Aspartate Receptor.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2020
    Article
  16. Article
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  18. Article
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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

6 authors at 1 institution in 1 country.

Marek LadislavDepartment of Cellular Neurophysiology, Institute of Physiology of the Czech Academy of Sciences, Prague, Czechia.
Jiri CernyDepartment of Cellular Neurophysiology, Institute of Physiology of the Czech Academy of Sciences, Prague, Czechia.
Jan KrusekDepartment of Cellular Neurophysiology, Institute of Physiology of the Czech Academy of Sciences, Prague, Czechia.
Martin HorakDepartment of Cellular Neurophysiology, Institute of Physiology of the Czech Academy of Sciences, Prague, Czechia.
Ales BalikDepartment of Cellular Neurophysiology, Institute of Physiology of the Czech Academy of Sciences, Prague, Czechia.
Ladislav VyklickyDepartment of Cellular Neurophysiology, Institute of Physiology of the Czech Academy of Sciences, Prague, Czechia.
Czech Academy of Sciences · CZ

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

N-methyl-D-aspartate receptors (NMDARs) mediate excitatory synaptic transmission in the central nervous system, underlie the induction of synaptic plasticity, and their malfunction is associated with human diseases. Native NMDARs are tetramers composed of two obligatory GluN1 subunits and various combinations of GluN2A-D or, more rarely, GluN3A-B subunits. Each subunit consists of an amino-terminal, ligand-binding, transmembrane and carboxyl-terminal domain. The ligand-binding and transmembrane domains are interconnected via polypeptide chains (linkers). Upon glutamate and glycine binding, these receptors undergo a series of conformational changes leading to the opening of the Ca

Indexed as

channel open probabilityelectrophysiologyglutamate receptor gatingmolecular modelingprotein block alphabetspontaneous activity

Identifiers

PMID29681798
PMCPMC5897735
OpenAlexW2795778689

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.