Evidence map›Paper›PMID 16223763›Full record

ArticleThe Journal of physiology2005

Maximum likelihood fitting of single channel NMDA activity with a mechanism composed of independent dimers of subunits.

Stephanie Schorge, Sergio Elenes, David Colquhoun

Open access · greenAbstract read
In one paragraph

Article in The Journal of physiology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
1.7field-weighted citation impact, top 19% 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

65 citing papers in PubMed, 89 citations in OpenAlex.

  1. Article
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  6. Review
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  11. NMDA receptor channel gating control by the pre-M1 helix.The Journal of general physiology · 2020
    Article
  12. Article
  13. Article
  14. Review
  15. Memantine and Ketamine Differentially Alter NMDA Receptor Desensitization.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2017
    Article
  16. Review
  17. Review
  18. Review
  19. NMDA Receptors in the Central Nervous System.Methods in molecular biology (Clifton, N.J.) · 2017
    Article
  20. Review

5 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

3 authors at 1 institution in 1 country.

Stephanie SchorgeDepartment of Pharmacology, UCL, London WC1E 6BT, UK.
Sergio Elenes
David Colquhoun
University College London · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

Steady-state single channel activity from NMDA receptors was recorded at a range of concentrations of both glutamate and glycine. The results were fitted with several plausible mechanisms that describe both binding and gating. The mechanisms we have tested were based on our present understanding of receptor structure, or based on previously proposed mechanisms for these receptors. The steady-state channel properties appear to have virtually no dependence on the concentration of either ligand, other than the frequency of channel activations. This limited the ability to discriminate detail in the mechanism, and, along with the persistence of open-shut correlations in high agonist concentrations, suggests that NMDA channels, unlike other neurotransmitter receptors, cannot open unless all binding sites are occupied. As usual for analyses of NMDA channels, the applicability of our results to physiological observations is limited by uncertainties in synaptic zinc and hydrogen ion concentrations, both of these being known to affect the receptor. The mechanism that we propose, on the basis of steady-state single channel recordings, predicts with fair accuracy the apparent open and shut-time distributions in different concentrations of agonists, correlations between open and shut times, and both the rising and falling phases of the macroscopic response to concentration jumps, and can therefore account for the main features of synaptic currents.

Indexed as

AnimalsData Interpretation, StatisticalEdetic AcidFemaleGlutamic AcidGlycineHydrogen-Ion ConcentrationIon Channel GatingIon ChannelsLikelihood FunctionsMembrane PotentialsPatch-Clamp TechniquesProbabilityProtein BindingReceptors, GlutamateReceptors, GlycineEdetic AcidGlutamic AcidGlycineIon ChannelsReceptors, GlutamateReceptors, GlycineReceptors, N-Methyl-D-Aspartate

Identifiers

PMID16223763
PMCPMC1464248
OpenAlexW1487516183

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.