Evidence map›Paper›PMID 25964432›Full record

ArticleThe Journal of general physiology2015

Glycine-dependent activation of NMDA receptors.

Kirstie A Cummings, Gabriela K Popescu

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of general physiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed, 1 pooled it
2.1field-weighted citation impact, top 14% 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

52 citing papers in PubMed, 1 synthesis or guideline pooled it, 87 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Aloin attenuates NMDA receptor by modulating calcium response on substantia gelatinosa neurons of the trigeminal subnucleus caudalis in mice.The Korean journal of physiology & pharmacology : official journal of the Korean Physiological Society and the Korean Society of Pharmacology · 2026
    Article
  4. Review
  5. UntargetedTranslational psychiatry · 2026
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  9. Review
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  12. Review
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  16. d-Serine Inhibits Non-ionotropic NMDA Receptor Signaling.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2024
    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

2 authors at 1 institution in 1 country.

Kirstie A CummingsDepartment of Biochemistry, University at Buffalo, State University of New York, Buffalo, NY 14214.
Gabriela K PopescuDepartment of Biochemistry, University at Buffalo, State University of New York, Buffalo, NY 14214 popescu@buffalo.edu.
University at Buffalo, State University of New York · US

Funding

Probing allosteric surfaces of NMDA receptorsR01NS052669 · NINDS · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI POPESCU, GABRIELA K · 2006 to 2015
$3.4M
GATING KINETICS OF GLYCINERGIC NMDA RECEPTORSF31NS086765 · NINDS · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI CUMMINGS, KIRSTIE ALYSSA · 2013 to 2015
$77k
NINDS NIH HHS F31 NS086765NINDS NIH HHS F31NS086765NINDS NIH HHS R01 NS052669NINDS NIH HHS R01NS052669
6 · The paper itself

Abstract

N-methyl-d-aspartate (NMDA) receptors are the only neurotransmitter receptors whose activation requires two distinct agonists. Heterotetramers of two GluN1 and two GluN2 subunits, NMDA receptors are broadly distributed in the central nervous system, where they mediate excitatory currents in response to synaptic glutamate release. Pore opening depends on the concurrent presence of glycine, which modulates the amplitude and time course of the glutamate-elicited response. Gating schemes for fully glutamate- and glycine-bound NMDA receptors have been described in sufficient detail to bridge the gap between microscopic and macroscopic receptor behaviors; for several receptor isoforms, these schemes include glutamate-binding steps. We examined currents recorded from cell-attached patches containing one GluN1/GluN2A receptor in the presence of several glycine-site agonists and used kinetic modeling of these data to develop reaction schemes that include explicit glycine-binding steps. Based on the ability to match a series of experimentally observed macroscopic behaviors, we propose a model for activation of the glutamate-bound NMDA receptor by glycine that predicts apparent negative agonist cooperativity and glycine-dependent desensitization in the absence of changes in microscopic binding or desensitization rate constants. These results complete the basic steps of an NMDA receptor reaction scheme for the GluN1/GluN2A isoform and prompt a reevaluation of how glycine controls NMDA receptor activation. We anticipate that our model will provide a useful quantitative instrument to further probe mechanisms and structure-function relationships of NMDA receptors and to better understand the physiological and pathological implications of endogenous fluctuations in extracellular glycine concentrations.

Indexed as

Ion Channel GatingSynaptic TransmissionAction PotentialsComputer SimulationGlycineHEK293 CellsHumansKineticsModels, BiologicalMolecular Sequence DataProtein SubunitsReceptors, N-Methyl-D-AspartateTransfectionGlycineProtein SubunitsReceptors, N-Methyl-D-Aspartate

Identifiers

PMID25964432
PMCPMC4442789
OpenAlexW2163922059

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.