Evidence map›Paper›PMID 25231980›Full record

ArticleThe Journal of biological chemistry2014

Glycine induces bidirectional modifications in N-methyl-D-aspartate receptor-mediated synaptic responses in hippocampal CA1 neurons.

Xiao-Yan Zhang, Fang Ji, Ning Wang, Lin-Lin Chen, Tian Tian, Wei Lu

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.7field-weighted citation impact, top 36% 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

12 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
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  5. Dendritic Spines of Layer 5 Pyramidal Neurons of the Aging Somatosensory Cortex Exhibit Reduced Volumetric Remodeling.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2024
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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 2 institutions in 1 country.

Xiao-Yan ZhangFrom the Department of Neurobiology, Nanjing Medical University, Nanjing, Jiangsu Province 210029.
Fang JiFrom the Department of Neurobiology, Nanjing Medical University, Nanjing, Jiangsu Province 210029.
Ning WangFrom the Department of Neurobiology, Nanjing Medical University, Nanjing, Jiangsu Province 210029, The Key Laboratory of Developmental Genes and Human Disease, Ministry of Education, Institute of Life Sciences, Southeast University, Nanjing, Jiangsu Province 210096, China, and.
Lin-Lin ChenFrom the Department of Neurobiology, Nanjing Medical University, Nanjing, Jiangsu Province 210029.
Tian TianFrom the Department of Neurobiology, Nanjing Medical University, Nanjing, Jiangsu Province 210029.
Wei LuFrom the Department of Neurobiology, Nanjing Medical University, Nanjing, Jiangsu Province 210029, The Key Laboratory of Developmental Genes and Human Disease, Ministry of Education, Institute of Life Sciences, Southeast University, Nanjing, Jiangsu Province 210096, China, and Co-innovation Center of Neuroregeneration, Nantong University, Nantong, Jiangsu Province 226001, China lu@njmu.edu.cn luwei@seu.edu.cn.
Nanjing Medical University · CNSoutheast University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glycine can persistently potentiate or depress AMPA responses through differential actions on two binding sites: NMDA and glycine receptors. Whether glycine can induce long-lasting modifications in NMDA responses, however, remains unknown. Here, we report that glycine induces long-term potentiation (LTP) or long-term depression (LTD) of NMDA responses (Gly-LTP(NMDA) or Gly-LTD(NMDA)) in a dose-dependent manner in hippocampal CA1 neurons. These modifications of NMDA responses depend on NMDAR activation. In addition, the induction of Gly-LTP(NMDA) requires binding of glycine with NMDARs, whereas Gly-LTD(NMDA) requires that glycine bind with both sites on NMDARs and GlyRs. Moreover, activity-dependent exocytosis and endocytosis of postsynaptic NMDARs underlie glycine-induced bidirectional modification of NMDA excitatory postsynaptic currents. Thus, we conclude that glycine at different levels induces bidirectional plasticity of NMDA responses through differentially regulating NMDA receptor trafficking. Our present findings reveal important functions of the two glycine binding sites in gating the direction of synaptic plasticity in NMDA responses.

Indexed as

AnimalsBinding SitesBiological TransportBrainCA1 Region, HippocampalElectrophysiologyExcitatory Postsynaptic PotentialsGlycineMaleMembrane GlycoproteinsNeuronal PlasticityNeuronsN-MethylaspartateProtein BindingRatsRats, Sprague-DawleyGlycineGrin3a protein, ratMembrane GlycoproteinsN-MethylaspartateReceptors, GlycineReceptors, N-Methyl-D-AspartateGlycineGlycine ReceptorIonotropic Glutamate ReceptorLTDLTPMembrane TraffickingMembrane TransportNMDA ReceptorsSynaptic Plasticity

Identifiers

PMID25231980
PMCPMC4223322
OpenAlexW2089541589

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.