Evidence map›Paper›PMID 27040756›Full record

ArticleScientific reports2016

Fyn Kinase regulates GluN2B subunit-dominant NMDA receptors in human induced pluripotent stem cell-derived neurons.

Wen-Bo Zhang, P Joel Ross, YuShan Tu, Yongqian Wang, Simon Beggs, Ameet S Sengar, James Ellis, Michael W Salter

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.2field-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

18 citing papers in PubMed, 37 citations in OpenAlex.

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  5. Src dependency of the regulation of LTP by alternative splicing ofPhilosophical transactions of the Royal Society of London. Series B, Biological sciences · 2024
    Article
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  7. GSK-3β, FYN, and DYRK1A: Master Regulators in Neurodegenerative Pathways.International journal of molecular sciences · 2021
    Review
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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

8 authors at 2 institutions in 1 country.

Wen-Bo ZhangProgram in Neurosciences &Mental Health, The Hospital for Sick Children, Toronto, ON, M5G 0A4, Canada.
P Joel RossProgram in Developmental &Stem Cell Biology, The Hospital for Sick Children, Toronto, ON, M5G 0A4, Canada.
YuShan TuProgram in Neurosciences &Mental Health, The Hospital for Sick Children, Toronto, ON, M5G 0A4, Canada.
Yongqian WangProgram in Neurosciences &Mental Health, The Hospital for Sick Children, Toronto, ON, M5G 0A4, Canada.
Simon BeggsProgram in Neurosciences &Mental Health, The Hospital for Sick Children, Toronto, ON, M5G 0A4, Canada.
Ameet S SengarProgram in Neurosciences &Mental Health, The Hospital for Sick Children, Toronto, ON, M5G 0A4, Canada.
James EllisProgram in Developmental &Stem Cell Biology, The Hospital for Sick Children, Toronto, ON, M5G 0A4, Canada.
Michael W SalterProgram in Neurosciences &Mental Health, The Hospital for Sick Children, Toronto, ON, M5G 0A4, Canada.
Hospital for Sick Children · CAUniversity of Toronto · CA

Funding

Canadian Institutes of Health Research MOP-133423
6 · The paper itself

Abstract

NMDA receptor (NMDAR)-mediated fast excitatory neurotransmission is implicated in a broad range of physiological and pathological processes in the mammalian central nervous system. The function and regulation of NMDARs have been extensively studied in neurons from rodents and other non-human species, and in recombinant expression systems. Here, we investigated human NMDARs in situ by using neurons produced by directed differentiation of human induced pluripotent stem cells (iPSCs). The resultant cells showed electrophysiological characteristics demonstrating that they are bona fide neurons. In particular, human iPSC-derived neurons expressed functional ligand-gated ion channels, including NMDARs, AMPA receptors, GABAA receptors, as well as glycine receptors. Pharmacological and electrophysiological properties of NMDAR-mediated currents indicated that these were dominated by receptors containing GluN2B subunits. The NMDAR currents were suppressed by genistein, a broad-spectrum tyrosine kinase inhibitor. The NMDAR currents were also inhibited by a Fyn-interfering peptide, Fyn(39-57), but not a Src-interfering peptide, Src(40-58). Together, these findings are the first evidence that tyrosine phosphorylation regulates the function of NMDARs in human iPSC-derived neurons. Our findings provide a basis for utilizing human iPSC-derived neurons in screening for drugs targeting NMDARs in neurological disorders.

Indexed as

Cell DifferentiationCells, CulturedGenisteinHumansInduced Pluripotent Stem CellsNeuronal PlasticityNeuronsProto-Oncogene Proteins c-fynReceptors, N-Methyl-D-AspartateSynaptic TransmissionFYN protein, humanGenisteinNR2B NMDA receptorProto-Oncogene Proteins c-fynReceptors, N-Methyl-D-Aspartate

Identifiers

PMID27040756
PMCPMC4819183
OpenAlexW2340986337

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

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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.