Evidence map›Paper›PMID 10489260›Full record

ArticleLearning & memory (Cold Spring Harbor, N.Y.)

Higher seizure susceptibility and enhanced tyrosine phosphorylation of N-methyl-D-aspartate receptor subunit 2B in fyn transgenic mice.

N Kojima, H Ishibashi, K Obata, E R Kandel

Open access · bronzeAbstract read
In one paragraph

Article in Learning & memory (Cold Spring Harbor, N.Y.). The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
–field-weighted citation impact
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

39 citing papers in PubMed, 91 citations in OpenAlex.

  1. Article
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  3. Review
  4. Review
  5. Apoptosis regulation by the tyrosine-protein kinase CSK.Frontiers in cell and developmental biology · 2022
    Review
  6. Article
  7. Differential Impact of Severity and Duration ofFrontiers in cellular neuroscience · 2021
    Article
  8. Review
  9. Article
  10. Article
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  12. Article
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  14. Article
  15. Article
  16. Src family kinases in chronic kidney disease.American journal of physiology. Renal physiology · 2017
    Review
  17. Article
  18. Review
  19. 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

4 authors at 3 institutions in 2 countries.

N KojimaLaboratory of Neurochemistry, National Institute for Physiological Sciences, Okazaki, Japan.
H Ishibashi
K Obata
E R Kandel
Howard Hughes Medical Institute · USColumbia University · USNew York State Psychiatric Institute

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Earlier work has suggested that Fyn tyrosine kinase plays an important role in synaptic plasticity. To understand the downstream targets of Fyn signaling cascade in neurons, we generated transgenic mice expressing either a constitutively activated form of Fyn or native Fyn in neurons of the forebrain. Transgenic mice expressing mutant Fyn exhibited higher seizure activity and were prone to sudden death. Mice overexpressing native Fyn did not show such an obvious epileptic phenotype, but they exhibited accelerated kindling in response to once-daily stimulation of the amygdala. Tyrosine phosphorylation of at least three proteins was enhanced in the forebrains of both native and mutant fyn transgenic mice; tyrosine phosphorylation of these three proteins was reduced in fyn knockout mice, suggesting that they are substrates of Fyn. One of these proteins was identified as the subunit 2B (NR2B) of the N-methyl-D-aspartate (NMDA) receptor. Administration of MK-801, a noncompetitive NMDA receptor antagonist, retarded kindling in mice overexpressing native Fyn, as well as wild-type mice, suggests that the accelerated kindling in mice overexpressing Fyn is also mediated by the NMDA receptor activity. Our results thus suggest that tyrosine phosphorylation by Fyn might be involved in regulation of the susceptibility of kindling, one form of the NMDA receptor-mediated neuronal plasticity.

Indexed as

Amino Acid SequenceAnimalsCalcium-Calmodulin-Dependent Protein KinasesCalcium-Calmodulin-Dependent Protein Kinase Type 2Disease SusceptibilityMiceMice, TransgenicMolecular Sequence DataNeuronal PlasticityNeuronsPeptide FragmentsPhosphorylationPromoter Regions, GeneticProsencephalonProtein-Tyrosine KinasesProto-Oncogene ProteinsCalcium-Calmodulin-Dependent Protein KinasesCalcium-Calmodulin-Dependent Protein Kinase Type 2Fyn protein, mousePeptide FragmentsProtein-Tyrosine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-fynReceptors, N-Methyl-D-Aspartate

Identifiers

PMID10489260
PMCPMC311255
OpenAlexW1859114794

What OpenQuestion holds

Textmetadata
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.