Evidence map›Paper›PMID 9305637›Full record

ArticleThe EMBO journal1997

Association of muscle-specific kinase MuSK with the acetylcholine receptor in mammalian muscle.

C Fuhrer, J E Sugiyama, R G Taylor, Z W Hall

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
3.2field-weighted citation impact, top 7% 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

40 citing papers in PubMed, 108 citations in OpenAlex.

  1. Article
  2. Review
  3. Functional monovalency amplifies the pathogenicity of anti-MuSK IgG4 in myasthenia gravis.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
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  7. The MuSK activator agrin has a separate role essential for postnatal maintenance of neuromuscular synapses.Proceedings of the National Academy of Sciences of the United States of America · 2014
    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 1 institution in 1 country.

C FuhrerSection on Synaptic Mechanisms, Laboratory of Cellular and Molecular Regulation, National Institute of Mental Health, NIH, Bethesda, MD 20892, USA.
J E Sugiyama
R G Taylor
Z W Hall
National Institute of Mental Health · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

During synaptogenesis at the neuromuscular junction, a neurally released factor, agrin, causes the clustering of acetylcholine receptors (AChRs) in the muscle membrane beneath the nerve terminal. Agrin acts through a specific receptor which is thought to have a receptor tyrosine kinase, MuSK, as one of its components. In agrin-treated muscle cells, both MuSK and the AChR become tyrosine phosphorylated. To determine how the activation of MuSK leads to AChR clustering, we have investigated their interaction in cultured C2 myotubes. Immunoprecipitation experiments showed that MuSK is associated with the AChR and that this association is increased by agrin treatment. Agrin also caused a transient activation of the AChR-associated MuSK, as demonstrated by MuSK phosphorylation. In agrin-treated myotubes, MuSK phosphorylation increased with the same time course as phosphorylation of the beta subunit of the AChR, but declined more quickly. Although both herbimycin and staurosporine blocked agrin-induced AChR phosphorylation, only herbimycin inhibited the phosphorylation of MuSK. These results suggest that although agrin increases the amount of activated MuSK that is associated with the AChR, MuSK is not directly responsible for AChR phosphorylation but acts through other kinases.

Indexed as

AgrinAnimalsBenzoquinonesBlotting, WesternBungarotoxinsCells, CulturedEnzyme ActivationHumansLactams, MacrocyclicMiceModels, BiologicalMusclesPhosphorylationPhosphotyrosinePrecipitin TestsProtein-Tyrosine KinasesAgrinBenzoquinonesBungarotoxinsherbimycinLactams, MacrocyclicMUSK protein, humanPhosphotyrosineProtein-Tyrosine KinasesQuinonesReceptor Protein-Tyrosine KinasesReceptors, CholinergicRifabutinStaurosporine

Identifiers

PMID9305637
PMCPMC1170130
OpenAlexW2089260073

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.