Evidence map›Paper›PMID 11425875›Full record

ArticleThe Journal of cell biology2001

Muscle activity and muscle agrin regulate the organization of cytoskeletal proteins and attached acetylcholine receptor (AchR) aggregates in skeletal muscle fibers.

G Bezakova, T Lømo

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

24 citing papers in PubMed, 71 citations in OpenAlex.

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  18. Synapse loss in cortex of agrin-deficient mice after genetic rescue of perinatal death.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2007
    Article
  19. Regulation of the intermediate filament protein nestin at rodent neuromuscular junctions by innervation and activity.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2007
    Article
  20. The discovery of long-term potentiation.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2003
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

G BezakovaDepartment of Physiology, University of Oslo, 0317 Oslo, Norway. gabriela.bizakova@unibas.ch
T Lømo
University of Oslo · NO

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In innervated skeletal muscle fibers, dystrophin and beta-dystroglycan form rib-like structures (costameres) that appear as predominantly transverse stripes over Z and M lines. Here, we show that the orientation of these stripes becomes longitudinal in denervated muscles and transverse again in denervated electrically stimulated muscles. Skeletal muscle fibers express nonneural (muscle) agrin whose function is not well understood. In this work, a single application of > or = 10 nM purified recombinant muscle agrin into denervated muscles preserved the transverse orientation of costameric proteins that is typical for innervated muscles, as did a single application of > or = 1 microM neural agrin. At lower concentration, neural agrin induced acetylcholine receptor aggregates, which colocalized with longitudinally oriented beta-dystroglycan, dystrophin, utrophin, syntrophin, rapsyn, and beta 2-laminin in denervated unstimulated fibers and with the same but transversely oriented proteins in innervated or denervated stimulated fibers. The results indicate that costameres are plastic structures whose organization depends on electrical muscle activity and/or muscle agrin.

Indexed as

Dystrophin-Associated ProteinsAgrinAnimalsCytoskeletal ProteinsDose-Response Relationship, DrugDystroglycansDystrophinElectric StimulationHumansLamininMaleMembrane GlycoproteinsMembrane ProteinsMuscle ContractionMuscle DenervationMuscle Fibers, SkeletalAgrinCytoskeletal ProteinsDAG1 protein, humanDystroglycansDystrophinDystrophin-Associated ProteinsLamininlaminin beta2Membrane GlycoproteinsMembrane ProteinsMuscle Proteinsperipheral membrane protein 43KProtein IsoformsReceptors, CholinergicRecombinant ProteinssyntrophinUtrophin

Identifiers

PMID11425875
PMCPMC2150728
OpenAlexW1976581133

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.