Evidence map›Paper›PMID 17710131›Full record

ArticlePloS one2007

C. elegans agrin is expressed in pharynx, IL1 neurons and distal tip cells and does not genetically interact with genes involved in synaptogenesis or muscle function.

Ana Hrus, Gordon Lau, Harald Hutter, Susanne Schenk, Jacqueline Ferralli, Marianne Brown-Luedi, Ruth Chiquet-Ehrismann, Stefano Canevascini

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
0.5field-weighted citation impact, top 43% 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

19 citing papers in PubMed, 29 citations in OpenAlex.

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  9. TheGenetics · 2019
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  17. The molecular basis of organ formation: insights from the C. elegans foregut.Annual review of cell and developmental biology · 2009
    Review
  18. Atomic force microscopy analysis of cell volume regulation.Physical review. E, Statistical, nonlinear, and soft matter physics · 2008
    Article
  19. Article
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 3 institutions in 2 countries.

Ana HrusFriedrich Miescher Institute for Biomedical Research, Novartis Research Foundation, Basel, Switzerland.
Gordon Lau
Harald Hutter
Susanne Schenk
Jacqueline Ferralli
Marianne Brown-Luedi
Ruth Chiquet-Ehrismann
Stefano Canevascini
Friedrich Miescher Institute · CHNovartis (Switzerland) · CHSimon Fraser University · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Agrin is a basement membrane protein crucial for development and maintenance of the neuromuscular junction in vertebrates. The C. elegans genome harbors a putative agrin gene agr-1. We have cloned the corresponding cDNA to determine the primary structure of the protein and expressed its recombinant fragments to raise specific antibodies. The domain organization of AGR-1 is very similar to the vertebrate orthologues. C. elegans agrin contains a signal sequence for secretion, seven follistatin domains, three EGF-like repeats and two laminin G domains. AGR-1 loss of function mutants did not exhibit any overt phenotypes and did not acquire resistance to the acetylcholine receptor agonist levamisole. Furthermore, crossing them with various mutants for components of the dystrophin-glycoprotein complex with impaired muscle function did not lead to an aggravation of the phenotypes. Promoter-GFP translational fusion as well as immunostaining of worms revealed expression of agrin in buccal epithelium and the protein deposition in the basal lamina of the pharynx. Furthermore, dorsal and ventral IL1 head neurons and distal tip cells of the gonad arms are sources of agrin production, but no expression was detectable in body muscles or in the motoneurons innervating them. Recombinant worm AGR-1 fragment is able to cluster vertebrate dystroglycan in cultured cells, implying a conservation of this interaction, but since neither of these proteins is expressed in muscle of C. elegans, this interaction may be required in different tissues. The connections between muscle cells and the basement membrane, as well as neuromuscular junctions, are structurally distinct between vertebrates and nematodes.

Indexed as

Caenorhabditis elegansAgrinAmino Acid SequenceAnimalsAnimals, Genetically ModifiedBase SequenceCaenorhabditis elegans ProteinsCell LineChickensDystroglycansGenes, ReporterHumansMolecular Sequence DataMusclesNeuromuscular JunctionNeuronsAgrinCaenorhabditis elegans ProteinsDystroglycansRecombinant Fusion Proteins

Identifiers

PMID17710131
PMCPMC1939731
OpenAlexW2087893647

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.