Evidence map›Paper›PMID 11305946›Full record

ReviewGenome biology2001

Dystrophins and dystrobrevins.

R G Roberts

Abstract readReview
In one paragraph

Review in Genome biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed.

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  11. Missense mutations in dystrophin that trigger muscular dystrophy decrease protein stability and lead to cross-beta aggregates.Proceedings of the National Academy of Sciences of the United States of America · 2010
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  17. Diversity of the Brain Dystrophin-Glycoprotein Complex.Journal of biomedicine & biotechnology · 2002
    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

1 author.

R G RobertsDivision of Medical and Molecular Genetics, Guy's, King's and St Thomas' Medical School, Guy's Hospital, London, SE1 9RT, UK. roland.roberts@kcl.ac.uk

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

summaryA unique arrangement of domains makes up the common region of two otherwise very different proteins - long, elegant dystrophin, and its rather dumpy distant cousin, dystrobrevin. The two work in concert, forming the core of a large membrane-bound complex in all metazoa. Like many proteins, dystrophin and dystrobrevin have diversified in the vertebrate clade, as have their binding partners, yielding specialized complexes tailored to different cellular and subcellular locations. Disruption of several components of the complex is known to result in syndromes that include progressive myopathy, sometimes combined with cognitive defects; the best known of these is Duchenne muscular dystrophy. Despite a wealth of biochemical, cell biological and genetic information, the precise role of dystrophins, dystrobrevins and their collaborators remains unclear.

Indexed as

Dystrophin-Associated ProteinsAnimalsCytoskeletal ProteinsDystrophinEvolution, MolecularGenesHumansMembrane ProteinsMuscular Dystrophy, DuchenneMutationNeuropeptidesPhylogenyCytoskeletal ProteinsDTNA protein, humandystrobrevinDystrophinDystrophin-Associated ProteinsMembrane ProteinsNeuropeptides

Identifiers

PMID11305946
PMCPMC138928

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.