Evidence map›Paper›PMID 21124995›Full record

ArticlePLoS genetics2010

Sarcomere formation occurs by the assembly of multiple latent protein complexes.

Yanning Rui, Jianwu Bai, Norbert Perrimon

Open access · goldAbstract read
In one paragraph

Article in PLoS genetics, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
2.9field-weighted citation impact, top 8% 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

48 citing papers in PubMed, 94 citations in OpenAlex.

  1. Article
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  8. Sarcomere maturation: function acquisition, molecular mechanism, and interplay with other organelles.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2022
    Review
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  19. Defective sarcomere organization and reduced larval locomotion and fish survival in slow muscle heavy chain 1 (smyhc1) mutants.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2020
    Article
  20. 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

3 authors at 3 institutions in 1 country.

Yanning RuiDepartment of Genetics, Harvard Medical School, Boston, MA, USA. yrui@genetics.med.harvard.edu
Jianwu Bai
Norbert Perrimon
Harvard University · USHoward Hughes Medical Institute · USPediatrics and Genetics · US

Funding

Characterization of the Insulin to Autophagy Pathway in MusclesR01AR057352 · NIAMS · HARVARD MEDICAL SCHOOL · PI NORBERT PERRIMON · 2010 to 2026
$8.2M
Howard Hughes Medical InstituteNIAMS NIH HHS R01 AR057352
6 · The paper itself

Abstract

The stereotyped striation of myofibrils is a conserved feature of muscle organization that is critical to its function. Although most components that constitute the basic myofibrils are well-characterized biochemically and are conserved across the animal kingdom, the mechanisms leading to the precise assembly of sarcomeres, the basic units of myofibrils, are poorly understood. To gain insights into this process, we investigated the functional relationships of sarcomeric protein complexes. Specifically, we systematically analyzed, using either RNAi in primary muscle cells or available genetic mutations, the organization of myofibrils in Drosophila muscles that lack one or more sarcomeric proteins. Our study reveals that the thin and thick filaments are mutually dependent on each other for striation. Further, the tension sensor complex comprised of zipper/Zasp/α-actinin is involved in stabilizing the sarcomere but not in its initial formation. Finally, integrins appear essential for the interdigitation of thin and thick filaments that occurs prior to striation. Thus, sarcomere formation occurs by the coordinated assembly of multiple latent protein complexes, as opposed to sequential assembly.

Indexed as

AnimalsDrosophila melanogasterDrosophila ProteinsIntegrinsModels, BiologicalMultiprotein ComplexesMuscle ProteinsMyosin Heavy ChainsSarcomeresTropomyosinTroponinDrosophila ProteinsIntegrinsMultiprotein ComplexesMuscle ProteinsMyosin Heavy ChainsTropomyosinTroponin

Identifiers

PMID21124995
PMCPMC2987826
OpenAlexW2133085510

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.