Evidence map›Paper›PMID 16450058›Full record

ReviewJournal of muscle research and cell motility2005

The function of elastic proteins in the oscillatory contraction of insect flight muscle.

Belinda Bullard, Christoph Burkart, Siegfried Labeit, Kevin Leonard

Abstract readReview
PubMed Publisher
In one paragraph

Review in Journal of muscle research and cell motility, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
1.5field-weighted citation impact, top 20% 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

33 citing papers in PubMed, 57 citations in OpenAlex.

  1. Review
  2. The cryo-EM 3D image reconstruction of isolated Lethocerus indicus Z-discs.Journal of muscle research and cell motility · 2023
    Review
  3. The self-oscillation paradox in the flight motor ofJournal of the Royal Society, Interface · 2023
    Article
  4. Article
  5. Article
  6. Article
  7. CryoEM structure ofLife science alliance · 2020
    Article
  8. Article
  9. Article
  10. Article
  11. The giant titin: how to evaluate its role in cardiomyopathies.Journal of muscle research and cell motility · 2019
    Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Elastic proteins in the flight muscle of Manduca sexta.Archives of biochemistry and biophysics · 2015
    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

4 authors at 3 institutions in 1 country.

Belinda BullardEuropean Molecular Biology Laboratory, D-69117, Heidelberg, Germany. bb500@york.ac.uk
Christoph Burkart
Siegfried Labeit
Kevin Leonard
European Molecular Biology Laboratory · DEDeutsche Gesellschaft für Anästhesiologie und Intensivmedizin · DEUniversity Hospital Heidelberg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Oscillatory contraction of asynchronous insect flight muscle is activated by periodic stretches at constant low concentrations of Ca2+. The fibres must be relatively stiff to respond to small length changes occurring at high frequency. Several proteins in the flight muscle may determine the overall stiffness of the fibres. The Drosophila sallimus (sls) gene codes for multiple isoforms with a modular structure made up of immunoglobulin (Ig) and elastic PEVK domains, unique sequence, and a few fibronectin (Fn) domains at the end of the molecule. Kettin, derived from the sls gene, has Ig domains separated by linker sequences and is bound to actin near the Z-disc; the C-terminus is associated with the end of the A-band. Flight muscle also has longer isoforms of Sls, with extensible PEVK sequence, and C-terminal Fn domains; all extend from the Z-disc to the end of the A-band. Projectin, from a different gene, has repeating modules of Fn and Ig domains, and is associated with the end of thick filaments; tandem Ig and PEVK domains at the N-terminus are in the I-band. Projectin, kettin and other Sls isoforms form a mechanical link between thick and thin filaments; all are probably part of the connecting filaments, which branch from the thick filaments and are linked to actin near the Z-disc. The elasticity of fibres may depend on the relative amounts of those isoforms with extensible PEVK sequence. Flightin is bound on the outside of thick filaments and maintains the stiffness necessary for the transmission of stress along the filaments. Insect flight muscle has multiple elastic proteins to give the sarcomere the optimum compliance necessary for high frequency oscillatory contraction.

Indexed as

AnimalsConnectinDrosophila ProteinsElasticityFlight, AnimalInsectaInsect ProteinsModels, BiologicalMuscle ContractionMuscle ProteinsMuscle, SkeletalConnectinDrosophila ProteinsInsect ProteinsMuscle Proteinsprojectinsls protein, Drosophila

Identifiers

PMID16450058
OpenAlexW2046656332

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.