Evidence map›Paper›PMID 16470337›Full record

ArticleJournal of muscle research and cell motility2005

The sarcomeric M-band during development and in disease.

Stephan Lange, Irina Agarkova, Jean-Claude Perriard, Elisabeth Ehler

Abstract read
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In one paragraph

Article 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 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.4field-weighted citation impact, top 17% 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

21 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
  2. Article
  3. The M-band: The underestimated part of the sarcomere.Biochimica et biophysica acta. Molecular cell research · 2020
    Review
  4. Article
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  8. Review
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  10. Article
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  12. Article
  13. Myofibrillogenesis regulator 1 induces hypertrophy by promoting sarcomere organization in neonatal rat cardiomyocytes.Hypertension research : official journal of the Japanese Society of Hypertension · 2012
    Article
  14. Review
  15. Article
  16. Review
  17. Article
  18. New aspects of obscurin in human striated muscles.Histochemistry and cell biology · 2008
    Article
  19. 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 2 institutions in 2 countries.

Stephan LangeThe Randall Division of Cell & Molecular Biophysics and the Cardiovascular Division, King's College London, SE1 1UL, London, UK.
Irina Agarkova
Jean-Claude Perriard
Elisabeth Ehler
ETH Zurich · CHKing's College London · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The C-terminus of connectin/titin at the M-band of the sarcomere interacts with several structural as well as potential signalling proteins. One of these is myomesin, which can also bind to myosin and has been suggested to function as an integral structural linker of the thick filaments into the sarcomere. Recent evidence that myomesin possesses the ability to form antiparallel dimers via its C-terminal domain has prompted us to propose a novel three-dimensional model for the sarcomeric M-band. A splice variant of myomesin, termed EH-myomesin, contains an additional segment that has disordered conformation and functions as an entropic spring. It is expressed in a subset of muscle types that are characterised by a broader operational range and are more resistant to damage caused by eccentric contraction. In addition, it is also re-expressed in dilated cardiomyopathy. DRAL/FHL-2 is another protein that interacts with the M-band portion of connectin/titin and which probably functions as an adaptor for the compartmentalisation of metabolic enzymes. Together these results suggest that the M-band is crucial for sarcomere function and maintenance and that its molecular composition can be adapted to divergent physiological needs in different muscle types, which may help to cope with pathological alterations.

Indexed as

AnimalsConnectinHumansModels, BiologicalModels, MolecularMuscle DevelopmentMuscle Fibers, SkeletalMuscle ProteinsMuscular DiseasesMyocytes, CardiacMyosinsProtein IsoformsProtein KinasesSarcomeresSignal TransductionConnectinMuscle ProteinsMyosinsProtein IsoformsProtein KinasesTTN protein, human

Identifiers

PMID16470337
OpenAlexW2055285720

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.