Evidence map›Paper›PMID 20338847›Full record

ArticleBiophysical journal2010

Theoretical predictions of the effects of force transmission by desmin on intersarcomere dynamics.

Gretchen A Meyer, Balázs Kiss, Samuel R Ward, David L Morgan, Miklós S Z Kellermayer, Richard L Lieber

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2010. 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
1.5field-weighted citation impact, top 19% 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

17 citing papers in PubMed, 27 citations in OpenAlex.

  1. Nucleus Mechanosensing in Cardiomyocytes.International journal of molecular sciences · 2023
    Review
  2. Desmin Knock-Out Cardiomyopathy: A Heart on the Verge of Metabolic Crisis.International journal of molecular sciences · 2022
    Article
  3. Article
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  5. Review
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  7. Review
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  11. Skeletal muscle fibrosis develops in response to desmin deletion.American journal of physiology. Cell physiology · 2012
    Article
  12. Article
  13. Article
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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

6 authors at 4 institutions in 3 countries.

Gretchen A MeyerDepartment of Bioengineering, University of California, San Diego, California, USA.
Balázs Kiss
Samuel R Ward
David L Morgan
Miklós S Z Kellermayer
Richard L Lieber
University of California, San Diego · USMonash University · AUSemmelweis University · HUUniversity of Pecs · HU

Funding

Skeletal Muscle Injury: Mechanism Prevention &TreatmentR01AR040050 · NIAMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI LIEBER, RICHARD L · 1989 to 2007
$1.6M
NIAMS NIH HHS AR40050NIAMS NIH HHS R01 AR040050
6 · The paper itself

Abstract

Desmin is an intermediate filament protein in skeletal muscle that forms a meshlike network around Z-disks. A model of a muscle fiber was developed to investigate the mechanical role of desmin. A two-dimensional mesh of viscoelastic sarcomere elements was connected laterally by elastic elements representing desmin. The equations of motion for each sarcomere boundary were evaluated at quasiequilibrium to determine sarcomere stresses and strains. Simulations of passive stretch and fixed-end contractions yielded values for sarcomere misalignment and stress in wild-type and desmin null fibers. Passive sarcomere misalignment increased nonlinearly with fiber strain in both wild-type and desmin null simulations and was significantly larger without desmin. During fixed-end contraction, desmin null simulations also demonstrated greater sarcomere misalignment and reduced stress production compared with wild-type. In simulations with only a fraction of wild-type desmin present, fixed-end stress increased as a function of desmin concentration and this relationship was influenced by the cellular location of the desmin filaments. This model suggests that desmin stabilizes Z-disks and enables greater stress production by providing a mechanical tether between adjacent myofibrils and to the extracellular matrix and that the significance of the tether is a function of its location within the cell.

Indexed as

Models, BiologicalAlgorithmsAnimalsComputer SimulationDesminElasticityExtracellular MatrixFinite Element AnalysisMiceMotionMuscle ContractionMuscle Fibers, SkeletalMuscle, SkeletalNonlinear DynamicsSarcomeresStress, MechanicalDesmin

Identifiers

PMID20338847
PMCPMC2808486
OpenAlexW2031782498

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.