Evidence map›Paper›PMID 15778440›Full record

ArticleBiophysical journal2005

Dynamics of myosin-driven skeletal muscle contraction: I. Steady-state force generation.

Ganhui Lan, Sean X Sun

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

12 citing papers in PubMed, 60 citations in OpenAlex.

  1. Actin Stress Fibers Response and Adaptation under Stretch.International journal of molecular sciences · 2022
    Article
  2. Article
  3. Article
  4. Robust mechanobiological behavior emerges in heterogeneous myosin systems.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  5. Article
  6. Article
  7. Quantification of the forces driving self-assembly of three-dimensional microtissues.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  8. Article
  9. Article
  10. Mechanistic role of movement and strain sensitivity in muscle contraction.Proceedings of the National Academy of Sciences of the United States of America · 2009
    Article
  11. Article
  12. 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

2 authors at 1 institution in 1 country.

Ganhui LanDepartment of Mechanical Engineering, Johns Hopkins University, Baltimore, Maryland, USA.
Sean X Sun
Johns Hopkins University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Skeletal muscle contraction is a canonical example of motor-driven force generation. Despite the long history of research in this topic, a mechanistic explanation of the collective myosin force generation is lacking. We present a theoretical model of muscle contraction based on the conformational movements of individual myosins and experimentally measured chemical rate constants. Detailed mechanics of the myosin motor and the geometry of the sarcomere are taken into account. Two possible scenarios of force generation are examined. We find only one of the scenarios can give rise to a plausible contraction mechanism. We propose that the synchrony in muscle contraction is due to a force-dependent ADP release step. Computational results of a half sarcomere with 150 myosin heads can explain the experimentally measured force-velocity relationship and efficiency data. We predict that the number of working myosin motors increases as the load force is increased, thus showing synchrony among myosin motors during muscle contraction. We also find that titin molecules anchoring the thick filament are passive force generators in assisting muscle contraction.

Indexed as

Adenosine DiphosphateBiomechanical PhenomenaBiophysical PhenomenaBiophysicsElasticityEnergy TransferIn Vitro TechniquesKineticsModels, BiologicalMolecular Motor ProteinsMuscle ContractionMuscle, SkeletalMyosinsProtein ConformationSarcomeresThermodynamicsAdenosine DiphosphateMolecular Motor ProteinsMyosins

Identifiers

PMID15778440
PMCPMC1305641
OpenAlexW1971662505

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.