Evidence map›Paper›PMID 21152002›Full record

ArticlePLoS computational biology2010

Axial and radial forces of cross-bridges depend on lattice spacing.

C David Williams, Michael Regnier, Thomas L Daniel

Abstract read
In one paragraph

Article in PLoS computational biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
–field-weighted citation impact
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

40 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. In defense of Huxley.Biophysical journal · 2024
    Article
  10. Article
  11. AnBioMed research international · 2024
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Hypertrophic cardiomyopathy β-cardiac myosin mutation (P710R) leads to hypercontractility by disrupting super relaxed state.Proceedings of the National Academy of Sciences of the United States of America · 2021
    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.

C David WilliamsDepartment of Physiology and Biophysics, University of Washington, Seattle, Washington, United States of America.
Michael Regnier
Thomas L Daniel

Funding

COOPERATIVE THIN FILAMENT ACTIVATION IN STRIATED MUSCLER01HL065497 · NHLBI · UNIVERSITY OF WASHINGTON · PI REGNIER, MICHAEL · 2001 to 2012
$4.5M
Bioengineering Cardiovascular Training GrantT32EB001650 · NIBIB · UNIVERSITY OF WASHINGTON · PI REGNIER, MICHAEL · 2004 to 2019
$3.6M
NHLBI NIH HHS R01 HL065497NHLBI NIH HHS R01 HL65497-05-09NIBIB NIH HHS T32 EB001650
6 · The paper itself

Abstract

Nearly all mechanochemical models of the cross-bridge treat myosin as a simple linear spring arranged parallel to the contractile filaments. These single-spring models cannot account for the radial force that muscle generates (orthogonal to the long axis of the myofilaments) or the effects of changes in filament lattice spacing. We describe a more complex myosin cross-bridge model that uses multiple springs to replicate myosin's force-generating power stroke and account for the effects of lattice spacing and radial force. The four springs which comprise this model (the 4sXB) correspond to the mechanically relevant portions of myosin's structure. As occurs in vivo, the 4sXB's state-transition kinetics and force-production dynamics vary with lattice spacing. Additionally, we describe a simpler two-spring cross-bridge (2sXB) model which produces results similar to those of the 4sXB model. Unlike the 4sXB model, the 2sXB model requires no iterative techniques, making it more computationally efficient. The rate at which both multi-spring cross-bridges bind and generate force decreases as lattice spacing grows. The axial force generated by each cross-bridge as it undergoes a power stroke increases as lattice spacing grows. The radial force that a cross-bridge produces as it undergoes a power stroke varies from expansive to compressive as lattice spacing increases. Importantly, these results mirror those for intact, contracting muscle force production.

Indexed as

Molecular Dynamics SimulationMyosinsActinsAdenosine DiphosphateAdenosine TriphosphateBiomechanical PhenomenaComputational BiologyModels, BiologicalProtein BindingProtein Structure, QuaternarySarcomeresTorqueActinsAdenosine DiphosphateAdenosine TriphosphateMyosins

Identifiers

PMID21152002
PMCPMC2996315

What OpenQuestion holds

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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.