Evidence map›Paper›PMID 10047985›Full record

ArticleJournal of muscle research and cell motility1998

Estimation of cross-bridge stiffness from maximum thermodynamic efficiency.

C J Barclay

Abstract read
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Article in Journal of muscle research and cell motility, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing 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

18 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Design principles governing the motility of myosin V.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Mechanics of actomyosin bonds in different nucleotide states are tuned to muscle contraction.Proceedings of the National Academy of Sciences of the United States of America · 2006
    Article
  16. Article
  17. Article
  18. 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

1 author.

C J BarclayDepartment of Physiology, Monash University, Clayton, Victoria, Australia. chris.barclay@med.monash.edu.au

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In muscle, work is performed by myosin cross-bridges during interactions with actin filaments. The amount of work performed during each interaction can be related to the mechanical properties of the cross-bridge; work is the integral of the force produced with respect to the distance that the cross-bridge moves the actin filament, and force is determined by the stiffness of the attached cross-bridge. In this paper, cross-bridge stiffness in frog sartorius muscle was estimated from thermodynamic efficiency (work/free energy change) using a two-state cross-bridge model, assuming constant stiffness over the working range and tight-coupling between cross-bridge cycles and ATP use. This model accurately predicts mechanical efficiency (work/enthalpy output). A critical review of the literature indicates that a realistic value for maximum thermodynamic efficiency of frog sartorius is 0.45 under conditions commonly used in experiments on isolated muscle. Cross-bridge stiffness was estimated for a range of power stroke amplitudes. For realistic amplitudes (10-15 nm), estimated cross-bridge stiffness was between 1 and 2.2 pN nm-1. These values are similar to those estimated from quick-release experiments, taking into account compliance arising from structures other than cross-bridges, but are substantially higher than those from isolated protein studies. The effects on stiffness estimates of relaxing the tight-coupling requirement and of incorporating more force-producing cross-bridge states are also considered.

Indexed as

Models, ChemicalThermodynamicsActinsAnimalsAnuraCross-Linking ReagentsEnergy MetabolismMuscle ContractionMuscle, SkeletalActinsCross-Linking Reagents

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What OpenQuestion holds

Texttitle and abstract
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Registered trials

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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.