Evidence map›Paper›PMID 11032344›Full record

ArticleJournal of muscle research and cell motility2000

A thermodynamic muscle model and a chemical basis for A.V. Hill's muscle equation.

J E Baker, D D Thomas

Abstract readComparative Study
PubMed Publisher
In one paragraph

Article in Journal of muscle research and cell motility, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.6field-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

15 citing papers in PubMed, 44 citations in OpenAlex.

  1. Scaling in Biological Systems: A Molecular-Ensemble Duality.bioRxiv : the preprint server for biology · 2025
    Article
  2. Article
  3. Four phases of a force transient emerge from a binary mechanical system.Journal of muscle research and cell motility · 2024
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Heart failure drug changes the mechanoenzymology of the cardiac myosin powerstroke.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  11. Review
  12. Article
  13. The energetics of allosteric regulation of ADP release from myosin heads.Physical chemistry chemical physics : PCCP · 2009
    Article
  14. Review
  15. 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 2 institutions in 1 country.

J E BakerDepartment of Molecular Physiology and Biophysics, University of Vermonnt, Burlinglon, 05405 USA. jbaker@salus.med.uvm.edu
D D Thomas
University of Minnesota Medical Center · USUniversity of Vermont · US

Funding

Structural Dynamics of Muscle ContractionR01AR032961 · NIAMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI THOMAS, DAVID D · 1986 to 2018
$8.0M
MOLECULAR DYNAMICS OF MUSCLE CONTRACTIONR37AR032961 · NIAMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI THOMAS, DAVID DALE · 1994 to 2003
$2.1M
NIAMS NIH HHS AR32961
6 · The paper itself

Abstract

Direct measurements of a relationship between force and actin-myosin biochemistry in muscle suggest that molecular forces in active muscle rapidly equilibrate among. not within, individual myosin crossbridges [Baker et al. (1999) Biophys J 77: 2657 2664]. This observation suggests a thermodynamic model of muscle contraction in which muscle, not an individual myosin crossbridge, is treated as a near-equilibrium system. The general approach can be applied to any ensemble of molecular motors that undergo a physicochemical step against a constant external potential. In this paper we apply the model to a simple two-state crossbridge scheme like that proposed by A.F. Huxley (1957) [Prog Biophys 7: 255 317], and we immediately obtain A.V. Hill's muscle equation. We show that this equation accurately describes steady-state muscle mechanics, biochemistry and energetics. This thermodynamic model provides a novel description of force-dependent actin-myosin kinetics in muscle and provides precise chemical expressions for myosin cooperativity, myosinduty ratios, the number of working strokes per ATP hydrolyzed, muscle efficiency. and energy transfer.

Indexed as

Muscle ContractionEnergy MetabolismModels, TheoreticalMuscle, SkeletalThermodynamics

Identifiers

PMID11032344
OpenAlexW2122646705

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.