Evidence map›Paper›PMID 15454448›Full record

ArticleBiophysical journal2004

The force exerted by a muscle cross-bridge depends directly on the strength of the actomyosin bond.

Christina Karatzaferi, Marc K Chinn, Roger Cooke

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

33 citing papers in PubMed, 65 citations in OpenAlex.

  1. Trial
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Creatine Kinase Equilibration and ΔGInternational journal of molecular sciences · 2023
    Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Structural and functional impact of troponin C-mediated CaJournal of molecular and cellular cardiology · 2018
    Article
  15. Article
  16. 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
  17. Review
  18. Article
  19. Review
  20. Article
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Christina KaratzaferiDepartment of Biochemistry and Biophysics, Cardiovascular Research Institute, University of California, San Francisco, California 94193-2240, USA.
Marc K Chinn
Roger Cooke
University of California, San Francisco · US

Funding

MYOSIN PHOSPHORYLATION IN SKELETAL AND CARDIAC MUSCLER01HL032145 · NHLBI · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI COOKE, ROGER A · 1985 to 2009
$2.7M
NHLBI NIH HHS HL32145NHLBI NIH HHS R01 HL032145
6 · The paper itself

Abstract

Myosin produces force in a cyclic interaction, which involves alternate tight binding to actin and to ATP. We have investigated the energetics associated with force production by measuring the force generated by skinned muscle fibers as the strength of the actomyosin bond is changed. We varied the strength of the actomyosin bond by addition of a polymer that promotes protein-protein association or by changing temperature or ionic strength. We estimated the free energy available to generate force by measuring isometric tension, as the free energy of the states that precede the working stroke are lowered with increasing phosphate. We found that the free energy available to generate force and the force per attached cross-bridge at low [Pi] were both proportional to the free energy available from the formation of the actomyosin bond. We conclude that the formation of the actomyosin bond is involved in providing the free energy driving the production of isometric tension and mechanical work. Because the binding of myosin to actin is an endothermic, entropically driven reaction, work must be performed by a "thermal ratchet" in which a thermal fluctuation in Brownian motion is captured by formation of the actomyosin bond.

Indexed as

ActomyosinAnimalsBinding SitesCells, CulturedEnergy TransferHydrogen-Ion ConcentrationIsometric ContractionMolecular Motor ProteinsMuscle Fibers, Fast-TwitchMuscle, SkeletalPhosphatesProtein BindingRabbitsSarcomeresStress, MechanicalTemperatureActomyosinMolecular Motor ProteinsPhosphates

Identifiers

PMID15454448
PMCPMC1304672
OpenAlexW2050871560

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.