Evidence map›Paper›PMID 27717739›Full record

ReviewTrends in biochemical sciences2016

How Myosin Generates Force on Actin Filaments.

Anne Houdusse, H Lee Sweeney

Abstract readReview
In one paragraph

Review in Trends in biochemical sciences, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 110 papers.

0numbers the graph read from it
0cells of the map it votes in
110citing 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

110 citing papers in PubMed.

  1. Article
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  6. Article
  7. Review
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  9. Article
  10. Review
  11. Characterizing the concentration and load dependence of phosphate binding to rabbit fast skeletal actomyosin.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Research and practice in thrombosis and haemostasis · 2024
    Review
  19. Article
  20. Article

50 more citing papers are in PubMed but not listed here.

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.

Anne HoudusseStructural Motility, Institut Curie, PSL Research University, CNRS, UMR 144, F-75005, Paris, France; Sorbonne Universités, UPMC Univ Paris06, Sorbonne Universités, IFD, 4 Place Jussieu, 75252 Paris cedex 05, France. Electronic address: anne.houdusse@curie.fr.
H Lee SweeneyDepartment of Pharmacology & Therapeutics and the Myology Institute, University of Florida College of Medicine, PO Box 100267, Gainesville, FL 32610-0267, USA. Electronic address: Lsweeney@ufl.edu.

Funding

Pathology and Molecular Imaging CoreP01HL110869 · NHLBI · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI STULL, JAMES T · 2012 to 2016
$10.4M
Structure and Function of Myosin VIR01DC009100 · NIDCD · UNIVERSITY OF PENNSYLVANIA · PI SWEENEY, H LEE · 2007 to 2022
$6.0M
NHLBI NIH HHS P01 HL110869NIDCD NIH HHS R01 DC009100
6 · The paper itself

Abstract

How myosin interacts with actin to generate force is a subject of considerable controversy. The major debate centers on understanding at what point in force generation the inorganic phosphate is released with respect to the lever arm swing, or powerstroke. Resolving the controversy is essential for understanding how force is produced as well as the mechanisms underlying disease-causing mutations in myosin. Recent structural insights into the powerstroke have come from a high-resolution structure of myosin in a previously unseen state and from an electron cryomicroscopy (cryo-EM) 3D reconstruction of the actin-myosin-MgADP complex. Here, we argue that seemingly contradictory data from time-resolved fluorescence resonance energy transfer (FRET) studies can be reconciled, and we put forward a model for myosin force generation on actin.

Indexed as

Actin CytoskeletonActinsAdenosine DiphosphateAdenosine TriphosphateAmino Acid MotifsBinding SitesBiomechanical PhenomenaCatalytic DomainFluorescence Resonance Energy TransferHumansMechanotransduction, CellularMyosinsPhosphatesProtein BindingProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandActinsAdenosine DiphosphateAdenosine TriphosphateMyosinsPhosphatesallosterychemo-mechanical transductionforce generationmolecular motors

Identifiers

PMID27717739
PMCPMC5123969

What OpenQuestion holds

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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.