Evidence map›Paper›PMID 26578772›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2015

Direct real-time detection of the structural and biochemical events in the myosin power stroke.

Joseph M Muretta, John A Rohde, Daniel O Johnsrud, Sinziana Cornea, David D Thomas

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.

0numbers the graph read from it
0cells of the map it votes in
70citing 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

70 citing papers in PubMed.

  1. Article
  2. A FRET assay to monitor different structural states of human β-cardiac myosin including the interacting-heads motif.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Article
  4. Article
  5. Review
  6. 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
  7. Article
  8. Review
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  11. Article
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10 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

5 authors.

Joseph M MurettaDepartment of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, Minneapolis, MN 55455 muret003@umn.edu ddt@umn.edu.
John A RohdeDepartment of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, Minneapolis, MN 55455.
Daniel O JohnsrudDepartment of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, Minneapolis, MN 55455.
Sinziana CorneaDepartment of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, Minneapolis, MN 55455.
David D ThomasDepartment of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, Minneapolis, MN 55455 muret003@umn.edu ddt@umn.edu.

Funding

Structural Dynamics of Muscle ContractionR01AR032961 · NIAMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI THOMAS, DAVID D · 1986 to 2018
$8.0M
Use of specific transcription factors to promote limb regeneration capacityP30AR057220 · NIAMS · UNIVERSITY OF MINNESOTA · PI ERVASTI, JAMES M · 2009 to 2013
$3.0M
Protein Oxidation, Structure, &Function in Aging MuscleR01AG026160 · NIA · UNIVERSITY OF MINNESOTA TWIN CITIES · PI THOMAS, DAVID D · 2004 to 2008
$2.2M
MOLECULAR DYNAMICS OF MUSCLE CONTRACTIONR37AR032961 · NIAMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI THOMAS, DAVID DALE · 1994 to 2003
$2.1M
NIAMS NIH HHS 5 P30 AR05722NIAMS NIH HHS AR32961NIAMS NIH HHS P30 AR057220NIAMS NIH HHS R01 AR032961NIAMS NIH HHS R37 AR032961NIA NIH HHS R01 AG026160
6 · The paper itself

Abstract

A principal goal of molecular biophysics is to show how protein structural transitions explain physiology. We have developed a strategic tool, transient time-resolved FRET [(TR)(2)FRET], for this purpose and use it here to measure directly, with millisecond resolution, the structural and biochemical kinetics of muscle myosin and to determine directly how myosin's power stroke is coupled to the thermodynamic drive for force generation, actin-activated phosphate release, and the weak-to-strong actin-binding transition. We find that actin initiates the power stroke before phosphate dissociation and not after, as many models propose. This result supports a model for muscle contraction in which power output and efficiency are tuned by the distribution of myosin structural states. This technology should have wide application to other systems in which questions about the temporal coupling of allosteric structural and biochemical transitions remain unanswered.

Indexed as

Models, ChemicalAllosteric RegulationAnimalsAvian ProteinsChickensFluorescence Resonance Energy TransferKineticsMyosinsRabbitsAvian ProteinsMyosinsFRETmyosinphosphate releasepower strokestructural kinetics

Identifiers

PMID26578772
PMCPMC4655543

What OpenQuestion holds

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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.