Evidence map›Paper›PMID 19651765›Full record

ArticleThe Journal of physiology2009

Structural changes in myosin motors and filaments during relaxation of skeletal muscle.

E Brunello, L Fusi, M Reconditi, M Linari, P Bianco, P Panine, T Narayanan, G Piazzesi, V Lombardi, M Irving

Open access · greenAbstract read
In one paragraph

Article in The Journal of physiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.1field-weighted citation impact, top 19% 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

25 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Dual-filament regulation of relaxation in mammalian fast skeletal muscle.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Myosin filament-based regulation of the dynamics of contraction in heart muscle.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  13. Article
  14. Article
  15. Review
  16. Myocardial relaxation is accelerated by fast stretch, not reduced afterload.Journal of molecular and cellular cardiology · 2017
    Article
  17. Article
  18. Article
  19. Article
  20. Structural dynamics of troponin during activation of skeletal muscle.Proceedings of the National Academy of Sciences of the United States of America · 2014
    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

10 authors at 4 institutions in 3 countries.

E BrunelloLaboratorio di Fisiologia, Dipartimento di Biologia Evoluzionistica, Universitá di Firenze, Firenze, Italy.
L Fusi
M Reconditi
M Linari
P Bianco
P Panine
T Narayanan
G Piazzesi
V Lombardi
M Irving
University of Florence · ITEuropean Synchrotron Radiation Facility · FRNational Interuniversity Consortium for the Physical Sciences of Matter · ITKing's College London · GB

Funding

The molecular mechanism of muscle contractionR01AR049033 · NIAMS · UNIVERSITY OF FLORENCE · PI LOMBARDI, VINCENZO · 2003 to 2006
$422k
Medical Research Council G0601065NIAMS NIH HHS R01 AR049033NIAMS NIH HHS R01AR049033
6 · The paper itself

Abstract

Structural changes in myosin motors and filaments during relaxation from short tetanic contractions of intact single fibres of frog tibialis anterior muscles at sarcomere length 2.14 mum, 4 degrees C were investigated by X-ray diffraction. Force declined at a steady rate for several hundred milliseconds after the last stimulus, while sarcomere lengths remained almost constant. During this isometric phase of relaxation the intensities of the equatorial and meridional M3 X-ray reflections associated with the radial and axial distributions of myosin motors also recovered at a steady rate towards their resting values, consistent with progressive net detachment of myosin motors from actin filaments. Stiffness measurements confirmed that the fraction of motors attached to actin declined at a constant rate, but also revealed a progressive increase in force per motor. The interference fine structure of the M3 reflection suggested that actin-attached myosin motors are displaced towards the start of their working stroke during isometric relaxation. There was negligible recovery of the intensities of the meridional and layer-line reflections associated with the quasi-helical distribution of myosin motors in resting muscle during isometric relaxation, and the 1.5% increase in the axial periodicity of the myosin filament associated with muscle activation was not reversed. When force had decreased to roughly half its tetanus plateau value, the isometric phase of relaxation abruptly ended, and the ensuing chaotic relaxation had an exponential half-time of ca 60 ms. Recovery of the equatorial X-ray intensities was largely complete during chaotic relaxation, but the other X-ray signals recovered more slowly than force.

Indexed as

Actin CytoskeletonAnimalsCells, CulturedMolecular Motor ProteinsMuscle ContractionMuscle Fibers, SkeletalMuscle RelaxationMuscle, SkeletalMyosinsProtein ConformationRana temporariaStructure-Activity RelationshipMolecular Motor ProteinsMyosins

Identifiers

PMID19651765
PMCPMC2766654
OpenAlexW2137471276

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.