Evidence map›Paper›PMID 16990403›Full record

ArticleThe Journal of physiology2006

Structural changes in the myosin filament and cross-bridges during active force development in single intact frog muscle fibres: stiffness and X-ray diffraction measurements.

E Brunello, P Bianco, G Piazzesi, M Linari, M Reconditi, P Panine, T Narayanan, W I Helsby, M Irving, V Lombardi

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of physiology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

35 citing papers in PubMed, 63 citations in OpenAlex.

  1. The Mechanism of Modulation of Cardiac Force by Temperature.International journal of molecular sciences · 2025
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  9. The Journal of experimental biology · 2020
    Article
  10. 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
  11. Review
  12. Article
  13. Article
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  15. Article
  16. Review
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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 BrunelloLaboratory of Physiology, Department of Animal Biology and Genetics, University of Florence, Via G. Sansone 1, 50019 Sesto Fiorentino, Italy.
P Bianco
G Piazzesi
M Linari
M Reconditi
P Panine
T Narayanan
W I Helsby
M Irving
V Lombardi
University of Florence · ITEuropean Synchrotron Radiation Facility · FRSapienza University of Rome · ITKing's College London · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Structural and mechanical changes occurring in the myosin filament and myosin head domains during the development of the isometric tetanus have been investigated in intact frog muscle fibres at 4 degrees C and 2.15 microm sarcomere length, using sarcomere level mechanics and X-ray diffraction at beamline ID2 of the European Synchrotron Radiation Facility (Grenoble, France). The time courses of changes in both the M3 and M6 myosin-based reflections were recorded with 5 ms frames using the gas-filled RAPID detector (MicroGap Technology). Following the end of the latent period (11 ms after the start of stimulation), force increases to the tetanus plateau value (T(0)) with a half-time of 40 ms, and the spacings of the M3 and M6 reflections (S(M3) and S(M6)) increase by 1.5% from their resting values, with time courses that lead that of force by approximately 10 and approximately 20 ms, respectively. These temporal relations are maintained when the increase of force is delayed by approximately 10 ms by imposing, from 5 ms after the first stimulus, 50 nm (half-sarcomere)(-1) shortening at the velocity (V(0)) that maintains zero force. Shortening at V(0) transiently reduces S(M3) following the latent period and delays the subsequent increase in S(M3), but only delays the S(M6) increase without a transient decrease. Shortening at V(0) imposed at the tetanus plateau causes an abrupt reduction of the intensity of the M3 reflection (I(M3)), whereas the intensity of the M6 reflection (I(M6)) is only slightly reduced. The changes in half-sarcomere stiffness indicate that the isometric force at each time point is proportional to the number of myosin heads bound to actin. The different sensitivities of the intensity and spacing of the M3 and M6 reflections to the mechanical responses support the view that the M3 reflection in active muscle originates mainly from the myosin heads attached to the actin filament and the M6 reflection originates mainly from a fixed structure in the myosin filament signalling myosin filament length changes during the tetanus rise.

Indexed as

X-Ray DiffractionActin CytoskeletonAnimalsElasticityElectric StimulationIn Vitro TechniquesIsometric ContractionMuscle Fibers, SkeletalMuscle, SkeletalMyosinsProtein IsoformsRadiographyRana temporariaSarcomeresTime FactorsMyosinsProtein Isoforms

Identifiers

PMID16990403
PMCPMC1890380
OpenAlexW1598494409

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.