Evidence map›Paper›PMID 15647164›Full record

ReviewPhilosophical transactions of the Royal Society of London. Series B, Biological sciences2004

X-ray diffraction studies of the contractile mechanism in single muscle fibres.

Vincenzo Lombardi, Gabriella Piazzesi, Massimo Reconditi, Marco Linari, Leonardo Lucii, Alex Stewart, Yin-Biao Sun, Peter Boesecke, Theyencheri Narayanan, Tom Irving and 1 more

Abstract readReview
In one paragraph

Review in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing 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

20 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Theoretical Hill-type muscle and stability: numerical model and application.Computational and mathematical methods in medicine · 2013
    Article
  16. Article
  17. Visualizing key hinges and a potential major source of compliance in the lever arm of myosin.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  18. Review
  19. Fifty years on: where have we reached?Journal of muscle research and cell motility · 2006
    Article
  20. Introduction.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2004
    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

11 authors.

Vincenzo LombardiLaboratorio di Fisiologia, DBAG, Universitá di Firenze, I-50134 Firenze, Italy.
Gabriella Piazzesi
Massimo Reconditi
Marco Linari
Leonardo Lucii
Alex Stewart
Yin-Biao Sun
Peter Boesecke
Theyencheri Narayanan
Tom Irving
Malcolm Irving

Funding

NCRR NIH HHS RR-08630
6 · The paper itself

Abstract

The molecular mechanism of muscle contraction was investigated in intact muscle fibres by X-ray diffraction. Changes in the intensities of the axial X-ray reflections produced by imposing rapid changes in fibre length establish the average conformation of the myosin heads during active isometric contraction, and show that the heads tilt during the elastic response to a change in fibre length and during the elementary force generating process: the working stroke. X-ray interference between the two arrays of myosin heads in each filament allows the axial motions of the heads following a sudden drop in force from the isometric level to be measured in situ with unprecedented precision. At low load, the average working stroke is 12 nm, which is consistent with crystallographic studies. The working stroke is smaller and slower at a higher load. The compliance of the actin and myosin filaments was also determined from the change in the axial spacings of the X-ray reflections following a force step, and shown to be responsible for most of the sarcomere compliance. The mechanical properties of the sarcomere depend on both the motor actions of the myosin heads and the compliance of the myosin and actin filaments.

Indexed as

Models, MolecularActinsAnimalsBiomechanical PhenomenaMuscle ContractionMuscle Fibers, SkeletalMyosinsProtein ConformationRadiographySarcomeresX-Ray DiffractionActinsMyosins

Identifiers

PMID15647164
PMCPMC1693470

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.