Evidence map›Paper›PMID 12547790›Full record

ArticleBiophysical journal2003

An x-ray diffraction study on early structural changes in skeletal muscle contraction.

Naoto Yagi

Open access · bronzeAbstract readComparative StudyEvaluation StudyValidation Study
In one paragraph

Article in Biophysical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
1.2field-weighted citation impact, top 18% 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

28 citing papers in PubMed, 43 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Modeling CaFrontiers in physiology · 2016
    Article
  10. Article
  11. Structural dynamics of troponin during activation of skeletal muscle.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  12. Article
  13. Pointed-end capping by tropomodulin modulates actomyosin crossbridge formation in skeletal muscle fibers.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2014
    Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Disrupted myosin cross-bridge cycling kinetics triggers muscle weakness in nebulin-related myopathy.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2011
    Article
  20. Motion of myosin head domains during activation and force development in skeletal muscle.Proceedings of the National Academy of Sciences of the United States of America · 2011
    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

1 author at 1 institution in 1 country.

Naoto YagiJapan Synchrotron Radiation Research Institute, SPring-8, Kouto, Mikazuki-cho, Sayo-gun, Hyogo 679-5198, Japan. yagi@spring8.or.jp
SPring-8 · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Structural changes in frog skeletal muscle were studied using x-ray diffraction with a time resolution of 0.53-1.02 ms after a single electrical stimulus at 8 degrees C. Tension began to drop at 6 ms (latency relaxation), reached a minimum at 8 ms, and then twitch tension developed. The intensity of the meridional reflection at 1/38.5 nm(-1), from troponin molecules on the thin filament, began to increase at 4-5 ms and reached a maximum at approximately 12 ms. The meridional reflections based on the myosin 43-nm repeat began to decrease when the tension began to develop. The peak position of the third-order myosin meridional reflection began to shift toward the higher angle at approximately 5 ms, reached a maximum shift (0.02%) at 10 ms, and then moved toward the lower angle. The intensity of the second actin layer line at 1/18 nm(-1) in the axial direction, which was measured at 12 degrees C, began to rise at 5 ms, whereas the latency relaxation started at 3.5 ms. These results suggest that 1), the Ca(2+)-induced structural changes in the thin filament and a structural change in the thick filament have already taken place during latency relaxation; and 2), the Ca(2+) regulation of the thin filament is highly cooperative.

Indexed as

ActinsAnimalsCarrier ProteinsElectric StimulationHindlimbIn Vitro TechniquesIsometric ContractionMolecular Motor ProteinsMotionMuscle ProteinsMuscle, SkeletalMyosin Binding Protein CMyosinsProtein ConformationRana catesbeianaSensitivity and SpecificityActinsCarrier ProteinsMolecular Motor ProteinsMuscle ProteinsMyosin Binding Protein CMyosinsTroponin

Identifiers

PMID12547790
PMCPMC1302686
OpenAlexW2050701613

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.