Evidence map›Paper›PMID 14507712›Full record

ArticleBiophysical journal2003

Static and dynamic x-ray diffraction recordings from living mammalian and amphibian skeletal muscles.

Hiroyuki Iwamoto, Jun'ichi Wakayama, Tetsuro Fujisawa, 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
0.8field-weighted citation impact, top 24% 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, 41 citations in OpenAlex.

  1. Article
  2. Mammalian muscle fibers may be simple as well as slow.The Journal of general physiology · 2019
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  15. 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
  16. Article
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  18. 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
  19. Article
  20. A myopathy-linked tropomyosin mutation severely alters thin filament conformational changes during activation.Proceedings of the National Academy of Sciences of the United States of America · 2010
    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

4 authors at 3 institutions in 1 country.

Hiroyuki IwamotoLife and Environment Division, SPring-8, Japan Synchrotron Radiation Research Institute, Hyogo 679-5198, Japan. iwamoto@spring8.or.jp
Jun'ichi Wakayama
Tetsuro Fujisawa
Naoto Yagi
Japan Synchrotron Radiation Research Institute · JPRIKEN · JPSPring-8 · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Static and time-resolved two-dimensional x-ray diffraction patterns, recorded from the living mouse diaphragm muscle, were compared with those from living frog sartorius muscle. The resting pattern of mouse muscle was similar to that of frog muscle, and consisted of actin- and myosin-based reflections with spacings basically identical to those of frog. As a notable exception, the sampling pattern of the myosin layer lines (MLL's) indicated that the mouse myofilaments were not organized into a superlattice as in frog. The intensity changes of reflections upon activation were also similar. The MLL's of both muscles were markedly weakened. Stereospecific (rigorlike) actomyosin species were not significantly populated in either muscle, as was evidenced by the 6th actin layer line (ALL), which was substantially enhanced but without a shift in its peak position or a concomitant rise of lower order ALL's. On close examination of the mouse pattern, however, a few lower order ALL's were found to rise, slightly but definitely, at the position expected for stereospecific binding. Their quick rise after the onset of stimulation indicates that this stereospecific complex is generated in the process of normal contraction. However, their rise is still too small to account for the marked enhancement of the 6th ALL, which is better explained by a myosin-induced structural change of actin. Since the forces of the two muscles are comparable regardless of the amount of stereospecific complex, it would be natural to consider that most of the force of skeletal muscle is supported by nonstereospecific actomyosin species.

Indexed as

ActinsAmphibiansAnimalsBinding SitesDiaphragmHindlimbIn Vitro TechniquesIsometric ContractionMacromolecular SubstancesMammalsMiceMolecular Motor ProteinsMuscle, SkeletalMyosinsProtein BindingProtein ConformationActinsMacromolecular SubstancesMolecular Motor ProteinsMyosins

Identifiers

PMID14507712
PMCPMC1303473
OpenAlexW2007936803

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.