ArticleBiophysical journal2005
Structural changes of actin-bound myosin heads after a quick length change in frog skeletal muscle.
Article in Biophysical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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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.
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.
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Who cites it
9 citing papers in PubMed.
- Small Angle X-ray Diffraction as a Tool for Structural Characterization of Muscle Disease.International journal of molecular sciences · 2022Review
- Synchrotron radiation X-ray diffraction studies on muscle: past, present, and future.Biophysical reviews · 2019Review
- Myosin Head Configurations in Resting and Contracting Murine Skeletal Muscle.International journal of molecular sciences · 2018Article
- Monitoring the structural behavior of troponin and myoplasmic free Ca2+ concentration during twitch of frog skeletal muscle.Biophysical journal · 2010Article
- Inter-sarcomere coordination in muscle revealed through individual sarcomere response to quick stretch.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Force-generating cross-bridges during ramp-shaped releases: evidence for a new structural state.Biophysical journal · 2009Article
- Direct modeling of X-ray diffraction pattern from contracting skeletal muscle.Biophysical journal · 2008Article
- A structural origin of latency relaxation in frog skeletal muscle.Biophysical journal · 2007Article
- Structural changes of cross-bridges on transition from isometric to shortening state in frog skeletal muscle.Biophysical journal · 2006Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Changes in the x-ray diffraction pattern from a frog skeletal muscle were recorded after a quick release or stretch, which was completed within one millisecond, at a time resolution of 0.53 ms using the high-flux beamline at the SPring-8 third-generation synchrotron radiation facility. Reversibility of the effects of the length changes was checked by quickly restoring the muscle length. Intensities of seven reflections were measured. A large, instantaneous intensity drop of a layer line at an axial spacing of 1/10.3 nm(-1) after a quick release and stretch, and its partial recovery by reversal of the length change, indicate a conformational change of myosin heads that are attached to actin. Intensity changes on the 14.5-nm myosin layer line suggest that the attached heads alter their radial mass distribution upon filament sliding. Intensity changes of the myosin reflections at 1/21.5 and 1/7.2 nm(-1) are not readily explained by a simple axial swing of cross-bridges. Intensity changes of the actin-based layer lines at 1/36 and 1/5.9 nm(-1) are not explained by it either, suggesting a structural change in actin molecules.
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Registered trials
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.