ArticleJournal of muscle research and cell motility1995
The chicken muscle thick filament: temperature and the relaxed cross-bridge arrangement.
Article in Journal of muscle research and cell motility, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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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.
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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
7 citing papers in PubMed, 19 citations in OpenAlex.
- Relaxed tarantula skeletal muscle has two ATP energy-saving mechanisms.The Journal of general physiology · 2021Article
- Lessons from a tarantula: new insights into muscle thick filament and myosin interacting-heads motif structure and function.Biophysical reviews · 2017Review
- Three-dimensional structure of the human myosin thick filament: clinical implications.Global cardiology science & practice · 2013Review
- Myosin heads contribute to the maintenance of filament order in relaxed rabbit muscle.Biophysical journal · 2010Article
- Myosin filament 3D structure in mammalian cardiac muscle.Journal of structural biology · 2008Article
- Mammalian cardiac muscle thick filaments: their periodicity and interactions with actin.Biophysical journal · 2002Article
- Differences in myosin head arrangement on relaxed thick filaments from Lethocerus and rabbit muscles.Journal of muscle research and cell motility · 1997Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
Abstract
Although chicken myosin S1 has recently been crystallized and its structure analysed, the relaxed periodic arrangement of myosin heads on the chicken thick filament has not been determined. We report here that the cross-bridge array of chicken filaments is temperature sensitive, and the myosin heads become disordered at temperatures near 4 degrees C. At 25 degrees C, however, thick filaments from chicken pectoralis muscle can be isolated with a well ordered, near-helical, arrangement of cross-bridges as seen in negatively stained preparations. This periodicity is confirmed by optical diffraction and computed transforms of images of the filaments. These show a strong series of layer lines near the orders of a 43 nm near-helical periodicity as expected from X-ray diffraction. Both analysis of phases on the first layer line, and computer filtered images of the filaments, are consistent with a three-stranded arrangement of the myosin heads on the filament.
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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.