ArticleProceedings of the National Academy of Sciences of the United States of America1997
Probes bound to myosin Cys-707 rotate during length transients in contraction.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 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
7 citing papers in PubMed.
- Auxotonic to isometric contraction transitioning in a beating heart causes myosin step-size to down shift.PloS one · 2017Article
- GFP-tagged regulatory light chain monitors single myosin lever-arm orientation in a muscle fiber.Biophysical journal · 2007Article
- In situ fluorescent protein imaging with metal film-enhanced total internal reflection microscopy.Biophysical journal · 2006Article
- Polarized fluorescence depletion reports orientation distribution and rotational dynamics of muscle cross-bridges.Biophysical journal · 2002Article
- Conformational selection during weak binding at the actin and myosin interface.Biophysical journal · 2000Article
- Backward movements of cross-bridges by application of stretch and by binding of MgADP to skeletal muscle fibers in the rigor state as studied by x-ray diffraction.Biophysical journal · 1999Article
- Fluorescence polarization transients from rhodamine isomers on the myosin regulatory light chain in skeletal muscle fibers.Biophysical journal · 1998Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
It is widely conjectured that muscle shortens because portions of myosin molecules (the "cross-bridges") impel the actin filament to which they transiently attach and that the impulses result from rotation of the cross-bridges. Crystallography indicates that a cross-bridge is articulated-consisting of a globular catalytic/actin-binding domain and a long lever arm that may rotate. Conveniently, a rhodamine probe with detectable attitude can be attached between the globular domain and the lever arm, enabling the observer to tell whether the anchoring region rotates. Well-established signature effects observed in shortening are tension changes resulting from the sudden release or quick stretch of active muscle fibers. In this investigation we found that closely correlated with such tension changes are changes in the attitude of the rhodamine probes. This correlation strongly supports the conjecture about how shortening is achieved.
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Registered trials
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