ArticleProceedings of the National Academy of Sciences of the United States of America2002
Coordination of the two heads of myosin during muscle contraction.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. 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.
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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
9 citing papers in PubMed, 12 citations in OpenAlex.
- Research reviews on myosin head interactions with F-actin.Applied microscopy · 2024Review
- Actomyosin interaction at low ATP concentrations.European biophysics journal : EBJ · 2017Article
- Poorly understood aspects of striated muscle contraction.BioMed research international · 2015Review
- Stiffness, working stroke, and force of single-myosin molecules in skeletal muscle: elucidation of these mechanical properties via nonlinear elasticity evaluation.Cellular and molecular life sciences : CMLS · 2013Review
- Actomyosin-ADP states, interhead cooperativity, and the force-velocity relation of skeletal muscle.Biophysical journal · 2010Article
- Site-directed spectroscopic probes of actomyosin structural dynamics.Annual review of biophysics · 2009Review
- Invertebrate muscles: thin and thick filament structure; molecular basis of contraction and its regulation, catch and asynchronous muscle.Progress in neurobiology · 2008Review
- Site-directed spin labeling reveals a conformational switch in the phosphorylation domain of smooth muscle myosin.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- A mutant heterodimeric myosin with one inactive head generates maximal displacement.The Journal of cell biology · 2003Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
We have used luminescence resonance energy transfer between regulatory light chains (RLC) to detect structural changes within the dimeric myosin molecule in contracting muscle fibers. Fully functional scallop muscle fibers were prepared such that each myosin molecule contained a terbium-labeled (luminescent donor) RLC on one head and a rhodamine-labeled (acceptor) RLC on the other. Time-resolved luminescence energy transfer between the two heads increased upon the transition from relaxation (ATP) to contraction (ATP plus Ca) and increased further in rigor (no ATP). Combined with experiments on mutant RLCs labeled specifically at other sites, these results support a model in which the force-generating weak-to-strong transition causes one myosin LC domain to tilt through a 30 degrees angle toward the other, thus acting as a coordinated lever arm.
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What OpenQuestion holds
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.