Muscle contraction and in vitro actin? movement: role of
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- Type
- article
- Published
- 1992-01-01
- Cited by
- 0
- References
- 10
- OpenAlex
- https://openalex.org/W2374539542
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:87495838
Keywords
Actin, Contraction (grammar), Muscle contraction, Sarcomere, Cell biology
References
- Electrostatic contributions to the binding of myosin and myosin-MgADP to F-actin in solution.
- Muscles and Molecules: Uncovering the Principles of Biological Motion
- Alteration in crossbridge kinetics caused by mutations in actin
- Binding and hydrolysis of ATP by cardiac myosin subfragment 1: effect of solution parameters on transient kinetics.
- Velocity-induced modifications in the crossbridge and/or the actin filament behavior during shortening of muscle fibers.
- Time-resolved cryo-electron microscopic study of the dissociation of actomyosin induced by photolysis of photolabile nucleotides.
- Interactions of myosin subfragment 1 isozymes with G-actin.
- Inhibition of sliding movement of F-actin by crosslinking emphasizes the role of actin structure in the mechanism of motility.
- Atomic structure of the actin: DNase I complex
- Subtilisin cleavage of actin inhibits in vitro sliding movement of actin filaments over myosin
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