ArticleThe Journal of physiology2014
The contributions of filaments and cross-bridges to sarcomere compliance in skeletal muscle.
Article in The Journal of physiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 58 citations in OpenAlex.
- Dual-filament regulation of relaxation in mammalian fast skeletal muscle.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Multiple pathways of the actin-myosin cycle in energy transduction and the release of orthophosphate in muscle.Frontiers in physiology · 2025Review
- Matching Mechanics and Energetics of Muscle Contraction Suggests Unconventional Chemomechanical Coupling during the Actin-Myosin Interaction.International journal of molecular sciences · 2023Article
- Thick filament activation is different in fast- and slow-twitch skeletal muscle.The Journal of physiology · 2022Article
- Anisotropic Elasticity of the Myosin Motor in Muscle.International journal of molecular sciences · 2022Article
- A Physiology-Guided Classification of Active-Stress and Active-Strain Approaches for Continuum-Mechanical Modeling of Skeletal Muscle Tissue.Frontiers in physiology · 2021Article
- Active Force Generation in Cardiac Muscle Cells: Mathematical Modeling and Numerical Simulation of the Actin-Myosin Interaction.Vietnam journal of mathematics · 2021Review
- Straightening Out the Elasticity of Myosin Cross-Bridges.Biophysical journal · 2020Review
- Estimation of Forces on Actin Filaments in Living Muscle from X-ray Diffraction Patterns and Mechanical Data.International journal of molecular sciences · 2019Article
- Myosin Cross-Bridge Behaviour in Contracting Muscle-The TInternational journal of molecular sciences · 2019Article
- Thick Filament Length Changes in Muscle Have Both Elastic and Structural Components.Biophysical journal · 2019Article
- A mechanical model of the half-sarcomere which includes the contribution of titin.Journal of muscle research and cell motility · 2019Article
- Inotropic interventions do not change the resting state of myosin motors during cardiac diastole.The Journal of general physiology · 2019Article
- Thick-Filament Extensibility in Intact Skeletal Muscle.Biophysical journal · 2018Article
- Nebulin stiffens the thin filament and augments cross-bridge interaction in skeletal muscle.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- A myosin II nanomachine mimicking the striated muscle.Nature communications · 2018Article
- The force and stiffness of myosin motors in the isometric twitch of a cardiac trabecula and the effect of the extracellular calcium concentration.The Journal of physiology · 2018Article
- Mechanical parameters of the molecular motor myosin II determined in permeabilised fibres from slow and fast skeletal muscles of the rabbit.The Journal of physiology · 2018Article
- Standard Loading Profile in Matrix Rigidity Sensing.Biophysical journal · 2018Article
- New Insights in Cardiac Calcium Handling and Excitation-Contraction Coupling.Advances in experimental medicine and biology · 2018Review
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 3 countries.
Funding
Abstract
Force generation in the muscle sarcomere is driven by the head domain of the myosin molecule extending from the thick filament to form cross-bridges with the actin-containing thin filament. Following attachment, a structural working stroke in the head pulls the thin filament towards the centre of the sarcomere, producing, under unloaded conditions, a filament sliding of ∼ 11 nm. The mechanism of force generation by the myosin head depends on the relationship between cross-bridge force and movement, which is determined by compliances of the cross-bridge (C(cb)) and filaments. By measuring the force dependence of the spacing of the high-order myosin- and actin-based X-ray reflections from sartorius muscles of Rana esculenta we find a combined filament compliance (Cf) of 13.1 ± 1.2 nm MPa(-1), close to recent estimates from single fibre mechanics (12.8 ± 0.5 nm MPa(-1)). C(cb) calculated using these estimates is 0.37 ± 0.12 nm pN(-1), a value fully accounted for by the compliance of the myosin head domain, 0.38 ± 0.06 nm pN(-1), obtained from the intensity changes of the 14.5 nm myosin-based X-ray reflection in response to 3 kHz oscillations imposed on single muscle fibres in rigor. Thus, a significant contribution to C(cb) from the myosin tail that joins the head to the thick filament is excluded. The low C(cb) value indicates that the myosin head generates isometric force by a small sub-step of the 11 nm stroke that drives filament sliding at low load. The implications of these results for the mechanism of force generation by myosins have general relevance for cardiac and non-muscle myosins as well as for skeletal muscle.
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