ArticleThe Journal of physiology2018
Mechanical parameters of the molecular motor myosin II determined in permeabilised fibres from slow and fast skeletal muscles of the rabbit.
Article in The Journal of physiology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 34 citations in OpenAlex.
- Cross-bridge model for predicting muscle short-range stiffness during movement.PLoS computational biology · 2026Article
- Distinct distributions of myosin motor conformations during contraction of slow and fast skeletal muscle.The Journal of physiology · 2026Article
- Force and kinetics of fast and slow muscle myosin determined with a synthetic sarcomere-like nanomachine.Communications biology · 2024Article
- Matching Mechanics and Energetics of Muscle Contraction Suggests Unconventional Chemomechanical Coupling during the Actin-Myosin Interaction.International journal of molecular sciences · 2023Article
- Developmental, physiologic and phylogenetic perspectives on the expression and regulation of myosin heavy chains in mammalian skeletal muscles.Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology · 2023Review
- The molecular athlete: exercise physiology from mechanisms to medals.Physiological reviews · 2023Review
- Theoretical efficiency limits and speed-efficiency trade-off in myosin motors.PLoS computational biology · 2023Article
- Thick filament activation is different in fast- and slow-twitch skeletal muscle.The Journal of physiology · 2022Article
- The force of the myosin motor sets cooperativity in thin filament activation of skeletal muscles.Communications biology · 2022Article
- Anisotropic Elasticity of the Myosin Motor in Muscle.International journal of molecular sciences · 2022Article
- A reverse stroke characterizes the force generation of cardiac myofilaments, leading to an understanding of heart function.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- A Myosin II-Based Nanomachine Devised for the Study of CaInternational journal of molecular sciences · 2020Article
- Muscle hypertrophy and muscle strength: dependent or independent variables? A provocative review.European journal of translational myology · 2020Article
- Orthophosphate increases the efficiency of slow muscle-myosin isoform in the presence of omecamtiv mecarbil.Nature communications · 2020Article
- Single-molecule analysis reveals that regulatory light chains fine-tune skeletal myosin II function.The Journal of biological chemistry · 2020Article
- Current Understanding of Residual Force Enhancement: Cross-Bridge Component and Non-Cross-Bridge Component.International journal of molecular sciences · 2019Review
- 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
- Cross-bridges in slow skeletal muscle: not only slow but also soft.The Journal of physiology · 2018Article
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6 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
key pointsThe different performance of slow and fast muscles is mainly attributed to diversity of the myosin heavy chain (MHC) isoform expressed within them. In this study fast sarcomere-level mechanics has been applied to Ca ABSTRACT: The skeletal muscle exhibits large functional differences depending on the myosin heavy chain (MHC) isoform expressed in its molecular motor, myosin II. The differences in the mechanical features of force generation by myosin isoforms were investigated in situ by using fast sarcomere-level mechanical methods in permeabilised fibres (sarcomere length 2.4 μm, temperature 12°C, 4% dextran T-500) from slow (soleus, containing the MHC-1 isoform) and fast (psoas, containing the MHC-2X isoform) skeletal muscle of the rabbit. The stiffness of the half-sarcomere was determined at the plateau of Ca
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