ArticleThe Journal of physiology2003
Temperature dependence of the force-generating process in single fibres from frog skeletal muscle.
Article in The Journal of physiology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.
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Who cites it
64 citing papers in PubMed, 110 citations in OpenAlex.
- Acute Local Cooling to the Lower Body during Recovery Does Not Improve Repeated Vertical Jump Performance.International journal of environmental research and public health · 2021Trial
- Menopause alters temperature sensitivity of muscle force in humans.European journal of applied physiology · 2012Trial
- Isometric slow- and fast-contracting skeletal muscle fibres have more similar cellular and molecular properties at 37°C than at 25°C in older adults.The Journal of physiology · 2026Article
- Ice gliding diatoms establish record-low temperature limits for motility in a eukaryotic cell.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Temperature affects the torque-velocity relationship of the ankle plantar flexor muscles.Scientific reports · 2025Article
- The elementary step that generates force and sinusoidal analysis in striated muscle fibers.Journal of muscle research and cell motility · 2025Review
- Resolving the kinetics of an ensemble of muscle myosin motors via a temperature-dependent fitting procedure.Journal of the Royal Society, Interface · 2025Article
- The Mechanism of Modulation of Cardiac Force by Temperature.International journal of molecular sciences · 2025Article
- Predicting myosin heavy chain isoform from postdissection fiber length in human skeletal muscle fibers.American journal of physiology. Cell physiology · 2024Article
- Effects of Hydrostatic-Pressure on Muscle Contraction: A Look Back on Some Experimental Findings.International journal of molecular sciences · 2023Review
- The force of the myosin motor sets cooperativity in thin filament activation of skeletal muscles.Communications biology · 2022Article
- A myosin-based mechanism for stretch activation and its possible role revealed by varying phosphate concentration in fast and slow mouse skeletal muscle fibers.American journal of physiology. Cell physiology · 2019Article
- Low temperature traps myosin motors of mammalian muscle in a refractory state that prevents activation.The Journal of general physiology · 2019Article
- Temperature Effects on Force and Actin⁻Myosin Interaction in Muscle: A Look Back on Some Experimental Findings.International journal of molecular sciences · 2018Review
- Standard Loading Profile in Matrix Rigidity Sensing.Biophysical journal · 2018Article
- X-ray Diffraction Evidence for Low Force Actin-Attached and Rigor-Like Cross-Bridges in the Contractile Cycle.Biology · 2016Article
- Age-related maintenance of eccentric strength: a study of temperature dependence.Age (Dordrecht, Netherlands) · 2016Article
- Temperature effect on the chemomechanical regulation of substeps within the power stroke of a single Myosin II.Scientific reports · 2016Article
- The endothermic ATP hydrolysis and crossbridge attachment steps drive the increase of force with temperature in isometric and shortening muscle.The Journal of physiology · 2015Article
- Poorly understood aspects of striated muscle contraction.BioMed research international · 2015Review
4 more citing papers are in PubMed but not listed here.
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Generation of force and shortening in striated muscle is due to the cyclic interactions of the globular portion (the head) of the myosin molecule, extending from the thick filament, with the actin filament. The work produced in each interaction is due to a conformational change (the working stroke) driven by the hydrolysis of ATP on the catalytic site of the myosin head. However, the precise mechanism and the size of the force and length step generated in one interaction are still under question. Here we reinvestigate the endothermic nature of the force-generating process by precisely determining, in tetanized intact frog muscle fibres under sarcomere length control, the effect of temperature on both isometric force and force response to length changes. We show that raising the temperature: (1) increases the force and the strain of the myosin heads attached in the isometric contraction by the same amount (approximately 70 %, from 2 to 17 degrees C); (2) increases the rate of quick force recovery following small length steps (range between -3 and 2 nm (half-sarcomere)-1) with a Q10 (between 2 and 12 degrees C) of 1.9 (releases) and 2.3 (stretches); (3) does not affect the maximum extent of filament sliding accounted for by the working stroke in the attached heads (10 nm (half-sarcomere)-1). These results indicate that in isometric conditions the structural change leading to force generation in the attached myosin heads can be modulated by temperature at the expense of the structural change responsible for the working stroke that drives filament sliding. The energy stored in the elasticity of the attached myosin heads at the plateau of the isometric tetanus increases with temperature, but even at high temperature this energy is only a fraction of the mechanical energy released by attached heads during filament sliding.
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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.