ReviewInternational journal of molecular sciences2018
Temperature Effects on Force and Actin⁻Myosin Interaction in Muscle: A Look Back on Some Experimental Findings.
Review in International journal of molecular sciences, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 41 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
- Temperature dependence of activation of thick and thin filaments in skeletal and cardiac muscles.Journal of muscle research and cell motility · 2026Review
- 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
- Starting length and temperature dependence of eccentric muscle force-velocity behaviour.The Journal of experimental biology · 2026Article
- Impacts of exercise, renin-angiotensin system modulation or both on skeletal muscle circadian gene expression.Experimental physiology · 2026Article
- Acute effects of movement-specific warm-up on force production and neuromuscular activation during maximal isometric squat in resistance-trained men: a pilot study.European journal of translational myology · 2026Article
- Basal Heat Capacity of Skinned Skeletal Muscle with Selective Removal and Denaturation of Myoproteins: A Study with Differential Scanning Calorimetry.International journal of molecular sciences · 2026Article
- 24-hourFrontiers in transplantation · 2026Article
- Microscale velocity-dependent unbinding generates a macroscale performance-efficiency tradeoff in actomyosin systems.Communications biology · 2025Article
- Circadian Regulation for Optimizing Sport and Exercise Performance.Clocks & sleep · 2025Review
- Why so slow? Models of parkinsonian bradykinesia.Nature reviews. Neuroscience · 2024Review
- Effects of physical activity levels on characteristic pain in temporomandibular dysfunctions: a cross-sectional study.Head & face medicine · 2024Observational
- Myosin and tropomyosin-troponin complementarily regulate thermal activation of muscles.The Journal of general physiology · 2023Article
- A mechano- and heat-gated two-pore domain KProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Cooperative & competitive binding of anti-myosin tail antibodies revealed by super-resolution microscopy.Archives of biochemistry and biophysics · 2023Article
- Matching Mechanics and Energetics of Muscle Contraction Suggests Unconventional Chemomechanical Coupling during the Actin-Myosin Interaction.International journal of molecular sciences · 2023Article
- Effects of Hydrostatic-Pressure on Muscle Contraction: A Look Back on Some Experimental Findings.International journal of molecular sciences · 2023Review
- Influence of weighted downhill running training on serial sarcomere number and work loop performance in the rat soleus.Biology open · 2022Article
- Influence and Mechanisms of Action of Environmental Stimuli on Work Near and Above the Severe Domain Boundary (Critical Power).Sports medicine - open · 2022Review
- Opto-thermal technologies for microscopic analysis of cellular temperature-sensing systems.Biophysical reviews · 2022Review
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
Abstract
Observations made in temperature studies on mammalian muscle during force development, shortening, and lengthening, are re-examined. The isometric force in active muscle goes up substantially on warming from less than 10 °C to temperatures closer to physiological (>30 °C), and the sigmoidal temperature dependence of this force has a half-maximum at ~10 °C. During steady shortening, when force is decreased to a steady level, the sigmoidal curve is more pronounced and shifted to higher temperatures, whereas, in lengthening muscle, the curve is shifted to lower temperatures, and there is a less marked increase with temperature. Even with a small rapid temperature-jump (T-jump), force in active muscle rises in a definitive way. The rate of tension rise is slower with adenosine diphosphate (ADP) and faster with increased phosphate. Analysis showed that a T-jump enhances an early, pre-phosphate release step in the acto-myosin (crossbridge) ATPase cycle, thus inducing a force-rise. The sigmoidal dependence of steady force on temperature is due to this endothermic nature of crossbridge force generation. During shortening, the force-generating step and the ATPase cycle are accelerated, whereas during lengthening, they are inhibited. The endothermic force generation is seen in different muscle types (fast, slow, and cardiac). The underlying mechanism may involve a structural change in attached myosin heads and/or their attachments on heat absorption.
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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.