ArticleThe Journal of physiology2005
The structural basis of the increase in isometric force production with temperature in frog skeletal muscle.
Article in The Journal of physiology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- Comparing acute effects of heavy resistance, plyometric, and complex training on post-activation performance enhancement in elite swimmers: a randomized controlled trial.Frontiers in physiology · 2026Article
- Temperature affects the torque-velocity relationship of the ankle plantar flexor muscles.Scientific reports · 2025Article
- 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
- The force of the myosin motor sets cooperativity in thin filament activation of skeletal muscles.Communications biology · 2022Article
- Analysis methods and quality criteria for investigating muscle physiology using x-ray diffraction.The Journal of general physiology · 2021Article
- Low temperature traps myosin motors of mammalian muscle in a refractory state that prevents activation.The Journal of general physiology · 2019Article
- Temperature effect on the chemomechanical regulation of substeps within the power stroke of a single Myosin II.Scientific reports · 2016Article
- Motor force homeostasis in skeletal muscle contraction.Biophysical journal · 2011Article
- The fraction of myosin motors that participate in isometric contraction of rabbit muscle fibers at near-physiological temperature.Biophysical journal · 2011Article
- Geometrical conditions indispensable for muscle contraction.International journal of molecular sciences · 2011Article
- Force and power generating mechanism(s) in active muscle as revealed from temperature perturbation studies.The Journal of physiology · 2010Review
- Actomyosin-ADP states, interhead cooperativity, and the force-velocity relation of skeletal muscle.Biophysical journal · 2010Article
- The mechanism of the resistance to stretch of isometrically contracting single muscle fibres.The Journal of physiology · 2010Article
- The temperature dependence of cell mechanics measured by atomic force microscopy.Physical biology · 2009Article
- Tropomyosin period 3 is essential for enhancement of isometric tension in thin filament-reconstituted bovine myocardium.Journal of biophysics (Hindawi Publishing Corporation : Online) · 2009Article
- Direct modeling of X-ray diffraction pattern from contracting skeletal muscle.Biophysical journal · 2008Article
- Residual force enhancement in myofibrils and sarcomeres.Proceedings. Biological sciences · 2008Article
- Skeletal muscle resists stretch by rapid binding of the second motor domain of myosin to actin.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Sarcomere length dependence of rat skinned cardiac myocyte mechanical properties: dependence on myosin heavy chain.The Journal of physiology · 2007Article
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9 authors.
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Abstract
X-ray diffraction patterns were recorded from isolated single fibres of frog skeletal muscle during isometric contraction at temperatures between 0 and 17 degrees C. Isometric force was 43 +/- 2% (mean +/- S.E.M., n = 10) higher at 17 degrees C than 0 degrees C. The intensity of the first actin layer line increased by 57 +/- 18% (n = 5), and the ratio of the intensities of the equatorial 1,1 and 1,0 reflections by 20 +/- 7% (n = 10), signalling radial or azimuthal motions of the myosin head domains. The M3 X-ray reflection from the axial repeat of the heads along the filaments was 27 +/- 4% more intense at 17 degrees C, suggesting that the heads became more perpendicular to the filaments. The ratio of the intensities of the higher and lower angle peaks of the M3 reflection (R(M3)) was 0.93 +/- 0.02 (n = 5) at 0 degrees C and 0.77 +/- 0.02 at 17 degrees C. These peaks are due to interference between the two halves of each myosin filament, and the R(M3) decrease shows that heads move towards the midpoint of the myosin filament at the higher temperature. Calculations based on a crystallographic model of the heads indicated that the observed R(M3) change corresponds to tilting of their light-chain domains by 9 deg, producing an axial displacement of 1.4 nm, which is equal to that required to strain the actin and myosin filaments under the increased force. We conclude that the higher force generated by skeletal muscle at higher temperature can be accounted for by axial tilting of the myosin heads.
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