ArticleBiophysical journal2009
The effect of myofilament compliance on kinetics of force generation by myosin motors in muscle.
Article in Biophysical journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 43 citations in OpenAlex.
- Theoretical treatment of tension transients in muscle following sudden changes in orthophosphate concentration: implications for energy transduction.Journal of muscle research and cell motility · 2025Article
- Multiple pathways of the actin-myosin cycle in energy transduction and the release of orthophosphate in muscle.Frontiers in physiology · 2025Review
- A novel kinetic model to demonstrate the independent effects of ATP and ADP/Pi concentrations on sarcomere function.PLoS computational biology · 2024Article
- Cross-bridge mechanics estimated from skeletal muscles' work-loop responses to impacts in legged locomotion.Scientific reports · 2021Article
- Evolution of mechanical cooperativity among myosin II motors.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Thick-Filament Extensibility in Intact Skeletal Muscle.Biophysical journal · 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
- Standard Loading Profile in Matrix Rigidity Sensing.Biophysical journal · 2018Article
- Effects of myosin inhibitors on the X-ray diffraction patterns of relaxed and calcium-activated rabbit skeletal muscle fibers.Biophysics and physicobiology · 2018Article
- Reinterpretation of the Tension Response of Muscle to Stretches and Releases.Biophysical journal · 2016Article
- Size and speed of the working stroke of cardiac myosin in situ.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Temperature effect on the chemomechanical regulation of substeps within the power stroke of a single Myosin II.Scientific reports · 2016Article
- Force and number of myosin motors during muscle shortening and the coupling with the release of the ATP hydrolysis products.The Journal of physiology · 2015Article
- The cross-bridge of skeletal muscle is not synchronized either by length or force step.International journal of molecular sciences · 2015Article
- Poorly understood aspects of striated muscle contraction.BioMed research international · 2015Review
- The contributions of filaments and cross-bridges to sarcomere compliance in skeletal muscle.The Journal of physiology · 2014Article
- Structural dynamics of troponin during activation of skeletal muscle.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- The non-linear elasticity of the muscle sarcomere and the compliance of myosin motors.The Journal of physiology · 2014Article
- Stiffness, working stroke, and force of single-myosin molecules in skeletal muscle: elucidation of these mechanical properties via nonlinear elasticity evaluation.Cellular and molecular life sciences : CMLS · 2013Review
- Nonlinear cross-bridge elasticity and post-power-stroke events in fast skeletal muscle actomyosin.Biophysical journal · 2013Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
We use the inhibitor of isometric force of skeletal muscle N-benzyl-p-toluene sulfonamide (BTS) to decrease, in a dose dependent way, the number of myosin motors attached to actin during the steady isometric contraction of single fibers from frog skeletal muscle (4 degrees C, 2.1 microm sarcomere length). In this way we can reduce the strain in the myofilament compliance during the isometric tetanus (T(0)) from 3.54 nm in the control solution (T(0,NR)) to approximately 0.5 nm in 1 microM BTS, where T(0) is reduced to approximately 0.15 T(0,NR). The quick force recovery after a step release (1-3 nm per half-sarcomere) becomes faster with the increase of BTS concentration and the decrease of T(0). The simulation of quick force recovery with a multistate model of force generation, that adapts Huxley and Simmons model to account for both the high stiffness of the myosin motor (approximately 3 pN/nm) and the myofilament compliance, shows that the increase in the rate of quick force recovery by BTS is explained by the reduced strain in the myofilaments, consequent to the decrease in half-sarcomere force. The model estimates that i), for the same half-sarcomere release the state transition kinetics in the myosin motor are five times faster in the absence of filament compliance than in the control; and ii), the rate of force recovery from zero to T(0) is approximately 6000/s in the absence of filament compliance.
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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.