ArticleAmerican journal of physiology. Cell physiology2010
Regulation of muscle force in the absence of actin-myosin-based cross-bridge interaction.
Article in American journal of physiology. Cell physiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 89 papers, 2 of them syntheses that pooled it.
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Who cites it
89 citing papers in PubMed, 2 syntheses or guidelines pooled it, 206 citations in OpenAlex.
- Non-local acute stretching effects on strength performance in healthy young adults.European journal of applied physiology · 2021Pooled it
- Mechanisms underlying performance impairments following prolonged static stretching without a comprehensive warm-up.European journal of applied physiology · 2021Pooled it
- Activation and aponeurosis morphology affect in vivo muscle tissue strains near the myotendinous junction.Journal of biomechanics · 2012Trial
- Mechanisms Influencing Maximum Joint Range of Motion and Stiffness: A Narrative Review.Sports medicine (Auckland, N.Z.) · 2026Review
- Integrated Opto-Biomechatronics For Single Muscle Fibre Structure-Function Assessment: The MyoRobot 3.0.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Effects of chemical myosin II cross-bridge inhibitors on eccentric force production in skinned muscle fibres.Experimental physiology · 2026Article
- Fascicle lengthening during a large torque reduction subsequently decreases dorsiflexion torque steadiness.Scientific reports · 2026Article
- CaBiophysical journal · 2025Article
- Consecutive SSCs increase the SSC effect in skinned rat muscle fibres.Pflugers Archiv : European journal of physiology · 2025Article
- Does force depression resulting from shortening against series elasticity contribute to the activation dependence of optimum length?American journal of physiology. Cell physiology · 2025Article
- Levosimendan's Effects on Length-Dependent Activation in Murine Fast-Twitch Skeletal Muscle.International journal of molecular sciences · 2024Article
- Modeling thick filament activation suggests a molecular basis for force depression.Biophysical journal · 2024Article
- TTN truncation variants produce sarcomere-integrating proteins of uncertain functional significance.The Journal of clinical investigation · 2024Article
- Re‑examining the mechanism of eccentric exercise‑induced skeletal muscle damage from the role of the third filament, titin (Review).Biomedical reports · 2024Review
- Alterations in skeletal muscle morphology and mechanics in juvenile male Sprague Dawley rats exposed to a high-fat high-sucrose diet.Scientific reports · 2023Article
- Characterizing residual and passive force enhancements in cardiac myofibrils.Biophysical journal · 2023Article
- Eccentric muscle contractions: from single muscle fibre to whole muscle mechanics.Pflugers Archiv : European journal of physiology · 2023Review
- Gaining new understanding of sarcomere length non-uniformities in skeletal muscles.Frontiers in physiology · 2023Article
- Signaling network model of cardiomyocyte morphological changes in familial cardiomyopathy.Journal of molecular and cellular cardiology · 2023Article
- Fast stretching of skeletal muscle fibres abolishes residual force enhancement.The Journal of experimental biology · 2022Article
29 more citing papers are in PubMed but not listed here.
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
For the past half century, the sliding filament-based cross-bridge theory has been the cornerstone of our understanding of how muscles contract. According to this theory, active force can only occur if there is overlap between the contractile filaments, actin and myosin. Otherwise, forces are thought to be caused by passive structural elements and are assumed to vary solely because of the length of the muscle. We observed increases in muscle force by a factor of 3 to 4 above the purely passive forces for activated and stretched myofibrils in the absence of actin-myosin overlap. We show that this dramatic increase in force is crucially dependent on the presence of the structural protein titin, cannot be explained with calcium activation, and is regulated by actin-myosin-based cross-bridge forces before stretching. We conclude from these observations that titin is a strong regulator of muscle force and propose that this regulation is based on cross-bridge force-dependent titin-actin interactions. These results suggest a mechanism for stability of sarcomeres on the "inherently unstable" descending limb of the force-length relationship, and they further provide an explanation for the protection of muscles against stretch-induced muscle injuries.
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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.