ArticleBiophysical journal2001
Unfolding of titin domains explains the viscoelastic behavior of skeletal myofibrils.
Article in Biophysical journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 82 papers.
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Who cites it
82 citing papers in PubMed, 207 citations in OpenAlex.
- Caenorhabditis elegans small heat-shock protein HSP-12.6 has a highly specialized protective function towards muscle thick filaments in vivo.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026Article
- Integrated Opto-Biomechatronics For Single Muscle Fibre Structure-Function Assessment: The MyoRobot 3.0.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Titin's P-zone domains A164-167 are essential for thick filament structural arrangement.The Journal of general physiology · 2026Article
- Viscoelasticity of the Heart: An Overview of Viscoelastic Measurements at Different Scales.Annual review of biomedical engineering · 2026Review
- Mending the Achilles heels of titin in cardiac and musculoskeletal disease.Biophysical reviews · 2026Review
- Chronic and acute mediators of passive viscoelasticity in human skeletal muscle fibres.Experimental physiology · 2025Article
- Kinesin-14 HSET and KlpA are non-processive microtubule motors with load-dependent power strokes.Nature communications · 2024Article
- Tough Hydrogels for Load-Bearing Applications.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Review
- Article
- Effect of strain rates on the mechanical response of whole muscle bundle.Journal of biological physics · 2023Article
- Heat Shock Proteins: Important Helpers for the Development, Maintenance and Regeneration of Skeletal Muscles.Muscles (Basel, Switzerland) · 2023Review
- Hysteresis behavior in the unfolding/refolding processes of a protein trapped in metallo-cages.Chemical science · 2023Article
- Oxidative stress and inflammation distinctly drive molecular mechanisms of diastolic dysfunction and remodeling in female and male heart failure with preserved ejection fraction rats.Frontiers in cardiovascular medicine · 2023Article
- Simulation of the 3D Hyperelastic Behavior of Ventricular Myocardium using a Finite-Element Based Neural-Network Approach.Computer methods in applied mechanics and engineering · 2022Article
- Single-Molecule Force Spectroscopy Studies of Missense Titin Mutations That Are Likely Causing Cardiomyopathy.Langmuir : the ACS journal of surfaces and colloids · 2021Article
- Why exercise builds muscles: titin mechanosensing controls skeletal muscle growth under load.Biophysical journal · 2021Article
- Characterization of the structural forces governing the reversibility of the thermal unfolding of the human acidic fibroblast growth factor.Scientific reports · 2021Article
- History-dependence of muscle slack length in humans: effects of contraction intensity, stretch amplitude, and time.Journal of applied physiology (Bethesda, Md. : 1985) · 2020Article
- Stretching single titin molecules from failing human hearts reveals titin's role in blunting cardiac kinetic reserve.Cardiovascular research · 2020Article
- Passive force and viscoelastic properties of single fibers in human aging muscles.European journal of applied physiology · 2019Article
22 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
The elastic section of the giant muscle protein titin contains many immunoglobulin-like domains, which have been shown by single-molecule mechanical studies to unfold and refold upon stretch-release. Here we asked whether the mechanical properties of Ig domains and/or other titin regions could be responsible for the viscoelasticity of nonactivated skeletal-muscle sarcomeres, particularly for stress relaxation and force hysteresis. We show that isolated psoas myofibrils respond to a stretch-hold protocol with a characteristic force decay that becomes more pronounced following stretch to above 2.6-microm sarcomere length. The force decay was readily reproducible by a Monte Carlo simulation taking into account both the kinetics of Ig-domain unfolding and the worm-like-chain model of entropic elasticity used to describe titin's elastic behavior. The modeling indicated that the force decay is explainable by the unfolding of only a very small number of Ig domains per titin molecule. The simulation also predicted that a unique sequence in titin, the PEVK domain, may undergo minor structural changes during sarcomere extension. Myofibrils subjected to 1-Hz cycles of stretch-release exhibited distinct hysteresis that persisted during repetitive measurements. Quick stretch-release protocols, in which variable pauses were introduced after the release, revealed a two-exponential time course of hysteresis recovery. The rate constants of recovery compared well with the refolding rates of Ig-like or fibronectin-like domains measured by single-protein mechanical analysis. These findings suggest that in the sarcomere, titin's Ig-domain regions may act as entropic springs capable of adjusting their contour length in response to a stretch.
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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.