ArticleBiophysical journal1999
Extensibility and symmetry of actin filaments in contracting muscles.
Article in Biophysical journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
What it found
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Who cites it
37 citing papers in PubMed.
- Distinct distributions of myosin motor conformations during contraction of slow and fast skeletal muscle.The Journal of physiology · 2026Article
- Comparison of Predicted X-Ray Fiber Diffraction Patterns from All-Atom and Coarse-Grained Actin Filament Models Under Nonuniform Strain.International journal of molecular sciences · 2025Article
- Popping the hood of muscle motors using time-resolved, small-angle X-ray diffraction.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Dual-filament regulation of relaxation in mammalian fast skeletal muscle.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- The distinctive mechanical and structural signatures of residual force enhancement in myofibers.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Differences in thick filament activation in fast rodent skeletal muscle and slow porcine cardiac muscle.The Journal of physiology · 2024Article
- Molecular Dynamics Assessment of Mechanical Properties of the Thin Filaments in Cardiac Muscle.International journal of molecular sciences · 2023Article
- Thick filament activation is different in fast- and slow-twitch skeletal muscle.The Journal of physiology · 2022Article
- Small Angle X-ray Diffraction as a Tool for Structural Characterization of Muscle Disease.International journal of molecular sciences · 2022Review
- Triggering typical nemaline myopathy with compound heterozygous nebulin mutations reveals myofilament structural changes as pathomechanism.Nature communications · 2020Article
- Estimation of Forces on Actin Filaments in Living Muscle from X-ray Diffraction Patterns and Mechanical Data.International journal of molecular sciences · 2019Article
- Nebulin and titin modulate cross-bridge cycling and length-dependent calcium sensitivity.The Journal of general physiology · 2019Article
- Physiological Mechanisms of Eccentric Contraction and Its Applications: A Role for the Giant Titin Protein.Frontiers in physiology · 2017Review
- Three-dimensional stochastic model of actin-myosin binding in the sarcomere lattice.The Journal of general physiology · 2016Article
- Myopathy-inducing mutation H40Y in ACTA1 hampers actin filament structure and function.Biochimica et biophysica acta · 2016Article
- Sarcomere length dependent effects on the interaction between cTnC and cTnI in skinned papillary muscle strips.Archives of biochemistry and biophysics · 2016Article
- The contributions of filaments and cross-bridges to sarcomere compliance in skeletal muscle.The Journal of physiology · 2014Article
- Is titin a 'winding filament'? A new twist on muscle contraction.Proceedings. Biological sciences · 2012Article
- 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
Corrections and comments
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
When isometrically contracting muscles are subjected to a quick release followed by a shortening ramp of appropriate speed (V(o)), tension decays from its value at the isometric plateau (P(o)) to <0. 05 P(o) with the same time course as the quick part of the release; thereafter, tension remains at a negligible level for the duration of the shortening ramp. X-ray diffraction data obtained under these conditions provide evidence that 1) at V(o) very few heads form an actomyosin complex, while the number of heads doing so at P(o) is significant; 2) relative to rest the actin filament at V(o) is approximately 0.12% shorter and more twisted, while it is approximately 0.3% longer and less twisted at P(o); and 3) the myosin heads attaching to actin during force development do so against a thin filament compliance of at least 0.646 +/- 0.046% nm per P(o).
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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.