ArticleBiophysical journal2005
A new muscle contractile system composed of a thick filament lattice and a single actin filament.
Article in Biophysical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 22 citations in OpenAlex.
- Mice with R2509C-RYR1 mutation exhibit dysfunctional Ca2+ dynamics in primary skeletal myocytes.The Journal of general physiology · 2022Article
- Nanoscopic changes in the lattice structure of striated muscle sarcomeres involved in the mechanism of spontaneous oscillatory contraction (SPOC).Scientific reports · 2020Article
- Functional significance of HCM mutants of tropomyosin, V95A and D175N, studied withBiophysics and physicobiology · 2019Article
- Article
- Cardiac tissue structure, properties, and performance: a materials science perspective.Annals of biomedical engineering · 2014Review
- Future challenges in single-molecule fluorescence and laser trap approaches to studies of molecular motors.Developmental cell · 2012Review
- Quasiperiodic distribution of rigor cross-bridges along a reconstituted thin filament in a skeletal myofibril.Biophysical journal · 2011Article
- Assessment of contractility in intact ventricular cardiomyocytes using the dimensionless 'Frank-Starling Gain' index.Pflugers Archiv : European journal of physiology · 2011Review
- Thin filament-reconstituted skinned muscle fibers for the study of muscle physiology.Journal of biomedicine & biotechnology · 2011Review
- Molecular motors as an auto-oscillator.HFSP journal · 2010Article
- Mechanical distortion of single actin filaments induced by external force: detection by fluorescence imaging.Biophysical journal · 2009Article
- Interaction forces between F-actin and titin PEVK domain measured with optical tweezers.Biophysical journal · 2007Article
- New techniques in linear and non-linear laser optics in muscle research.Journal of muscle research and cell motility · 2006Review
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
To bridge the gap between the contractile system in muscle and in vitro motility assay, we have devised an A-band motility assay system. A glycerinated skeletal myofibril was treated with gelsolin to selectively remove the thin filaments and expose a single A-band. A single bead-tailed actin filament trapped by optical tweezers was made to interact with the inside or the outer surface of the A-band, and the displacement of the bead-tailed filament was measured in a physiological ionic condition by phase-contrast and fluorescence microscopy. We observed large back-and-forth displacement of the filament accompanied by a large change in developed force. Despite this large tension fluctuation, we found that the average force was proportional to the overlap inside and outside the A-band up to approximately 150 nm and 300 nm from the end of the A-band, respectively. Consistent with the difference in the density of myosin molecules, the average force per unit length of the overlap inside the A-band (the time-averaged force/myosin head was approximately 1 pN) was approximately twice as large as that outside. Thus, we conclude that the A-band motility assay system described here is suitable for studying force generation on a single actin filament, and its sliding movement within a regular three-dimensional thick filament lattice.
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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.