ArticleBiophysical journal2002
Direct measurement of single synthetic vertebrate thick filament elasticity using nanofabricated cantilevers.
Article in Biophysical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
12 citing papers in PubMed, 21 citations in OpenAlex.
- Emergent spatiotemporal dynamics of the actomyosin network in the presence of chemical gradients.Integrative biology : quantitative biosciences from nano to macro · 2019Article
- Thick-Filament Extensibility in Intact Skeletal Muscle.Biophysical journal · 2018Article
- Emergent mechanics of actomyosin drive punctuated contractions and shape network morphology in the cell cortex.PLoS computational biology · 2018Article
- Rotational model for actin filament alignment by myosin.Journal of theoretical biology · 2012Article
- Thick-filament strain and interfilament spacing in passive muscle: effect of titin-based passive tension.Biophysical journal · 2011Article
- Crossbridge and filament compliance in muscle: implications for tension generation and lever arm swing.Journal of muscle research and cell motility · 2010Review
- Significant impact on muscle mechanics of small nonlinearities in myofilament elasticity.Biophysical journal · 2010Article
- Comparative biomechanics of thick filaments and thin filaments with functional consequences for muscle contraction.Journal of biomedicine & biotechnology · 2010Review
- Molecular basis of the catch state in molluscan smooth muscles: a catchy challenge.Journal of muscle research and cell motility · 2008Review
- Passive stiffness in Drosophila indirect flight muscle reduced by disrupting paramyosin phosphorylation, but not by embryonic myosin S2 hinge substitution.Biophysical journal · 2006Article
- Stepwise length changes in single invertebrate thick filaments.Biophysical journal · 2005Article
- Mechanics of F-actin characterized with microfabricated cantilevers.Biophysical journal · 2002Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Thick filaments are generally thought to be effectively inextensible. Here we use novel nanofabricated cantilevers to carry out the first direct force-elongation measurements on single vertebrate thick filaments. Cantilevers are ideal for these experiments: force ranges are from pico- to micronewtons, specimens can be visualized during the experiment, and attachment surfaces are in the same plane as the filament. Synthetic thick filaments from rabbit myosin were suspended between two cantilevers and stretched. With stretch, stiffness increased gradually and then became nearly constant after approximately 100 pN. Stretch rate had little or no effect on force-elongation behavior. Under physiological loads (approximately 240 pN axially averaged with full activation) filaments elongated by 1.1 +/- 0.3%. Previous x-ray diffraction results showed a 1.0 to 1.5% increase in myosin head spacing with activation; however, this increase in spacing has been interpreted as change in the state of the cross-bridges, not as elasticity in the thick filament backbone. Comparison with our data suggests that changes in the myosin x-ray reflections seen during activation may be due to elongation of the thick filament backbone. Recognition of thick filament elasticity is important because it affects the interpretation of mechanical experiments and inferences drawn on the molecular mechanism of contraction.
Indexed as
Identifiers
What OpenQuestion holds
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.