ArticleBiophysical journal2009
Stabilization of helical order in the thick filaments by blebbistatin: further evidence of coexisting multiple conformations of myosin.
Article in Biophysical journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 43 citations in OpenAlex.
- Temperature dependence of activation of thick and thin filaments in skeletal and cardiac muscles.Journal of muscle research and cell motility · 2026Review
- Thick-Filament-Based Regulation and the Determinants of Force Generation.Biomedicines · 2025Article
- Skeletal muscle fiber hypercontraction induced by Bothrops asper myotoxic phospholipases APflugers Archiv : European journal of physiology · 2023Article
- Structural basis of the super- and hyper-relaxed states of myosin II.The Journal of general physiology · 2022Review
- Two Classes of Myosin Inhibitors, Para-nitroblebbistatin and Mavacamten, Stabilize β-Cardiac Myosin in Different Structural and Functional States.Journal of molecular biology · 2021Article
- Article
- Structural and Computational Insights into a Blebbistatin-Bound Myosin•ADP Complex with Characteristics of an ADP-Release Conformation along the Two-Step Myosin Power Stoke.International journal of molecular sciences · 2020Article
- Nanomolar ATP binding to single myosin cross-bridges in rigor: a molecular approach to studying myosin ATP kinetics using single human cardiomyocytes.Biophysical reviews · 2020Review
- Cycling Cross-Bridges Contribute to Thin Filament Activation in Human Slow-Twitch Fibers.Frontiers in physiology · 2020Article
- Dr Gerald W. Offer (1938-2019); an appreciation.Journal of muscle research and cell motility · 2019Article
- Low temperature traps myosin motors of mammalian muscle in a refractory state that prevents activation.The Journal of general physiology · 2019Article
- Altered force generation and cell-to-cell contractile imbalance in hypertrophic cardiomyopathy.Pflugers Archiv : European journal of physiology · 2019Review
- Response to: Thick Filament Length Changes in Muscle Have Both Elastic and Structural Components.Biophysical journal · 2019Article
- Myosin Head Configurations in Resting and Contracting Murine Skeletal Muscle.International journal of molecular sciences · 2018Article
- Mavacamten stabilizes an autoinhibited state of two-headed cardiac myosin.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Blebbistatin Effects Expose Hidden Secrets in the Force-Generating Cycle of Actin and Myosin.Biophysical journal · 2018Article
- Do Actomyosin Single-Molecule Mechanics Data Predict Mechanics of Contracting Muscle?International journal of molecular sciences · 2018Review
- Thick Filament Mechano-Sensing in Skeletal and Cardiac Muscles: A Common Mechanism Able to Adapt the Energetic Cost of the Contraction to the Task.Frontiers in physiology · 2018Article
- Effects of myosin inhibitors on the X-ray diffraction patterns of relaxed and calcium-activated rabbit skeletal muscle fibers.Biophysics and physicobiology · 2018Article
- Regulation of Contraction by the Thick Filaments in Skeletal Muscle.Biophysical journal · 2017Review
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
Abstract
The degree of helical order of the thick filament of mammalian skeletal muscle is highly dependent on temperature and the nature of the ligand. Previously, we showed that there was a close correlation between the conformation of the myosin heads on the surface of the thick filaments and the extent of their helical order. Helical order required the heads to be in the closed conformation. In addition, we showed that, with the same ligand bound at the active site, three conformations of myosin coexisted in equilibrium. Hitherto, however, there was no detectable helical order as measured by x-ray diffraction under the temperatures studied for myosin with MgADP and the nucleotide-free myosin, raising the possibility that the concept of multiple conformations has limited validity. In this study, blebbistatin was used to stabilize the closed conformation of myosin. The degree of helical order is substantially improved with MgATP at low temperature or with MgADP or in the absence of nucleotide. The thermodynamic parameters of the disorder<-->order transition and the characteristics of the ordered array were not significantly altered by binding blebbistatin. The simplest explanation is that the binding of blebbistatin increases the proportion of myosin in the closed conformation from being negligible to substantial. These results provide further evidence for the coexistence of multiple conformations of myosin under a wide range of conditions and for the closed conformation being directly coupled to helical order.
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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.