ReviewAnnual review of biophysics2009
Site-directed spectroscopic probes of actomyosin structural dynamics.
Review in Annual review of biophysics, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
What it found
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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.
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Who cites it
31 citing papers in PubMed, 54 citations in OpenAlex.
- Probing relaxed myosin states in hypertrophic cardiomyopathy by second harmonic-generation microscopy.eLife · 2026Article
- Article
- Structural role of essential light chains in the apicomplexan glideosome.Communications biology · 2020Article
- Special Issue: The Actin-Myosin Interaction in Muscle: Background and Overview.International journal of molecular sciences · 2019Review
- Myosin lever arm orientation in muscle determined with high angular resolution using bifunctional spin labels.The Journal of general physiology · 2019Article
- Comparative analysis of widely used methods to remove nonfunctional myosin heads for the in vitro motility assay.Journal of muscle research and cell motility · 2018Article
- Actin-Myosin Interaction: Structure, Function and Drug Discovery.International journal of molecular sciences · 2018Review
- Unconventional Imaging Methods to Capture Transient Structures during Actomyosin Interaction.International journal of molecular sciences · 2018Review
- Chemical Crosslinking Mass Spectrometry Analysis of Protein Conformations and Supercomplexes in Heart Tissue.Cell systems · 2018Article
- Kinetic coupling of phosphate release, force generation and rate-limiting steps in the cross-bridge cycle.Journal of muscle research and cell motility · 2017Review
- A Cardiomyopathy Mutation in the Myosin Essential Light Chain Alters Actomyosin Structure.Biophysical journal · 2017Article
- Physiological and pathophysiological reactive oxygen species as probed by EPR spectroscopy: the underutilized research window on muscle ageing.The Journal of physiology · 2016Review
- Direct real-time detection of the structural and biochemical events in the myosin power stroke.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- High-resolution helix orientation in actin-bound myosin determined with a bifunctional spin label.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Amplitude of the actomyosin power stroke depends strongly on the isoform of the myosin essential light chain.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Filming biomolecular processes by high-speed atomic force microscopy.Chemical reviews · 2014Review
- Electron paramagnetic resonance resolves effects of oxidative stress on muscle proteins.Exercise and sport sciences reviews · 2014Review
- Direct real-time detection of the actin-activated power stroke within the myosin catalytic domain.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- The structural dynamics of actin during active interaction with myosin depends on the isoform of the essential light chain.Biochemistry · 2013Article
- Conformationally trapping the actin-binding cleft of myosin with a bifunctional spin label.The Journal of biological chemistry · 2013Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Spectroscopy of myosin and actin has entered a golden age. High-resolution crystal structures of isolated actin and myosin have been used to construct detailed models for the dynamic actomyosin interactions that move muscle. Improved protein mutagenesis and expression technologies have facilitated site-directed labeling with fluorescent and spin probes. Spectroscopic instrumentation has achieved impressive advances in sensitivity and resolution. Here we highlight the contributions of site-directed spectroscopic probes to understanding the structural dynamics of myosin II and its actin complexes in solution and muscle fibers. We emphasize studies that probe directly the movements of structural elements within the myosin catalytic and light-chain domains, and changes in the dynamics of both actin and myosin due to their alternating strong and weak interactions in the ATPase cycle. A moving picture emerges in which single biochemical states produce multiple structural states, and transitions between states of order and dynamic disorder power the actomyosin engine.
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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.