ReviewJournal of muscle research and cell motility2020
Quantitative high-precision imaging of myosin-dependent filamentous actin dynamics.
Review in Journal of muscle research and cell motility, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 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.
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Who cites it
2 citing papers in PubMed.
- Remodeling the epigenome and (epi)cytoskeleton: a new paradigm for co-regulation by methylation.The Journal of experimental biology · 2020Review
- Lamellipodium tip actin barbed ends serve as a force sensor.Genes to cells : devoted to molecular & cellular mechanisms · 2019Article
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Authors and funding
2 authors.
Funding
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Abstract
Over recent decades, considerable effort has been made to understand how mechanical stress applied to the actin network alters actin assembly and disassembly dynamics. However, there are conflicting reports concerning the issue both in vitro and in cells. In this review, we discuss concerns regarding previous quantitative live-cell experiments that have attempted to evaluate myosin regulation of filamentous actin (F-actin) turnover. In particular, we highlight an error-generating mechanism in quantitative live-cell imaging, namely convection-induced misdistribution of actin-binding probes. Direct observation of actin turnover at the single-molecule level using our improved electroporation-based Single-Molecule Speckle (eSiMS) microscopy technique overcomes these concerns. We introduce our recent single-molecule analysis that unambiguously demonstrates myosin-dependent regulation of F-actin stability in live cells. We also discuss the possible application of eSiMS microscopy in the analysis of actin remodeling in striated muscle cells.
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Registered trials
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