ArticleMethods (San Diego, Calif.)2012
Biochemical and cell biological analysis of actin in the nematode Caenorhabditis elegans.
Article in Methods (San Diego, Calif.), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 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
7 citing papers in PubMed, 16 citations in OpenAlex.
- Multiscale characterization ofiScience · 2025Article
- Transcriptomic Analysis of the Spatiotemporal Axis of Oogenesis and Fertilization inbioRxiv : the preprint server for biology · 2024Article
- Transcriptomic analysis of the spatiotemporal axis of oogenesis and fertilization inFrontiers in cell and developmental biology · 2024Article
- Imaging of Actin Cytoskeleton in the Nematode Caenorhabditis elegans.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Imaging of Actin Cytoskeletal Integrity During Aging in C. elegans.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Mutations inF1000Research · 2019Article
- Regulation of structure and function of sarcomeric actin filaments in striated muscle of the nematode Caenorhabditis elegans.Anatomical record (Hoboken, N.J. : 2007) · 2014Review
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
The nematode Caenorhabditis elegans has long been a useful model organism for muscle research. Its body wall muscle is obliquely striated muscle and exhibits structural similarities with vertebrate striated muscle. Actin is the core component of the muscle thin filaments, which are highly ordered in sarcomeric structures in striated muscle. Genetic studies have identified genes that regulate proper organization and function of actin filaments in C. elegans muscle, and sequence of the worm genome has revealed a number of conserved candidate genes that may regulate actin. To precisely understand the functions of actin-binding proteins, such genetic and genomic studies need to be complemented by biochemical characterization of these actin-binding proteins in vitro. This article describes methods for purification and biochemical characterization of actin from C. elegans. Although rabbit muscle actin is commonly used to characterize actin-binding proteins from many eukaryotic organisms, we detect several quantitative differences between C. elegans actin and rabbit muscle actin, highlighting that use of actin from an appropriate source is important in some cases. Additionally, we describe probes for cell biological analysis of actin in C. elegans.
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Registered trials
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