ArticleFEBS letters2016
Analysis of biophysical and functional consequences of tropomyosin-fluorescent protein fusions.
Article in FEBS letters, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 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
8 citing papers in PubMed, 12 citations in OpenAlex.
- Functional redundancy and formin-isoform independent localization of tropomyosin paralogs in Saccharomyces cerevisiae.PLoS genetics · 2025Article
- mNG-tagged fusion proteins and nanobodies to visualize tropomyosins in yeast and mammalian cells.Journal of cell science · 2022Article
- Novel human cell expression method reveals the role and prevalence of posttranslational modification in nonmuscle tropomyosins.The Journal of biological chemistry · 2021Article
- Dynamics of Tpm1.8 domains on actin filaments with single-molecule resolution.Molecular biology of the cell · 2020Article
- Visualizing the in vitro assembly of tropomyosin/actin filaments using TIRF microscopy.Biophysical reviews · 2020Review
- Article
- Tropomyosin Isoforms Specify Functionally Distinct Actin Filament Populations In Vitro.Current biology : CB · 2017Article
- Recruitment Kinetics of Tropomyosin Tpm3.1 to Actin Filament Bundles in the Cytoskeleton Is Independent of Actin Filament Kinetics.PloS one · 2016Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The dynamic nature of actin polymers is modulated to facilitate a diverse range of cellular processes. These dynamic properties are determined by different isoforms of tropomyosin which are recruited to distinct subpopulations of actin polymers to differentially regulate their functional properties. This makes tropomyosin an attractive target for labelling discrete actin populations. We have assessed the effect of different fluorescent labelling strategies for this protein. Although tropomyosin-fluorescent fusions decorate actin in vivo, they are either nonfunctional or perturb regulation of actin nucleation and cell cycle timings. Thus, conclusions and physiological relevance should be carefully evaluated when using tropomyosin fusions.
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Registered trials
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