ArticleNature biotechnology2023
Extending fluorescence anisotropy to large complexes using reversibly switchable proteins.
Article in Nature biotechnology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Nanoscale Spatial Organization of ARC High- and Low-Order Assemblies at Excitatory Synapses.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- SurFlex microscopy: Measuring flexibility of surface-tethered biomolecules.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- All-optical strategies to minimize photobleaching in reversibly switchable fluorescent proteins.Nature communications · 2025Article
- Motion of Molecules in Supramolecular Scaffolds Enhances Bone Regeneration.Journal of the American Chemical Society · 2025Article
- Single-shot two-dimensional nano-size mapping of fluorescent molecules by ultrafast polarization anisotropy imaging.Nature communications · 2025Article
- A Nanobody-Based Proximity Ligation Assay Detects Constitutive and Stimulus-Regulated Native Arc/Arg3.1 Oligomers in Hippocampal Neuronal Dendrites.Molecular neurobiology · 2025Article
- Resolving the Orientations of and Angular Separation Between a Pair of Dipole Emitters.Physical review letters · 2025Article
- Article
- Volumetric imaging of the 3D orientation of cellular structures with a polarized fluorescence light-sheet microscope.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Super-sectioning with multi-sheet reversible saturable optical fluorescence transitions (RESOLFT) microscopy.Nature methods · 2024Article
- Three-dimensional spatio-angular fluorescence microscopy with a polarized dual-view inverted selective-plane illumination microscope (pol-diSPIM).bioRxiv : the preprint server for biology · 2024Article
- Detection of Arc/Arg3.1 oligomers in rat brain: constitutive and synaptic activity-evoked dimer expressionFrontiers in molecular neuroscience · 2023Article
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Authors and funding
8 authors.
Funding
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Abstract
The formation of macromolecular complexes can be measured by detection of changes in rotational mobility using time-resolved fluorescence anisotropy. However, this method is limited to relatively small molecules (~0.1-30 kDa), excluding the majority of the human proteome and its complexes. We describe selective time-resolved anisotropy with reversibly switchable states (STARSS), which overcomes this limitation and extends the observable mass range by more than three orders of magnitude. STARSS is based on long-lived reversible molecular transitions of switchable fluorescent proteins to resolve the relatively slow rotational diffusivity of large complexes. We used STARSS to probe the rotational mobility of several molecular complexes in cells, including chromatin, the retroviral Gag lattice and activity-regulated cytoskeleton-associated protein oligomers. Because STARSS can probe arbitrarily large structures, it is generally applicable to the entire human proteome.
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