ArticleJournal of the American Chemical Society2023
Multidimensional Super-Resolution Microscopy Unveils Nanoscale Surface Aggregates in the Aging of FUS Condensates.
Article in Journal of the American Chemical Society, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed.
- Programmable DNA protonuclei reveal environmental context on protein phase separation.Nature communications · 2026Article
- Single Fluorogens and Orientation-Localization Microscopy for Quantifying Chemical and Biomolecular Dynamics at the Nanoscale.Accounts of chemical research · 2026Article
- Phase separation across membranes and condensates in cell organization and function.Nature reviews. Molecular cell biology · 2026Review
- A series of spontaneously blinking dyes for super-resolution microscopy.Nature methods · 2026Article
- Solvatochromic BODIPYs with Polarity-Independent Absorption for Functional Super-resolution Imaging of Live Cell Membranes.Chemical & biomedical imaging · 2026Article
- Spectroscopic DNA-PAINT for simultaneous multiplexed super-resolution microscopy.bioRxiv : the preprint server for biology · 2026Article
- Nanoscale domains govern local diffusion and ageing within fused-in-sarcoma condensates.Nature nanotechnology · 2026Article
- Surface-Tethering Enhances Precision in Measuring Diffusion Within 3D Protein Condensates.Journal of molecular biology · 2026Article
- Multiplexed Analysis of Multicomponent Biomolecular Condensates without Any Tag.Journal of the American Chemical Society · 2025Article
- Single-molecule live-cell RNA imaging with CRISPR-Csm.Nature biotechnology · 2025Article
- Biomolecular condensate microstructure is invariant to sequence-encoded molecular and macroscopic properties.Soft matter · 2025Article
- Controlling interfacial protein adsorption, desorption and aggregation in biomolecular condensates.Nature communications · 2025Article
- FUS nanoclusters are a distinct state within the dilute phase.Nature communications · 2025Article
- Single molecule spectrum dynamics imaging with 3D target-locking tracking.Nature communications · 2025Article
- In situ secondary structure imaging of protein phase separation and aggregation by hyperspectral stimulated Raman scattering microscopy.Nature communications · 2025Article
- Nanoscale profiling of evolving intermolecular interactions in ageing FUS condensates.Communications chemistry · 2025Article
- Lipid-Mediated Assembly of Biomolecular Condensates: Mechanisms, Regulation, and Therapeutic Implications.Biology · 2025Review
- Computational rheometry of viscoelastic networks: From random graphs to biomolecular condensates.bioRxiv : the preprint server for biology · 2025Article
- Clustering within a single-component biomolecular condensate.bioRxiv : the preprint server for biology · 2025Article
- Biomolecular condensate microstructure couples molecular and mesoscale properties.bioRxiv : the preprint server for biology · 2025Article
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Abstract
The intracellular liquid-liquid phase separation (LLPS) of biomolecules gives rise to condensates that act as membrane-less organelles with vital functions. FUS, an RNA-binding protein, natively forms condensates through LLPS and further provides a model system for the often disease-linked liquid-to-solid transition of biomolecular condensates during aging. However, the mechanism of such maturation processes, as well as the structural and physical properties of the system, remains unclear, partly attributable to difficulties in resolving the internal structures of the micrometer-sized condensates with diffraction-limited optical microscopy. Harnessing a set of multidimensional super-resolution microscopy tools that uniquely map out local physicochemical parameters through single-molecule spectroscopy, here, we uncover nanoscale heterogeneities in FUS condensates and elucidate their evolution over aging. Through spectrally resolved single-molecule localization microscopy (SR-SMLM) with a solvatochromic dye, we unveil distinct hydrophobic nanodomains at the condensate surface. Through SMLM with a fluorogenic amyloid probe, we identify these nanodomains as amyloid aggregates. Through single-molecule displacement/diffusivity mapping (SM
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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 Socratic graph.