ArticleNature methods2026
A highly photostable monomeric red fluorescent protein for dual-color 3D STED and time-lapse 3D SIM imaging.
Article in Nature methods, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
5 citing papers in PubMed.
- A CandiChrome toolkit for multicolor labeling ofbioRxiv : the preprint server for biology · 2026Article
- Dark-State-Mediated Photobleaching in mCherry-Based Red Fluorescent Proteins.The journal of physical chemistry letters · 2026Article
- Year in review 2025.Nature methods · 2026Article
- MultiSite Assembly of Gateway Induced Clones (MAGIC): a flexible cloning toolbox for use in vertebrate model systems.Development (Cambridge, England) · 2025Article
- Quantitative comparison of fluorescent proteins using protein nanocages in live cells.Journal of cell science · 2025Article
Corrections and comments
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Authors and funding
14 authors.
Funding
Abstract
Highly photostable red fluorescent proteins (RFPs) are invaluable for dual-color fluorescence microscopy, including super-resolution microscopy. Here we present mScarlet3‑S2, an RFP that exhibits a 29-fold improvement in photostability over its predecessor, mScarlet3, and outperforms other existing RFPs. This high photostability enables prolonged 2D and 3D imaging using both structured illumination microscopy and stimulated emission depletion microscopy. Using mScarlet3‑S2, we achieved over 150 Z-stacks in 3D STED imaging, revealing the architecture of the endoplasmic reticulum (ER) in detail. Key findings facilitated by mScarlet3‑S2 include nonplanar ER junctions, nuclear envelope (NE) invaginations, 3D maps of ER-NE contacts, diverse contact morphotypes (punctate, ribbon-like and branched) and polarized ER-NE junction distributions. These findings redefine our structural understanding of the ER-NE interface and demonstrate the value of mScarlet3‑S2 in revealing subcellular complexity.
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Registered trials
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