ArticleNature communications2022
Extra kinetic dimensions for label discrimination.
Article in Nature communications, 2022. 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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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
12 citing papers in PubMed.
- Non-Covalent Reversibly Photoconvertible Fluorescent Tags for Wash-Free Protein Labeling.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Interplay between high-energy quenching and state transitions in Chlamydomonas reinhardtii: a single-cell approach.The New phytologist · 2026Article
- All-optical strategies to minimize photobleaching in reversibly switchable fluorescent proteins.Nature communications · 2025Article
- Periodic Light Modulations for Low-Cost Wide-Field Imaging of Luminescence Kinetics Under Ambient Light.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Article
- Controlling the sound of light: photoswitching optoacoustic imaging.Nature methods · 2024Review
- Leaves to Measure Light Intensity.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Structural Heterogeneity in a Phototransformable Fluorescent Protein Impacts its Photochemical Properties.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Article
- Fluorescence to measure light intensity.Nature methods · 2023Article
- Proton-Coupled Photochromic Hemithioindigo: Toward Photoactivated Chemical Sensing and Imaging.Analytical chemistry · 2023Article
- Resonances at Fundamental and Harmonic Frequencies for Selective Imaging of Sine-Wave Illuminated Reversibly Photoactivatable Labels.Chemphyschem : a European journal of chemical physics and physical chemistry · 2022Article
Corrections and comments
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Authors and funding
15 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Due to its sensitivity and versatility, fluorescence is widely used to detect specifically labeled biomolecules. However, fluorescence is currently limited by label discrimination, which suffers from the broad full width of the absorption/emission bands and the narrow lifetime distribution of the bright fluorophores. We overcome this limitation by introducing extra kinetic dimensions through illuminations of reversibly photoswitchable fluorophores (RSFs) at different light intensities. In this expanded space, each RSF is characterized by a chromatic aberration-free kinetic fingerprint of photochemical reactivity, which can be recovered with limited hardware, excellent photon budget, and minimal data processing. This fingerprint was used to identify and discriminate up to 20 among 22 spectrally similar reversibly photoswitchable fluorescent proteins (RSFPs) in less than 1s. This strategy opens promising perspectives for expanding the multiplexing capabilities of fluorescence imaging.
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