ArticleProceedings of the National Academy of Sciences of the United States of America2016
Small fluorescence-activating and absorption-shifting tag for tunable protein imaging in vivo.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 132 papers.
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Who cites it
132 citing papers in PubMed, 282 citations in OpenAlex.
- Non-Covalent Reversibly Photoconvertible Fluorescent Tags for Wash-Free Protein Labeling.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Reversible, Chemically Gated FRET via Ligand-Activated Acceptors.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Discerning protein pools by selective staining with self-labeling tags.FEBS letters · 2026Review
- Lighting Up Biology: GFP-Inspired Fluorescent Probes for Sensing and Imaging.Journal of the American Chemical Society · 2026Article
- Advancing the monitoring of organelle contact sites in vitro and in vivo.Biochemical Society transactions · 2026Review
- The fluorescence-activating and absorption-shifting tag (FAST), a versatile protein marker for live plant cell imaging.The Plant journal : for cell and molecular biology · 2026Article
- NirFAP680: a highly bright and stable large Stokes shift near-infrared fluorogen-activating protein.Nature methods · 2026Article
- A color-tailored fluorogenic sensor for hydrogen peroxide.Nature chemical biology · 2026Article
- Reversible Chemogenetic Fluorescence Labeling with pFAST inmicroPublication biology · 2026Article
- Sugar-inducible promoters for manipulation of core metabolic pathways in the thermophilic acetogenApplied and environmental microbiology · 2025Article
- Bathochromic Shift via C=O to C=S Substitution: A Far-Red Fluorogen for Multiplexed FLIM with FAST Fluorogen-Activating Protein.International journal of molecular sciences · 2025Article
- Human MX1 orchestrates the cytoplasmic sequestration of neosynthesized influenza A virus vRNPs.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Fluorescence Lifetime-Based Separation of FAST-Labeled Cellular Compartment.Bio-protocol · 2025Article
- Key challenges and recommendations for defining organelle membrane contact sites.Nature reviews. Molecular cell biology · 2025Review
- Decoding Molecular Network Dynamics in Cells: Advances in Multiplexed Live Imaging of Fluorescent Biosensors.Biosensors · 2025Review
- Design and evaluation of a tripartite chemogenetic fluorescent reporter for visualizing ternary protein complexes.Nature communications · 2025Article
- Protein Engineering for Spatiotemporally Resolved Cellular Monitoring.Annual review of analytical chemistry (Palo Alto, Calif.) · 2025Review
- Fluorescence Lifetime Multiplexing with Fluorogen-Activating FAST Protein Variants and Red-Shifted Arylidene-Imidazolone Derivative as Fluorogen.Biosensors · 2025Article
- A tunable and versatile chemogenetic near-infrared fluorescent reporter.Nature communications · 2025Article
- Deletion of atypical type II restriction genes in Clostridium cellulovorans using a Cas9-based gene editing system.Applied microbiology and biotechnology · 2025Article
72 more citing papers are in PubMed but not listed here.
Corrections and comments
- Erratum issued
Authors and funding
20 authors at 8 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
This paper presents Yellow Fluorescence-Activating and absorption-Shifting Tag (Y-FAST), a small monomeric protein tag, half as large as the green fluorescent protein, enabling fluorescent labeling of proteins in a reversible and specific manner through the reversible binding and activation of a cell-permeant and nontoxic fluorogenic ligand (a so-called fluorogen). A unique fluorogen activation mechanism based on two spectroscopic changes, increase of fluorescence quantum yield and absorption red shift, provides high labeling selectivity. Y-FAST was engineered from the 14-kDa photoactive yellow protein by directed evolution using yeast display and fluorescence-activated cell sorting. Y-FAST is as bright as common fluorescent proteins, exhibits good photostability, and allows the efficient labeling of proteins in various organelles and hosts. Upon fluorogen binding, fluorescence appears instantaneously, allowing monitoring of rapid processes in near real time. Y-FAST distinguishes itself from other tagging systems because the fluorogen binding is highly dynamic and fully reversible, which enables rapid labeling and unlabeling of proteins by addition and withdrawal of the fluorogen, opening new exciting prospects for the development of multiplexing imaging protocols based on sequential labeling.
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Registered trials
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 OpenQuestion graph.