ArticleScientific reports2015
A dark green fluorescent protein as an acceptor for measurement of Förster resonance energy transfer.
Article in Scientific reports, 2015. 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 38 papers.
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Who cites it
38 citing papers in PubMed, 56 citations in OpenAlex.
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- Development of three-colour FRET cascade for force sensing of the putative RIAM-vinculin interaction in fibroblasts.Communications chemistry · 2025Article
- Optogenetic actin network assembly on lipid bilayer uncovers the network density-dependent functions of actin-binding proteins.Nature communications · 2025Article
- A fluorescence lifetime-based FLIM-timer for measuring the protein turnover of transcription factor Nrf2 in live cells.Scientific reports · 2025Article
- Molecular Spies in Action: Genetically Encoded Fluorescent Biosensors Light up Cellular Signals.Chemical reviews · 2024Review
- Next-Generation Genetically Encoded Fluorescent Biosensors Illuminate Cell Signaling and Metabolism.Annual review of biophysics · 2024Review
- A chemical solution for FRET(ful) pairs.Nature chemical biology · 2023Article
- A general method for the development of multicolor biosensors with large dynamic ranges.Nature chemical biology · 2023Article
- Structure-based analysis and evolution of a monomerized red-colored chromoprotein from the Olindias formosa jellyfish.Protein science : a publication of the Protein Society · 2022Article
- Article
- Engineering of a fluorescent chemogenetic reporter with tunable color for advanced live-cell imaging.Nature communications · 2021Article
- Quantification of FRET-induced angular displacement by monitoring sensitized acceptor anisotropy using a dim fluorescent donor.Nature communications · 2021Article
- Photoactivatable CaMKII induces synaptic plasticity in single synapses.Nature communications · 2021Article
- Optogenetic Imaging of Protein Activity Using Two-Photon Fluorescence Lifetime Imaging Microscopy.Advances in experimental medicine and biology · 2021Review
- Tension Sensor Based on Fluorescence Resonance Energy Transfer Reveals Fiber Diameter-Dependent Mechanical Factors During Myelination.Frontiers in cellular neuroscience · 2021Article
- Strategies for Multiplexed Biosensor Imaging to Study Intracellular Signaling Networks.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Absolute quantum yield measurements of fluorescent proteins using a plasmonic nanocavity.Communications biology · 2020Article
- Fluorescent Biosensors for Neuronal Metabolism and the Challenges of Quantitation.Current opinion in neurobiology · 2020Review
- Fluorescence lifetime imaging microscopy: fundamentals and advances in instrumentation, analysis, and applications.Journal of biomedical optics · 2020Review
Corrections and comments
- Erratum issued
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Measurement of Förster resonance energy transfer by fluorescence lifetime imaging microscopy (FLIM-FRET) is a powerful method for visualization of intracellular signaling activities such as protein-protein interactions and conformational changes of proteins. Here, we developed a dark green fluorescent protein (ShadowG) that can serve as an acceptor for FLIM-FRET. ShadowG is spectrally similar to monomeric enhanced green fluorescent protein (mEGFP) and has a 120-fold smaller quantum yield. When FRET from mEGFP to ShadowG was measured using an mEGFP-ShadowG tandem construct with 2-photon FLIM-FRET, we observed a strong FRET signal with low cell-to-cell variability. Furthermore, ShadowG was applied to a single-molecule FRET sensor to monitor a conformational change of CaMKII and of the light oxygen voltage (LOV) domain in HeLa cells. These sensors showed reduced cell-to-cell variability of both the basal fluorescence lifetime and response signal. In contrast to mCherry- or dark-YFP-based sensors, our sensor allowed for precise measurement of individual cell responses. When ShadowG was applied to a separate-type Ras FRET sensor, it showed a greater response signal than did the mCherry-based sensor. Furthermore, Ras activation and translocation of its effector ERK2 into the nucleus could be observed simultaneously. Thus, ShadowG is a promising FLIM-FRET acceptor.
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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 OpenQuestion graph.