ArticlePloS one2013
N-way FRET microscopy of multiple protein-protein interactions in live cells.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 46 citations in OpenAlex.
- TFAM promotes mitochondrial division by increasing mitochondrial Sirt3.Cell death & disease · 2026Article
- Unravelling molecular dynamics in living cells: Fluorescent protein biosensors for cell biology.Journal of microscopy · 2025Review
- Three-Fluorophore FRET Enables the Analysis of Ternary Protein Association in Living Plant Cells.Plants (Basel, Switzerland) · 2022Article
- Isolation of Lipid Rafts by the Detergent-Based and Non-detergent-Based Methods for Localization of GPCRs with Immunoblotting and Laser Scanning Confocal Microscopy.Methods in molecular biology (Clifton, N.J.) · 2021Article
- A Combined Acceptor Photobleaching and Donor Fluorescence Lifetime Imaging Microscopy Approach to Analyze Multi-Protein Interactions in Living Cells.Frontiers in molecular biosciences · 2021Article
- Profiling Cell Signaling Networks at Single-cell Resolution.Molecular & cellular proteomics : MCP · 2020Review
- FRETting about the affinity of bimolecular protein-protein interactions.Protein science : a publication of the Protein Society · 2018Article
- Optimal fluorescent protein tags for quantifying protein oligomerization in living cells.Scientific reports · 2018Article
- SensorFRET: A Standardless Approach to Measuring Pixel-based Spectral Bleed-through and FRET Efficiency using Spectral Imaging.Scientific reports · 2017Article
- RNA Polymerase Tags To Monitor Multidimensional Protein-Protein Interactions Reveal Pharmacological Engagement of Bcl-2 Proteins.Journal of the American Chemical Society · 2017Article
- Optical sensors to gain mechanistic insights into signaling assemblies.Current opinion in structural biology · 2016Review
- A Guide to Fluorescent Protein FRET Pairs.Sensors (Basel, Switzerland) · 2016Review
- Wide-field microscopic FRET imaging using simultaneous spectral unmixing of excitation and emission spectra.Optics express · 2016Article
- Measurements of absolute concentrations of NADH in cells using the phasor FLIM method.Biomedical optics express · 2016Article
- Three-Dimensional Reconstruction of Three-Way FRET Microscopy Improves Imaging of Multiple Protein-Protein Interactions.PloS one · 2016Article
- Optimizing fluorescent protein trios for 3-Way FRET imaging of protein interactions in living cells.Scientific reports · 2015Article
- Pulse-shaping based two-photon FRET stoichiometry.Optics express · 2015Article
- Delivery of CSF-1R to the lumen of macropinosomes promotes its destruction in macrophages.Journal of cell science · 2014Article
- Determining protein complex structures based on a Bayesian model of in vivo Förster resonance energy transfer (FRET) data.Molecular & cellular proteomics : MCP · 2014Article
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Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
Fluorescence Resonance Energy Transfer (FRET) microscopy has emerged as a powerful tool to visualize nanoscale protein-protein interactions while capturing their microscale organization and millisecond dynamics. Recently, FRET microscopy was extended to imaging of multiple donor-acceptor pairs, thereby enabling visualization of multiple biochemical events within a single living cell. These methods require numerous equations that must be defined on a case-by-case basis. Here, we present a universal multispectral microscopy method (N-Way FRET) to enable quantitative imaging for any number of interacting and non-interacting FRET pairs. This approach redefines linear unmixing to incorporate the excitation and emission couplings created by FRET, which cannot be accounted for in conventional linear unmixing. Experiments on a three-fluorophore system using blue, yellow and red fluorescent proteins validate the method in living cells. In addition, we propose a simple linear algebra scheme for error propagation from input data to estimate the uncertainty in the computed FRET images. We demonstrate the strength of this approach by monitoring the oligomerization of three FP-tagged HIV Gag proteins whose tight association in the viral capsid is readily observed. Replacement of one FP-Gag molecule with a lipid raft-targeted FP allowed direct observation of Gag oligomerization with no association between FP-Gag and raft-targeted FP. The N-Way FRET method provides a new toolbox for capturing multiple molecular processes with high spatial and temporal resolution in living cells.
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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.