ArticleScientific reports2019
Advanced FRET normalization allows quantitative analysis of protein interactions including stoichiometries and relative affinities in living cells.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- The NF-κB Isoform p65 iso5 Is Associated with Distinct Transcriptional Programs and Signaling Pathways.Cells · 2026Article
- Quantitative FRET FLIM imaging reveals multiple interactions between proteins of the ESYT, ORP, and VAP families at the endoplasmic reticulum membrane.The Journal of biological chemistry · 2026Article
- Unravelling molecular dynamics in living cells: Fluorescent protein biosensors for cell biology.Journal of microscopy · 2025Review
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- PKCϵ-mediated phosphorylation of TRPC3 channel at S712 is essential for its inactivation during inflammatory signaling.Frontiers in immunology · 2025Article
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- Far-Red Fluorescent Proteins: Tools for Advancing In Vivo Imaging.Biosensors · 2024Review
- Multiplexed imaging for probing RAS-RAF interactions in living cells.Biochimica et biophysica acta. Biomembranes · 2023Article
- Pixel-by-pixel autofluorescence corrected FRET in fluorescence microscopy improves accuracy for samples with spatially varied autofluorescence to signal ratio.Scientific reports · 2023Article
- Detecting Förster resonance energy transfer in living cells by conventional and spectral flow cytometry.Cytometry. Part A : the journal of the International Society for Analytical Cytology · 2022Article
- Pathological structural conversion of α-synuclein at the mitochondria induces neuronal toxicity.Nature neuroscience · 2022Article
- The TH1 cell lineage-determining transcription factor T-bet suppresses TH2 gene expression by redistributing GATA3 away from TH2 genes.Nucleic acids research · 2022Article
- Large scale, single-cell FRET-based glucose uptake measurements within heterogeneous populations.iScience · 2022Article
- Flow cytometry based-FRET: basics, novel developments and future perspectives.Cellular and molecular life sciences : CMLS · 2022Review
- Rac Inhibition Causes Impaired GPVI Signalling in Human Platelets through GPVI Shedding and Reduction in PLCγ2 Phosphorylation.International journal of molecular sciences · 2022Article
- Ultrabright Pdots with a Large Absorbance Cross Section and High Quantum Yield.ACS applied materials & interfaces · 2022Article
- Studying the interaction between PEX5 and its full-length cargo proteins in living cells by a novel Försteŕs resonance energy transfer-based competition assay.Frontiers in cell and developmental biology · 2022Article
- Biomedical Applications of Quantum Dots: Overview, Challenges, and Clinical Potential.International journal of nanomedicine · 2022Review
- The inflammatory kinase IKKα phosphorylates and stabilizes c-Myc and enhances its activity.Molecular cancer · 2021Article
- Probing ion channel macromolecular interactions using fluorescence resonance energy transfer.Methods in enzymology · 2021Article
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4 authors.
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Abstract
FRET (Fluorescence Resonance Energy Transfer) measurements are commonly applied to proof protein-protein interactions. However, standard methods of live cell FRET microscopy and signal normalization only allow a principle assessment of mutual binding and are unable to deduce quantitative information of the interaction. We present an evaluation and normalization procedure for 3-filter FRET measurements, which reflects the process of complex formation by plotting FRET-saturation curves. The advantage of this approach relative to traditional signal normalizations is demonstrated by mathematical simulations. Thereby, we also identify the contribution of critical parameters such as the total amount of donor and acceptor molecules and their molar ratio. When combined with a fitting procedure, this normalization facilitates the extraction of key properties of protein complexes such as the interaction stoichiometry or the apparent affinity of the binding partners. Finally, the feasibility of our method is verified by investigating three exemplary protein complexes. Altogether, our approach offers a novel method for a quantitative analysis of protein interactions by 3-filter FRET microscopy, as well as flow cytometry. To facilitate the application of this method, we created macros and routines for the programs ImageJ, R and MS-Excel, which we make publicly available.
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