ArticleScientific reports2016
Screening for protein-protein interactions using Förster resonance energy transfer (FRET) and fluorescence lifetime imaging microscopy (FLIM).
Article in Scientific reports, 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 56 papers.
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Who cites it
56 citing papers in PubMed.
- Emerging trends of fluorescence lifetime imaging microscopy (FLIM): advances, challenges, and prospects.Biophysics reports · 2026Article
- Multi-parameter fluorescence lifetime imaging for high-noise neuroscience applications.Biomedical optics express · 2026Article
- Integrating Molecular Dynamics Simulations and Single-molecule FRET Spectroscopy: From Computational FRET Estimation to Experimental Data Interpretation.The journal of physical chemistry. B · 2026Review
- Expanding the multiplexing capability of HIDE probes via fluorescence lifetime imaging microscopy.Methods in enzymology · 2026Article
- Label-free protein-structure-sensitive live-cell microscopy for patient-specific assessment of myeloma therapy.Nature biomedical engineering · 2026Article
- Fluorescence Lifetime Microscopy Methods for Studying Dynamics of Fluorescent Proteins In Vivo and In Vitro.Advances in experimental medicine and biology · 2026Review
- Fast volumetric fluorescence lifetime imaging of multicellular systems using single-objective light-sheet microscopy.Communications biology · 2025Article
- Engineering a new tripartite split-ccGFP system from Corynactis californica for detecting protein-protein interactions.Scientific reports · 2025Article
- Loss of SPRED3 Causes Primary Hypothyroidism and Alters Thyroidal Expression of Autophagy Regulators LC3, p62, and ATG5 in Mice.International journal of molecular sciences · 2025Article
- Practical guide to fluorescence lifetime imaging microscopy.Molecular biology of the cell · 2025Review
- Calibration approaches for fluorescence lifetime applications using time-domain measurements.Methods in microscopy · 2025Article
- Enabling simultaneous photoluminescence spectroscopy and X-ray footprinting mass spectrometry to study protein conformation and interactions.Analytical methods : advancing methods and applications · 2025Article
- Ranking Single Fluorescent Protein-Based Calcium Biosensor Performance by Molecular Dynamics Simulations.Journal of chemical information and modeling · 2025Article
- Bax- Bcl-xL interaction dynamics during the progression of cell cycle and cell death using FLIM-FRET.Cell stress · 2025Review
- Therapeutic Applications of Aptamers.International journal of molecular sciences · 2024Review
- Implementation of FRET Spectrometry Using Temporally Resolved Fluorescence: A Feasibility Study.International journal of molecular sciences · 2024Article
- Exploring the dynamics and structure of PpiB in living Escherichia coli cells using electron paramagnetic resonance spectroscopy.Protein science : a publication of the Protein Society · 2024Article
- Cytosolic and mitochondrial translation elongation are coordinated through the molecular chaperone TRAP1 for the synthesis and import of mitochondrial proteins.Genome research · 2023Article
- Bone Marrow Mesenchymal Stem Cells Induce Metabolic Plasticity in Estrogen Receptor-Positive Breast Cancer.Molecular cancer research : MCR · 2023Article
- Crystal Structure of Bright Fluorescent Protein BrUSLEE with Subnanosecond Fluorescence Lifetime; Electric and Dynamic Properties.International journal of molecular sciences · 2023Article
Corrections and comments
- Erratum issued
Authors and funding
9 authors.
Funding
Abstract
We present a high content multiwell plate cell-based assay approach to quantify protein interactions directly in cells using Förster resonance energy transfer (FRET) read out by automated fluorescence lifetime imaging (FLIM). Automated FLIM is implemented using wide-field time-gated detection, typically requiring only 10 s per field of view (FOV). Averaging over biological, thermal and shot noise with 100's to 1000's of FOV enables unbiased quantitative analysis with high statistical power. Plotting average donor lifetime vs. acceptor/donor intensity ratio clearly identifies protein interactions and fitting to double exponential donor decay models provides estimates of interacting population fractions that, with calibrated donor and acceptor fluorescence intensities, can yield dissociation constants. We demonstrate the application to identify binding partners of MST1 kinase and estimate interaction strength among the members of the RASSF protein family, which have important roles in apoptosis via the Hippo signalling pathway. KD values broadly agree with published biochemical measurements.
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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.