ArticleMethods (San Diego, Calif.)2014
Measuring protein interactions using Förster resonance energy transfer and fluorescence lifetime imaging microscopy.
Article in Methods (San Diego, Calif.), 2014. 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.
- Article
- Identification of Plant Chromatin Interaction Networks Using IP-MS and co-IP.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Chemical and Biological Strategies for Profiling Protein-Protein Interactions in Living Cells.Chemistry, an Asian journal · 2023Review
- Clustering of phosphatase RPTPα promotes Src signaling and the arthritogenic action of synovial fibroblasts.Science signaling · 2023Article
- SPLIT-PIN software enabling confocal and super-resolution imaging with a virtually closed pinhole.Scientific reports · 2023Article
- FLUTE: A Python GUI for interactive phasor analysis of FLIM data.Biological imaging · 2023Article
- A phasor-based approach to improve optical sectioning in any confocal microscope with a tunable pinhole.Microscopy research and technique · 2022Article
- Efficacy and specificity of inhibitors of BCL-2 family protein interactions assessed by affinity measurements in live cells.Science advances · 2022Article
- Imaging developmental cell cycles.Biophysical journal · 2021Review
- Direct visualization by FRET-FLIM of a putative mechanosome complex involving Src, Pyk2 and MBD2 in living MLO-Y4 cells.PloS one · 2021Article
- Article
- PIE-FLIM Measurements of Two Different FRET-Based Biosensor Activities in the Same Living Cells.Biophysical journal · 2020Article
- FRET efficiency measurement in a molecular tension probe with a low-cost frequency-domain fluorescence lifetime imaging microscope.Journal of biomedical optics · 2019Article
- Phasor histone FLIM-FRET microscopy quantifies spatiotemporal rearrangement of chromatin architecture during the DNA damage response.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Structural mapping of fluorescently-tagged, functional nhTMEM16 scramblase in a lipid bilayer.The Journal of biological chemistry · 2018Article
- Advanced Confocal Microscopy Techniques to Study Protein-protein Interactions and Kinetics at DNA Lesions.Journal of visualized experiments : JoVE · 2017Article
- Intravital microscopy of biosensor activities and intrinsic metabolic states.Methods (San Diego, Calif.) · 2017Article
- A simple approach for measuring FRET in fluorescent biosensors using two-photon microscopy.Nature protocols · 2016Article
- Screening for protein-protein interactions using Förster resonance energy transfer (FRET) and fluorescence lifetime imaging microscopy (FLIM).Scientific reports · 2016Article
- A practical method for monitoring FRET-based biosensors in living animals using two-photon microscopy.American journal of physiology. Cell physiology · 2015Review
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
Abstract
The method of fluorescence lifetime imaging microscopy (FLIM) is a quantitative approach that can be used to detect Förster resonance energy transfer (FRET). The use of FLIM to measure the FRET that results from the interactions between proteins labeled with fluorescent proteins (FPs) inside living cells provides a non-invasive method for mapping interactomes. Here, the use of the phasor plot method to analyze frequency domain (FD) FLIM measurements is described, and measurements obtained from cells producing the 'FRET standard' fusion proteins are used to validate the FLIM system for FRET measurements. The FLIM FRET approach is then used to measure both homologous and heterologous protein-protein interactions (PPI) involving the CCAAT/enhancer-binding protein alpha (C/EBPα). C/EBPα is a transcription factor that controls cell differentiation, and localizes to heterochromatin where it interacts with the heterochromatin protein 1 alpha (HP1α). The FLIM-FRET method is used to quantify the homologous interactions between the FP-labeled basic leucine zipper (BZip) domain of C/EBPα. Then the heterologous interactions between the C/EBPa BZip domain and HP1a are quantified using the FRET-FLIM method. The results demonstrate that the basic region and leucine zipper (BZip) domain of C/EBPα is sufficient for the interaction with HP1α in regions of heterochromatin.
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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.