ArticleJournal of microscopy2007
Characterization of spectral FRET imaging microscopy for monitoring nuclear protein interactions.
Article in Journal of microscopy, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 82 citations in OpenAlex.
- Unravelling molecular dynamics in living cells: Fluorescent protein biosensors for cell biology.Journal of microscopy · 2025Review
- Clustering of phosphatase RPTPα promotes Src signaling and the arthritogenic action of synovial fibroblasts.Science signaling · 2023Article
- A FRET-based respirasome assembly screen identifies spleen tyrosine kinase as a target to improve muscle mitochondrial respiration and exercise performance in mice.Nature communications · 2023Article
- Measurement of 3-Dimensional cAMP Distributions in Living Cells using 4-Dimensional (x, y, z, and λ) Hyperspectral FRET Imaging and Analysis.Journal of visualized experiments : JoVE · 2020Article
- New Techniques to Study Intracellular Receptors in Living Cells: Insights Into RIG-I-Like Receptor Signaling.Advances in experimental medicine and biology · 2019Review
- SensorFRET: A Standardless Approach to Measuring Pixel-based Spectral Bleed-through and FRET Efficiency using Spectral Imaging.Scientific reports · 2017Article
- A Protocol for Using Förster Resonance Energy Transfer (FRET)-force Biosensors to Measure Mechanical Forces across the Nuclear LINC Complex.Journal of visualized experiments : JoVE · 2017Article
- Quantifying macromolecular interactions in living cells using FRET two-hybrid assays.Nature protocols · 2016Article
- Wide-field microscopic FRET imaging using simultaneous spectral unmixing of excitation and emission spectra.Optics express · 2016Article
- Nesprin-2G, a Component of the Nuclear LINC Complex, Is Subject to Myosin-Dependent Tension.Biophysical journal · 2016Article
- Article
- Understanding FRET as a research tool for cellular studies.International journal of molecular sciences · 2015Review
- Progressive accumulation of activated ERK2 within highly stable ORF45-containing nuclear complexes promotes lytic gammaherpesvirus infection.PLoS pathogens · 2014Article
- Automated selection of regions of interest for intensity-based FRET analysis of transferrin endocytic trafficking in normal vs. cancer cells.Methods (San Diego, Calif.) · 2014Article
- FRET spectrometry: a new tool for the determination of protein quaternary structure in living cells.Biophysical journal · 2013Article
- Quantification of Förster resonance energy transfer by monitoring sensitized emission in living plant cells.Frontiers in plant science · 2013Review
- Assessing FRET using spectral techniques.Cytometry. Part A : the journal of the International Society for Analytical Cytology · 2013Article
- Förster resonance energy transfer microscopy and spectroscopy for localizing protein-protein interactions in living cells.Cytometry. Part A : the journal of the International Society for Analytical Cytology · 2013Review
- Fluorescence resonance energy transfer microscopy as demonstrated by measuring the activation of the serine/threonine kinase Akt.Nature protocols · 2013Article
- Förster resonance energy transfer photoacoustic microscopy.Journal of biomedical optics · 2012Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The spectral processed Förster resonance energy transfer (psFRET) imaging method provides an effective and fast method for measuring protein-protein interactions in living specimens. The commercially available linear unmixing algorithms efficiently remove the contribution of donor spectral bleedthrough to the FRET signal. However, the acceptor contribution to spectral bleedthrough in the FRET image cannot be similarly removed, since the acceptor spectrum is identical to the FRET spectrum. Here, we describe the development of a computer algorithm that measures and removes the contaminating ASBT signal in the sFRET image. The new method is characterized in living cells that expressed FRET standards in which the donor and acceptor fluorescent proteins are tethered by amino acid linkers of specific lengths. The method is then used to detect the homo-dimerization of a transcription factor in the nucleus of living cells, and then to measure the interactions of that protein with a second transcription factor.
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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.