ArticleEuropean biophysics journal : EBJ2010
Time-resolved FRET fluorescence spectroscopy of visible fluorescent protein pairs.
Article in European biophysics journal : EBJ, 2010. 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 14 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
14 citing papers in PubMed, 52 citations in OpenAlex.
- Ubiquitination detection techniques.Experimental biology and medicine (Maywood, N.J.) · 2023Review
- Key interactions with deazariboflavin cofactor for light-driven energy transfer in Xenopus (6-4) photolyase.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2021Article
- A Bright and Colorful Future for G-Protein Coupled Receptor Sensors.Frontiers in cellular neuroscience · 2020Article
- Investigating State Restriction in Fluorescent Protein FRET Using Time-Resolved Fluorescence and Anisotropy.The journal of physical chemistry. C, Nanomaterials and interfaces · 2017Article
- Determining protein complex structures based on a Bayesian model of in vivo Förster resonance energy transfer (FRET) data.Molecular & cellular proteomics : MCP · 2014Article
- Parallel excitation-emission multiplexed fluorescence lifetime confocal microscopy for live cell imaging.Optics express · 2014Article
- Application of phasor plot and autofluorescence correction for study of heterogeneous cell population.Journal of biomedical optics · 2014Article
- FRET-FLIM applications in plant systems.Protoplasma · 2014Review
- 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
- Article
- Membrane environment exerts an important influence on rac-mediated activation of phospholipase Cγ2.Molecular and cellular biology · 2011Article
- FLIM FRET technology for drug discovery: automated multiwell-plate high-content analysis, multiplexed readouts and application in situ.Chemphyschem : a European journal of chemical physics and physical chemistry · 2011Article
- Wide-Field Multi-Parameter FLIM: long-term minimal invasive observation of proteins in living cells.PloS one · 2011Article
- Genetically encoded probes for measurement of intracellular calcium.Methods in cell biology · 2010Article
Corrections and comments
- Erratum issued
Authors and funding
7 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Förster resonance energy transfer (FRET) is a powerful method for obtaining information about small-scale lengths between biomacromolecules. Visible fluorescent proteins (VFPs) are widely used as spectrally different FRET pairs, where one VFP acts as a donor and another VFP as an acceptor. The VFPs are usually fused to the proteins of interest, and this fusion product is genetically encoded in cells. FRET between VFPs can be determined by analysis of either the fluorescence decay properties of the donor molecule or the rise time of acceptor fluorescence. Time-resolved fluorescence spectroscopy is the technique of choice to perform these measurements. FRET can be measured not only in solution, but also in living cells by the technique of fluorescence lifetime imaging microscopy (FLIM), where fluorescence lifetimes are determined with the spatial resolution of an optical microscope. Here we focus attention on time-resolved fluorescence spectroscopy of purified, selected VFPs (both single VFPs and FRET pairs of VFPs) in cuvette-type experiments. For quantitative interpretation of FRET-FLIM experiments in cellular systems, details of the molecular fluorescence are needed that can be obtained from experiments with isolated VFPs. For analysis of the time-resolved fluorescence experiments of VFPs, we have utilised the maximum entropy method procedure to obtain a distribution of fluorescence lifetimes. Distributed lifetime patterns turn out to have diagnostic value, for instance, in observing populations of VFP pairs that are FRET-inactive.
Indexed as
Identifiers
What OpenQuestion holds
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.