ReviewBiophysical journal2012
Quantitative intensity-based FRET approaches--a comparative snapshot.
Review in Biophysical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 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
55 citing papers in PubMed.
- Automated FLIM-FRET Segmentation Within RNP Condensates.Bio-protocol · 2026Article
- From Population Averaging to Single Event Resolution: Evolution of Sensing Platforms for Membrane Fusion.Sensors (Basel, Switzerland) · 2026Review
- Cell-cell communication: new insights and clinical implications.Signal transduction and targeted therapy · 2024Review
- Lattice matching enables construction of CaS@NaYFMikrochimica acta · 2024Article
- Assessment of the FRET-based Teen sensor to monitor ERK activation changes preceding morphological defects in a RASopathy zebrafish model and phenotypic rescue by MEK inhibitor.Molecular medicine (Cambridge, Mass.) · 2024Article
- Dimerization of iLID optogenetic proteins observed using 3D single-molecule tracking in live E. coli.Biophysical journal · 2023Article
- One pattern analysis (OPA) for the quantitative determination of protein interactions in plant cells.Plant methods · 2023Article
- In vivo quantitative FRET small animal imaging: Intensity versus lifetime-based FRET.Biophysical reports · 2023Article
- Article
- Optimal inference of molecular interaction dynamics in FRET microscopy.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Spectrally Resolved FRET Microscopy of α-Synuclein Phase-Separated Liquid Droplets.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Single-photon smFRET. III. Application to pulsed illumination.Biophysical reports · 2022Article
- Determination of FRET orientation factor between artificial fluorophore and photosynthetic light-harvesting 2 complex (LH2).Scientific reports · 2022Article
- Interaction of human CRX and NRL in live HEK293T cells measured using fluorescence resonance energy transfer (FRET).Scientific reports · 2022Article
- Oligomerization of yeast α-factor receptor detected by fluorescent energy transfer between ligands.Biophysical journal · 2021Article
- Single-Molecular Förster Resonance Energy Transfer Measurement on Structures and Interactions of Biomolecules.Micromachines · 2021Review
- Simultaneous readout of multiple FRET pairs using photochromism.Nature communications · 2021Article
- Direct measurement of protein-protein interactions by FLIM-FRET at UV laser-induced DNA damage sites in living cells.Nucleic acids research · 2020Article
- Bacterial Vivisection: How Fluorescence-Based Imaging Techniques Shed a Light on the Inner Workings of Bacteria.Microbiology and molecular biology reviews : MMBR · 2020Review
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Förster resonance energy transfer (FRET) has become an important tool for analyzing different aspects of interactions among biological macromolecules in their native environments. FRET analysis has also been successfully applied to study the spatiotemporal regulation of various cellular processes using genetically encoded FRET-based biosensors. A variety of procedures have been described for measuring FRET efficiency or the relative abundance of donor-acceptor complexes, based on analysis of the donor fluorescence lifetime or the spectrally resolved fluorescence intensity. The latter methods are preferable if one wants to not only quantify the apparent FRET efficiencies but also calculate donor-acceptor stoichiometry and observe fast dynamic changes in the interactions among donor and acceptor molecules in live cells. This review focuses on a comparison of the available intensity-based approaches used to measure FRET. We discuss their strengths and weaknesses in terms of FRET quantification, and provide several examples of biological applications.
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.