ReviewBiophysical reviews2011
Non fitting based FRET-FLIM analysis approaches applied to quantify protein-protein interactions in live cells.
Review in Biophysical reviews, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 34 citations in OpenAlex.
- Fluorescence Lifetime Imaging Application to Probe GTPase Activation in Macrophage Cell Line, Using the Time-Domain FastFLIM Modality.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Rapid Acquisition of High-Pixel Fluorescence Lifetime Images of Living Cells via Image Reconstruction Based on Edge-Preserving Interpolation.Biosensors · 2025Article
- Multicolor lifetime imaging and its application to HIV-1 uptake.Nature communications · 2023Article
- Structure dynamics of HIV-1 Env trimers on native virions engaged with living T cells.Communications biology · 2021Article
- Review
- Quantitative real-time imaging of intracellular FRET biosensor dynamics using rapid multi-beam confocal FLIM.Scientific reports · 2020Article
- Wide-field time-gated SPAD imager for phasor-based FLIM applications.Methods and applications in fluorescence · 2020Article
- In vitro and in vivo phasor analysis of stoichiometry and pharmacokinetics using short-lifetime near-infrared dyes and time-gated imaging.Journal of biophotonics · 2019Article
- Article
- FLIM-FRET for Cancer Applications.Current molecular imagingArticle
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
New imaging methodologies in quantitative fluorescence microscopy and nanoscopy have been developed in the last few years and are beginning to be extensively applied to biological problems, such as the localization and quantification of protein interactions. Fluorescence resonance energy transfer (FRET) detected by fluorescence lifetime imaging microscopy (FLIM) is currently employed not only in biophysics or chemistry but also in bio-medicine, thanks to new advancements in technology and also new developments in data treatment. FRET-FLIM can be a very useful tool to ascertain protein interactions occurring in single living cells. In this review, we stress the importance of increasing the acquisition speed when working in vivo employing Time-Domain FLIM. The development of the new mathematical-based non-fitting methods allows the determining of the fraction of interacting donor without the requirement of high count statistics, and thus allows the performing of high speed acquisitions in FRET-FLIM to still be quantitative.
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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.