Fluorescent protein FRET: the good, the bad and the ugly.

By David W. Piston, G. Kremers. TIBS -Trends in Biochemical Sciences. Regular ed, 2007

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A Guide to Fluorescent Protein FRET Pairs (2016, background): “suffer from the phototoxicity of near-UV excitation, limiting their applications in long-term live cell imaging [4].”
Fluorescent proteins and their applications in imaging living cells and tissues. (2010, methodology): “The measurement of energy transfer efficiency between two FP molecules is currently one of the most commonly used approaches to monitor protein-protein interactions in living cells (343) and is also utilized in genetically encoded sensors (see sect.”
Improving FRET dynamic range with bright green and red fluorescent proteins (2012, neutral): “New FPs that perform well in FRET and avoid the drawbacks of CFPs and YFPs would thus be useful 11,12 .”
Dynamics of proteins in solution (2019, background): “…exhibits a strong distance dependence on the scale of a few nanometers, which allows for high-precision measurements of the distance between labeled sites by measuring the efficiency of the transfer (Deniz et al., 2001; Lippincott-Schwartz et al., 2001; Piston and Kremers, 2007; Roy et al., 2008).”
Intrinsic Tryptophan Fluorescence in the Detection and Analysis of Proteins: A Focus on Förster Resonance Energy Transfer Techniques (2014, background): “This long-range (1–10 nm) dipole-dipole coupling has emerged as a powerful technique to unravel the dynamics of biomolecules [25].”