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Biosensors 2018, 8(4), 89;

Homotransfer FRET Reporters for Live Cell Imaging

Department of Physiology, University of Maryland School of Medicine, 660 W Redwood St/HH525B, Baltimore, MD 21201, USA
Author to whom correspondence should be addressed.
Received: 6 September 2018 / Revised: 27 September 2018 / Accepted: 10 October 2018 / Published: 11 October 2018
(This article belongs to the Special Issue FRET-Based Biosensors)
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Förster resonance energy transfer (FRET) between fluorophores of the same species was recognized in the early to mid-1900s, well before modern heterotransfer applications. Recently, homotransfer FRET principles have re-emerged in biosensors that incorporate genetically encoded fluorescent proteins. Homotransfer offers distinct advantages over the standard heterotransfer FRET method, some of which are related to the use of fluorescence polarization microscopy to quantify FRET between two fluorophores of identical color. These include enhanced signal-to-noise, greater compatibility with other optical sensors and modulators, and new design strategies based upon the clustering or dimerization of singly-labeled sensors. Here, we discuss the theoretical basis for measuring homotransfer using polarization microscopy, procedures for data collection and processing, and we review the existing genetically-encoded homotransfer biosensors. View Full-Text
Keywords: FRET; anisotropy; GFP; fluorescent protein; biosensor; homotransfer FRET; anisotropy; GFP; fluorescent protein; biosensor; homotransfer

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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

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Snell, N.E.; Rao, V.P.; Seckinger, K.M.; Liang, J.; Leser, J.; Mancini, A.E.; Rizzo, M.A. Homotransfer FRET Reporters for Live Cell Imaging. Biosensors 2018, 8, 89.

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