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FRET microscopy in the living cell: Different approaches, strengths and weaknesses.

Abstract : New imaging methodologies in quantitative fluorescence microscopy, such as Förster resonance energy transfer (FRET), have been developed in the last few years and are beginning to be extensively applied to biological problems. FRET is employed for the detection and quantification of protein interactions, and of biochemical activities. Herein, we review the different methods to measure FRET in microscopy, and more importantly, their strengths and weaknesses. In our opinion, fluorescence lifetime imaging microscopy (FLIM) is advantageous for detecting inter-molecular interactions quantitatively, the intensity ratio approach representing a valid and straightforward option for detecting intra-molecular FRET. Promising approaches in single molecule techniques and data analysis for quantitative and fast spatio-temporal protein-protein interaction studies open new avenues for FRET in biological research.
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Contributor : Hervé De Villemeur Connect in order to contact the contributor
Submitted on : Wednesday, March 28, 2012 - 1:58:18 PM
Last modification on : Tuesday, March 29, 2022 - 10:33:01 AM

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Sergi Padilla-Parra, Marc Tramier. FRET microscopy in the living cell: Different approaches, strengths and weaknesses.. BioEssays, Wiley-VCH Verlag, 2012, 34 (5), pp.369-376. ⟨10.1002/bies.201100086⟩. ⟨inserm-00683306⟩



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