FRET & FRAP

 

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• Van der Krogt, et al. (2008). A Comparison of Donor-Acceptor Pairs for Genetically Encoded FRET Sensors: Application to the Epac cAMP Sensor as an Example. PloS ONE. 3, e1916.
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• Periasamy, et al. (2008). Chapter 22 Quantitation of Protein–Protein Interactions: Confocal FRET Microscopy. Methods in Cell Biology. 89, 569-598.
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• Weinthal and Tzfira. (2009). Imaging protein–protein interactions in plant cells by bimolecular fluorescence complementation assay. Trends in Plant Science. 14, 59-63.
• Shcherbo, et al. (2009). Practical and reliable FRET/FLIM pair of fluorescent proteins. BMC Biotechnol. 9: 24.
• Kang, et al. (2009). A Generalization of Theory for Two-Dimensional Fluorescence Recovery after Photobleaching Applicable to Confocal Laser Scanning Microscopes. Biophysical Journal. 97, 1501-1511.
• Padilla-Parra, et al. (2009). In The Quest Of The Best Fluorescent Protein Couple For Quantitative FRET-FLIM. Biophysical Journal. 96, 403a.
• Padilla-Parra, et al. (2009). Quantitative Comparison of Different Fluorescent Protein Couples for Fast FRET-FLIM Acquisition. Biophysical Journal. 97. 2368-2376.
• Brzostowski, et al. (2009). Imaging Protein-Protein Interactions by Förster Resonance Energy Transfer (FRET) Microscopy in Live Cells. Current Protocols in Protein Science. UNIT 19.5
• Nakamura and Matsuda. (2009). In Vivo Imaging of Signal Transduction Cascades with Probes Based on Förster Resonance Energy Transfer (FRET). Current Protocols in Cell Biol. Unit 14.10.
• Trembecka, et al. (2010). Conditions for using FRAP as a quantitative technique – Influence of the bleaching protocol. Cytometry. Part A. 77A, 366 – 370.
• Mueller, et al. (2010). FRAP and kinetic modeling in the analysis of nuclear protein dynamics: what do we really know?. Current Opinion in Cell Biology. 22, 403-411.
• C. Depry and J. Zhang (2010). Visualization of Kinase Activity with FRET-Based Activity Biosensors. Current Protocols in Molecular Biology UNIT 18.15.
• Yuansheng, et al. (2010). FRET microscopy in 2010: The legacy of Theodor Förster in the 100th Anninversary of his birth. ChemPhysChem. doi: 10.1002/cphc.201000664.
• Hernán, et al. (2010). FRET in Cell Biology: Still shining in the age of super-resolution? ChemPhysChem. doi: 10.1002/cphc.201000795.
• Pietraszewska-Bogiel and Gadella. (2010). FRET microscopy: from principle to routine technology in cell biology. J. Microscopy. 241, 111-118.
• Ishikawa-Ankerhold. (2012). Advanced Fluorescence Microscopy Techniques-FRAP, FLIP, FLAP, FRET and FLIM. Molecules. 17, 4047-4132.
• Mueller, et al. (2012). Minimizing the impact of photoswitching of fluorescent proteins on FRAP analysis. Biophys. J. 102, 1656-1665.
• Seits, et al. (2012). Quatifying the influence of yellow fluorescent photoconversion on acceptor photobleaching-based fluorescence energy transfer measurements. Biomd. Opt. 17, 011010.
• W. Becker. (2012). Fluorescence lifetime imaging- techniques and applications. J. Microscopy. 247, 119-136.
• Kodama and Hu. (2012). Bimolecular Fluorescence Complementation (BiFC): A 5-year update and future prespectives. Biotechniques. 53, 285-298.
• Broussard, et al. (2013). Fluorescence resonance energy transfer microscopy as demonstrated by measuring the activation of the serine/threonine kinase Akt. Nature Protocols. 8, 265-281.
• Grecco and Bastiaens. (2013). Quantifying cellular dynamics by Fluorescence Resonance Energy Transfer (FRET) microscopy. Curr. Protocol. Neurosci. 5.22.1-5.22.14.
• Kemp-O´Brien and Parsons. (2013), Using FRET to analyse signals controlling cell adhesion and migration. Journal of Microscopy, 251: 270–278.
• Grünberg, et all. (2013). Engineering of weak helper interactions for high-efficiency FRET probes. Nature Methods. 10, 1021-1027.
• Joosen ,et al. (2014). Effects of fixation procedures on the fluorescence lifetimesof Aequorea victoria derived fluorescent protein. J. Microscopy. 256, 166-176.
• Lorén, et al. (2015). Fluorescence recovery after photobleaching in material and life sciences: putting theory into practice. Quarterly Reviews of Biophysics. 48, 323-387.