מעבר אנרגיה בתהודה פלואורסצנטית
הערות שוליים

↑  Yuansheng Sun, Horst Wallrabe, Soo-Ah Seo, Ammasi Periasamy, FRET Microscopy in 2010: The Legacy of Theodor Förster on the 100th Anniversary of his Birth, ChemPhysChem 12, 2011-02-25, עמ' 462–474 doi: 10.1002/cphc.201000664
1 2  Clegge R.M., The history of FRET, Geddes, C. D. and Lakowicz, J. R, 2006
↑  Hans Kuhn, Classical Aspects of Energy Transfer in Molecular Systems, The Journal of Chemical Physics 53, 1970-07-01, עמ' 101–108 doi: 10.1063/1.1673749
↑  Jörg Enderlein, Modification of Förster Resonance Energy Transfer Efficiencyat Interfaces, International Journal of Molecular Sciences 13, 2012-11-19, עמ' 15227–15240 doi: 10.3390/ijms131115227
↑  Cristobal G dos Remedios, eLS, John Wiley & Sons, Ltd, 2001. (באנגלית)
1 2  Majoul, Irina; Jia, Yiwei; Duden, Rainer (2006). "Practical Fluorescence Resonance Energy Transfer or Molecular Nanobioscopy of Living Cells". In Pawley, James B. Handbook Of Biological Confocal Microscopy (3rd ed.). New York, NY: Springer. pp. 788–808. ISBN 978-0-387-25921-5. doi:10.1007/978-0-387-45524-2_45.
↑  Meir Cohen-Kashi, Sergey Moshkov, Naomi Zurgil, and Mordechai Deutsch, Fluorescence Resonance Energy Transfers Measurements on Cell Surfaces via Fluorescence Polarization, Biophysical Journal 83, 2002, עמ' 1402–1395
↑  Yitzhak Yishai, Dror Fixler, Meir Cohen-Kashi, Naomi Zurgil and Mordechai Deutsch, Ratiometric fluorescence polarization as a cytometric functional parameter: theory and practice, Phys. Med. Biol 48, 2003, עמ' 2268–2255
1 2  Clegg, Robert (2009). "Förster resonance energy transfer—FRET: what is it, why do it, and how it's done". In Gadella, Theodorus W. J. FRET and FLIM Techniques. Laboratory Techniques in Biochemistry and Molecular Biology, Volume 33. Elsevier. pp. 1–57. ISBN 978-0-08-054958-3. doi:10.1016/S0075-7535(08)00001-6
↑  zöllősi, János; Alexander, Denis R. (2007). "The Application of Fluorescence Resonance Energy Transfer to the Investigation of Phosphatases". In Klumpp, Susanne; Krieglstein, Josef. Protein Phosphatases. Methods in Enzymology, Volume 366. Amsterdam: Elsevier. pp. 203–24. ISBN 978-0-12-182269-9. doi:10.1016/S0076-6879(03)66017-9.
↑  eriasamy, Ammasi (July 2001). "Fluorescence resonance energy transfer microscopy: a mini review". Journal of Biomedical Optics. 6 (3): 287–291. Bibcode:2001JBO.....6..287P. PMID 11516318. doi:10.1117/1.1383063.
↑  guyen, AW; Daugherty, PS (March 2005). "Evolutionary optimization of fluorescent proteins for intracellular FRET.". Nature Biotechnology. 23 (3): 355–60. PMID 15696158. doi:10.1038/nbt1066.
↑  Bevan, Nicola; Rees, Stephen (2006). "Pharmaceutical Applications of GFP and RCFP". In Chalfie, Martin; Kain, Steven R. Green Fluorescent Protein: Properties, Applications and Protocols. Methods of Biochemical Analysis, Volume 47 (2nd ed.). Hoboken, NJ: John Wiley & Sons. pp. 361–90. ISBN 978-0-471-73682-0. doi:10.1002/0471739499.ch16.
↑  Pfleger, Kevin D G; Eidne, Karin A. "Illuminating insights into protein-protein interactions using bioluminescence resonance energy transfer (BRET)". Nature Methods. 3 (3): 165–174. PMID 16489332. doi:10.1038/nmeth841.
↑  Pfleger, Kevin D. G.; Eidne, Karin A. (2005-02-01). "Monitoring the formation of dynamic G-protein-coupled receptor–protein complexes in living cells". Biochemical Journal. 385 (3): 625–637. ISSN 0264-6021. PMC 1134737 . PMID 15504107. doi:10.1042/BJ20041361.
↑  Gautier, I.; Tramier, M.; Durieux, C.; Coppey, J.; Pansu, R.B.; Nicolas, J.-C.; Kemnitz, K.; Coppey-Moisan, M. (2001). "Homo-FRET Microscopy in Living Cells to Measure Monomer-Dimer Transition of GFP-Tagged Proteins". Biophysical Journal. 80 (6): 3000–8. Bibcode:2001BpJ....80.3000G. PMC 1301483 . PMID 11371472
↑  Bader, Arjen N.; Hofman, Erik G.; Voortman, Jarno; Van Bergen En Henegouwen, Paul M.P.; Gerritsen, Hans C. (2009). "Homo-FRET Imaging Enables Quantification of Protein Cluster Sizes with Subcellular Resolution". Biophysical Journal. 97 (9): 2613–22. Bibcode:2009BpJ....97.2613B. PMC 2770629 . PMID 19883605
↑  Gradinaru, Claudiu C.; Marushchak, Denys O.; Samim, Masood; Krull, Ulrich J. (2010). "Fluorescence anisotropy: From single molecules to live cells". The Analyst. 135 (3): 452–9. Bibcode:2010Ana...135..452G. PMID 20174695. doi:10.1039/b920242k
↑  Lakowicz, Joseph R. (1999). Principles of fluorescence spectroscopy (2nd ed.). New York, NY: Kluwer Acad./Plenum Publ. pp. 374–443. ISBN 978-0-306-46093-7.
↑  Truong, Kevin; Ikura, Mitsuhiko (2001). "The use of FRET imaging microscopy to detect protein–protein interactions and protein conformational changes in vivo". Current Opinion in Structural Biology. 11 (5): 573–8. PMID 11785758. doi:10.1016/S0959-440X(00)00249-9.
↑  Sekar, R. B.; Periasamy, A (2003). "Fluorescence resonance energy transfer (FRET) microscopy imaging of live cell protein localizations". The Journal of Cell Biology. 160 (5): 629–33. PMC 2173363 . PMID 12615908. doi:10.1083/jcb.200210140.
↑  Ni, Qiang; Zhang, Jin (2010). "Dynamic Visualization of Cellular Signaling". In Endo, Isao; Nagamune, Teruyuki. Nano/Micro Biotechnology. Advances in Biochemical Engineering/Biotechnology, Volume 119. Springer. pp. 79–97. Bibcode:2010nmb..book...79N. ISBN 978-3-642-14946-7. PMID 19499207. doi:10.1007/10_2008_48.
↑  Silvius, John R.; Nabi, Ivan Robert (2006). "Fluorescence-quenching and resonance energy transfer studies of lipid microdomains in model and biological membranes (Review)". Molecular Membrane Biology. 23 (1): 5–16. PMID 16611577. doi:10.1080/09687860500473002.
↑  Acrylamide and iodide fluorescence quenching as a structural probe of tryptophan microenvironment in bovine lens crystallins. Phillips SR, Wilson LJ, Borkman RF. Curr Eye Res. 1986 Aug;5(8):611-9.
↑  James E. O'Reilly, Fluorescence experiments with quinine, Journal of Chemical Education 52, 1975-09-01, עמ' 610 doi: 10.1021/ed052p610
↑  Blum G, Weimer RM, Edgington LE, Adams W, Bogyo M (2009) Comparative Assessment of Substrates and Activity Based Probes as Tools for Non- Invasive Optical Imaging of Cysteine Protease Activity. PLoS ONE 4(7): e6374. doi:10.1371/journal.pone.0006374. Download PDF
↑  FRET – מעבר אנרגיה ליצירת פלורסנציה, באתר davidson.weizmann.ac.il
↑  Elena Bollati, Daniel Plimmer, Cecilia D’Angelo, Jörg Wiedenmann, FRET-Mediated Long-Range Wavelength Transformation by Photoconvertible Fluorescent Proteins as an Efficient Mechanism to Generate Orange-Red Light in Symbiotic Deep Water Corals, International Journal of Molecular Sciences 18, 2017-07-04 doi: 10.3390/ijms18071174
↑  Hu, Chang-Deng; Chinenov, Yurii; Kerppola, Tom K. (2002). "Visualization of Interactions among bZIP and Rel Family Proteins in Living Cells Using Bimolecular Fluorescence Complementation". Molecular Cell. 9 (4): 789–98. PMID 11983170. doi:10.1016/S1097-2765(02)00496-3
הקונספט של FRET.
כאשר החלבונים קשורים, עירור ה-CFP על ידי בליעה באורך גל של 414 ננומטר גורם פליטה של YFP באורך גל של 525 ננומטר עקב FRET. אם הקשר מפורק על ידי הפרוטאז, תהליך ה-FRET מפסיק להתקיים והעירור גורם לפליטת CFP באורך גל של 475 ננומטר.