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Fluorescence Resonance Energy Transfer (FRET) Literature Sources

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Section Overview:

Understanding the dynamic interactions between proteins within living cells is fundamental to a basic knowledge of the underlying concepts that guide molecular and cellular biology. Over the past few years, the rapid development of fluorescent proteins and their application as fusion products and biosensors has significantly expanded the molecular toolkit available for probing the mysteries of cellular physiology and pathology. In this regard, fluorescence (or Förster) resonance energy transfer (FRET) is emerging as a powerful optical microscopy technique for examining physiological processes with high temporal and spatial resolution. The references listed below highlight important literature sources for review articles and original research reports on the construction and applications of fluorescent proteins for resonance energy transfer experiments.

Literature Sources

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  • Bastiaens, P. I. H. and Jovin, T. M., Fluorescence resonance energy transfer microscopy., in Cell Biology: A Laboratory Handbook, Volume 3, Celis, J. E. (ed.), Academic Press, New York, pages 136-146 (1998).| Amazon |
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  • Förster, T., Delocalized excitation and excitation transfer., in Modern Quantum Chemistry, Sinanoglu, O. (ed.), Academic Press, New York, pages 93-137 (1965).| Abe Books |
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  • Gordon, G. W., Berry, G., Liang, X. H., Levine, B., and Herman, B., Quantitative fluorescence resonance energy transfer measurements using fluorescence microscopy., Biophysical Journal 74: 2702-2713 (1998). | PubMed |
  • Gryczynski, Z., Gryczynski, I., and Lakowicz, J. R., Basics of Fluorescence and FRET., in Molecular Imaging: FRET Microscopy and Spectroscopy, Periasamy, A. and Day, R. N. (eds.), Oxford University Press, New York, pages 21-56 (2005). | Molecular Imaging |
  • Harpur, A. G., Wouters, F. S., and Bastiaens, P. I. H., Imaging FRET between spectrally similar GFP molecules in single cells., Nature Biotechnology 19: 167-169 (2001).| PubMed |
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  • Heim, R., Green fluorescent protein forms for energy transfer., Methods in Enzymology 302: 408-423 (1999). | PubMed |
  • Herman, B., Resonance energy transfer microscopy., Methods in Cell Biology 30: 219-243 (1989). | PubMed |
  • Hink, M. A., Visser, N. A., Borst, J. W., van Hoek, A., and Visser, A. J. W. G., Practical use of corrected fluorescence excitation and emission spectra of fluorescent proteins in Förster resonance energy transfer (FRET) studies., Journal of Fluorescence 13: 185-188 (2003). | J Fluorescence |
  • Hohng, S. and Ha, T., Single-molecule FRET., in Molecular Imaging: FRET Microscopy and Spectroscopy, Periasamy, A. and Day, R. N. (eds.), Oxford University Press, New York, pages 165-179 (2005). | Molecular Imaging |
  • Hoppe, A., Christensen, K., and Swanson, J. A., Fluorescence resonance energy transfer-based stoichiometry in living cells., Biophysical Journal 83: 3652-3664 (2002).| PubMed |
  • Jares-Erijman, E. A. and Jovin, T. M., FRET imaging., Nature Biotechnology 21: 1387-1395 (2003). | PubMed |
  • Karasawa, A., Araki, T., Nagai, T., Mizuno, H., and Miyawaki, A., Cyan-emitting and orange-emitting fluorescent proteins as a donor/acceptor pair for fluorescence resonance energy transfer., Biochemical Journal (Great Britain) 381: 307-312 (2004).| PubMed |
  • Karpova, T. S., Baumann, C. T., He, L., Wu, X., Grammer, A., Lipsky, P., Hager, G. L., and McNally, J. G., Fluorescence resonance energy transfer from cyan to yellow fluorescent protein detected by acceptor photobleaching using confocal microscopy and a single laser., Journal of Microscopy 209: 56-70 (2003). | PubMed |
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