Fanciful FRET
- 18 April 2006
- journal article
- review article
- Published by American Association for the Advancement of Science (AAAS) in Science's STKE
- Vol. 2006 (331) , re2
- https://doi.org/10.1126/stke.3312006re2
Abstract
The validity of experiments based on Förster resonance energy transfer (FRET), an imaging technique widely used to measure protein-protein interactions in living cells, critically depends on the accurate and precise measurement of FRET efficiency. The use of FRET standards to determine FRET efficiency, and a consideration of such factors as how the abundance of FRET acceptors and the stoichiometry of donors and acceptors in a molecular complex can affect measured FRET efficiency, will enhance the usefulness with which FRET experiments can be interpreted.Keywords
This publication has 48 references indexed in Scilit:
- A guide to choosing fluorescent proteinsNature Methods, 2005
- Reversible Photobleaching of Enhanced Green Fluorescent ProteinsBiochemistry, 2005
- Applying spectral fingerprinting to the analysis of FRET imagesMicroscopy Research and Technique, 2004
- An improved cyan fluorescent protein variant useful for FRETNature Biotechnology, 2004
- A Photoactivatable GFP for Selective Photolabeling of Proteins and CellsScience, 2002
- Partitioning of Lipid-Modified Monomeric GFPs into Membrane Microdomains of Live CellsScience, 2002
- Inhibition of T Cell Receptor-Coreceptor Interactions by Antagonist Ligands Visualized by Live FRET Imaging of the T-Hybridoma Immunological SynapseImmunity, 2002
- A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applicationsNature Biotechnology, 2002
- Green Fluorescent Protein as a Marker for Gene ExpressionScience, 1994
- A novel genetic system to detect protein–protein interactionsNature, 1989