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.
Publication types
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Research Support, N.I.H., Extramural
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Review
MeSH terms
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Algorithms
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Animals
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Bacterial Proteins / analysis
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Bacterial Proteins / chemistry
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Bibliometrics
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Electromagnetic Fields
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Fluorescence Polarization
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Fluorescence Resonance Energy Transfer* / instrumentation
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Fluorescence Resonance Energy Transfer* / methods
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Fluorescence Resonance Energy Transfer* / standards
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Fluorescence Resonance Energy Transfer* / trends
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Fluorescent Dyes / analysis
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Fluorescent Dyes / chemistry
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Fluorometry / methods
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Green Fluorescent Proteins / analysis
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Green Fluorescent Proteins / chemistry
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Humans
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Luminescent Proteins / analysis
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Luminescent Proteins / chemistry
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Microscopy, Fluorescence / instrumentation
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Microscopy, Fluorescence / methods
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Photobleaching
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Protein Interaction Mapping / methods*
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PubMed / statistics & numerical data
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Reference Standards
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Research Design
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Two-Hybrid System Techniques
Substances
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Bacterial Proteins
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Cyan Fluorescent Protein
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Fluorescent Dyes
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Luminescent Proteins
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yellow fluorescent protein, Bacteria
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Green Fluorescent Proteins