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- W2037502977 endingPage "031207" @default.
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- W2037502977 abstract "Förster resonance energy transfer (FRET) detection of protein interaction in living cells is commonly measured following the expression of interacting proteins genetically fused to the cyan (CFP) and yellow (YFP) derivatives of the Aequorea victoria fluorescent protein (FP). These FPs can dimerize at mM concentrations, which may introduce artifacts into the measurement of interaction between proteins that are fused with the FPs. Here, FRET analysis of the interaction between estrogen receptors (alpha isoform, ER) labeled with “wild-type” CFP and YFP is compared with that of ER labeled with “monomeric” A206K mutants of CFP and YFP. The intracellular equilibrium dissociation constant for the hormone-induced ER-ER interaction is similar for ER labeled with wild-type or monomeric FPs. However, the measurement of energy transfer measured for ER-ER interaction in each cell is less consistent with the monomeric FPs. Thus, dimerization of the FPs does not affect the kinetics of ER-ER interaction but, when brought close together via ER-ER interaction, FP dimerization modestly improves FRET measurement." @default.
- W2037502977 created "2016-06-24" @default.
- W2037502977 creator A5034080122 @default.
- W2037502977 creator A5045803872 @default.
- W2037502977 creator A5060915596 @default.
- W2037502977 date "2008-01-01" @default.
- W2037502977 modified "2023-10-11" @default.
- W2037502977 title "Dimerization between aequorea fluorescent proteins does not affect interaction between tagged estrogen receptors in living cells" @default.
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- W2037502977 doi "https://doi.org/10.1117/1.2940366" @default.
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