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- W4244852251 abstract "Tools and assays that characterize protein-protein interactions are of fundamental importance to biology, because protein assemblies play a critical role in the control and regulation of nearly every cellular process. The availability of fluorescent proteins has facilitated the direct and real-time observation of protein-protein interactions inside living cells, but existing methods are mostly limited to binary interactions between two proteins. Because of the scarcity of techniques capable of identifying ternary interactions, we developed tricolor heterospecies partition analysis. The technique is based on brightness analysis of fluorescence fluctuations from three fluorescent proteins that serve as protein labels. We identified three fluorescent proteins suitable for tricolor brightness experiments. In addition, we developed the theory of identifying interactions in a ternary protein system using tricolor heterospecies partition analysis. The theory was verified by experiments on well-characterized protein systems. A graphical representation of the heterospecies partition data was introduced to visualize interactions in ternary protein systems. Lastly, we performed fluorescence fluctuation experiments on cells expressing a coactivator and two nuclear receptors and applied heterospecies partition analysis to explore the interactions of this ternary protein system. This work has been supported by grants from the National Institutes of Health (R01 GM64589) and the National Science Foundation (PHY 0957728)." @default.
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- W4244852251 date "2016-02-01" @default.
- W4244852251 modified "2023-09-30" @default.
- W4244852251 title "Characterization of Ternary Protein Systems in Living Cells with Tricolor Heterospecies Partition Analysis" @default.
- W4244852251 doi "https://doi.org/10.1016/j.bpj.2015.11.927" @default.
- W4244852251 hasPublicationYear "2016" @default.
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