Visualization of AP-1 NF- B ternary complexes in living cells by using a BiFC-based FRET

Visualization of AP-1 NF-kappaB ternary complexes in living cells by using a BiFC-based FRET.

Protein-protein interactions are essential for maintaining cell structure and for executing almost all cellular processes. Determination of where and how each protein interacts with its partners provides significant insight into proteins' cellular roles. Although several assays, such as FRET and bimolecular fluorescence complementation (BiFC), have been developed and widely used for visualizati...

Combined Bimolecular Fluorescence Complementation (BiFC) and Förster Resonance Energy Transfer (FRET) Reveals Ternary SNARE Complex Formation in Living Plant Cells

NF- B and AP-1 Connection: Mechanism of NF- B-Dependent Regulation of AP-1 Activity

Breakthrough Technologies Combined Bimolecular Fluorescence Complementation and Förster Resonance Energy Transfer Reveals Ternary SNARE Complex Formation in Living Plant Cells

Various fluorophore-based microscopic methods, comprising Förster resonance energy transfer (FRET) and bimolecular fluorescence complementation (BiFC), are suitable to study pairwise interactions of proteins in living cells. The analysis of interactions between more than two protein partners using these methods, however, remains difficult. In this study, we report the successful application of ...

Combined bimolecular fluorescence complementation and Forster resonance energy transfer reveals ternary SNARE complex formation in living plant cells.

Various fluorophore-based microscopic methods, comprising Förster resonance energy transfer (FRET) and bimolecular fluorescence complementation (BiFC), are suitable to study pairwise interactions of proteins in living cells. The analysis of interactions between more than two protein partners using these methods, however, remains difficult. In this study, we report the successful application of ...