In Vivo Analysis of Protein-Protein Interactions with Bioluminescence Resonance Energy Transfer (BRET): Progress and Prospects. [PDF]
Int J Mol Sci, 2016 Proteins are the elementary machinery of life, and their functions are carried out mostly by molecular interactions. Among those interactions, protein–protein interactions (PPIs) are the most important as they participate in or mediate all essential biological processes.
Sun S, Yang X, Wang Y, Shen X.
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Image Processing for Bioluminescence Resonance Energy Transfer Measurement—BRET-Analyzer [PDF]
Frontiers in Computational Neuroscience, 2018 A growing number of tools now allow live recordings of various signaling pathways and protein-protein interaction dynamics in time and space by ratiometric measurements, such as Bioluminescence Resonance Energy Transfer (BRET) Imaging.
Yan Chastagnier +11 more
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Bioluminescence Resonance Energy Transfer (BRET) Assay for Determination of Molecular Interactions in Living Cells [PDF]
Bio-Protocol, 2017 The bioluminescence resonance energy transfer (BRET) assay can be used as an indicator of molecular approximation and/or interaction. A significant resonance energy transfer signal is generated when the acceptor, having the appropriate spectral overlap ...
Kaleeckal Harikumar +5 more
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Enhanced Molecular Tension Sensor Based on Bioluminescence Resonance Energy Transfer (BRET). [PDF]
ACS Sens, 2020 Molecular tension sensors measure piconewton forces experienced by individual proteins in the context of the cellular microenvironment. Current genetically encoded tension sensors use FRET to report on extension of a deformable peptide encoded in a cellular protein of interest.
Aird EJ +3 more
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Genetically Encoded RNA-Based Bioluminescence Resonance Energy Transfer (BRET) Sensors. [PDF]
ACS Sens, 2023 Abstract RNA-based nanostructures and molecular devices have become popular for developing biosensors and genetic regulators. These programmable RNA nanodevices can be genetically encoded and modularly engineered to detect various cellular targets and then induce output signals, most often a fluorescence readout ...
Mi L +7 more
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Bioluminescence Resonance Energy Transfer (BRET) Allows Monitoring the Barnase-Barstar Complex In Vivo [PDF]
Biophysica, 2022 Bioluminescence resonance energy transfer (BRET) seems to be a promising biophysical technique to study protein–protein interactions within living cells due to a very specific reaction of bioluminescence that essentially decreases the background of other
Victor Marchenkov +4 more
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Experimental determination of the bioluminescence resonance energy transfer (BRET) Förster distances of NanoBRET and red-shifted BRET pairs. [PDF]
Anal Chim Acta X, 2020 Bioluminescence Resonance Energy Transfer (BRET) is widely applied to study protein-protein interactions, as well as increasingly to monitor both ligand binding and molecular rearrangements. The Förster distance (R0) describes the physical distance between the two chromophores at which 50% of the maximal energy transfer occurs and it depends on the ...
Weihs F, Wang J, Pfleger KDG, Dacres H.
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Identification of Heteroreceptors Complexes and Signal Transduction Events Using Bioluminescence Resonance Energy Transfer (BRET) [PDF]
Bio-Protocol, 2019 Detecting protein-protein interactions by co-immunoprecipitation provided a major advancement in the immunology research field. In the G-protein-coupled receptors (GPCRs) research field, colocalization and co-immunoprecipitation were used to detect ...
Irene Reyes-Resina +3 more
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Analysis of RXR/THR and RXR/PPARG2 heterodimerization by bioluminescence resonance energy transfer (BRET). [PDF]
PLoS ONE, 2013 BACKGROUND: Nuclear receptors (NR) regulate transcription of genes involved in many biological processes such as development, cell proliferation, differentiation and cell death.
Miquel Mulero +4 more
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Bioluminescence resonance energy transfer (BRET) imaging in plant seedlings and mammalian cells. [PDF]
Methods Mol Biol, 2011 Bioluminescence resonance energy transfer (BRET) has become a widely used technique to monitor protein-protein interactions. It involves resonance energy transfer between a bioluminescent donor and a fluorescent acceptor. Because the donor emits photons intrinsically, fluorescence excitation is unnecessary.
Xie Q +4 more
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