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Measuring Protein-Protein Interactions of Melatonin Receptors by Bioluminescence Resonance Energy Transfer (BRET)

2022
The melatonin receptor subfamily belongs to the G protein-coupled receptor superfamily and consists of three members in mammals, MT1, MT2, and GPR50. These receptors can interact with each other to form homo- and heterodimers that are part of larger molecular complexes composed of G proteins, β-arrestins, and other membrane and cytosolic proteins. BRET
Atsuro, Oishi, Ralf, Jockers
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Bioluminescence Resonance Energy Transfer (BRET) Imaging in Living Cells: Image Acquisition and Quantification

2021
Bioluminescence resonance energy transfer (BRET) is an energy transfer phenomenon from a luciferase donor to a fluorescence acceptor and serves as an indicator of protein-protein interaction or protein proximity. BRET imaging is a powerful tool in the investigation of signaling proteins because it enables spatial analysis of such protein interactions ...
Hiroyuki, Kobayashi, Michel, Bouvier
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Firefly Luciferase-Based Sequential Bioluminescence Resonance Energy Transfer (BRET)-Fluorescence Resonance Energy Transfer (FRET) Protease Assays

Methods in Molecular Biology, 2016
We describe here the preparation of ratiometric luminescent probes that contain two well-separated emission peaks produced by a sequential bioluminescence resonance energy transfer (BRET)-fluorescence resonance energy transfer (FRET) process. The probes are single soluble fusion proteins consisting of a thermostable firefly luciferase variant that ...
Bruce R Branchini
exaly   +3 more sources

Illuminating insights into protein-protein interactions using bioluminescence resonance energy transfer (BRET)

Nature Methods, 2006
Bioluminescence resonance energy transfer (BRET) is a straightforward biophysical technique for studying protein-protein interactions. It requires: (1) that proteins of interest and suitable controls be labeled with either a donor or acceptor molecule, (2) placement of these labeled proteins in the desired environment for assessing their potential ...
Kevin D G, Pfleger, Karin A, Eidne
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Bioluminescence resonance energy transfer (BRET) for the real-time detection of protein-protein interactions

Nature Protocols, 2006
A substantial range of protein-protein interactions can be readily monitored in real time using bioluminescence resonance energy transfer (BRET). The procedure involves heterologous coexpression of fusion proteins, which link proteins of interest to a bioluminescent donor enzyme or acceptor fluorophore.
Kevin D G, Pfleger   +2 more
openaire   +2 more sources

Bioluminescence Resonance Energy Transfer (BRET) Coupled Near-Infrared Imaging of Apoptotic Cells

2019
Detection of apoptotic cells is crucial for understanding the mechanism of diseases and for therapy development. So far, visible-emitting fluorescent probes such as FITC-labeled Annexin V has been widely used for the detection of apoptotic cells. However, such probes cannot be applied to noninvasive imaging in the near-infrared (NIR) region.
Setsuko, Tsuboi, Takashi, Jin
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Real-time, continuous detection of maltose using bioluminescence resonance energy transfer (BRET) on a microfluidic system

Biosensors and Bioelectronics, 2014
We have previously shown that a genetically encoded bioluminescent resonance energy transfer (BRET) biosensor, comprising maltose binding protein (MBP) flanked by a green fluorescent protein (GFP(2)) at the N-terminus and a variant of Renilla luciferase (RLuc2) at the C-terminus, has superior sensitivity and limits of detection for maltose, compared ...
Alisha Anderson   +2 more
exaly   +3 more sources

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