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Application of Bioluminescence Resonance Energy Transfer (BRET) for Biomolecular Interaction Studies
ChemBioChem, 2006AbstractChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 200 leading journals. To access a ChemInform Abstract, please click on HTML or PDF.
A. Prinz, M. Diskar, F. Herberg
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Analysis of in vitro SUMOylation using bioluminescence resonance energy transfer (BRET).
Biochemical and Biophysical Research Communications, 2009We demonstrated in vitro small ubiquitin-like modifier (SUMO)-mediated modification (SUMOylation) of RanGTPase activating protein-1 (RanGAP1) by using bioluminescence resonance energy transfer (BRET) for studying protein interactions. Renilla luciferase (Rluc) was fused to SUMO, and RanGAP1, the binding partner of SUMO, was fused to enhanced yellow ...
Young-Pil Kim +5 more
semanticscholar +6 more sources
Analytica Chimica Acta, 2020
Proteases are key signalling molecules for many physiological processes and their dysregulation is implicated in the progression of a range of diseases. Sensitive methods to measure protease activities in complex biological samples are critical for rapid
F. Weihs, Alex Peh, H. Dacres
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Proteases are key signalling molecules for many physiological processes and their dysregulation is implicated in the progression of a range of diseases. Sensitive methods to measure protease activities in complex biological samples are critical for rapid
F. Weihs, Alex Peh, H. Dacres
semanticscholar +3 more sources
Bioluminescence Resonance Energy Transfer (BRET)‐Based Synthetic Sensor Platform for Drug Discovery
Current Protocols in Protein Science, 2017AbstractBioluminescence resonance energy transfer (BRET) is a technique that analyzes protein‐protein interactions (PPIs). The unique feature of BRET delineates that the resonance energy is generated by the resonance energy donor, Renilla luciferase by the oxidative decarboxylation of coelenterazine substrate. BRET is superior to FRET where issues such
J. Woo, Jason I. Hong, S. Dinesh-Kumar
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Biosensors and Bioelectronics, 2011
Here we report the design of a bioluminescence resonance energy transfer (BRET)-based sensing system that could detect nucleic acid target in 5 min with high sensitivity and selectivity.
M. Kumar +3 more
semanticscholar +3 more sources
Here we report the design of a bioluminescence resonance energy transfer (BRET)-based sensing system that could detect nucleic acid target in 5 min with high sensitivity and selectivity.
M. Kumar +3 more
semanticscholar +3 more sources
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 ...
K. Pfleger, K. Eidne
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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 ...
K. Pfleger, K. Eidne
semanticscholar +3 more sources
Methods in molecular biology, 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, R. Jockers
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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, R. Jockers
semanticscholar +3 more sources
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.
K. Pfleger, R. Seeber, K. Eidne
semanticscholar +3 more sources
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.
K. Pfleger, R. Seeber, K. Eidne
semanticscholar +3 more sources