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Protocol for Measuring Drug-Target Engagement in Mouse Colorectal Cancer Organoids Using NanoBRET Assay. [PDF]
Badmos HA, Steele C, Cagan R.
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Mechanisms and Applications of Photocatalytic Proximity Labeling. [PDF]
Gong E, Xie Y, Qin W.
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Synthetic Multidomain Proteins Containing Unstructured and α‑Helical Linkers Reveal a Differential Impact of Molecular Crowding on Catalytic Activity and Conformation. [PDF]
Sultana A +3 more
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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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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
openaire +2 more sources
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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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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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
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
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) 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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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
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
2019Detection 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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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
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

