Results 31 to 40 of about 5,054 (183)

Bioluminescence Resonance Energy Transfer (BRET)-Mediated Protein Release from Self-Illuminating Photoresponsive Biomaterials. [PDF]

open access: yesJ Am Chem Soc
Phototriggered release of various cargos, including soluble protein factors and small molecules, has the potential to correct aberrant biological events by offering spatiotemporal control over local therapeutic levels. However, the poor penetration depth of light historically limits implementation to subdermal regions, necessitating alternative methods
Rapp TL   +3 more
europepmc   +4 more sources

Improved HaloTag Ligand Enables BRET Imaging With NanoLuc

open access: yesFrontiers in Chemistry, 2020
Bioluminescence resonance energy transfer (BRET) from an exceptionally bright luciferase, NanoLuc, to a fluorescent HaloTag ligand is gaining momentum to monitor molecular interactions.
Ovia Margaret Thirukkumaran   +8 more
doaj   +1 more source

Bioluminescence resonance energy transfer (BRET) imaging of protein-protein interactions within deep tissues of living subjects. [PDF]

open access: yesProc Natl Acad Sci U S A, 2011
Identifying protein–protein interactions (PPIs) is essential for understanding various disease mechanisms and developing new therapeutic approaches.
Dragulescu-Andrasi A   +4 more
europepmc   +2 more sources

Luciferase–Rose Bengal conjugates for singlet oxygen generation by bioluminescence resonance energy transfer [PDF]

open access: yes, 2017
Luciferase–Rose Bengal conjugates generated reactive oxygen species (ROS) inside cells via bioluminescence resonance energy transfer (BRET) without external light irradiation.
Sei Kwang Hahn   +5 more
core   +2 more sources

Luciferase-induced photoreductive uncaging of small-molecule effectors

open access: yesNature Communications, 2018
Bioluminescence resonance energy transfer (BRET) has been mostly employed in imaging applications. Here the authors use BRET to activate a ruthenium-based photocatalyst and perform a bioorthogonal chemical reaction, which can be used to uncage small ...
Eric Lindberg   +3 more
doaj   +1 more source

A bioluminescence resonance energy transfer (BRET) system: Application to interacting circadian clock proteins [PDF]

open access: yesProceedings of the National Academy of Sciences, 1999
We describe a method for assaying protein interactions that offers some attractive advantages over previous assays. This method, called bioluminescence resonance energy transfer (BRET), uses a bioluminescent luciferase that is genetically fused to one candidate protein, and a green fluorescent protein mutant fused to another protein of interest ...
Y, Xu, D W, Piston, C H, Johnson
openaire   +2 more sources

Optimization of BRET saturation assays for robust and sensitive cytosolic protein–protein interaction studies

open access: yesScientific Reports, 2022
Bioluminescence resonance energy transfer (BRET) saturation is a method of studying protein–protein interaction (PPI) upon quantification of the dependence of the BRET signal on the acceptor/donor (A:D) expression ratio.
Benoit Besson   +5 more
doaj   +1 more source

Thermostable Bioluminescent Intercalating Dyes for Real‐Time, Integrated Nucleic Acid Amplification and Detection

open access: yesAngewandte Chemie, EarlyView.
We present a bioluminescent diagnostic platform that integrates DNA amplification and detection in a single step. The engineering of thermostable luciferase‐intercalating dye conjugates and controlled release of caged luciferin substrates enable real‐time, detection of attomolar concentrations of viral DNA within 30 min.
Yosta de Stigter   +8 more
wiley   +2 more sources

Coupling optogenetic stimulation with NanoLuc-based luminescence (BRET) Ca++ sensing

open access: yesNature Communications, 2016
The coupling of optogenetics with fluorescent Ca2+ sensors is confounded by sensitivity of optogenetic probes to light used to excite the sensors. Here the authors develop a Ca2+ sensor based on bioluminescence resonance energy transfer (BRET) that ...
Jie Yang   +6 more
doaj   +1 more source

An endogenous green fluorescent protein–photoprotein pair in Clytia hemisphaerica eggs shows co-targeting to mitochondria and efficient bioluminescence energy transfer [PDF]

open access: yesOpen Biology, 2014
Green fluorescent proteins (GFPs) and calcium-activated photoproteins of the aequorin/clytin family, now widely used as research tools, were originally isolated from the hydrozoan jellyfish Aequora victoria.
Cécile Fourrage   +4 more
doaj   +1 more source

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