Source:http://linkedlifedata.com/resource/pubmed/id/16492395
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
10
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pubmed:dateCreated |
2006-8-21
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pubmed:abstractText |
Bioluminescence resonance energy transfer (BRET) is an increasingly popular technique for studying protein-protein interactions in live cells. It is particularly suitable for real-time monitoring of such interactions, however, the timescale over which assays can be carried out is currently relatively short (minutes) due to substrate instability. We present a new derivation of the BRET technology, termed 'extended BRET' (eBRET), which now enables protein-protein interactions to be monitored in real-time for many hours. This capability has significant benefits for investigating cellular function over extended timescales, as we have illustrated using the agonist-induced G-protein coupled receptor/beta-arrestin interaction. The potential for studying the modulation of such interactions by agonists, antagonists, inhibitors, dominant negative mutants and co-expressed accessory proteins is substantial. Furthermore, the advantages of eBRET have important implications for the development of high-throughput BRET screening systems, an ever-expanding area of interest for the pharmaceutical industry.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Imidazoles,
http://linkedlifedata.com/resource/pubmed/chemical/Luciferases, Renilla,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Pyrazines,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/coelenterazine
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0898-6568
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
18
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1664-70
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:16492395-Animals,
pubmed-meshheading:16492395-COS Cells,
pubmed-meshheading:16492395-Cell Survival,
pubmed-meshheading:16492395-Cells, Cultured,
pubmed-meshheading:16492395-Cercopithecus aethiops,
pubmed-meshheading:16492395-Energy Transfer,
pubmed-meshheading:16492395-Humans,
pubmed-meshheading:16492395-Imidazoles,
pubmed-meshheading:16492395-Kinetics,
pubmed-meshheading:16492395-Luciferases, Renilla,
pubmed-meshheading:16492395-Protein Binding,
pubmed-meshheading:16492395-Proteins,
pubmed-meshheading:16492395-Pyrazines,
pubmed-meshheading:16492395-Recombinant Fusion Proteins,
pubmed-meshheading:16492395-Reproducibility of Results,
pubmed-meshheading:16492395-Spectrometry, Fluorescence,
pubmed-meshheading:16492395-Substrate Specificity
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pubmed:year |
2006
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pubmed:articleTitle |
Extended bioluminescence resonance energy transfer (eBRET) for monitoring prolonged protein-protein interactions in live cells.
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pubmed:affiliation |
7TM Laboratory/Laboratory for Molecular Endocrinology, Western Australian Institute for Medical Research (WAIMR) and Centre for Medical Research, University of Western Australia, Nedlands, Perth, WA 6009, Australia. kpfleger@waimr.uwa.edu.au
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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