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10.1002/0471141755.ph0214s70

http://scihub22266oqcxt.onion/10.1002/0471141755.ph0214s70
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C4583203!4583203!26331887
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suck abstract from ncbi


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pmid26331887      Curr+Protoc+Pharmacol 2015 ; 70 (ä): 2.14.1-2.14.14
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  • Using bioluminescent resonance energy transfer (BRET) to characterize agonist-induced arrestin recruitment to modified and unmodified G protein-coupled receptors (GPCRs) #MMPMID26331887
  • Donthamsetti P; Quejada JR; Javitch JA; Gurevich VV; Lambert NA
  • Curr Protoc Pharmacol 2015[]; 70 (ä): 2.14.1-2.14.14 PMID26331887show ga
  • G protein-coupled receptors (GPCRs) represent ~25% of current drug targets. Ligand binding to these receptors activates G proteins and arrestins, which are involved in differential signaling pathways. Functionally selective or biased ligands activate one of these two pathways and may be superior medications for certain diseases states. The identification of these ligands requires robust drug screening assays for both G protein and arrestin activity. Here we describe in detail the technical aspects of two bioluminescence resonance energy (BRET)-based assays that can be used to monitor arrestin recruitment to GPCRs. One assay requires modification of GPCRs by fusion to a BRET donor or acceptor moiety, whereas the other can detect recruitment of arrestin to unmodified GPCRs.
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