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10.1002/0471141755.ph0214s70 http://scihub22266oqcxt.onion/10.1002/0471141755.ph0214s70 C4583203!4583203 !26331887     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=26331887 &cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215       Curr+Protoc+Pharmacol 2015 ; 70 (?): 2.14.1-2.14.14 Nephropedia Template TP {{tp|p=26331887 |t=2015. Using Bioluminescence Resonance Energy Transfer (BRET) to Characterize Agonist-Induced Arrestin Recruitment to Modified and Unmodified G Protein-Coupled Receptors |pdf=|usr=}}{{26331887 }} gab.com Text Using Bioluminescence Resonance Energy Transfer (BRET) to Characterize Agonist-Induced Arrestin Recruitment to Modified and Unmodified G Protein-Coupled Receptors JO: Curr Protoc Pharmacol http://www.kidney.de/pget.php?&tw=1&pmid=26331887 #FOAvip 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. Because functionally selective or biased ligands activate one of these two pathways, they may be superior medications for certain diseases states. The identification of such ligands requires robust drug screening assays for both G protein and arrestin activity. This unit describes protocols for two bioluminescence resonance energy transfer (BRET)-based assays 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 arrestin recruitment to unmodified GPCRs. Twit Text FOAVip Using Bioluminescence Resonance Energy Transfer (BRET) to Characterize Agonist-Induced Arrestin Recruitment to Modified and Unmodified G Protein-Coupled Receptors ????Curr Protoc Pharmacol http://www.kidney.de/pget.php?&tw=1&pmid=26331887 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26331887 #FOAvip English Wikipedia <ref>{{Cite pmid|26331887 }}</ref> Using Bioluminescence Resonance Energy Transfer (BRET) to Characterize Agonist-Induced Arrestin Recruitment to Modified and Unmodified G Protein-Coupled Receptors #MMPMID26331887 Donthamsetti P ; Quejada JR ; Javitch JA ; Gurevich VV ; Lambert NA Curr Protoc Pharmacol 2015[Sep]; 70 (?): 2.14.1-2.14.14 PMID26331887 show 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. Because functionally selective or biased ligands activate one of these two pathways, they may be superior medications for certain diseases states. The identification of such ligands requires robust drug screening assays for both G protein and arrestin activity. This unit describes protocols for two bioluminescence resonance energy transfer (BRET)-based assays 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 arrestin recruitment to unmodified GPCRs. |Arrestin/*agonists/antagonists & inhibitors/*metabolism [MESH] |Cell Membrane/metabolism [MESH] |GTP-Binding Proteins/metabolism [MESH] |HEK293 Cells [MESH] |Humans [MESH] |Ligands [MESH] |Luminescent Measurements/*methods [MESH] |Polyethyleneimine/pharmacology [MESH] |Receptors, G-Protein-Coupled/*drug effects [MESH]Using Bioluminescence Resonance Energy Transfer (BRET) to Characterize(epmc).pdf DeepDyve Pubget Overpricing