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10.1038/s41467-017-01855-z http://scihub22266oqcxt.onion/10.1038/s41467-017-01855-z 29167435!5700200!29167435     free     free     free Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Nat+Commun 2017 ; 8 (1): 1706 Nephropedia Template TP {{tp|p=29167435|t=2017. Galpha(i) is required for carvedilol-induced beta(1) adrenergic receptor beta-arrestin biased signaling |pdf=|usr=}}{{29167435}} gab.com Text Galpha(i) is required for carvedilol-induced beta(1) adrenergic receptor beta-arrestin biased signaling JO: Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=29167435 #FOAvip The beta(1) adrenergic receptor (beta(1)AR) is recognized as a classical Galpha(s)-coupled receptor. Agonist binding not only initiates G protein-mediated signaling but also signaling through the multifunctional adapter protein beta-arrestin. Some betaAR ligands, such as carvedilol, stimulate betaAR signaling preferentially through beta-arrestin, a concept known as beta-arrestin-biased agonism. Here, we identify a signaling mechanism, unlike that previously known for any Galpha(s)-coupled receptor, whereby carvedilol induces the transition of the beta(1)AR from a classical Galpha(s)-coupled receptor to a Galpha(i)-coupled receptor stabilizing a distinct receptor conformation to initiate beta-arrestin-mediated signaling. Recruitment of Galpha(i) is not induced by any other betaAR ligand screened, nor is it required for beta-arrestin-bias activated by the beta(2)AR subtype of the betaAR family. Our findings demonstrate a previously unrecognized role for Galpha(i) in beta(1)AR signaling and suggest that the concept of beta-arrestin-bias may need to be refined to incorporate the selective bias of receptors towards distinct G protein subtypes. Twit Text FOAVip Galpha(i) is required for carvedilol-induced beta(1) adrenergic receptor beta-arrestin biased signaling ????Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=29167435 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=29167435 #FOAvip English Wikipedia <ref>{{Cite pmid|29167435}}</ref> Galpha(i) is required for carvedilol-induced beta(1) adrenergic receptor beta-arrestin biased signaling #MMPMID29167435 Wang J; Hanada K; Staus DP; Makara MA; Dahal GR; Chen Q; Ahles A; Engelhardt S; Rockman HA Nat Commun 2017[Nov]; 8 (1): 1706 PMID29167435show ga The beta(1) adrenergic receptor (beta(1)AR) is recognized as a classical Galpha(s)-coupled receptor. Agonist binding not only initiates G protein-mediated signaling but also signaling through the multifunctional adapter protein beta-arrestin. Some betaAR ligands, such as carvedilol, stimulate betaAR signaling preferentially through beta-arrestin, a concept known as beta-arrestin-biased agonism. Here, we identify a signaling mechanism, unlike that previously known for any Galpha(s)-coupled receptor, whereby carvedilol induces the transition of the beta(1)AR from a classical Galpha(s)-coupled receptor to a Galpha(i)-coupled receptor stabilizing a distinct receptor conformation to initiate beta-arrestin-mediated signaling. Recruitment of Galpha(i) is not induced by any other betaAR ligand screened, nor is it required for beta-arrestin-bias activated by the beta(2)AR subtype of the betaAR family. Our findings demonstrate a previously unrecognized role for Galpha(i) in beta(1)AR signaling and suggest that the concept of beta-arrestin-bias may need to be refined to incorporate the selective bias of receptors towards distinct G protein subtypes. |Adrenergic alpha-1 Receptor Antagonists/pharmacology[MESH] |Adrenergic beta-Antagonists/pharmacology[MESH] |Animals[MESH] |Carbazoles/*pharmacology[MESH] |Carvedilol[MESH] |Female[MESH] |GTP-Binding Protein alpha Subunits, Gi-Go/deficiency/genetics/*metabolism[MESH] |Gene Knockdown Techniques[MESH] |HEK293 Cells[MESH] |Humans[MESH] |Ligands[MESH] |MAP Kinase Signaling System/drug effects[MESH] |Male[MESH] |Mice[MESH] |Mice, Knockout[MESH] |Propanolamines/*pharmacology[MESH] |Protein Conformation/drug effects[MESH] |Receptors, Adrenergic, beta-1/chemistry/*metabolism[MESH]Galpha(i) is required for carvedilol-induced beta(1) adrenergic recept(epmc).pdf DeepDyve Pubget Overpricing