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10.1038/s41467-017-00444-4 http://scihub22266oqcxt.onion/10.1038/s41467-017-00444-4 C5577305!5577305!28855508     free     free     free Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Nat+Commun 2017 ; 8 (ä): ä Nephropedia Template TP {{tp|p=28855508|t=2017. Chaperones rescue the energetic landscape of mutant CFTR at single molecule and in cell |pdf=|usr=}}{{28855508}} gab.com Text Chaperones rescue the energetic landscape of mutant CFTR at single molecule and in cell JO: Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=28855508 #FOAvip Molecular chaperones are pivotal in folding and degradation of the cellular proteome but their impact on the conformational dynamics of near-native membrane proteins with disease relevance remains unknown. Here we report the effect of chaperone activity on the functional conformation of the temperature-sensitive mutant cystic fibrosis channel (?F508-CFTR) at the plasma membrane and after reconstitution into phospholipid bilayer. Thermally induced unfolding at 37?°C and concomitant functional inactivation of ?F508-CFTR are partially suppressed by constitutive activity of Hsc70 and Hsp90 chaperone/co-chaperone at the plasma membrane and post-endoplasmic reticulum compartments in vivo, and at single-molecule level in vitro, indicated by kinetic and thermodynamic remodeling of the mutant gating energetics toward its wild-type counterpart. Thus, molecular chaperones can contribute to functional maintenance of ?F508-CFTR by reshaping the conformational energetics of its final fold, a mechanism with implication in the regulation of metastable ABC transporters and other plasma membrane proteins activity in health and diseases. Twit Text FOAVip Chaperones rescue the energetic landscape of mutant CFTR at single molecule and in cell ????Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=28855508 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28855508 #FOAvip English Wikipedia <ref>{{Cite pmid|28855508}}</ref> Chaperones rescue the energetic landscape of mutant CFTR at single molecule and in cell #MMPMID28855508 Bagdany M; Veit G; Fukuda R; Avramescu RG; Okiyoneda T; Baaklini I; Singh J; Sovak G; Xu H; Apaja PM; Sattin S; Beitel LK; Roldan A; Colombo G; Balch W; Young JC; Lukacs GL Nat Commun 2017[]; 8 (ä): ä PMID28855508show ga Molecular chaperones are pivotal in folding and degradation of the cellular proteome but their impact on the conformational dynamics of near-native membrane proteins with disease relevance remains unknown. Here we report the effect of chaperone activity on the functional conformation of the temperature-sensitive mutant cystic fibrosis channel (?F508-CFTR) at the plasma membrane and after reconstitution into phospholipid bilayer. Thermally induced unfolding at 37?°C and concomitant functional inactivation of ?F508-CFTR are partially suppressed by constitutive activity of Hsc70 and Hsp90 chaperone/co-chaperone at the plasma membrane and post-endoplasmic reticulum compartments in vivo, and at single-molecule level in vitro, indicated by kinetic and thermodynamic remodeling of the mutant gating energetics toward its wild-type counterpart. Thus, molecular chaperones can contribute to functional maintenance of ?F508-CFTR by reshaping the conformational energetics of its final fold, a mechanism with implication in the regulation of metastable ABC transporters and other plasma membrane proteins activity in health and diseases. äChaperones rescue the energetic landscape of mutant CFTR at single mol(epmc).pdf DeepDyve Pubget Overpricing