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10.1016/j.jmb.2015.05.013 http://scihub22266oqcxt.onion/10.1016/j.jmb.2015.05.013 C4569523!4569523!26003922     free     free     free Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\26003922.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       J+Mol+Biol 2015 ; 427 (18): 2983-94 Nephropedia Template TP {{tp|p=26003922|t=2015. Folding optimization in vivo uncovers new chaperones |pdf=|usr=}}{{26003922}} gab.com Text Folding optimization in vivo uncovers new chaperones JO: J Mol Biol http://www.kidney.de/pget.php?&tw=1&pmid=26003922 #FOAvip By employing a genetic selection that forces the cell to fold an unstable, aggregation prone test protein in order to survive, we have generated bacterial strains with enhanced periplasmic folding capacity. These strains enhance the soluble steady state level of the test protein. Most of the bacterial variants we isolated were found to overexpress one or more periplasmic proteins including OsmY, Ivy, DppA, OppA, and HdeB. Of these proteins, only HdeB has convincingly been previously shown to function as chaperone in vivo. By giving bacteria the stark choice between death and stabilizing a poorly folded protein, we have now generated designer bacteria selected for their ability to stabilize specific proteins. Twit Text FOAVip Folding optimization in vivo uncovers new chaperones ????J Mol Biol http://www.kidney.de/pget.php?&tw=1&pmid=26003922 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26003922 #FOAvip English Wikipedia <ref>{{Cite pmid|26003922}}</ref> Folding optimization in vivo uncovers new chaperones #MMPMID26003922 Lennon CW; Thamsen M; Friman ET; Cacciaglia A; Sachsenhauser V; Sorgenfrei FA; Wasik MA; Bardwell JC J Mol Biol 2015[Sep]; 427 (18): 2983-94 PMID26003922show ga By employing a genetic selection that forces the cell to fold an unstable, aggregation prone test protein in order to survive, we have generated bacterial strains with enhanced periplasmic folding capacity. These strains enhance the soluble steady state level of the test protein. Most of the bacterial variants we isolated were found to overexpress one or more periplasmic proteins including OsmY, Ivy, DppA, OppA, and HdeB. Of these proteins, only HdeB has convincingly been previously shown to function as chaperone in vivo. By giving bacteria the stark choice between death and stabilizing a poorly folded protein, we have now generated designer bacteria selected for their ability to stabilize specific proteins. äFolding optimization in vivo uncovers new chaperones (epmc).pdf DeepDyve Pubget Overpricing