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10.1016/j.redox.2015.06.002 http://scihub22266oqcxt.onion/10.1016/j.redox.2015.06.002 C4477112!4477112!26087116     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Redox+Biol 2015 ; 5 (ä): 290-300 Nephropedia Template TP {{tp|p=26087116|t=2015. Sch9 regulates intracellular protein ubiquitination by controlling stress responses |pdf=|usr=}}{{26087116}} gab.com Text Sch9 regulates intracellular protein ubiquitination by controlling stress responses JO: Redox Biol http://www.kidney.de/pget.php?&tw=1&pmid=26087116 #FOAvip Protein ubiquitination and the subsequent degradation are important means by which aberrant proteins are removed from cells, a key requirement for long-term survival. In this study, we found that the overall level of ubiquitinated proteins dramatically decreased as yeast cell grew from log to stationary phase. Deletion of SCH9, a gene encoding a key protein kinase for longevity control, decreased the level of ubiquitinated proteins in log phase and this effect could be reversed by restoring Sch9 function. We demonstrate here that the decrease of ubiquitinated proteins in sch9? cells in log phase is not caused by changes in ubiquitin expression, proteasome activity, or autophagy, but by enhanced expression of stress response factors and a decreased level of oxidative stress. Our results revealed for the first time how Sch9 regulates the level of ubiquitinated proteins and provides new insight into how Sch9 controls longevity. Twit Text FOAVip Sch9 regulates intracellular protein ubiquitination by controlling stress responses ????Redox Biol http://www.kidney.de/pget.php?&tw=1&pmid=26087116 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26087116 #FOAvip English Wikipedia <ref>{{Cite pmid|26087116}}</ref> Sch9 regulates intracellular protein ubiquitination by controlling stress responses #MMPMID26087116 Qie B; Lyu Z; Lyu L; Liu J; Gao X; Liu Y; Duan W; Zhang N; Du L; Liu K Redox Biol 2015[Aug]; 5 (ä): 290-300 PMID26087116show ga Protein ubiquitination and the subsequent degradation are important means by which aberrant proteins are removed from cells, a key requirement for long-term survival. In this study, we found that the overall level of ubiquitinated proteins dramatically decreased as yeast cell grew from log to stationary phase. Deletion of SCH9, a gene encoding a key protein kinase for longevity control, decreased the level of ubiquitinated proteins in log phase and this effect could be reversed by restoring Sch9 function. We demonstrate here that the decrease of ubiquitinated proteins in sch9? cells in log phase is not caused by changes in ubiquitin expression, proteasome activity, or autophagy, but by enhanced expression of stress response factors and a decreased level of oxidative stress. Our results revealed for the first time how Sch9 regulates the level of ubiquitinated proteins and provides new insight into how Sch9 controls longevity. äSch9 regulates intracellular protein ubiquitination by controlling str(epmc).pdf DeepDyve Pubget Overpricing