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10.1242/jcs.176479 http://scihub22266oqcxt.onion/10.1242/jcs.176479 C4893652!4893652!27026526     free     free     free Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Cell+Sci 2016 ; 129 (9): 1892-901 Nephropedia Template TP {{tp|p=27026526|t=2016. Vulnerability of newly synthesized proteins to proteostasis stress |pdf=|usr=}}{{27026526}} gab.com Text Vulnerability of newly synthesized proteins to proteostasis stress JO: J Cell Sci http://www.kidney.de/pget.php?&tw=1&pmid=27026526 #FOAvip The capacity of the cell to produce, fold and degrade proteins relies on components of the proteostasis network. Multiple types of insults can impose a burden on this network, causing protein misfolding. Using thermal stress, a classic example of acute proteostatic stress, we demonstrate that ?5?10% of the soluble cytosolic and nuclear proteome in human HEK293 cells is vulnerable to misfolding when proteostatic function is overwhelmed. Inhibiting new protein synthesis for 30?min prior to heat-shock dramatically reduced the amount of heat-stress induced polyubiquitylation, and reduced the misfolding of proteins identified as vulnerable to thermal stress. Following prior studies in C. elegans in which mutant huntingtin (Q103) expression was shown to cause the secondary misfolding of cytosolic proteins, we also demonstrate that mutant huntingtin causes similar ?secondary? misfolding in human cells. Similar to thermal stress, inhibiting new protein synthesis reduced the impact of mutant huntingtin on proteostatic function. These findings suggest that newly made proteins are vulnerable to misfolding when proteostasis is disrupted by insults such as thermal stress and mutant protein aggregation. Twit Text FOAVip Vulnerability of newly synthesized proteins to proteostasis stress ????J Cell Sci http://www.kidney.de/pget.php?&tw=1&pmid=27026526 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27026526 #FOAvip English Wikipedia <ref>{{Cite pmid|27026526}}</ref> Vulnerability of newly synthesized proteins to proteostasis stress #MMPMID27026526 Xu G; Pattamatta A; Hildago R; Pace MC; Brown H; Borchelt DR J Cell Sci 2016[May]; 129 (9): 1892-901 PMID27026526show ga The capacity of the cell to produce, fold and degrade proteins relies on components of the proteostasis network. Multiple types of insults can impose a burden on this network, causing protein misfolding. Using thermal stress, a classic example of acute proteostatic stress, we demonstrate that ?5?10% of the soluble cytosolic and nuclear proteome in human HEK293 cells is vulnerable to misfolding when proteostatic function is overwhelmed. Inhibiting new protein synthesis for 30?min prior to heat-shock dramatically reduced the amount of heat-stress induced polyubiquitylation, and reduced the misfolding of proteins identified as vulnerable to thermal stress. Following prior studies in C. elegans in which mutant huntingtin (Q103) expression was shown to cause the secondary misfolding of cytosolic proteins, we also demonstrate that mutant huntingtin causes similar ?secondary? misfolding in human cells. Similar to thermal stress, inhibiting new protein synthesis reduced the impact of mutant huntingtin on proteostatic function. These findings suggest that newly made proteins are vulnerable to misfolding when proteostasis is disrupted by insults such as thermal stress and mutant protein aggregation. äVulnerability of newly synthesized proteins to proteostasis stress (epmc).pdf DeepDyve Pubget Overpricing