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10.3389/fnmol.2017.00078 http://scihub22266oqcxt.onion/10.3389/fnmol.2017.00078 C5360718!5360718!28381987     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 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       Front+Mol+Neurosci 2017 ; 10 (ä): ä Nephropedia Template TP {{tp|p=28381987|t=2017. The Ubiquitination, Disaggregation and Proteasomal Degradation Machineries in Polyglutamine Disease |pdf=|usr=}}{{28381987}} gab.com Text The Ubiquitination, Disaggregation and Proteasomal Degradation Machineries in Polyglutamine Disease JO: Front Mol Neurosci http://www.kidney.de/pget.php?&tw=1&pmid=28381987 #FOAvip Polyglutamine disorders are chronic, progressive neurodegenerative diseases caused by expansion of a glutamine tract in widely expressed genes. Despite excellent models of disease, a well-documented clinical history and progression, and established genetic causes, there are no FDA approved, disease modifying treatments for these disorders. Downstream of the mutant protein, several divergent pathways of toxicity have been identified over the last several decades, supporting the idea that targeting only one of these pathways of toxicity is unlikely to robustly alleviate disease progression. As a result, a vast body of research has focused on eliminating the mutant protein to broadly prevent downstream toxicity, either by silencing mutant protein expression or leveraging the endogenous protein quality control machinery. In the latter approach, a focus has been placed on four critical components of mutant protein degradation that are active in the nucleus, a key site of toxicity: disaggregation, ubiquitination, deubiquitination, and proteasomal activity. These machineries have unique functional components, but work together as a cellular defense system that can be successfully leveraged to alleviate disease phenotypes in several models of polyglutamine toxicity. This review will highlight recent advances in understanding both the potential and role of these components of the protein quality control machinery in polyglutamine disease pathophysiology. Twit Text FOAVip The Ubiquitination, Disaggregation and Proteasomal Degradation Machineries in Polyglutamine Disease ????Front Mol Neurosci http://www.kidney.de/pget.php?&tw=1&pmid=28381987 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28381987 #FOAvip English Wikipedia <ref>{{Cite pmid|28381987}}</ref> The Ubiquitination, Disaggregation and Proteasomal Degradation Machineries in Polyglutamine Disease #MMPMID28381987 Nath SR; Lieberman AP Front Mol Neurosci 2017[]; 10 (ä): ä PMID28381987show ga Polyglutamine disorders are chronic, progressive neurodegenerative diseases caused by expansion of a glutamine tract in widely expressed genes. Despite excellent models of disease, a well-documented clinical history and progression, and established genetic causes, there are no FDA approved, disease modifying treatments for these disorders. Downstream of the mutant protein, several divergent pathways of toxicity have been identified over the last several decades, supporting the idea that targeting only one of these pathways of toxicity is unlikely to robustly alleviate disease progression. As a result, a vast body of research has focused on eliminating the mutant protein to broadly prevent downstream toxicity, either by silencing mutant protein expression or leveraging the endogenous protein quality control machinery. In the latter approach, a focus has been placed on four critical components of mutant protein degradation that are active in the nucleus, a key site of toxicity: disaggregation, ubiquitination, deubiquitination, and proteasomal activity. These machineries have unique functional components, but work together as a cellular defense system that can be successfully leveraged to alleviate disease phenotypes in several models of polyglutamine toxicity. This review will highlight recent advances in understanding both the potential and role of these components of the protein quality control machinery in polyglutamine disease pathophysiology. äThe Ubiquitination, Disaggregation and Proteasomal Degradation Machine(epmc).pdf DeepDyve Pubget Overpricing