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10.1093/jb/mvv125 http://scihub22266oqcxt.onion/10.1093/jb/mvv125 C4885936!4885936!26839319     free     free     free Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Biochem 2016 ; 159 (4): 379-85 Nephropedia Template TP {{tp|p=26839319|t=2016. Phospho-ubiquitin: upending the PINK?Parkin?ubiquitin cascade |pdf=|usr=}}{{26839319}} gab.com Text Phospho-ubiquitin: upending the PINK Parkin ubiquitin cascade JO: J Biochem http://www.kidney.de/pget.php?&tw=1&pmid=26839319 #FOAvip Mitochondria with decreased membrane potential are characterized by defects in protein import into the matrix and impairments in high-efficiency synthesis of ATP. These low-quality mitochondria are marked with ubiquitin for selective degradation. Key factors in this mechanism are PTEN-induced putative kinase 1 (PINK1, a mitochondrial kinase) and Parkin (a ubiquitin ligase), disruption of which has been implicated in predisposition to Parkinson?s disease. Previously, the clearance of damaged mitochondria had been thought to be the end result of a simple cascading reaction of PINK1?Parkin?ubiquitin. However, in the past year, several research groups including ours unexpectedly revealed that Parkin regulation is mediated by PINK1-dependent phosphorylation of ubiquitin. These results overturned the simple hierarchy that posited PINK1 and ubiquitin as the upstream and downstream factors of Parkin, respectively. Although ubiquitylation is well-known as a post-translational modification, it has recently become clear that ubiquitin itself can be modified, and that this modification unexpectedly converts ubiquitin to a factor that functions in retrograde signalling. Twit Text FOAVip Phospho-ubiquitin: upending the PINK Parkin ubiquitin cascade ????J Biochem http://www.kidney.de/pget.php?&tw=1&pmid=26839319 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26839319 #FOAvip English Wikipedia <ref>{{Cite pmid|26839319}}</ref> Phospho-ubiquitin: upending the PINK?Parkin?ubiquitin cascade #MMPMID26839319 Matsuda N J Biochem 2016[Apr]; 159 (4): 379-85 PMID26839319show ga Mitochondria with decreased membrane potential are characterized by defects in protein import into the matrix and impairments in high-efficiency synthesis of ATP. These low-quality mitochondria are marked with ubiquitin for selective degradation. Key factors in this mechanism are PTEN-induced putative kinase 1 (PINK1, a mitochondrial kinase) and Parkin (a ubiquitin ligase), disruption of which has been implicated in predisposition to Parkinson?s disease. Previously, the clearance of damaged mitochondria had been thought to be the end result of a simple cascading reaction of PINK1?Parkin?ubiquitin. However, in the past year, several research groups including ours unexpectedly revealed that Parkin regulation is mediated by PINK1-dependent phosphorylation of ubiquitin. These results overturned the simple hierarchy that posited PINK1 and ubiquitin as the upstream and downstream factors of Parkin, respectively. Although ubiquitylation is well-known as a post-translational modification, it has recently become clear that ubiquitin itself can be modified, and that this modification unexpectedly converts ubiquitin to a factor that functions in retrograde signalling. äPhospho-ubiquitin: upending the PINK?Parkin?ubiquitin cascade (epmc).pdf DeepDyve Pubget Overpricing