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10.1111/febs.13249 http://scihub22266oqcxt.onion/10.1111/febs.13249 C4672691!4672691 !25712550     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=25712550 &cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\25712550 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       FEBS+J 2015 ; 282 (11 ): 2076-88 Nephropedia Template TP {{tp|p=25712550 |t=2015. Parkin structure and function |pdf=|usr=}}{{25712550 }} gab.com Text Parkin structure and function JO: FEBS J http://www.kidney.de/pget.php?&tw=1&pmid=25712550 #FOAvip Mutations in the parkin or PINK1 genes are the leading cause of the autosomal recessive form of Parkinson's disease. The gene products, the E3 ubiquitin ligase parkin and the serine/threonine kinase PINK1, are neuroprotective proteins, which act together in a mitochondrial quality control pathway. Here, we review the structure of parkin and mechanisms of its autoinhibition and function as a ubiquitin ligase. We present a model for the recruitment and activation of parkin as a key regulatory step in the clearance of depolarized or damaged mitochondria by autophagy (mitophagy). We conclude with a brief overview of other functions of parkin and considerations for drug discovery in the mitochondrial quality control pathway. Twit Text FOAVip Parkin structure and function ????FEBS J http://www.kidney.de/pget.php?&tw=1&pmid=25712550 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25712550 #FOAvip English Wikipedia <ref>{{Cite pmid|25712550 }}</ref> Parkin structure and function #MMPMID25712550 Seirafi M ; Kozlov G ; Gehring K FEBS J 2015[Jun]; 282 (11 ): 2076-88 PMID25712550 show ga Mutations in the parkin or PINK1 genes are the leading cause of the autosomal recessive form of Parkinson's disease. The gene products, the E3 ubiquitin ligase parkin and the serine/threonine kinase PINK1, are neuroprotective proteins, which act together in a mitochondrial quality control pathway. Here, we review the structure of parkin and mechanisms of its autoinhibition and function as a ubiquitin ligase. We present a model for the recruitment and activation of parkin as a key regulatory step in the clearance of depolarized or damaged mitochondria by autophagy (mitophagy). We conclude with a brief overview of other functions of parkin and considerations for drug discovery in the mitochondrial quality control pathway. |Amino Acid Sequence [MESH] |Animals [MESH] |Humans [MESH] |Mitochondria/enzymology [MESH] |Mitophagy [MESH] |Molecular Sequence Data [MESH] |Neurons/enzymology [MESH] |Parkinson Disease/*enzymology/pathology [MESH] |Protein Transport [MESH] |Ubiquitin-Protein Ligases/chemistry/*physiology [MESH]Parkin structure and function (epmc).pdf DeepDyve Pubget Overpricing