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10.1002/pro.2415 http://scihub22266oqcxt.onion/10.1002/pro.2415 C3970886!3970886 !24403057     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=24403057 &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\24403057 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Protein+Sci 2014 ; 23 (4 ): 344-53 Nephropedia Template TP {{tp|p=24403057 |t=2014. Mechanisms for regulating deubiquitinating enzymes |pdf=|usr=}}{{24403057 }} gab.com Text Mechanisms for regulating deubiquitinating enzymes JO: Protein Sci http://www.kidney.de/pget.php?&tw=1&pmid=24403057 #FOAvip Ubiquitination is a reversible post-translational modification that plays a dynamic role in regulating most eukaryotic processes. Deubiquitinating enzymes (DUBs), which hydrolyze the isopeptide or peptide linkages joining ubiquitin to substrate lysines or N-termini, therefore play a key role in ubiquitin signaling. Cells employ multiple mechanisms to regulate DUB activity and thus ensure the appropriate biological response. Recent structural studies have shed light on several different mechanisms by which DUB activity and specificity is regulated. Twit Text FOAVip Mechanisms for regulating deubiquitinating enzymes ????Protein Sci http://www.kidney.de/pget.php?&tw=1&pmid=24403057 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=24403057 #FOAvip English Wikipedia <ref>{{Cite pmid|24403057 }}</ref> Mechanisms for regulating deubiquitinating enzymes #MMPMID24403057 Wolberger C Protein Sci 2014[Apr]; 23 (4 ): 344-53 PMID24403057 show ga Ubiquitination is a reversible post-translational modification that plays a dynamic role in regulating most eukaryotic processes. Deubiquitinating enzymes (DUBs), which hydrolyze the isopeptide or peptide linkages joining ubiquitin to substrate lysines or N-termini, therefore play a key role in ubiquitin signaling. Cells employ multiple mechanisms to regulate DUB activity and thus ensure the appropriate biological response. Recent structural studies have shed light on several different mechanisms by which DUB activity and specificity is regulated. |Humans [MESH] |Models, Molecular [MESH] |Peptides/chemistry/metabolism [MESH] |Signal Transduction [MESH] |Ubiquitin-Specific Proteases/chemistry/genetics/*metabolism [MESH] |Ubiquitin/chemistry/metabolism [MESH]Mechanisms for regulating deubiquitinating enzymes (epmc).pdf DeepDyve Pubget Overpricing