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10.1038/cr.2016.38 http://scihub22266oqcxt.onion/10.1038/cr.2016.38 C4822132!4822132 !27012468     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=27012468 &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 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\27012468 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Cell+Res 2016 ; 26 (4 ): 441-56 Nephropedia Template TP {{tp|p=27012468 |t=2016. Substrate specificity of the ubiquitin and Ubl proteases |pdf=|usr=}}{{27012468 }} gab.com Text Substrate specificity of the ubiquitin and Ubl proteases JO: Cell Res http://www.kidney.de/pget.php?&tw=1&pmid=27012468 #FOAvip Conjugation and deconjugation of ubiquitin and ubiquitin-like proteins (Ubls) to cellular proteins are highly regulated processes integral to cellular homeostasis. Most often, the C-termini of these small polypeptides are attached to lysine side chains of target proteins by an amide (isopeptide) linkage. Deubiquitinating enzymes (DUBs) and Ubl-specific proteases (ULPs) comprise a diverse group of proteases that recognize and remove ubiquitin and Ubls from their substrates. How DUBs and ULPs distinguish among different modifiers, or different polymeric forms of these modifiers, remains poorly understood. The specificity of ubiquitin/Ubl-deconjugating enzymes for particular substrates depends on multiple factors, ranging from the topography of specific substrate features, as in different polyubiquitin chain types, to structural elements unique to each enzyme. Here we summarize recent structural and biochemical studies that provide insights into mechanisms of substrate specificity among various DUBs and ULPs. We also discuss the unexpected specificities of non-eukaryotic proteases in these families. Twit Text FOAVip Substrate specificity of the ubiquitin and Ubl proteases ????Cell Res http://www.kidney.de/pget.php?&tw=1&pmid=27012468 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27012468 #FOAvip English Wikipedia <ref>{{Cite pmid|27012468 }}</ref> Substrate specificity of the ubiquitin and Ubl proteases #MMPMID27012468 Ronau JA ; Beckmann JF ; Hochstrasser M Cell Res 2016[Apr]; 26 (4 ): 441-56 PMID27012468 show ga Conjugation and deconjugation of ubiquitin and ubiquitin-like proteins (Ubls) to cellular proteins are highly regulated processes integral to cellular homeostasis. Most often, the C-termini of these small polypeptides are attached to lysine side chains of target proteins by an amide (isopeptide) linkage. Deubiquitinating enzymes (DUBs) and Ubl-specific proteases (ULPs) comprise a diverse group of proteases that recognize and remove ubiquitin and Ubls from their substrates. How DUBs and ULPs distinguish among different modifiers, or different polymeric forms of these modifiers, remains poorly understood. The specificity of ubiquitin/Ubl-deconjugating enzymes for particular substrates depends on multiple factors, ranging from the topography of specific substrate features, as in different polyubiquitin chain types, to structural elements unique to each enzyme. Here we summarize recent structural and biochemical studies that provide insights into mechanisms of substrate specificity among various DUBs and ULPs. We also discuss the unexpected specificities of non-eukaryotic proteases in these families. |Catalytic Domain [MESH] |Deubiquitinating Enzymes/metabolism [MESH] |Humans [MESH] |Protein Conformation [MESH] |Structure-Activity Relationship [MESH] |Substrate Specificity [MESH] |Ubiquitin/chemistry/*metabolism [MESH]Substrate specificity of the ubiquitin and Ubl proteases (epmc).pdf DeepDyve Pubget Overpricing