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10.1038/ncomms10239 http://scihub22266oqcxt.onion/10.1038/ncomms10239 C4729826!4729826 !26732515     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 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 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 245.2 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\26732515 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Nat+Commun 2016 ; 7 (ä): 10239 Nephropedia Template TP {{tp|p=26732515 |t=2016. Tripartite degrons confer diversity and specificity on regulated protein degradation in the ubiquitin-proteasome system |pdf=|usr=}}{{26732515 }} gab.com Text Tripartite degrons confer diversity and specificity on regulated protein degradation in the ubiquitin-proteasome system JO: Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=26732515 #FOAvip Specific signals (degrons) regulate protein turnover mediated by the ubiquitin-proteasome system. Here we systematically analyse known degrons and propose a tripartite model comprising the following: (1) a primary degron (peptide motif) that specifies substrate recognition by cognate E3 ubiquitin ligases, (2) secondary site(s) comprising a single or multiple neighbouring ubiquitinated lysine(s) and (3) a structurally disordered segment that initiates substrate unfolding at the 26S proteasome. Primary degron sequences are conserved among orthologues and occur in structurally disordered regions that undergo E3-induced folding-on-binding. Posttranslational modifications can switch primary degrons into E3-binding-competent states, thereby integrating degradation with signalling pathways. Degradation-linked lysines tend to be located within disordered segments that also initiate substrate degradation by effective proteasomal engagement. Many characterized mutations and alternative isoforms with abrogated degron components are implicated in disease. These effects result from increased protein stability and interactome rewiring. The distributed nature of degrons ensures regulation, specificity and combinatorial control of degradation. Twit Text FOAVip Tripartite degrons confer diversity and specificity on regulated protein degradation in the ubiquitin-proteasome system ????Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=26732515 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26732515 #FOAvip English Wikipedia <ref>{{Cite pmid|26732515 }}</ref> Tripartite degrons confer diversity and specificity on regulated protein degradation in the ubiquitin-proteasome system #MMPMID26732515 Guharoy M ; Bhowmick P ; Sallam M ; Tompa P Nat Commun 2016[Jan]; 7 (ä): 10239 PMID26732515 show ga Specific signals (degrons) regulate protein turnover mediated by the ubiquitin-proteasome system. Here we systematically analyse known degrons and propose a tripartite model comprising the following: (1) a primary degron (peptide motif) that specifies substrate recognition by cognate E3 ubiquitin ligases, (2) secondary site(s) comprising a single or multiple neighbouring ubiquitinated lysine(s) and (3) a structurally disordered segment that initiates substrate unfolding at the 26S proteasome. Primary degron sequences are conserved among orthologues and occur in structurally disordered regions that undergo E3-induced folding-on-binding. Posttranslational modifications can switch primary degrons into E3-binding-competent states, thereby integrating degradation with signalling pathways. Degradation-linked lysines tend to be located within disordered segments that also initiate substrate degradation by effective proteasomal engagement. Many characterized mutations and alternative isoforms with abrogated degron components are implicated in disease. These effects result from increased protein stability and interactome rewiring. The distributed nature of degrons ensures regulation, specificity and combinatorial control of degradation. |*Proteolysis [MESH] |Animals [MESH] |Gene Expression Regulation [MESH] |Humans [MESH] |Mammals [MESH] |Models, Molecular [MESH] |Proteasome Endopeptidase Complex/*metabolism [MESH] |Protein Conformation [MESH] |Proteins/genetics/*metabolism [MESH]Tripartite degrons confer diversity and specificity on regulated prote(epmc).pdf DeepDyve Pubget Overpricing