Use my Search Websuite to scan PubMed, PMCentral, Journal Hosts and Journal Archives, FullText. Kick-your-searchterm to multiple Engines kick-your-query now !>

A dictionary by aggregated review articles of nephrology, medicine and the life sciences Your one-stop-run pathway from word to the immediate pdf of peer-reviewed on-topic knowledge.

10.1074/jbc.M115.649269 http://scihub22266oqcxt.onion/10.1074/jbc.M115.649269 C4583040!4583040!26245901     free     free     free Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Biol+Chem 2015 ; 290 (39): 23875-87 Nephropedia Template TP {{tp|p=26245901|t=2015. Itch WW Domains Inhibit Its E3 Ubiquitin Ligase Activity by Blocking E2-E3 Ligase Trans-thiolation* |pdf=|usr=}}{{26245901}} gab.com Text Itch WW Domains Inhibit Its E3 Ubiquitin Ligase Activity by Blocking E2-E3 Ligase Trans-thiolation* JO: J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=26245901 #FOAvip Background: The activity of Itch and related E3 ligases is restricted by autoinhibition.Results: Itch autoinhibition is maintained by an intramolecular interaction between its WW and HECT domains, and Ndfip1 relieves this interaction to allow trans-thiolation.Conclusion: The primary role of Ndfip is to relieve autoinhibition of Itch and related ligases.Significance: We describe a novel mechanism that regulates the activity of several catalytic E3 ligases. Twit Text FOAVip Itch WW Domains Inhibit Its E3 Ubiquitin Ligase Activity by Blocking E2-E3 Ligase Trans-thiolation* ????J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=26245901 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26245901 #FOAvip English Wikipedia <ref>{{Cite pmid|26245901}}</ref> Itch WW Domains Inhibit Its E3 Ubiquitin Ligase Activity by Blocking E2-E3 Ligase Trans-thiolation* #MMPMID26245901 Riling C; Kamadurai H; Kumar S; O'Leary CE; Wu KP; Manion EE; Ying M; Schulman BA; Oliver PM J Biol Chem 2015[Sep]; 290 (39): 23875-87 PMID26245901show ga Background: The activity of Itch and related E3 ligases is restricted by autoinhibition.Results: Itch autoinhibition is maintained by an intramolecular interaction between its WW and HECT domains, and Ndfip1 relieves this interaction to allow trans-thiolation.Conclusion: The primary role of Ndfip is to relieve autoinhibition of Itch and related ligases.Significance: We describe a novel mechanism that regulates the activity of several catalytic E3 ligases. äItch WW Domains Inhibit Its E3 Ubiquitin Ligase Activity by Blocking E(epmc).pdf DeepDyve Pubget Overpricing