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.

10.1016/j.cell.2016.05.048 http://scihub22266oqcxt.onion/10.1016/j.cell.2016.05.048 C4946995!4946995!27321670     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       Cell 2016 ; 166 (2): 394-407 Nephropedia Template TP {{tp|p=27321670|t=2016. Autoubiquitination of the Hrd1 ligase triggers protein retrotranslocation in ERAD |pdf=|usr=}}{{27321670}} gab.com Text Autoubiquitination of the Hrd1 ligase triggers protein retrotranslocation in ERAD JO: Cell http://www.kidney.de/pget.php?&tw=1&pmid=27321670 #FOAvip Misfolded proteins of the endoplasmic reticulum (ER) are retrotranslocated to the cytosol, where they are polyubiquitinated, extracted from the membrane, and degraded by the proteasome. To investigate how the ER-associated Degradation (ERAD) machinery can accomplish retrotranslocation of a misfolded luminal protein domain across a lipid bilayer, we have reconstituted retrotranslocation with purified S. cerevisiae proteins, using proteoliposomes containing the multi-spanning ubiquitin ligase Hrd1. Retrotranslocation of the luminal domain of a membrane-spanning substrate is triggered by autoubiquitination of Hrd1. Substrate ubiquitination is a subsequent event, and the Cdc48 ATPase that completes substrate extraction from the membrane is not required for retrotranslocation. Ubiquitination of lysines in Hrd1?s RING-finger domain is required for substrate retrotranslocation in vitro and for ERAD in vivo. Our results suggest that Hrd1 forms a ubiquitin-gated protein-conducting channel. Twit Text FOAVip Autoubiquitination of the Hrd1 ligase triggers protein retrotranslocation in ERAD ????Cell http://www.kidney.de/pget.php?&tw=1&pmid=27321670 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27321670 #FOAvip English Wikipedia <ref>{{Cite pmid|27321670}}</ref> Autoubiquitination of the Hrd1 ligase triggers protein retrotranslocation in ERAD #MMPMID27321670 Baldridge RD; Rapoport TA Cell 2016[Jul]; 166 (2): 394-407 PMID27321670show ga Misfolded proteins of the endoplasmic reticulum (ER) are retrotranslocated to the cytosol, where they are polyubiquitinated, extracted from the membrane, and degraded by the proteasome. To investigate how the ER-associated Degradation (ERAD) machinery can accomplish retrotranslocation of a misfolded luminal protein domain across a lipid bilayer, we have reconstituted retrotranslocation with purified S. cerevisiae proteins, using proteoliposomes containing the multi-spanning ubiquitin ligase Hrd1. Retrotranslocation of the luminal domain of a membrane-spanning substrate is triggered by autoubiquitination of Hrd1. Substrate ubiquitination is a subsequent event, and the Cdc48 ATPase that completes substrate extraction from the membrane is not required for retrotranslocation. Ubiquitination of lysines in Hrd1?s RING-finger domain is required for substrate retrotranslocation in vitro and for ERAD in vivo. Our results suggest that Hrd1 forms a ubiquitin-gated protein-conducting channel. äAutoubiquitination of the Hrd1 ligase triggers protein retrotranslocat(epmc).pdf DeepDyve Pubget Overpricing