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10.1016/j.ceb.2016.01.001 http://scihub22266oqcxt.onion/10.1016/j.ceb.2016.01.001 C4887320!4887320!26803745     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       Curr+Opin+Cell+Biol 2016 ; 40 (ä): 1-7 Nephropedia Template TP {{tp|p=26803745|t=2016. Torsin ATPases: Structural insights and functional perspectives |pdf=|usr=}}{{26803745}} gab.com Text Torsin ATPases: Structural insights and functional perspectives JO: Curr Opin Cell Biol http://www.kidney.de/pget.php?&tw=1&pmid=26803745 #FOAvip Torsin ATPases are the only members of the AAA+ ATPase family that localize to the endoplasmic reticulum and contiguous perinuclear space. Accordingly, they are well positioned to perform essential work in these compartments, but their precise functions remain elusive. Recent studies have deciphered an unusual ATPase activation mechanism relying on Torsin-associated transmembrane cofactors, LAP1 or LULL1. These findings profoundly change our molecular view of the Torsin machinery and rationalize several human mutations in TorsinA or LAP1 leading to congenital disorders, symptoms of which have recently been recapitulated in mouse models. Here, we review these recent advances in the Torsin field and discuss the most pressing questions in relation to nuclear envelope dynamics. Twit Text FOAVip Torsin ATPases: Structural insights and functional perspectives ????Curr Opin Cell Biol http://www.kidney.de/pget.php?&tw=1&pmid=26803745 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26803745 #FOAvip English Wikipedia <ref>{{Cite pmid|26803745}}</ref> Torsin ATPases: Structural insights and functional perspectives #MMPMID26803745 Laudermilch E; Schlieker C Curr Opin Cell Biol 2016[Jun]; 40 (ä): 1-7 PMID26803745show ga Torsin ATPases are the only members of the AAA+ ATPase family that localize to the endoplasmic reticulum and contiguous perinuclear space. Accordingly, they are well positioned to perform essential work in these compartments, but their precise functions remain elusive. Recent studies have deciphered an unusual ATPase activation mechanism relying on Torsin-associated transmembrane cofactors, LAP1 or LULL1. These findings profoundly change our molecular view of the Torsin machinery and rationalize several human mutations in TorsinA or LAP1 leading to congenital disorders, symptoms of which have recently been recapitulated in mouse models. Here, we review these recent advances in the Torsin field and discuss the most pressing questions in relation to nuclear envelope dynamics. äTorsin ATPases: Structural insights and functional perspectives (epmc).pdf DeepDyve Pubget Overpricing