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10.1073/pnas.1620813114 http://scihub22266oqcxt.onion/10.1073/pnas.1620813114 C5358389!5358389!28242696     free     free     free Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Proc+Natl+Acad+Sci+U+S+A 2017 ; 114 (11): E2096-105 Nephropedia Template TP {{tp|p=28242696|t=2017. Structural basis of autoregulatory scaffolding by apoptosis signal-regulating kinase 1 |pdf=|usr=}}{{28242696}} gab.com Text Structural basis of autoregulatory scaffolding by apoptosis signal-regulating kinase 1 JO: Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=28242696 #FOAvip Phosphorylation catalyzed by protein kinases governs many aspects of cellular behavior. Apoptosis signal-regulating kinases (ASK1?3) trigger responses to stress, but the structural basis of their regulation remains unclear. Here, we show that a domain directly adjacent to the ASK1 kinase domain promotes activity of ASK1 on a key substrate and also orients an additional ASK1 domain nearby to suppress kinase activity. The structure of this regulatory domain appears to be shared by all ASK kinases and provides a versatile mechanism to control ASK activity in response to various stress stimuli. Twit Text FOAVip Structural basis of autoregulatory scaffolding by apoptosis signal-regulating kinase 1 ????Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=28242696 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28242696 #FOAvip English Wikipedia <ref>{{Cite pmid|28242696}}</ref> Structural basis of autoregulatory scaffolding by apoptosis signal-regulating kinase 1 #MMPMID28242696 Weijman JF; Kumar A; Jamieson SA; King CM; Caradoc-Davies TT; Ledgerwood EC; Murphy JM; Mace PD Proc Natl Acad Sci U S A 2017[Mar]; 114 (11): E2096-105 PMID28242696show ga Phosphorylation catalyzed by protein kinases governs many aspects of cellular behavior. Apoptosis signal-regulating kinases (ASK1?3) trigger responses to stress, but the structural basis of their regulation remains unclear. Here, we show that a domain directly adjacent to the ASK1 kinase domain promotes activity of ASK1 on a key substrate and also orients an additional ASK1 domain nearby to suppress kinase activity. The structure of this regulatory domain appears to be shared by all ASK kinases and provides a versatile mechanism to control ASK activity in response to various stress stimuli. äStructural basis of autoregulatory scaffolding by apoptosis signal-reg(epmc).pdf DeepDyve Pubget Overpricing