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10.1038/s41467-017-00628-y http://scihub22266oqcxt.onion/10.1038/s41467-017-00628-y C5603566!5603566!28924239     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=28924239&cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215 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       Nat+Commun 2017 ; 8 (ä): ä Nephropedia Template TP {{tp|p=28924239|t=2017. The autophagy initiator ULK1 sensitizes AMPK to allosteric drugs |pdf=|usr=}}{{28924239}} gab.com Text The autophagy initiator ULK1 sensitizes AMPK to allosteric drugs JO: Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=28924239 #FOAvip AMP-activated protein kinase (AMPK) is a metabolic stress-sensing enzyme responsible for maintaining cellular energy homeostasis. Activation of AMPK by salicylate and the thienopyridone A-769662 is critically dependent on phosphorylation of Ser108 in the ?1 regulatory subunit. Here, we show a possible role for Ser108 phosphorylation in cell cycle regulation and promotion of pro-survival pathways in response to energy stress. We identify the autophagy initiator Unc-51-like kinase 1 (ULK1) as a ?1-Ser108 kinase in cells. Cellular ?1-Ser108 phosphorylation by ULK1 was dependent on AMPK ?-subunit myristoylation, metabolic stress associated with elevated AMP/ATP ratio, and the intrinsic energy sensing capacity of AMPK; features consistent with an AMP-induced myristoyl switch mechanism. We further demonstrate cellular AMPK signaling independent of activation loop Thr172 phosphorylation, providing potential insight into physiological roles for Ser108 phosphorylation. These findings uncover new mechanisms by which AMPK could potentially maintain cellular energy homeostasis independently of Thr172 phosphorylation. Twit Text FOAVip The autophagy initiator ULK1 sensitizes AMPK to allosteric drugs ????Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=28924239 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28924239 #FOAvip English Wikipedia <ref>{{Cite pmid|28924239}}</ref> The autophagy initiator ULK1 sensitizes AMPK to allosteric drugs #MMPMID28924239 Dite TA; Ling NXY; Scott JW; Hoque A; Galic S; Parker BL; Ngoei KRW; Langendorf CG; O?Brien MT; Kundu M; Viollet B; Steinberg GR; Sakamoto K; Kemp BE; Oakhill JS Nat Commun 2017[]; 8 (ä): ä PMID28924239show ga AMP-activated protein kinase (AMPK) is a metabolic stress-sensing enzyme responsible for maintaining cellular energy homeostasis. Activation of AMPK by salicylate and the thienopyridone A-769662 is critically dependent on phosphorylation of Ser108 in the ?1 regulatory subunit. Here, we show a possible role for Ser108 phosphorylation in cell cycle regulation and promotion of pro-survival pathways in response to energy stress. We identify the autophagy initiator Unc-51-like kinase 1 (ULK1) as a ?1-Ser108 kinase in cells. Cellular ?1-Ser108 phosphorylation by ULK1 was dependent on AMPK ?-subunit myristoylation, metabolic stress associated with elevated AMP/ATP ratio, and the intrinsic energy sensing capacity of AMPK; features consistent with an AMP-induced myristoyl switch mechanism. We further demonstrate cellular AMPK signaling independent of activation loop Thr172 phosphorylation, providing potential insight into physiological roles for Ser108 phosphorylation. These findings uncover new mechanisms by which AMPK could potentially maintain cellular energy homeostasis independently of Thr172 phosphorylation. äThe autophagy initiator ULK1 sensitizes AMPK to allosteric drugs (epmc).pdf DeepDyve Pubget Overpricing