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10.1016/j.tcb.2015.10.013 http://scihub22266oqcxt.onion/10.1016/j.tcb.2015.10.013 C5881568!5881568!26616193     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       Trends+Cell+Biol 2016 ; 26 (3): 190-201 Nephropedia Template TP {{tp|p=26616193|t=2016. AMPK: an energy-sensing pathway with multiple inputs and outputs |pdf=|usr=}}{{26616193}} gab.com Text AMPK: an energy-sensing pathway with multiple inputs and outputs JO: Trends Cell Biol http://www.kidney.de/pget.php?&tw=1&pmid=26616193 #FOAvip The AMP-activated protein kinase (AMPK) is a key regulator of energy balance expressed ubiquitously in eukaryotic cells. Here, we review the canonical adenine nucleotide-dependent mechanism that activates AMPK when cellular energy status is compromised, as well as other, non-canonical activation mechanisms. Once activated, AMPK acts to restore energy homeostasis by promoting catabolic pathways, resulting in ATP generation, and inhibiting anabolic pathways that consume ATP. We also review the various hypothesis-driven and unbiased approaches that have been used to identify AMPK substrates, which have revealed substrates involved in both metabolic and non-metabolic processes. We particularly focus on methods for identifying the AMPK target recognition motif, and how it can be used to predict new substrates. Twit Text FOAVip AMPK: an energy-sensing pathway with multiple inputs and outputs ????Trends Cell Biol http://www.kidney.de/pget.php?&tw=1&pmid=26616193 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26616193 #FOAvip English Wikipedia <ref>{{Cite pmid|26616193}}</ref> AMPK: an energy-sensing pathway with multiple inputs and outputs #MMPMID26616193 Hardie DG; Schaffer BE; Brunet A Trends Cell Biol 2016[Mar]; 26 (3): 190-201 PMID26616193show ga The AMP-activated protein kinase (AMPK) is a key regulator of energy balance expressed ubiquitously in eukaryotic cells. Here, we review the canonical adenine nucleotide-dependent mechanism that activates AMPK when cellular energy status is compromised, as well as other, non-canonical activation mechanisms. Once activated, AMPK acts to restore energy homeostasis by promoting catabolic pathways, resulting in ATP generation, and inhibiting anabolic pathways that consume ATP. We also review the various hypothesis-driven and unbiased approaches that have been used to identify AMPK substrates, which have revealed substrates involved in both metabolic and non-metabolic processes. We particularly focus on methods for identifying the AMPK target recognition motif, and how it can be used to predict new substrates. äAMPK: an energy-sensing pathway with multiple inputs and outputs (epmc).pdf DeepDyve Pubget Overpricing