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10.3390/mps1010003 http://scihub22266oqcxt.onion/10.3390/mps1010003 C5809138!5809138!29451563     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 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Methods+Protoc 2018 ; 1 (1): ä Nephropedia Template TP {{tp|p=29451563|t=2018. A Highly Sensitive Non-Radioactive Activity Assay for AMP-Activated Protein Kinase (AMPK) |pdf=|usr=}}{{29451563}} gab.com Text A Highly Sensitive Non-Radioactive Activity Assay for AMP-Activated Protein Kinase (AMPK) JO: Methods Protoc http://www.kidney.de/pget.php?&tw=1&pmid=29451563 #FOAvip While many methods exist to quantitatively determine protein kinase activities, 32P-based radioactive assays remain the workhorse of many laboratories due to their high sensitivity, high signal to noise ratio, lack of interference by fluorescent and light-absorbing small molecules, and easy quantitation. Here, we demonstrate that the interaction between the yeast Rad53 Forkhead-associated (FHA) domain and a peptide optimized for phosphorylation by AMP-Activated Protein Kinase (AMPK), which has previously been exploited for the generation of intracellular phosphorylation sensors, can serve as a readout for a highly sensitive two-step AMPK AlphaScreen kinase assay with exceptional signal-to-noise ratio. Twit Text FOAVip A Highly Sensitive Non-Radioactive Activity Assay for AMP-Activated Protein Kinase (AMPK) ????Methods Protoc http://www.kidney.de/pget.php?&tw=1&pmid=29451563 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=29451563 #FOAvip English Wikipedia <ref>{{Cite pmid|29451563}}</ref> A Highly Sensitive Non-Radioactive Activity Assay for AMP-Activated Protein Kinase (AMPK) #MMPMID29451563 Yan Y; Gu X; Xu HE; Melcher K Methods Protoc 2018[Mar]; 1 (1): ä PMID29451563show ga While many methods exist to quantitatively determine protein kinase activities, 32P-based radioactive assays remain the workhorse of many laboratories due to their high sensitivity, high signal to noise ratio, lack of interference by fluorescent and light-absorbing small molecules, and easy quantitation. Here, we demonstrate that the interaction between the yeast Rad53 Forkhead-associated (FHA) domain and a peptide optimized for phosphorylation by AMP-Activated Protein Kinase (AMPK), which has previously been exploited for the generation of intracellular phosphorylation sensors, can serve as a readout for a highly sensitive two-step AMPK AlphaScreen kinase assay with exceptional signal-to-noise ratio. äA Highly Sensitive Non-Radioactive Activity Assay for AMP-Activated Pr(epmc).pdf DeepDyve Pubget Overpricing