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10.1002/pmic.201600437 http://scihub22266oqcxt.onion/10.1002/pmic.201600437 C5526339!5526339 !28165663     free     free     free Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\28165663 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Proteomics 2017 ; 17 (6 ): ä Nephropedia Template TP {{tp|p=28165663 |t=2017. Interrogating the hidden phosphoproteome |pdf=|usr=}}{{28165663 }} gab.com Text Interrogating the hidden phosphoproteome JO: Proteomics http://www.kidney.de/pget.php?&tw=1&pmid=28165663 #FOAvip Postgenomic studies continue to highlight the potential clinical importance of protein phosphorylation signaling pathways in drug discovery. Unfortunately, the dynamic range and variable stoichiometry of protein phosphorylation continues to stymie efforts to achieve comprehensive characterization of the human phosphoproteome. In this study, we develop a complementary, two-stage method for enrichment of cysteine-containing phosphopeptides combined with TMT multiplex labeling for relative quantification. The use of this approach with multidimensional fractionation in mammalian cells yielded more than 7000 unique cys-phosphopeptide sequences, comprising 15-20% novel phosphorylation sites. The use of our approach in combination with pharmacologic inhibitors of the mechanistic target of rapamycin complex 1 and 2 identified several putatively novel protein substrates for the mechanistic target of rapamycin kinase. Twit Text FOAVip Interrogating the hidden phosphoproteome ????Proteomics http://www.kidney.de/pget.php?&tw=1&pmid=28165663 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28165663 #FOAvip English Wikipedia <ref>{{Cite pmid|28165663 }}</ref> Interrogating the hidden phosphoproteome #MMPMID28165663 Kang UB ; Alexander WM ; Marto JA Proteomics 2017[Mar]; 17 (6 ): ä PMID28165663 show ga Postgenomic studies continue to highlight the potential clinical importance of protein phosphorylation signaling pathways in drug discovery. Unfortunately, the dynamic range and variable stoichiometry of protein phosphorylation continues to stymie efforts to achieve comprehensive characterization of the human phosphoproteome. In this study, we develop a complementary, two-stage method for enrichment of cysteine-containing phosphopeptides combined with TMT multiplex labeling for relative quantification. The use of this approach with multidimensional fractionation in mammalian cells yielded more than 7000 unique cys-phosphopeptide sequences, comprising 15-20% novel phosphorylation sites. The use of our approach in combination with pharmacologic inhibitors of the mechanistic target of rapamycin complex 1 and 2 identified several putatively novel protein substrates for the mechanistic target of rapamycin kinase. |Computer Simulation [MESH] |Cysteine/metabolism [MESH] |HEK293 Cells [MESH] |Humans [MESH] |Phosphopeptides/metabolism [MESH] |Phosphoproteins/*metabolism [MESH] |Proteome/*metabolism [MESH] |Proteomics/*methods [MESH] |Signal Transduction [MESH] |Substrate Specificity [MESH]Interrogating the hidden phosphoproteome (epmc).pdf DeepDyve Pubget Overpricing