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10.1016/j.cell.2015.08.057 http://scihub22266oqcxt.onion/10.1016/j.cell.2015.08.057 C4644237!4644237!26388442     free     free     free Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Cell 2015 ; 163 (1): 187-201 Nephropedia Template TP {{tp|p=26388442|t=2015. Unmasking Determinants of Specificity in the Human Kinome |pdf=|usr=}}{{26388442}} gab.com Text Unmasking Determinants of Specificity in the Human Kinome JO: Cell http://www.kidney.de/pget.php?&tw=1&pmid=26388442 #FOAvip Protein kinases control cellular responses to environmental cues by swift and accurate signal processing. Breakdowns in this high-fidelity capability are a driving force in cancer and other diseases. Thus, our limited understanding of which amino acids in the kinase domain encode substrate specificity, the so-called determinants of specificity (DoS), constitutes a major obstacle in cancer signaling. Here, we systematically discover several DoS and experimentally validate three of them, named the ?C1, ?C3, and APE-7 residues. We demonstrate that DoS form sparse networks of non-conserved residues spanning distant regions. Our results reveal a likely role for inter-residue allostery in specificity and an evolutionary decoupling of kinase activity and specificity, which appear loaded on independent groups of residues. Finally, we uncover similar properties driving SH2 domain specificity and demonstrate how the identification of DoS can be utilized to elucidate a greater understanding of the role of signaling networks in cancer (Creixell et al., 2015 [this issue of Cell]). Twit Text FOAVip Unmasking Determinants of Specificity in the Human Kinome ????Cell http://www.kidney.de/pget.php?&tw=1&pmid=26388442 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26388442 #FOAvip English Wikipedia <ref>{{Cite pmid|26388442}}</ref> Unmasking Determinants of Specificity in the Human Kinome #MMPMID26388442 Creixell P; Palmeri A; Miller C; Lou H; Santini C; Nielsen M; Turk B; Linding R Cell 2015[Sep]; 163 (1): 187-201 PMID26388442show ga Protein kinases control cellular responses to environmental cues by swift and accurate signal processing. Breakdowns in this high-fidelity capability are a driving force in cancer and other diseases. Thus, our limited understanding of which amino acids in the kinase domain encode substrate specificity, the so-called determinants of specificity (DoS), constitutes a major obstacle in cancer signaling. Here, we systematically discover several DoS and experimentally validate three of them, named the ?C1, ?C3, and APE-7 residues. We demonstrate that DoS form sparse networks of non-conserved residues spanning distant regions. Our results reveal a likely role for inter-residue allostery in specificity and an evolutionary decoupling of kinase activity and specificity, which appear loaded on independent groups of residues. Finally, we uncover similar properties driving SH2 domain specificity and demonstrate how the identification of DoS can be utilized to elucidate a greater understanding of the role of signaling networks in cancer (Creixell et al., 2015 [this issue of Cell]). äUnmasking Determinants of Specificity in the Human Kinome (epmc).pdf DeepDyve Pubget Overpricing