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10.1073/pnas.1609675114 http://scihub22266oqcxt.onion/10.1073/pnas.1609675114 C5206511!5206511!27956599     free     free     free Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Proc+Natl+Acad+Sci+U+S+A 2016 ; 113 (52): 14976-81 Nephropedia Template TP {{tp|p=27956599|t=2016. Mimicking transient activation of protein kinases in living cells |pdf=|usr=}}{{27956599}} gab.com Text Mimicking transient activation of protein kinases in living cells JO: Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=27956599 #FOAvip Nearly all eukaryotic physiological events are regulated by protein kinases. Aberrations in functions of kinases are linked to numerous diseases. Significant progress has been made in dissecting the role of many kinases. However, understanding how specific kinases orchestrate complex signaling events remains challenging. Here we present a method to control the timing and the duration of kinase activity. This system provides the ability to mimic physiologically relevant transient activation of a kinase. We demonstrate the specificity and efficiency of this method by regulating tyrosine kinase (c-Src) and serine/threonine kinase (p38?). By using this approach, we identify morphological changes induced by transient activation of Src and demonstrate the role of sequential Src-PI3K and Src-Rac1 signaling in regulation of cell morphology. Twit Text FOAVip Mimicking transient activation of protein kinases in living cells ????Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=27956599 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27956599 #FOAvip English Wikipedia <ref>{{Cite pmid|27956599}}</ref> Mimicking transient activation of protein kinases in living cells #MMPMID27956599 Klomp JE; Huyot V; Ray AM; Collins KB; Malik AB; Karginov AV Proc Natl Acad Sci U S A 2016[Dec]; 113 (52): 14976-81 PMID27956599show ga Nearly all eukaryotic physiological events are regulated by protein kinases. Aberrations in functions of kinases are linked to numerous diseases. Significant progress has been made in dissecting the role of many kinases. However, understanding how specific kinases orchestrate complex signaling events remains challenging. Here we present a method to control the timing and the duration of kinase activity. This system provides the ability to mimic physiologically relevant transient activation of a kinase. We demonstrate the specificity and efficiency of this method by regulating tyrosine kinase (c-Src) and serine/threonine kinase (p38?). By using this approach, we identify morphological changes induced by transient activation of Src and demonstrate the role of sequential Src-PI3K and Src-Rac1 signaling in regulation of cell morphology. äMimicking transient activation of protein kinases in living cells (epmc).pdf DeepDyve Pubget Overpricing