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10.1093/bfgp/elv045 http://scihub22266oqcxt.onion/10.1093/bfgp/elv045 C4803063!4803063!26512033     free     free     free Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Brief+Funct+Genomics 2016 ; 15 (2): 109-18 Nephropedia Template TP {{tp|p=26512033|t=2016. Building a KATalogue of acetyllysine targeting and function |pdf=|usr=}}{{26512033}} gab.com Text Building a KATalogue of acetyllysine targeting and function JO: Brief Funct Genomics http://www.kidney.de/pget.php?&tw=1&pmid=26512033 #FOAvip Acetylation is a dynamic post-translational modification that is attached to protein substrates by lysine acetyltransferases (KATs) and removed by lysine deacetylases (KDACs). While these enzymes are best characterized as histone modifiers and regulators of gene transcription, work in a number of systems highlights that acetylation is a pervasive modification and suggests a broad scope for KAT and KDAC functions in the cell. As we move beyond generating lists of acetylated proteins, the acetylation field is in dire need of robust tools to connect acetylation and deacetylation machineries to their respective substrates and to dissect the function of individual sites. The Saccharomyces cerevisiae model system provides such a toolkit in the context of both tried and true genetic techniques and cutting-edge proteomic and cell imaging methods. Here, we review these methods in the context of their contributions to acetylation research thus far and suggest strategies for addressing lingering questions in the field. Twit Text FOAVip Building a KATalogue of acetyllysine targeting and function ????Brief Funct Genomics http://www.kidney.de/pget.php?&tw=1&pmid=26512033 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26512033 #FOAvip English Wikipedia <ref>{{Cite pmid|26512033}}</ref> Building a KATalogue of acetyllysine targeting and function #MMPMID26512033 Downey M; Baetz K Brief Funct Genomics 2016[Mar]; 15 (2): 109-18 PMID26512033show ga Acetylation is a dynamic post-translational modification that is attached to protein substrates by lysine acetyltransferases (KATs) and removed by lysine deacetylases (KDACs). While these enzymes are best characterized as histone modifiers and regulators of gene transcription, work in a number of systems highlights that acetylation is a pervasive modification and suggests a broad scope for KAT and KDAC functions in the cell. As we move beyond generating lists of acetylated proteins, the acetylation field is in dire need of robust tools to connect acetylation and deacetylation machineries to their respective substrates and to dissect the function of individual sites. The Saccharomyces cerevisiae model system provides such a toolkit in the context of both tried and true genetic techniques and cutting-edge proteomic and cell imaging methods. Here, we review these methods in the context of their contributions to acetylation research thus far and suggest strategies for addressing lingering questions in the field. äBuilding a KATalogue of acetyllysine targeting and function (epmc).pdf DeepDyve Pubget Overpricing