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10.1111/febs.13378 http://scihub22266oqcxt.onion/10.1111/febs.13378 C4869838!4869838!26185901     free     free     free       FEBS+J 2015 ; 282 (19): 3669-80 Nephropedia Template TP {{tp|p=26185901|t=2015. Mapping the SUMOylated landscape |pdf=|usr=}}{{26185901}} gab.com Text Mapping the SUMOylated landscape JO: FEBS J http://www.kidney.de/pget.php?&tw=1&pmid=26185901 #FOAvip SUMOylation is a post?translational modification that regulates a multitude of cellular processes, including replication, cell?cycle progression, protein transport and the DNA damage response. Similar to ubiquitin, SUMO (small ubiquitin?like modifier) is covalently attached to target proteins in a reversible process via an enzymatic cascade. SUMOylation is essential for nearly all eukaryotic organisms, and deregulation of the SUMO system is associated with human diseases such as cancer and neurodegenerative diseases. Therefore, it is of great interest to understand the regulation and dynamics of this post?translational modification. Within the last decade, mass spectrometry analyses of SUMO proteomes have overcome several obstacles, greatly expanding the number of known SUMO target proteins. In this review, we briefly outline the basic concepts of the SUMO system, and discuss the potential of proteomic approaches to decipher SUMOylation patterns in order to understand the role of SUMO in health and disease. Twit Text FOAVip Mapping the SUMOylated landscape ????FEBS J http://www.kidney.de/pget.php?&tw=1&pmid=26185901 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26185901 #FOAvip English Wikipedia <ref>{{Cite pmid|26185901}}</ref> Mapping the SUMOylated landscape #MMPMID26185901 Eifler K; Vertegaal AC FEBS J 2015[Oct]; 282 (19): 3669-80 PMID26185901show ga SUMOylation is a post?translational modification that regulates a multitude of cellular processes, including replication, cell?cycle progression, protein transport and the DNA damage response. Similar to ubiquitin, SUMO (small ubiquitin?like modifier) is covalently attached to target proteins in a reversible process via an enzymatic cascade. SUMOylation is essential for nearly all eukaryotic organisms, and deregulation of the SUMO system is associated with human diseases such as cancer and neurodegenerative diseases. Therefore, it is of great interest to understand the regulation and dynamics of this post?translational modification. Within the last decade, mass spectrometry analyses of SUMO proteomes have overcome several obstacles, greatly expanding the number of known SUMO target proteins. In this review, we briefly outline the basic concepts of the SUMO system, and discuss the potential of proteomic approaches to decipher SUMOylation patterns in order to understand the role of SUMO in health and disease. äMapping the SUMOylated landscape (epmc).pdf DeepDyve Pubget Overpricing