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10.1042/BST20160166 http://scihub22266oqcxt.onion/10.1042/BST20160166 C5095909!5095909 !27911715     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=27911715 &cmd=llinks): Failed to open stream: HTTP request failed! 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The control of inflammation via the phosphorylation and dephosphorylation of tristetraprolin: a tale of two phosphatases |pdf=|usr=}}{{27911715 }} gab.com Text The control of inflammation via the phosphorylation and dephosphorylation of tristetraprolin: a tale of two phosphatases JO: Biochem Soc Trans http://www.kidney.de/pget.php?&tw=1&pmid=27911715 #FOAvip Twenty years ago, the first description of a tristetraprolin (TTP) knockout mouse highlighted the fundamental role of TTP in the restraint of inflammation. Since then, work from several groups has generated a detailed picture of the expression and function of TTP. It is a sequence-specific RNA-binding protein that orchestrates the deadenylation and degradation of several mRNAs encoding inflammatory mediators. It is very extensively post-translationally modified, with more than 30 phosphorylations that are supported by at least two independent lines of evidence. The phosphorylation of two particular residues, serines 52 and 178 of mouse TTP (serines 60 and 186 of the human orthologue), has profound effects on the expression, function and localisation of TTP. Here, we discuss the control of TTP biology via its phosphorylation and dephosphorylation, with a particular focus on recent advances and on questions that remain unanswered. Twit Text FOAVip The control of inflammation via the phosphorylation and dephosphorylation of tristetraprolin: a tale of two phosphatases ????Biochem Soc Trans http://www.kidney.de/pget.php?&tw=1&pmid=27911715 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27911715 #FOAvip English Wikipedia <ref>{{Cite pmid|27911715 }}</ref> The control of inflammation via the phosphorylation and dephosphorylation of tristetraprolin: a tale of two phosphatases #MMPMID27911715 Clark AR ; Dean JL Biochem Soc Trans 2016[Oct]; 44 (5 ): 1321-1337 PMID27911715 show ga Twenty years ago, the first description of a tristetraprolin (TTP) knockout mouse highlighted the fundamental role of TTP in the restraint of inflammation. Since then, work from several groups has generated a detailed picture of the expression and function of TTP. It is a sequence-specific RNA-binding protein that orchestrates the deadenylation and degradation of several mRNAs encoding inflammatory mediators. It is very extensively post-translationally modified, with more than 30 phosphorylations that are supported by at least two independent lines of evidence. The phosphorylation of two particular residues, serines 52 and 178 of mouse TTP (serines 60 and 186 of the human orthologue), has profound effects on the expression, function and localisation of TTP. Here, we discuss the control of TTP biology via its phosphorylation and dephosphorylation, with a particular focus on recent advances and on questions that remain unanswered. |Amino Acid Sequence [MESH] |Animals [MESH] |Humans [MESH] |Inflammation/genetics/*metabolism [MESH] |Mice, Knockout [MESH] |Phosphoric Monoester Hydrolases/*metabolism [MESH] |Phosphorylation [MESH] |Serine/genetics/*metabolism [MESH] |Signal Transduction/genetics [MESH]The control of inflammation via the phosphorylation and dephosphorylat(epmc).pdf DeepDyve Pubget Overpricing