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10.1021/acschembio.5b00802 http://scihub22266oqcxt.onion/10.1021/acschembio.5b00802 C4861070!4861070!26726824     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       ACS+Chem+Biol 2016 ; 11 (3): 547-53 Nephropedia Template TP {{tp|p=26726824|t=2016. Regulation of Methyllysine Readers through Phosphorylation |pdf=|usr=}}{{26726824}} gab.com Text Regulation of Methyllysine Readers through Phosphorylation JO: ACS Chem Biol http://www.kidney.de/pget.php?&tw=1&pmid=26726824 #FOAvip Methyllysine post-translational modifications (PTMs) of histones create binding sites for evolutionarily conserved reader domains that link nuclear host proteins and chromatin-modifying complexes to specific genomic regions. In the context of these events, adjacent histone PTMs are capable of altering the binding activity of readers toward their target marks. This provides a mechanism of ?combinatorial readout? of PTMs that can enhance, decrease, or eliminate the association of readers with chromatin. In this Perspective, we focus on recent studies describing the impact of dynamic phospho-serine/threonine/tyrosine marks on the interaction of methyllysine readers with histones, summarize mechanistic aspects of the phospho/methyl readout, and highlight the significance of crosstalk between these PTMs. We also demonstrate that in addition to inhibiting binding and serving as a true switch, promoting dissociation of the methyllysine readers from chromatin, the phospho/methyl combination can act together in a cooperative manner?thus adding a new layer of regulatory information that can be encoded in these dual histone PTMs. Twit Text FOAVip Regulation of Methyllysine Readers through Phosphorylation ????ACS Chem Biol http://www.kidney.de/pget.php?&tw=1&pmid=26726824 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26726824 #FOAvip English Wikipedia <ref>{{Cite pmid|26726824}}</ref> Regulation of Methyllysine Readers through Phosphorylation #MMPMID26726824 Andrews FH; Gatchalian J; Krajewski K; Strahl BD; Kutateladze TG ACS Chem Biol 2016[Mar]; 11 (3): 547-53 PMID26726824show ga Methyllysine post-translational modifications (PTMs) of histones create binding sites for evolutionarily conserved reader domains that link nuclear host proteins and chromatin-modifying complexes to specific genomic regions. In the context of these events, adjacent histone PTMs are capable of altering the binding activity of readers toward their target marks. This provides a mechanism of ?combinatorial readout? of PTMs that can enhance, decrease, or eliminate the association of readers with chromatin. In this Perspective, we focus on recent studies describing the impact of dynamic phospho-serine/threonine/tyrosine marks on the interaction of methyllysine readers with histones, summarize mechanistic aspects of the phospho/methyl readout, and highlight the significance of crosstalk between these PTMs. We also demonstrate that in addition to inhibiting binding and serving as a true switch, promoting dissociation of the methyllysine readers from chromatin, the phospho/methyl combination can act together in a cooperative manner?thus adding a new layer of regulatory information that can be encoded in these dual histone PTMs. äRegulation of Methyllysine Readers through Phosphorylation (epmc).pdf DeepDyve Pubget Overpricing