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10.1146/annurev-biochem-072711-165700 http://scihub22266oqcxt.onion/10.1146/annurev-biochem-072711-165700 C4696766!4696766!23642229     free     free     free       Annu+Rev+Biochem 2013 ; 82 (ä): 81-118 Nephropedia Template TP {{tp|p=23642229|t=2013. Readout of Epigenetic Modifications |pdf=|usr=}}{{23642229}} gab.com Text Readout of Epigenetic Modifications JO: Annu Rev Biochem http://www.kidney.de/pget.php?&tw=1&pmid=23642229 #FOAvip This review focuses on a structure-based analysis of histone posttranslational modification (PTM) readout, where the PTMs serve as docking sites for reader modules as part of larger complexes displaying chromatin modifier and remodeling activities, with the capacity to alter chromatin architecture and templated processes. Individual topics addressed include the diversity of reader-binding pocket architectures and common principles underlying readout of methyl-lysine and methyl-arginine marks, their unmodified counterparts, as well as acetyl-lysine and phosphoserine marks. The review also discusses the impact of multivalent readout of combinations of PTMs localized at specific genomic sites by linked binding modules on processes ranging from gene transcription to repair. Additional topics include cross talk between histone PTMs, histone mimics, epigenetic-based diseases, and drug-based therapeutic intervention. The review ends by highlighting new initiatives and advances, as well as future challenges, toward the promise of enhancing our structural and mechanistic understanding of the readout of histone PTMs at the nucleosomal level. Twit Text FOAVip Readout of Epigenetic Modifications ????Annu Rev Biochem http://www.kidney.de/pget.php?&tw=1&pmid=23642229 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=23642229 #FOAvip English Wikipedia <ref>{{Cite pmid|23642229}}</ref> Readout of Epigenetic Modifications #MMPMID23642229 Patel DJ; Wang Z Annu Rev Biochem 2013[]; 82 (ä): 81-118 PMID23642229show ga This review focuses on a structure-based analysis of histone posttranslational modification (PTM) readout, where the PTMs serve as docking sites for reader modules as part of larger complexes displaying chromatin modifier and remodeling activities, with the capacity to alter chromatin architecture and templated processes. Individual topics addressed include the diversity of reader-binding pocket architectures and common principles underlying readout of methyl-lysine and methyl-arginine marks, their unmodified counterparts, as well as acetyl-lysine and phosphoserine marks. The review also discusses the impact of multivalent readout of combinations of PTMs localized at specific genomic sites by linked binding modules on processes ranging from gene transcription to repair. Additional topics include cross talk between histone PTMs, histone mimics, epigenetic-based diseases, and drug-based therapeutic intervention. The review ends by highlighting new initiatives and advances, as well as future challenges, toward the promise of enhancing our structural and mechanistic understanding of the readout of histone PTMs at the nucleosomal level. äReadout of Epigenetic Modifications (epmc).pdf DeepDyve Pubget Overpricing