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10.1186/s13072-017-0117-5 http://scihub22266oqcxt.onion/10.1186/s13072-017-0117-5 C5348760!5348760!28293301     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=28293301&cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215 Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 227.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 261.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Epigenetics+Chromatin 2017 ; 10 (ä): ä Nephropedia Template TP {{tp|p=28293301|t=2017. Histone peptide microarray screen of chromo and Tudor domains defines new histone lysine methylation interactions |pdf=|usr=}}{{28293301}} gab.com Text Histone peptide microarray screen of chromo and Tudor domains defines new histone lysine methylation interactions JO: Epigenetics Chromatin http://www.kidney.de/pget.php?&tw=1&pmid=28293301 #FOAvip Background: Histone posttranslational modifications (PTMs) function to regulate chromatin structure and function in part through the recruitment of effector proteins that harbor specialized ?reader? domains. Despite efforts to elucidate reader domain?PTM interactions, the influence of neighboring PTMs and the target specificity of many reader domains is still unclear. The aim of this study was to use a high-throughput histone peptide microarray platform to interrogate 83 known and putative histone reader domains from the chromo and Tudor domain families to identify their interactions and characterize the influence of neighboring PTMs on these interactions. Results: Nearly a quarter of the chromo and Tudor domains screened showed interactions with histone PTMs by peptide microarray, revealing known and several novel methyllysine interactions. Specifically, we found that the CBX/HP1 chromodomains that recognize H3K9me also recognize H3K23me2/3?a poorly understood histone PTM. We also observed that, in addition to their interaction with H3K4me3, Tudor domains of the Spindlin family also recognized H4K20me3?a previously uncharacterized interaction. Several Tudor domains also showed novel interactions with H3K4me as well. Conclusions: These results provide an important resource for the epigenetics and chromatin community on the interactions of many human chromo and Tudor domains. They also provide the basis for additional studies into the functional significance of the novel interactions that were discovered. Electronic supplementary material: The online version of this article (doi:10.1186/s13072-017-0117-5) contains supplementary material, which is available to authorized users. Twit Text FOAVip Histone peptide microarray screen of chromo and Tudor domains defines new histone lysine methylation interactions ????Epigenetics Chromatin http://www.kidney.de/pget.php?&tw=1&pmid=28293301 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28293301 #FOAvip English Wikipedia <ref>{{Cite pmid|28293301}}</ref> Histone peptide microarray screen of chromo and Tudor domains defines new histone lysine methylation interactions #MMPMID28293301 Shanle EK; Shinsky SA; Bridgers JB; Bae N; Sagum C; Krajewski K; Rothbart SB; Bedford MT; Strahl BD Epigenetics Chromatin 2017[]; 10 (ä): ä PMID28293301show ga Background: Histone posttranslational modifications (PTMs) function to regulate chromatin structure and function in part through the recruitment of effector proteins that harbor specialized ?reader? domains. Despite efforts to elucidate reader domain?PTM interactions, the influence of neighboring PTMs and the target specificity of many reader domains is still unclear. The aim of this study was to use a high-throughput histone peptide microarray platform to interrogate 83 known and putative histone reader domains from the chromo and Tudor domain families to identify their interactions and characterize the influence of neighboring PTMs on these interactions. Results: Nearly a quarter of the chromo and Tudor domains screened showed interactions with histone PTMs by peptide microarray, revealing known and several novel methyllysine interactions. Specifically, we found that the CBX/HP1 chromodomains that recognize H3K9me also recognize H3K23me2/3?a poorly understood histone PTM. We also observed that, in addition to their interaction with H3K4me3, Tudor domains of the Spindlin family also recognized H4K20me3?a previously uncharacterized interaction. Several Tudor domains also showed novel interactions with H3K4me as well. Conclusions: These results provide an important resource for the epigenetics and chromatin community on the interactions of many human chromo and Tudor domains. They also provide the basis for additional studies into the functional significance of the novel interactions that were discovered. Electronic supplementary material: The online version of this article (doi:10.1186/s13072-017-0117-5) contains supplementary material, which is available to authorized users. äHistone peptide microarray screen of chromo and Tudor domains defines (epmc).pdf DeepDyve Pubget Overpricing