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10.1016/j.molcel.2016.06.029 http://scihub22266oqcxt.onion/10.1016/j.molcel.2016.06.029 C5003815!5003815!27453046     free     free     free Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Mol+Cell 2016 ; 63 (4): 696-710 Nephropedia Template TP {{tp|p=27453046|t=2016. Comprehensive Identification of RNA-Binding Domains in Human Cells |pdf=|usr=}}{{27453046}} gab.com Text Comprehensive Identification of RNA-Binding Domains in Human Cells JO: Mol Cell http://www.kidney.de/pget.php?&tw=1&pmid=27453046 #FOAvip Mammalian cells harbor more than a thousand RNA-binding proteins (RBPs), with half of these employing unknown modes of RNA binding. We developed RBDmap to determine the RNA-binding sites of native RBPs on a proteome-wide scale. We identified 1,174 binding sites within 529 HeLa cell RBPs, discovering numerous RNA-binding domains (RBDs). Catalytic centers or protein-protein interaction domains are in close relationship with RNA-binding sites, invoking possible effector roles of RNA in the control of protein function. Nearly half of the RNA-binding sites map to intrinsically disordered regions, uncovering unstructured domains as prevalent partners in protein-RNA interactions. RNA-binding sites represent hot spots for defined posttranslational modifications such as lysine acetylation and tyrosine phosphorylation, suggesting metabolic and signal-dependent regulation of RBP function. RBDs display a high degree of evolutionary conservation and incidence of Mendelian mutations, suggestive of important functional roles. RBDmap thus yields profound insights into native protein-RNA interactions in living cells. Twit Text FOAVip Comprehensive Identification of RNA-Binding Domains in Human Cells ????Mol Cell http://www.kidney.de/pget.php?&tw=1&pmid=27453046 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27453046 #FOAvip English Wikipedia <ref>{{Cite pmid|27453046}}</ref> Comprehensive Identification of RNA-Binding Domains in Human Cells #MMPMID27453046 Castello A; Fischer B; Frese C; Horos R; Alleaume AM; Foehr S; Curk T; Krijgsveld J; Hentze M Mol Cell 2016[Aug]; 63 (4): 696-710 PMID27453046show ga Mammalian cells harbor more than a thousand RNA-binding proteins (RBPs), with half of these employing unknown modes of RNA binding. We developed RBDmap to determine the RNA-binding sites of native RBPs on a proteome-wide scale. We identified 1,174 binding sites within 529 HeLa cell RBPs, discovering numerous RNA-binding domains (RBDs). Catalytic centers or protein-protein interaction domains are in close relationship with RNA-binding sites, invoking possible effector roles of RNA in the control of protein function. Nearly half of the RNA-binding sites map to intrinsically disordered regions, uncovering unstructured domains as prevalent partners in protein-RNA interactions. RNA-binding sites represent hot spots for defined posttranslational modifications such as lysine acetylation and tyrosine phosphorylation, suggesting metabolic and signal-dependent regulation of RBP function. RBDs display a high degree of evolutionary conservation and incidence of Mendelian mutations, suggestive of important functional roles. RBDmap thus yields profound insights into native protein-RNA interactions in living cells. äComprehensive Identification of RNA-Binding Domains in Human Cells (epmc).pdf DeepDyve Pubget Overpricing