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10.1093/nar/gkw1199 http://scihub22266oqcxt.onion/10.1093/nar/gkw1199 C5388400!5388400!28180302     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=28180302&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 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\28180302.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Nucleic+Acids+Res 2017 ; 45 (3): 1345-54 Nephropedia Template TP {{tp|p=28180302|t=2017. Nucleobase modification by an RNA enzyme |pdf=|usr=}}{{28180302}} gab.com Text Nucleobase modification by an RNA enzyme JO: Nucleic Acids Res http://www.kidney.de/pget.php?&tw=1&pmid=28180302 #FOAvip Ribozymes can catalyze phosphoryl or nucleotidyl transfer onto ribose hydroxyls of RNA chains. We report a single ribozyme that performs both reactions, with a nucleobase serving as initial acceptor moiety. This unprecedented combined reaction was revealed while investigating potential contributions of ribose hydroxyls to catalysis by kinase ribozyme K28. For a 58nt, cis-acting form of K28, each nucleotide could be replaced with the corresponding 2?F analog without loss of activity, indicating that no particular 2?OH is specifically required. Reactivities of two-stranded K28 variants with oligodeoxynucleotide acceptor strands devoid of any 2?OH moieties implicate modification on an internal guanosine N-2, rather than a ribose hydroxyl. Product mass suggests formation of a GDP(S) adduct along with a second thiophosphorylation, implying that the ribozyme catalyzes both phosphoryl and nucleotidyl transfers. This is further supported by transfer of radiolabels into product from both ? and ? phosphates of donor molecules. Furthermore, periodate reactivity of the final product signifies acquisition of a ribose sugar with an intact 2?-3? vicinal diol. Neither nucleobase modification nor nucleotidyl transfer has previously been reported for a kinase ribozyme, making this a first-in-class ribozyme. Base-modifying ribozymes may have played important roles in early RNA world evolution by enhancing nucleic acid functions. Twit Text FOAVip Nucleobase modification by an RNA enzyme ????Nucleic Acids Res http://www.kidney.de/pget.php?&tw=1&pmid=28180302 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28180302 #FOAvip English Wikipedia <ref>{{Cite pmid|28180302}}</ref> Nucleobase modification by an RNA enzyme #MMPMID28180302 Poudyal RR; Nguyen P; Lokugamage MP; Callaway MK; Gavette JV; Krishnamurthy R; Burke DH Nucleic Acids Res 2017[Feb]; 45 (3): 1345-54 PMID28180302show ga Ribozymes can catalyze phosphoryl or nucleotidyl transfer onto ribose hydroxyls of RNA chains. We report a single ribozyme that performs both reactions, with a nucleobase serving as initial acceptor moiety. This unprecedented combined reaction was revealed while investigating potential contributions of ribose hydroxyls to catalysis by kinase ribozyme K28. For a 58nt, cis-acting form of K28, each nucleotide could be replaced with the corresponding 2?F analog without loss of activity, indicating that no particular 2?OH is specifically required. Reactivities of two-stranded K28 variants with oligodeoxynucleotide acceptor strands devoid of any 2?OH moieties implicate modification on an internal guanosine N-2, rather than a ribose hydroxyl. Product mass suggests formation of a GDP(S) adduct along with a second thiophosphorylation, implying that the ribozyme catalyzes both phosphoryl and nucleotidyl transfers. This is further supported by transfer of radiolabels into product from both ? and ? phosphates of donor molecules. Furthermore, periodate reactivity of the final product signifies acquisition of a ribose sugar with an intact 2?-3? vicinal diol. Neither nucleobase modification nor nucleotidyl transfer has previously been reported for a kinase ribozyme, making this a first-in-class ribozyme. Base-modifying ribozymes may have played important roles in early RNA world evolution by enhancing nucleic acid functions. äNucleobase modification by an RNA enzyme (epmc).pdf DeepDyve Pubget Overpricing