Cap analog substrates reveal three clades of cap guanine-N2 methyltransferases with distinct methyl acceptor specificities

RNA

Volumn 16, Issue 1, 2010, Pages 211-220

  Benarroch, Delphine ^a   Jankowska Anyszka, Marzena ^b   Stepinski, Janusz ^b   Darzynkiewicz, Edward ^b   Shuman, Stewart ^a  

^a MEMORIAL SLOAN KETTERING CANCER CENTER   (United States)

^b UNIVERSITY OF WARSAW   (Poland)

Author keywords

Cap hypermethylation; Dimethylguanosine; Giardia; Mimivirus

Indexed keywords

PROTEIN; RNA; RNA METHYLTRANSFERASE; TGS PROTEIN; UNCLASSIFIED DRUG; CAPPED RNA; DRUG DERIVATIVE; GUANOSINE; METHYLTRANSFERASE; N(2),N(2),7 TRIMETHYLGUANOSINE; N(2),N(2),7-TRIMETHYLGUANOSINE; TRIMETHYLGUANOSINE SYNTHASE;

ALKYLATION; ARTICLE; CLADISTICS; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME STRUCTURE; ENZYME SUBSTRATE; GIARDIA LAMBLIA; HUMAN; HUMAN VERSUS NONHUMAN DATA; MIMIVIRUS; NONHUMAN; PRIORITY JOURNAL; RNA CAPPING; CATALYSIS; CLASSIFICATION; ENZYME ACTIVE SITE; ENZYME SPECIFICITY; ENZYMOLOGY; METABOLISM; METHYLATION; PH; PHYSIOLOGY;

EUKARYOTA; GIARDIA; GIARDIA INTESTINALIS; MAMMALIA; MIMIVIRUS; PROTOZOA;

CATALYSIS; CATALYTIC DOMAIN; GIARDIA LAMBLIA; GUANOSINE; HUMANS; HYDROGEN-ION CONCENTRATION; METHYLATION; METHYLTRANSFERASES; MIMIVIRIDAE; RNA CAP ANALOGS; RNA CAPS; SUBSTRATE SPECIFICITY;

EID: 75649144466     PISSN: 13558382     EISSN: 14699001     Source Type: Journal    
DOI: 10.1261/rna.1872110     Document Type: Article

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