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1 did not affect the function of TFIIS or the mRNA capping enzyme.
2 and Cet1p, the two subunits of the yeast pre-mRNA capping enzyme.
3 ligase fused to the C-terminal domain 2 of a mRNA capping enzyme.
4 iphosphatase domain of the metazoan cellular mRNA capping enzyme.
5 ture-sensitive mutations of Ceg1p, the yeast mRNA capping enzyme.
6 triphosphatase domains of metazoan and plant mRNA capping enzymes.
7 cture in Rnl2-like ligases, DNA ligases, and mRNA capping enzymes.
8 completely different from those of mammalian mRNA capping enzymes.
9 vaccinia virus and Saccharomyces cerevisiae mRNA capping enzymes.
10 ATP-dependent DNA ligases and GTP-dependent mRNA capping enzymes.
11 5' end of nascent mRNA is carried out by the mRNA-capping enzyme, a two-domain protein that is a memb
12 e and with previously reported structures of mRNA capping enzymes, adenylate cyclases, and polyphosph
14 f conformational rearrangements spanning all mRNA-capping enzymes and all ATP-dependent DNA ligases.
18 gating RNA polymerase II, and recruitment of mRNA capping enzyme, cap-binding complex, and 3' end for
27 closest homologs, which include the metazoan mRNA capping enzymes, constitute a subgroup of the PTP f
29 NTase domain independently of the eukaryotic mRNA capping enzyme during evolution and PRNTase becomes
30 cruitment and exchange of factors, including mRNA capping enzymes, elongation factors, splicing facto
31 nts a functionally independent domain of the mRNA capping enzyme, fully competent in substrate bindin
35 7 methyltransferase domain of vaccinia virus mRNA capping enzyme is a heterodimer composed of a catal
37 to 545) of the D1 subunit of vaccinia virus mRNA capping enzyme is an autonomous bifunctional domain
39 thyltransferase domain of the vaccinia virus mRNA capping enzyme is composed of the C-terminal portio
40 phatase domain of the Caenorhabditis elegans mRNA capping enzyme is related to the PTP enzyme family
42 the CTD the ability to recruit the mammalian mRNA capping enzyme (Mce1) and stimulate its guanylyltra
43 a biochemical and genetic analysis of mouse mRNA capping enzyme (Mce1), a bifunctional 597-amino aci
44 yltransferase (PRNTase) is an unconventional mRNA capping enzyme of NNS RNA viruses that is distinct
45 omain of the large subunit of vaccinia virus mRNA capping enzyme possessing ATPase, RNA 5'-triphospha
46 tural differences between poxvirus and human mRNA capping enzymes recommend cap formation as a target
47 iption initiation factor subunits A8 and D6; mRNA capping enzyme subunits D1 and D12; RNA cap 2'-O-me
48 103R protein of Chlorella virus PBCV-1 is an mRNA capping enzyme that catalyzes the transfer of GMP f
50 While our results are specific to the PBCV-1 mRNA capping enzyme, they provide a useful context withi
51 owth is circumvented by covalently tethering mRNA capping enzymes to the CTD, thus proving that cappi
53 transferase activities of the vaccinia virus mRNA capping enzyme were previously localized to an NH2-
55 d baculovirus LEF4 protein is a bifunctional mRNA capping enzyme with triphosphatase and guanylyltran
56 d baculovirus Lef4 protein is a bifunctional mRNA capping enzyme with triphosphatase and guanylyltran
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