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1 capped structure as is formed by protein GTP:RNA guanylyltransferase.
2 f the capping enzymes RNA triphosphatase and RNA guanylyltransferase.
3 hosphate end that is then capped with GMP by RNA guanylyltransferase.
5 action of three enzymes: RNA triphosphatase, RNA guanylyltransferase, and RNA (guanine-7)-methyltrans
6 ifunctional protein with RNA triphosphatase, RNA guanylyltransferase, and RNA (guanine-7-) methyltran
8 ces cerevisiae RNA triphosphatase (Cet1) and RNA guanylyltransferase (Ceg1) interact in vivo and in v
9 Cet1(231-549)p binds in vitro to the yeast RNA guanylyltransferase Ceg1p to form a 7.1 S complex th
10 es cerevisiae RNA triphosphatase (Cet1p) and RNA guanylyltransferase (Ceg1p) interact in vivo and in
11 consisting of RNA 5'-triphosphatase (Cet1p), RNA guanylyltransferase (Ceg1p), and Abd1p could be repl
13 A triphosphatase (CaCet1p), a 449-amino acid RNA guanylyltransferase (Cgt1p), and a 474-amino acid RN
14 Here, we report the crystal structure of the RNA guanylyltransferase component of mammalian capping e
15 ysical linkage of the RNA triphosphatase and RNA guanylyltransferase enzymes that catalyze mRNA cap f
19 novel active-site motif is proposed for the RNA guanylyltransferases of mammalian reoviruses and oth
20 We show that P. falciparum encodes separate RNA guanylyltransferase (Pgt1) and RNA triphosphatase (P
21 , A103R is more closely related to the yeast RNA guanylyltransferases than it is to the multifunction
22 virus D1(1-545)p, an RNA triphosphatase and RNA guanylyltransferase-to function in the budding yeast
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