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1 iae, this reaction is catalyzed by Cet1p, an RNA triphosphatase.
2 is similarity to the active site of vaccinia RNA triphosphatase.
3 sform it into a strictly manganese-dependent RNA triphosphatase.
4 ce of a carboxylate general acid catalyst in RNA triphosphatase.
5 he guanylyltransferase docking site on yeast RNA triphosphatase.
6 al/viral/protozoal family of metal-dependent RNA triphosphatases.
7 talytic mechanism are conserved among fungal RNA triphosphatases.
8 in the absence of its two different types of RNA triphosphatases.
9  helicase (HEL) activities in addition to 5' RNA triphosphatase (5'RTP), which is involved in the RNA
10 pping of mammalian pre-mRNAs is initiated by RNA triphosphatase, a member of the cysteine phosphatase
11 p formation, a mutant virus that lacked both RNA triphosphatase activities was constructed.
12 S2B-dependent protease, RNA helicase, and 5'-RNA triphosphatase activities.
13 reas the N-terminal part exhibits NTPase and RNA triphosphatase activity and is proposed to have heli
14  truncated derivative Cet1(246-549) also has RNA triphosphatase activity but fails to stimulate Ceg1
15                                          The RNA triphosphatase activity depends absolutely on a diva
16 sly shown to be essential for vaccinia virus RNA triphosphatase activity inactivated the triphosphata
17                                    Hence, an RNA triphosphatase activity is essential for eukaryotic
18                                              RNA triphosphatase activity is optimal at pH 7.5 with ei
19                                          The RNA triphosphatase activity of Cet1p is magnesium-depend
20                       Here, we show that the RNA triphosphatase activity of DUSP11 promotes the RNA s
21      A truncated protein, Cet1(201-549), has RNA triphosphatase activity, heterodimerizes with and st
22 inal region (amino acids 265 to 549) carries RNA triphosphatase activity, while the region containing
23 f LEF-4 but resulted in a modest decrease in RNA triphosphatase activity.
24           The N-terminal domain of CEL-1 has RNA triphosphatase activity.
25 cleopolyhedrovirus encodes two proteins with RNA triphosphatase activity.
26 n N-terminal serine proteinase domain and an RNA triphosphatase, an NTPase domain, and an RNA helicas
27 ns within these motifs are essential for the RNA triphosphatase and ATPase activities of Cet1p in vit
28 their replacement by glutamine abolishes the RNA triphosphatase and ATPase activities.
29 ite nucleophile Cys-119 by alanine abrogates RNA triphosphatase and ATPase activity.
30 capping reactions, which are catalyzed by an RNA triphosphatase and guanylyltransferase.
31 karyotic phylogeny based on the structure of RNA triphosphatase and its physical linkage to the guany
32                                          The RNA triphosphatase and NTPase activities of baculovirus
33        Concordant mutational inactivation of RNA triphosphatase and nucleoside triphosphatase functio
34 , a bifunctional 597-amino acid protein with RNA triphosphatase and RNA guanylyltransferase activitie
35 on the structure and physical linkage of the RNA triphosphatase and RNA guanylyltransferase enzymes t
36 nosoma brucei consists of separately encoded RNA triphosphatase and RNA guanylyltransferase enzymes.
37 capping enzyme-vaccinia virus D1(1-545)p, an RNA triphosphatase and RNA guanylyltransferase-to functi
38 ted by overexpression of the capping enzymes RNA triphosphatase and RNA guanylyltransferase.
39 een in only three previous structures: yeast RNA triphosphatase and two proteins of unknown function
40        The structure and mechanism of fungal RNA triphosphatases are completely different from those
41                        Pct1p and other yeast RNA triphosphatases are completely unrelated, mechanisti
42  that protozoan, fungal, and Chlorella virus RNA triphosphatases belong to a single family of metal-d
43                       BVP and other metazoan RNA triphosphatases belong to a superfamily of phosphata
44 ian capping enzyme (Mce1) are members of the RNA triphosphatase branch of the cysteine phosphatase su
45 tructure conservation between members of the RNA triphosphatase branch, whether from cellular or vira
46                           PTP/BVP is also an RNA triphosphatase, but is not essential for viral repli
47 ty, and is conserved in the Candida albicans RNA triphosphatase CaCet1p.
48 sists of three components: a 520- amino acid RNA triphosphatase (CaCet1p), a 449-amino acid RNA guany
49 ize that the need for Ceg1p binding by yeast RNA triphosphatase can by bypassed when the triphosphata
50                                              RNA triphosphatase catalyzes the first step in mRNA cap
51                     Saccharomyces cerevisiae RNA triphosphatase Cet1 is an essential component of the
52  cvRtp1 is more similar to that of the yeast RNA triphosphatase Cet1 than it is to the RNA triphospha
53                     Saccharomyces cerevisiae RNA triphosphatase (Cet1) and RNA guanylyltransferase (C
54                     The 549-amino acid yeast RNA triphosphatase Cet1p catalyzes the first step in mRN
55        The 2.05 A crystal structure of yeast RNA triphosphatase Cet1p reveals a novel active site fol
56 catalytic domain of Saccharomyces cerevisiae RNA triphosphatase Cet1p.
57                     Saccharomyces cerevisiae RNA triphosphatase (Cet1p) and RNA guanylyltransferase (
58                                          The RNA triphosphatases characteristically hydrolyze nucleos
59                                          The RNA triphosphatase component (CaCet1p) of the mRNA cappi
60                       A binding site for the RNA triphosphatase component of the capping apparatus wa
61 iphosphatase enzyme family that includes the RNA triphosphatase component of the mRNA capping apparat
62 CES5 is identical to CET1, which encodes the RNA triphosphatase component of the yeast capping appara
63                                    Cet1, the RNA triphosphatase component of the yeast mRNA capping a
64                                    Cet1, the RNA triphosphatase component of the yeast mRNA capping a
65 zosaccharomyces pombe Pct1 are the essential RNA triphosphatase components of the mRNA capping appara
66 structural and mechanistic divergence of the RNA triphosphatase components of the yeast and metazoan
67                    These proteins are the 5' RNA triphosphatase Ctl1p, the cell cycle-regulated trans
68                              Chlorella virus RNA triphosphatase (cvRtp1) is the smallest member of a
69 of viral replication on an intact nucleotide/RNA triphosphatase domain and an N-terminal cluster of b
70                  We recently showed that the RNA triphosphatase domain of the Caenorhabditis elegans
71  AcNPV phosphatase is similar to that of the RNA triphosphatase domain of the metazoan cellular mRNA
72 ific cysteine phosphatases that includes the RNA triphosphatase domains of metazoan and plant mRNA ca
73                 Here we demonstrate that the RNA triphosphatase dual-specificity phosphatase 11 (DUSP
74          We suggest that the metal-dependent RNA triphosphatases encoded by yeast and DNA viruses com
75 hosphatase (BVP) is a member of the metazoan RNA triphosphatase enzyme family that includes the RNA t
76 which is the signature P-loop residue of the RNA triphosphatase family and a likely determinant of th
77       Ctl1 is the second member of the yeast RNA triphosphatase family, but is probably involved in a
78  distinct lineage within the metal-dependent RNA triphosphatase family.
79 y unrelated to the cysteine-phosphatase-type RNA triphosphatases found in metazoans and plants, which
80 y unrelated to the cysteine-phosphatase-type RNA triphosphatases found in metazoans and plants.
81  metal-independent cysteine phosphatase-type RNA triphosphatases found in metazoans and plants.
82 d by the crystal structure of the homologous RNA triphosphatase from Saccharomyces cerevisiae (Cet1p)
83 , or E192A into the fusion protein abrogates RNA triphosphatase function in vivo.
84 ential action of three enzymatic activities: RNA triphosphatase, guanylyl-transferase, and methyltran
85 ls, is catalyzed by the sequential action of RNA triphosphatase, guanylyltransferase, and (guanine-N-
86                                     Although RNA triphosphatases have a core alpha/beta fold similar
87 ally results in phosphatase functions, e.g., RNA triphosphatase, inorganic polyphosphatase, or thiami
88                                              RNA triphosphatase is an essential mRNA processing enzym
89                         The mechanism of the RNA triphosphatase is similar to that of PTPs: the activ
90 rface is uniquely deleterious when the yeast RNA triphosphatase must function in concert with the end
91 xhibits monomer-associated nucleoside and 5' RNA triphosphatase (NTPase/RTPase) activities that are m
92                       A second S. cerevisiae RNA triphosphatase/NTPase (named Cth1p) containing motif
93 e BVP, and were unable to complement a yeast RNA triphosphatase null mutant in vivo.
94 rs mechanistically and structurally from the RNA triphosphatase of mammals.
95 ependent phosphohydrolases that includes the RNA triphosphatases of fungi and other large eukaryotic
96 ependent phosphohydrolases that includes the RNA triphosphatases of fungi and the malaria parasite Pl
97 ependent phosphohydrolases that includes the RNA triphosphatases of fungi, microsporidia, and protozo
98 endent phosphohydrolases, which includes the RNA triphosphatases of fungi, protozoa, Chlorella virus
99 ependent phosphohydrolases that includes the RNA triphosphatases of fungi, protozoa, poxviruses, and
100 turally and mechanistically unrelated to the RNA triphosphatases of metazoans and plants.
101 st RNA triphosphatase Cet1 than it is to the RNA triphosphatases of other DNA viruses.
102 ion of yeast deletion strains missing either RNA triphosphatase or guanylyltransferase required termi
103 fy a novel interaction between fission yeast RNA triphosphatase Pct1, the enzyme that initiates cap f
104        Here we characterize a 303 amino acid RNA triphosphatase (Pct1p) encoded by the fission yeast
105                                              RNA triphosphatase presents an attractive target for ant
106                                       Hence, RNA triphosphatase presents an ideal target for structur
107  separate RNA guanylyltransferase (Pgt1) and RNA triphosphatase (Prt1) enzymes and that the triphosph
108  BVP structure to the apoenzyme of mammalian RNA triphosphatase reveals a concerted movement of the A
109 y by the sequential action of three enzymes: RNA triphosphatase, RNA guanylyltransferase, and RNA (gu
110 ing enzyme is a multifunctional protein with RNA triphosphatase, RNA guanylyltransferase, and RNA (gu
111 ere we report that PBCV-1 encodes a separate RNA triphosphatase (RTP) that catalyzes the initial step
112                                          The RNA triphosphatase (RTPase) activity of NSP2 may account
113 ping enzymes are bifunctional, carrying both RNA triphosphatase (RTPase) and guanylyltransferase (GTa
114 riphosphatase (NTPase)/RNA helicase and a 5'-RNA triphosphatase (RTPase).
115 nistically and structurally, to the metazoan RNA triphosphatases, suggesting an abrupt evolutionary d
116                           Trypanosoma brucei RNA triphosphatase TbCet1 is a 252-amino acid polypeptid
117 TP is more similar in structure to the yeast RNA triphosphatases than to the enzymes of metazoan DNA
118 nservation of quaternary structure in fungal RNA triphosphatases, whereby the delicate tunnel archite
119 report the 1.65 A crystal structure of mouse RNA triphosphatase, which reveals a deep, positively cha
120  TbCet1 is a monomeric enzyme, unlike fungal RNA triphosphatases, which are homodimers.
121 t understood family members are the eukaryal RNA triphosphatases, which catalyze the initial step in
122 cal members are the eukaryal metal-dependent RNA triphosphatases, which catalyze the initial step in

 
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