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1 cursors to nucleoside tetraphosphate (Np(4)) RNA caps.
2 ose caps set them apart from other bacterial RNA caps.
3 t remove the y phosphates of ppp-RNAs during RNA capping.
4 TbCMT1 did not affect parasite growth or SL RNA capping.
5 at are essential to virus replication and to RNA capping.
6 gation but also in stimulating nascent viral RNA capping.
7 move the gamma phosphates of ppp-RNAs during RNA capping.
8 is is the first observation of ATP-dependent RNA capping.
11 D6; mRNA capping enzyme subunits D1 and D12; RNA cap 2'-O-methyltransferase; A18 DNA helicase; DNA-de
12 y-mismatched receptor-binding o1 trimers and RNA-capping 2 pentamers balance competing needs of capsi
13 quent modifications characteristic of the SL RNA cap 4 were added successively in a 5' to 3' directio
15 itute the N7- and 2'-O-methylated SARS-CoV-2 RNA cap ((7Me)GpppA(2'-O-Me)) using virally encoded non-
16 oded methyltransferases (MTases) involved in RNA capping, a guanine-N7-MTase and a ribose-2'-O-MTase.
18 establish NAD(+) as an alternative mammalian RNA cap and DXO as a deNADding enzyme modulating cellula
21 ein 5 (NS5) contains a methyltransferase for RNA capping and a polymerase for viral RNA synthesis.
23 Here, we report a mechanism for SARS-CoV-2 RNA capping and document structural details at atomic re
25 al surfaces of two of its proteins; that the RNA capping and export apparatus is a hollow cylinder, w
26 al protein 1 (nsP1) is responsible for viral RNA capping and gates the replication organelles by asse
27 ation factors 1a, with domains implicated in RNA capping and helicase functions, and 2a, with a centr
28 RNA replication proteins: 1a, which contains RNA capping and helicase-like domains, and 2a, which is
29 RNA replication proteins: 1a, which contains RNA capping and helicase-like domains, and the polymeras
31 esults extend our understanding of nidovirus RNA capping and methylation beyond coronaviruses and als
32 only improve the understanding of SARS-CoV-2 RNA capping and the mode of action of NAIs but also prov
35 and an N-terminal domain implicated in viral RNA capping, and 2a contains a central polymerase-like d
36 icase-like domain and a domain implicated in RNA capping, and 2a, which contains a polymerase-like do
37 es incorporated into IAV mRNA, "snatched" 5' RNA caps, and corresponding RNA sequences from host RNAs
38 (ii) mutations D63A and Y248A, blocking the RNA capping; and (iii) mutation R252E, affecting nsP1 me
39 d that SARS-CoV-2 nsp12 is involved in viral RNA capping as a GTase, carrying out the addition of a G
42 our understanding of the mechanism of viral RNA cap binding we performed a detailed structural and b
44 Here we identify a component of the nuclear RNA cap-binding complex (CBC), Ars2, that is important f
45 effects on pre-mRNA splicing is the nuclear RNA cap-binding complex (CBC), which plays a key role in
46 tion is followed by formation of a messenger RNA cap-binding complex that includes the initiation fac
47 protein 2 (ARS2), a component of the nuclear RNA CAP-binding complex that is crucial for biogenesis o
48 supported and the mechanism for GTP-mediated RNA capping by the SARS-CoV-2 NiRAN domain remains unres
49 Our data support the idea that coronavirus RNA capping could be targeted for development of antivir
50 h mTOR is known as a controller of messenger RNA cap-dependent translation initiation, new advances i
51 a multifunctional protein with an N-terminal RNA capping domain and a C-terminal helicase-like domain
53 The 1a protein has putative helicase and RNA-capping domains, whereas 2a contains a polymerase-li
59 its well-characterized function as the viral RNA-capping enzyme.IMPORTANCE Rotaviruses are significan
60 Recent structural studies have shown that RNA capping enzymes and DNA ligases have similar protein
61 (+)-dependent DNA ligases, and GTP-dependent RNA capping enzymes are members of a covalent nucleotidy
62 t contemporary DNA ligases, RNA ligases, and RNA capping enzymes evolved by the fusion of ancillary e
68 f a shared structural basis for catalysis by RNA capping enzymes, DNA ligases, and RNA ligases, which
75 xtend our current understanding of nidovirus RNA cap formation and methylation beyond the coronavirus
76 e, and the recently recognized Mesoniviridae RNA cap formation and methylation have been best studied
77 ping enzyme guanylyltransferase activity and RNA cap formation by transcription factor IIH-mediated C
83 pAG-RNA), leading to the formation of the 5' RNA cap: G0pppAG-RNA --> (m7)G0pppAG-RNA ("cap-0")-->(m7
84 lates the N7 and 2'-O positions of the viral RNA cap (GpppA-RNA --> m(7)GpppA-RNA --> m(7)GpppAm-RNA)
86 ally catalyzes two methylations of the viral RNA cap, GpppA-RNA-->m(7)GpppA-RNA-->m(7)GpppAm-RNA, by
87 de for nsp14, a bifunctional enzyme carrying RNA cap guanine N7-methyltransferase (MTase) and 3'-5' e
94 nd Caenorhabditis elegans we have found that RNA capping is also essential for metazoan viability.
95 systems level, CapQuant can reveal both the RNA cap landscape and the transcription start site distr
96 the mRNA capping apparatus of VSV evolved an RNA capping machinery that functions in a sequence-speci
101 GFP) showed that sequences in the N-terminal RNA capping module of 1a mediate membrane association.
103 ose a wide repertoire of potential bacterial RNA capping molecules, and provide mechanistic insights
104 nal enzyme bearing 3'-5' exoribonuclease and RNA cap N7-guanine methyltransferase activities involved
106 ty of accurately and sensitively quantifying RNA caps on a systems level, CapQuant can reveal both th
114 ty and amino acid requirements typical of an RNA cap-specific, m(7)G-dependent N2 methyltransferase.
115 g with cellular metabolites as a novel viral RNA-capping strategy, which could be used by other virus
120 also utilize GTP to produce an authentic 5' RNA cap structure, though the GTP-mediated mechanism is
127 s to both N7 and 2'-O positions of the viral RNA cap, the GTP-binding pocket functions only during th
129 responsible for converting 7-methylguanosine RNA caps to the 2,2,7-trimethylguanosine cap structures
133 ific binding of the methyltransferase to the RNA cap was demonstrated by UV cross-linking to [32P]GMP