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1 etal binding site observed in the hammerhead catalytic RNA.
2 f pre-tRNA processing in vitro, i.e. it is a catalytic RNA.
3 understanding the structure and function of catalytic RNA.
4 up II introns are mobile elements as well as catalytic RNAs.
5 neral mechanism for the evolution of complex catalytic RNAs.
6 utionary roots in the chemical repertoire of catalytic RNAs.
7 de insights on the structure and function of catalytic RNAs.
8 terogeneous cleavage kinetics common to many catalytic RNAs.
11 Nase P is a ribonucleoprotein made up of one catalytic RNA and five protein cofactors including L7Ae,
12 the RNase P holoenzyme consists of one large catalytic RNA and one small protein subunit, in archaea
14 ncorporating ligand-responsive self-cleaving catalytic RNAs (aptazymes) into guide RNAs, we developed
17 of protein, but several distinct classes of catalytic RNAs are known to promote chemical transformat
20 tructed an empirical fitness landscape for a catalytic RNA by combining next-generation sequencing, c
21 n the tertiary folding of a variety of large catalytic RNAs by providing a specific binding site for
22 sequence) complementary to a target RNA, the catalytic RNA can be converted into a sequence-specific
23 ailed understanding of the biochemistry of a catalytic RNA can facilitate the design of customized ri
24 caged RNA molecules: the light-regulation of catalytic RNA cleavage by RISC and the light-regulation
26 prokaryotic RNaseP holoenzyme consists of a catalytic RNA component and a protein subunit (RNaseP pr
29 ssential for the folding and function of the catalytic RNA component of the tRNA processing enzyme ri
31 he mutations create local distortions of the catalytic RNA component.When combined with a variety of
34 Group II introns are structurally complex catalytic RNAs considered evolutionarily related to the
39 ) complex, consistent with the idea that the catalytic RNA core forms stepwise during the B to B(act)
42 e ancestors of nuclear pre-mRNA introns, are catalytic RNAs found in bacteria, archaea, and eukaryote
43 a point mutation at nucleotide 86 of RNase P catalytic RNA from Escherichia coli (A(86)-->C(86)) incr
44 tation at nucleotides 224 and 225 of RNase P catalytic RNA from Escherichia coli (G(224)G(225) --> AA
45 a point mutation at nucleotide 95 of RNase P catalytic RNA from Escherichia coli (G(95) --> U(95)) in
46 utation at nucleotide position 80 of RNase P catalytic RNA from Escherichia coli (U80--> C80) increas
48 iments revealed that we have selected a dual-catalytic RNA from random sequences: the RNA promotes bo
50 icated in the activities of three classes of catalytic RNA: group I introns, group II introns, and 23
51 nd hybridoma technology and the discovery of catalytic RNA have led to new and very promising alterna
55 ted in functionally critical motifs in large catalytic RNAs, in riboswitches, and in regulatory eleme
56 ent structures have been determined for this catalytic RNA, including two NMR structures of the isola
59 y to understanding the structural biology of catalytic RNA is determining the underlying networks of
61 the hepatitis delta virus (HDV) is the only catalytic RNA known to be required for the viability of
63 Nase MRP is a ribonucleoprotein with a large catalytic RNA moiety that is closely related to the RNA
78 also provided the platform to develop those catalytic RNA molecules, called ribozymes, as trans -act
81 ary antigenome contain the same cis-cleaving catalytic RNA motif that plays a crucial role in virus r
83 is delta virus (HDV) harbors a self-cleaving catalytic RNA motif, the genomic HDV ribozyme, whose cry
84 a virus (HDV) employs a unique self-cleaving catalytic RNA motif, the HDV ribozyme, during double-rol
85 ary antigenome contain a common cis-cleaving catalytic RNA motif, the HDV ribozyme, which plays a cru
86 among the smallest and simplest of the known catalytic RNA motifs and has a unique metal ion specific
87 Together, these results imply that similar catalytic RNA motifs can arise under fairly simple condi
88 nd glmS ribozymes comprise a family of small catalytic RNA motifs that catalyze the same reversible p
90 cted mutations within Ll.ltrB, either in the catalytic RNA or in the intron-encoded protein gene ltrA
91 cription can be extended to the synthesis of catalytic RNAs outside the hammerhead ribozyme motif; (i
95 mplexity and activity in a comparison of two catalytic RNAs (ribozyme ligases), raising the possibili
101 This enzyme from Escherichia coli contains a catalytic RNA subunit (M1 ribozyme) and a protein subuni
102 s a tRNA-processing enzyme and consists of a catalytic RNA subunit (M1 RNA) and a protein component (
108 dent reconstitutions of Pfu RNase P with its catalytic RNA subunit and two interacting protein cofact
109 cleaving the cognate RNA ligand, M1 RNA, the catalytic RNA subunit of E. coli RNase P, in the presenc
111 pecific ribozyme (M1GS RNA) derived from the catalytic RNA subunit of RNase P from Escherichia coli w
112 pecific ribozyme (M1GS RNA) derived from the catalytic RNA subunit of RNase P from Escherichia coli w
113 pecific ribozyme (M1GS RNA) derived from the catalytic RNA subunit of RNase P from Escherichia coli w
117 chia coli, this RNP complex is composed of a catalytic RNA subunit, M1 RNA, and a protein cofactor, C
118 tions in tRNA biosynthesis, is composed of a catalytic RNA subunit, M1 RNA, and a protein cofactor, C
124 he hairpin ribozyme is an example of a small catalytic RNA that catalyses the endonucleolytic transes
126 bozyme riboswitch is the first known natural catalytic RNA that employs a small-molecule cofactor.
127 examples of chemical modifications within a catalytic RNA that enhance the rate of the chemical step
128 se ribonuclease P (RNase P) is composed of a catalytic RNA that is assisted by protein subunits.
130 mS ribozyme is the first naturally occurring catalytic RNA that relies on an exogenous, nonnucleotide
134 rpin ribozyme belongs to the family of small catalytic RNAs that cleave RNA substrates in a reversibl
136 located in different folding domains of the catalytic RNA, the first in the substrate binding domain
137 crystal structure has been reported of a new catalytic RNA, the TS ribozyme, that has been identified
138 are predicted for several nucleotides in two catalytic RNAs, the hairpin ribozyme and the hepatitis d
141 on rate constant for every point mutant of a catalytic RNA, we demonstrated that abundance in seriall
143 s modified for nuclease stability can target catalytic RNAs when the elements of tertiary interaction
144 he hairpin ribozyme is an example of a small catalytic RNA which catalyses the endonucleolytic transe
146 ng-lived misfolded conformation of a group I catalytic RNA with efficiencies that depend on the stabi
148 ribozyme is among the smallest of the known catalytic RNAs, with an active site consisting of a six-
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