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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 its components, and the organization of its catalytic RNA.
4 understanding the structure and function of catalytic RNA.
5 up II introns are mobile elements as well as catalytic RNAs.
6 neral mechanism for the evolution of complex catalytic RNAs.
7 property has been shown in only a handful of catalytic RNAs.
8 utionary roots in the chemical repertoire of catalytic RNAs.
9 de insights on the structure and function of catalytic RNAs.
10 terogeneous cleavage kinetics common to many catalytic RNAs.
13 Nase P is a ribonucleoprotein made up of one catalytic RNA and five protein cofactors including L7Ae,
15 the RNase P holoenzyme consists of one large catalytic RNA and one small protein subunit, in archaea
18 ntegral subunits of RNase MRP, stabilize its catalytic RNA, and are required for rRNA maturation and
19 ncorporating ligand-responsive self-cleaving catalytic RNAs (aptazymes) into guide RNAs, we developed
22 of protein, but several distinct classes of catalytic RNAs are known to promote chemical transformat
25 tructed an empirical fitness landscape for a catalytic RNA by combining next-generation sequencing, c
27 n the tertiary folding of a variety of large catalytic RNAs by providing a specific binding site for
28 sequence) complementary to a target RNA, the catalytic RNA can be converted into a sequence-specific
29 ailed understanding of the biochemistry of a catalytic RNA can facilitate the design of customized ri
30 caged RNA molecules: the light-regulation of catalytic RNA cleavage by RISC and the light-regulation
32 prokaryotic RNaseP holoenzyme consists of a catalytic RNA component and a protein subunit (RNaseP pr
35 ssential for the folding and function of the catalytic RNA component of the tRNA processing enzyme ri
37 he mutations create local distortions of the catalytic RNA component.When combined with a variety of
40 Group II introns are structurally complex catalytic RNAs considered evolutionarily related to the
45 ) complex, consistent with the idea that the catalytic RNA core forms stepwise during the B to B(act)
50 e ancestors of nuclear pre-mRNA introns, are catalytic RNAs found in bacteria, archaea, and eukaryote
51 a point mutation at nucleotide 86 of RNase P catalytic RNA from Escherichia coli (A(86)-->C(86)) incr
52 tation at nucleotides 224 and 225 of RNase P catalytic RNA from Escherichia coli (G(224)G(225) --> AA
53 a point mutation at nucleotide 95 of RNase P catalytic RNA from Escherichia coli (G(95) --> U(95)) in
54 utation at nucleotide position 80 of RNase P catalytic RNA from Escherichia coli (U80--> C80) increas
56 iments revealed that we have selected a dual-catalytic RNA from random sequences: the RNA promotes bo
58 icated in the activities of three classes of catalytic RNA: group I introns, group II introns, and 23
59 nd hybridoma technology and the discovery of catalytic RNA have led to new and very promising alterna
63 ted in functionally critical motifs in large catalytic RNAs, in riboswitches, and in regulatory eleme
64 ent structures have been determined for this catalytic RNA, including two NMR structures of the isola
66 onent of ribonucleoprotein RNase P and other catalytic RNAs, indicating convergence on a common solut
69 y to understanding the structural biology of catalytic RNA is determining the underlying networks of
72 the hepatitis delta virus (HDV) is the only catalytic RNA known to be required for the viability of
74 Nase MRP is a ribonucleoprotein with a large catalytic RNA moiety that is closely related to the RNA
90 also provided the platform to develop those catalytic RNA molecules, called ribozymes, as trans -act
93 ary antigenome contain the same cis-cleaving catalytic RNA motif that plays a crucial role in virus r
95 is delta virus (HDV) harbors a self-cleaving catalytic RNA motif, the genomic HDV ribozyme, whose cry
96 a virus (HDV) employs a unique self-cleaving catalytic RNA motif, the HDV ribozyme, during double-rol
97 ary antigenome contain a common cis-cleaving catalytic RNA motif, the HDV ribozyme, which plays a cru
98 among the smallest and simplest of the known catalytic RNA motifs and has a unique metal ion specific
99 Together, these results imply that similar catalytic RNA motifs can arise under fairly simple condi
100 nd glmS ribozymes comprise a family of small catalytic RNA motifs that catalyze the same reversible p
101 This novel approach to the synthesis of catalytic RNAs offers a number of differences and potent
102 cted mutations within Ll.ltrB, either in the catalytic RNA or in the intron-encoded protein gene ltrA
103 cription can be extended to the synthesis of catalytic RNAs outside the hammerhead ribozyme motif; (i
104 The 154 kDa complex consists of a large catalytic RNA (P RNA), a small protein cofactor and a ma
108 n all domains of life and comprises a single catalytic RNA (ribozyme) and a variable number of protei
110 mplexity and activity in a comparison of two catalytic RNAs (ribozyme ligases), raising the possibili
116 tions are the only known methods to generate catalytic RNAs (ribozymes) that do not exist in nature.
117 assembly factor, Puf6, binds to the nascent catalytic RNA-rich subunit interface within the 60S pre-
119 le for Mg(2+) adds to the diversity of known catalytic RNA strategies and unifies functional features
121 This enzyme from Escherichia coli contains a catalytic RNA subunit (M1 ribozyme) and a protein subuni
122 s a tRNA-processing enzyme and consists of a catalytic RNA subunit (M1 RNA) and a protein component (
128 d the biological function of RNase P and its catalytic RNA subunit and to employ it as a tool to down
129 dent reconstitutions of Pfu RNase P with its catalytic RNA subunit and two interacting protein cofact
130 cleaving the cognate RNA ligand, M1 RNA, the catalytic RNA subunit of E. coli RNase P, in the presenc
132 pecific ribozyme (M1GS RNA) derived from the catalytic RNA subunit of RNase P from Escherichia coli w
133 pecific ribozyme (M1GS RNA) derived from the catalytic RNA subunit of RNase P from Escherichia coli w
134 pecific ribozyme (M1GS RNA) derived from the catalytic RNA subunit of RNase P from Escherichia coli w
137 is either a ribonucleoprotein complex with a catalytic RNA subunit or a protein-only RNase P (PRORP).
139 chia coli, this RNP complex is composed of a catalytic RNA subunit, M1 RNA, and a protein cofactor, C
140 tions in tRNA biosynthesis, is composed of a catalytic RNA subunit, M1 RNA, and a protein cofactor, C
144 o multi-subunit ribonucleoprotein forms with catalytic RNA subunits to protein-only enzymes, the latt
147 he hairpin ribozyme is an example of a small catalytic RNA that catalyses the endonucleolytic transes
149 bozyme riboswitch is the first known natural catalytic RNA that employs a small-molecule cofactor.
150 examples of chemical modifications within a catalytic RNA that enhance the rate of the chemical step
151 se ribonuclease P (RNase P) is composed of a catalytic RNA that is assisted by protein subunits.
153 mS ribozyme is the first naturally occurring catalytic RNA that relies on an exogenous, nonnucleotide
157 rpin ribozyme belongs to the family of small catalytic RNAs that cleave RNA substrates in a reversibl
160 located in different folding domains of the catalytic RNA, the first in the substrate binding domain
161 crystal structure has been reported of a new catalytic RNA, the TS ribozyme, that has been identified
162 are predicted for several nucleotides in two catalytic RNAs, the hairpin ribozyme and the hepatitis d
165 across a wastewater microbiome, a synthetic catalytic RNA was used to barcode a highly conserved seg
166 on rate constant for every point mutant of a catalytic RNA, we demonstrated that abundance in seriall
168 s modified for nuclease stability can target catalytic RNAs when the elements of tertiary interaction
169 he hairpin ribozyme is an example of a small catalytic RNA which catalyses the endonucleolytic transe
172 ng-lived misfolded conformation of a group I catalytic RNA with efficiencies that depend on the stabi
174 ribozyme is among the smallest of the known catalytic RNAs, with an active site consisting of a six-