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1 bonucleases followed by 5' end maturation by ribonuclease P.
2 e tRNA pool and the RNA-processing ribozyme, ribonuclease P.
3 of the RNA component of Thermotoga maritima ribonuclease P.
4 ly understanding the overall architecture of ribonuclease P.
5 heir discovery of RNA catalysts in bacterial ribonuclease P (an enzyme catalyzing 5' maturation of tR
6 ive structures that are not cleaved by mouse ribonuclease P and motivate a paradigm that may help to
7 ed nearly all components of three complexes: Ribonuclease P and the RNA Exosome, including nuclear DI
9 mponents-such as the RNA moiety of bacterial ribonuclease P-can sometimes be replaced with a highly d
16 y active in vitro, i.e. it is a ribozyme.The Ribonuclease P Database is a compilation of ribonuclease
19 dize with any mRNA and recruit intracellular ribonuclease P for specific degradation of the target mR
20 structure of the catalytic RNA component of ribonuclease P has been well characterized in Bacteria,
30 A, the catalytic subunit of Escherichia coli ribonuclease P, is accelerated by C5 protein (the protei
31 with MRPP2 and MRPP3, form the mitochondrial ribonuclease P (mt-RNase P) complex that cleaves the 5'
33 h the protein component of Bacillus subtilis ribonuclease P (P protein) site specifically modified wi
34 conformational dynamics of Bacillus subtilis ribonuclease P protein (P protein) in its folded state,
35 ies have demonstrated that Bacillus subtilis ribonuclease P protein (P protein) is conformationally h
38 The crystal structure of Bacillus subtilis ribonuclease P protein is reported at 2.6 angstroms reso
42 universal feature of the catalytic domain of ribonuclease P RNA is a bulged-helix motif within the P1
43 o humans and are likely to interact with the ribonuclease P RNA or other protein subunits are identif
45 RNA subunit of the ribonucleoprotein enzyme ribonuclease P (RNase P (P RNA) contains the active site
46 ysis are delineated for the RNA component of ribonuclease P (RNase P RNA) by a combination of steady-
49 ion of the tRNA processing ribonucleoprotein ribonuclease P (RNase P) and the mechanism of its intran
59 a ubiquitous human intracellular marker, the ribonuclease P (RNase P) in order to evaluate tissue inj
60 ing of precursor tRNAs (ptRNAs) by bacterial ribonuclease P (RNase P) involves an encounter complex (
77 and the eukaryote nucleus, the endonuclease ribonuclease P (RNase P) is composed of a catalytic RNA
78 om tRNA precursor transcripts (pre-tRNAs) by ribonuclease P (RNase P) is essential for protein synthe
88 ction procedure, we have previously isolated ribonuclease P (RNase P) ribozyme variants that efficien
89 k and statistical analyses, we show that the ribonuclease P (RNase P) RNA adopts heterogeneous confor
90 ive different RNAs: tRNA, 5S rRNA, bacterial ribonuclease P (RNase P) RNA, eukaryotic small subunit r
91 , P protein is the noncatalytic component of ribonuclease P (RNase P) that is critical for achieving
92 , the protein component of Bacillus subtilis ribonuclease P (RNase P) was overproduced in Escherichia
93 polypeptide and an RNA structural motif with ribonuclease P (RNase P), a nuclear endoribonuclease ori
96 re like a pre-tRNA and recruit intracellular ribonuclease P (RNase P), a tRNA processing enzyme, to d
98 0 is an essential component of mitochondrial Ribonuclease P (RNase P), an enzyme required for mitocho
102 ing in the most highly conserved P4 helix of ribonuclease P (RNase P), the ribonucleoprotein that cat
103 es induced in substrates by Escherichia coli ribonuclease P (RNase P), we have incorporated an inters
108 Ribonuclease P Database is a compilation of ribonuclease P sequences, sequence alignments, secondary
109 Ribonuclease P Database is a compilation of ribonuclease P sequences, sequence alignments, secondary
110 Ribonuclease P Database is a compilation of ribonuclease P sequences, sequence alignments, secondary
111 1-nucleotide specificity domain of an A-type ribonuclease P that differs in secondary and tertiary st
112 The protein subunit of Escherichia coli ribonuclease P (which has a cysteine residue at position