Guanosine 2-NH2 groups of Escherichia coli RNase P RNA involved in intramolecular tertiary contacts and direct interactions with tRNA.
about
The Diversity of Ribonuclease P: Protein and RNA Catalysts with Analogous Biological FunctionsPurine N7 groups that are crucial to the interaction of Escherichia coli rnase P RNA with tRNADistinct modes of mature and precursor tRNA binding to Escherichia coli RNase P RNA revealed by NAIM analysesOf proteins and RNA: the RNase P/MRP family.Helix P4 is a divalent metal ion binding site in the conserved core of the ribonuclease P ribozyme.Structural plasticity and Mg2+ binding properties of RNase P P4 from combined analysis of NMR residual dipolar couplings and motionally decoupled spin relaxationVerification of phylogenetic predictions in vivo and the importance of the tetraloop motif in a catalytic RNA.Probing the architecture of the B. subtilis RNase P holoenzyme active site by cross-linking and affinity cleavageThe putative RNase P motif in the DEAD box helicase Hera is dispensable for efficient interaction with RNA and helicase activity.Active site constraints in the hydrolysis reaction catalyzed by bacterial RNase P: analysis of precursor tRNAs with a single 3'-S-phosphorothiolate internucleotide linkageAntisense inhibition of Escherichia coli RNase P RNA: mechanistic aspects.Evaluation of bacterial RNase P RNA as a drug target.The contribution of the C5 protein subunit of Escherichia coli ribonuclease P to specificity for precursor tRNA is modulated by proximal 5' leader sequences.Thermostable RNase P RNAs lacking P18 identified in the Aquificales.The precursor tRNA 3'-CCA interaction with Escherichia coli RNase P RNA is essential for catalysis by RNase P in vivo.Structural basis of a ribozyme's thermostability: P1-L9 interdomain interaction in RNase P RNA.Minor changes largely restore catalytic activity of archaeal RNase P RNA from Methanothermobacter thermoautotrophicus.Archaeal-bacterial chimeric RNase P RNAs: towards understanding RNA's architecture, function and evolution.Catalysis by RNase P RNA: unique features and unprecedented active site plasticity.Exploring the minimal substrate requirements for trans-cleavage by RNase P holoenzymes from Escherichia coli and Bacillus subtilis.Understanding catalysis of phosphate-transfer reactions by the large ribozymes.
P2860
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P2860
Guanosine 2-NH2 groups of Escherichia coli RNase P RNA involved in intramolecular tertiary contacts and direct interactions with tRNA.
description
1999 nî lūn-bûn
@nan
1999年の論文
@ja
1999年学术文章
@wuu
1999年学术文章
@zh
1999年学术文章
@zh-cn
1999年学术文章
@zh-hans
1999年学术文章
@zh-my
1999年学术文章
@zh-sg
1999年學術文章
@yue
1999年學術文章
@zh-hant
name
Guanosine 2-NH2 groups of Esch ...... direct interactions with tRNA.
@en
Guanosine 2-NH2 groups of Esch ...... direct interactions with tRNA.
@nl
type
label
Guanosine 2-NH2 groups of Esch ...... direct interactions with tRNA.
@en
Guanosine 2-NH2 groups of Esch ...... direct interactions with tRNA.
@nl
prefLabel
Guanosine 2-NH2 groups of Esch ...... direct interactions with tRNA.
@en
Guanosine 2-NH2 groups of Esch ...... direct interactions with tRNA.
@nl
P2093
P2860
P1433
P1476
Guanosine 2-NH2 groups of Esch ...... direct interactions with tRNA.
@en
P2093
P2860
P304
P356
10.1017/S1355838299981499
P407
P577
1999-01-01T00:00:00Z