Sequence and structure of the catalytic RNA of hepatitis delta virus genomic RNA.
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Efficient trans-cleavage of a stem-loop RNA substrate by a ribozyme derived from neurospora VS RNADetermination of the secondary structure of and cellular protein binding to the 3'-untranslated region of the hepatitis C virus RNA genomeImino proton NMR analysis of HDV ribozymes: nested double pseudoknot structure and Mg2+ ion-binding site close to the catalytic core in solutionHepatitis delta virus: the molecular basis of laboratory diagnosis.Subcellular localization and expression of bamboo mosaic virus satellite RNA-encoded proteinAnalysis of the cleavage reaction of a trans-acting human hepatitis delta virus ribozyme.Mutagenesis analysis of a hepatitis delta virus genomic ribozyme.Ribozyme-based gene-inactivation systems require a fine comprehension of their substrate specificities; the case of delta ribozymeThe genomic HDV ribozyme utilizes a previously unnoticed U-turn motif to accomplish fast site-specific catalysisLarge hepatitis delta antigen in packaging and replication inhibition: role of the carboxyl-terminal 19 amino acids and amino-terminal sequences.A pseudoknot ribozyme structure is active in vivo and required for hepatitis delta virus RNA replicationRandom mutations to evaluate the role of bases at two important single-stranded regions of genomic HDV ribozyme.Mutagenesis analysis of the self-cleavage domain of hepatitis delta virus antigenomic RNARNA-binding activity of hepatitis delta antigen involves two arginine-rich motifs and is required for hepatitis delta virus RNA replication.Replication of hepatitis delta virus RNA: effect of mutations of the autocatalytic cleavage sites.Nuclear localization signals, but not putative leucine zipper motifs, are essential for nuclear transport of hepatitis delta antigenHepatitis delta antigens enhance the ribozyme activities of hepatitis delta virus RNA in vivoCore sequences and a cleavage site wobble pair required for HDV antigenomic ribozyme self-cleavage.Core-associated non-duplex sequences distinguishing the genomic and antigenomic self-cleaving RNAs of hepatitis delta virus.3-D models of the antigenomic ribozyme of the hepatitis delta agent with eight new contacts suggested by sequence analysis of 188 cDNA clonesAssessment of disparate structural features in three models of the hepatitis delta virus ribozyme.A circular trans-acting hepatitis delta virus ribozyme.Wobble pairs of the HDV ribozyme play specific roles in stabilization of active site dynamics.Substrate specificity of delta ribozyme cleavage.Addition of an extra substrate binding site and partial destabilization of stem structures in HDV ribozyme give rise to high sequence-specificity for its target RNA.The effect of Lp3 enlargement on the folding and catalysis of hepatitis delta virus cis-cleaving ribozyme.An AU at the first base pair of helix 3 elevates the catalytic activity of hepatitis delta virus ribozymes.The catalytic domain of human hepatitis delta virus RNA. A proton nuclear magnetic resonance study.Cleavage reaction of HDV ribozymes in the presence of Mg2+ is accompanied by a conformational change
P2860
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P2860
Sequence and structure of the catalytic RNA of hepatitis delta virus genomic RNA.
description
1992 nî lūn-bûn
@nan
1992年の論文
@ja
1992年学术文章
@wuu
1992年学术文章
@zh
1992年学术文章
@zh-cn
1992年学术文章
@zh-hans
1992年学术文章
@zh-my
1992年学术文章
@zh-sg
1992年學術文章
@yue
1992年學術文章
@zh-hant
name
Sequence and structure of the catalytic RNA of hepatitis delta virus genomic RNA.
@en
Sequence and structure of the catalytic RNA of hepatitis delta virus genomic RNA.
@nl
type
label
Sequence and structure of the catalytic RNA of hepatitis delta virus genomic RNA.
@en
Sequence and structure of the catalytic RNA of hepatitis delta virus genomic RNA.
@nl
prefLabel
Sequence and structure of the catalytic RNA of hepatitis delta virus genomic RNA.
@en
Sequence and structure of the catalytic RNA of hepatitis delta virus genomic RNA.
@nl
P2093
P1476
Sequence and structure of the catalytic RNA of hepatitis delta virus genomic RNA.
@en
P2093
P304
P356
10.1016/0022-2836(92)90728-3
P407
P577
1992-01-01T00:00:00Z