Antisense oligonucleotides targeted to the domain IIId of the hepatitis C virus IRES compete with 40S ribosomal subunit binding and prevent in vitro translation
about
A hepatitis C virus (HCV) internal ribosome entry site (IRES) domain III-IV-targeted aptamer inhibits translation by binding to an apical loop of domain IIIdA peptide derived from RNA recognition motif 2 of human la protein binds to hepatitis C virus internal ribosome entry site, prevents ribosomal assembly, and inhibits internal initiation of translation.Proteins surrounding hairpin IIIe of the hepatitis C virus internal ribosome entry site on the human 40S ribosomal subunitCationic phosphoramidate -oligonucleotides efficiently target single-stranded DNA and RNA and inhibit hepatitis C virus IRES-mediated translationTargeted inhibition of the hepatitis C internal ribosomal entry site genomic RNA with oligonucleotide conjugatesThe Picornavirus Avian Encephalomyelitis Virus Possesses a Hepatitis C Virus-Like Internal Ribosome Entry Site ElementHCV IRES interacts with the 18S rRNA to activate the 40S ribosome for subsequent steps of translation initiationChemical synthesis of LNA-2-thiouridine and its influence on stability and selectivity of oligonucleotide binding to RNA.Optimized high-throughput screen for hepatitis C virus translation inhibitors.The HCV IRES pseudoknot positions the initiation codon on the 40S ribosomal subunit.Hepatitis C virus translation inhibitors targeting the internal ribosomal entry site.Duck Hepatitis A virus possesses a distinct type IV internal ribosome entry site element of picornavirusThe 3'-terminal hexamer sequence of classical swine fever virus RNA plays a role in negatively regulating the IRES-mediated translation.Interference of ribosomal frameshifting by antisense peptide nucleic acids suppresses SARS coronavirus replication.Anti-HCV RNA Aptamers Targeting the Genomic cis-Acting Replication Element.Intracellular inhibition of hepatitis C virus (HCV) internal ribosomal entry site (IRES)-dependent translation by peptide nucleic acids (PNAs) and locked nucleic acids (LNAs).Unmasking the information encoded as structural motifs of viral RNA genomes: a potential antiviral target.RNA aptamer-mediated interference of HCV replication by targeting the CRE-5BSL3.2 domain.Hepatitis C virus nonstructural protein 5A (NS5A) is an RNA-binding protein.Interfering with hepatitis C virus IRES activity using RNA molecules identified by a novel in vitro selection method.Inhibition of hepatitis C virus IRES-mediated translation by small RNAs analogous to stem-loop structures of the 5'-untranslated region.Hepatitis C virus RNA: molecular switches mediated by long-range RNA-RNA interactions?Induced-Decay of Glycine Decarboxylase Transcripts as an Anticancer Therapeutic Strategy for Non-Small-Cell Lung Carcinoma.
P2860
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P2860
Antisense oligonucleotides targeted to the domain IIId of the hepatitis C virus IRES compete with 40S ribosomal subunit binding and prevent in vitro translation
description
2003 nî lūn-bûn
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2003 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Antisense oligonucleotides tar ...... d prevent in vitro translation
@ast
Antisense oligonucleotides tar ...... d prevent in vitro translation
@en
Antisense oligonucleotides tar ...... d prevent in vitro translation
@nl
type
label
Antisense oligonucleotides tar ...... d prevent in vitro translation
@ast
Antisense oligonucleotides tar ...... d prevent in vitro translation
@en
Antisense oligonucleotides tar ...... d prevent in vitro translation
@nl
prefLabel
Antisense oligonucleotides tar ...... d prevent in vitro translation
@ast
Antisense oligonucleotides tar ...... d prevent in vitro translation
@en
Antisense oligonucleotides tar ...... d prevent in vitro translation
@nl
P2093
P2860
P356
P1476
Antisense oligonucleotides tar ...... d prevent in vitro translation
@en
P2093
Béatrice Tallet-Lopez
Eric Dausse
Lydia Aldaz-Carroll
Sandrine Chabas
P2860
P304
P356
10.1093/NAR/GKG139
P407
P577
2003-01-01T00:00:00Z