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Article

Crystal structure of an RNA tertiary domain essential to HCV IRES-mediated translation initiation

1 Apr 2002

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Share to RNA and protein synthesis mechanisms
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Share to Viral Infections and Immunology Research

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Identifiers

PMID: 11927953
DOI: 10.1038/nsb781

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Related research

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Crystal structure of an RNA tertiary domain essential to HCV IRES-mediated translation initiationPMID 11927953Read ↗

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The hepatitis C virus internal ribosome entry site adopts an ion-dependent tertiary fold.Semantic proximity Read ↗

Cryo-EM structure of Hepatitis C virus IRES bound to the human ribosome at 3.9-Å resolutionSemantic proximity Read ↗

Translation initiation by the hepatitis C virus IRES requires eIF1A and ribosomal complex remodelingSemantic proximity Read ↗

Molecular architecture of 40S translation initiation complexes on the hepatitis C virus IRESSemantic proximity Read ↗

An accurately preorganized IRES RNA structure enables eIF4G capture for initiation of viral translationSemantic proximity Read ↗

Structural methods for studying IRES function.Semantic proximity Read ↗

Analysis of natural variants of the hepatitis C virus internal ribosome entry site reveals that primary sequence plays a key role in cap-independent translation.Semantic proximity Read ↗

HCV and CSFV IRES domain II mediate eIF2 release during 80S ribosome assemblySemantic proximity Read ↗

Two RNA-binding motifs in eIF3 direct HCV IRES-dependent translation.Semantic proximity Read ↗

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