ArticleJournal of virology2009
Hepatitis delta antigen requires a minimum length of the hepatitis delta virus unbranched rod RNA structure for binding.
Article in Journal of virology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
19 citing papers in PubMed, 29 citations in OpenAlex.
- Structural characterization of the HDV virion and its ribonucleoprotein.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Pathogenesis, prevention, and therapeutic advances in hepatitis B, C, and D.Virology journal · 2025Review
- Structure and nucleic acid interactions of the SProceedings of the National Academy of Sciences of the United States of America · 2025Article
- NJournal of virology · 2022Article
- Medical Advances in Hepatitis D Therapy: Molecular Targets.International journal of molecular sciences · 2022Review
- Enhancer RNAs stimulate Pol II pause release by harnessing multivalent interactions to NELF.Nature communications · 2022Article
- Hepatitis Delta Virus Genome RNA Synthesis Initiates at Position 1646 with a Nontemplated Guanosine.Journal of virology · 2022Article
- Hepatitis Delta Virus histone mimicry drives the recruitment of chromatin remodelers for viral RNA replication.Nature communications · 2020Article
- Structural Pattern Differences in Unbranched Rod-like RNA of Hepatitis Delta Virus affect RNA Editing.Viruses · 2019Article
- Hepatitis Delta Antigen Regulates mRNA and Antigenome RNA Levels during Hepatitis Delta Virus Replication.Journal of virology · 2019Article
- Structural and nucleic acid binding properties of hepatitis delta virus small antigen.World journal of virology · 2017Article
- Hepatitis D Virus Replication.Cold Spring Harbor perspectives in medicine · 2015Review
- RNA helicase A activity is inhibited by oncogenic transcription factor EWS-FLI1.Nucleic acids research · 2015Article
- Hepatitis delta antigen requires a flexible quasi-double-stranded RNA structure to bind and condense hepatitis delta virus RNA in a ribonucleoprotein complex.Journal of virology · 2014Article
- Arginine-rich motifs are not required for hepatitis delta virus RNA binding activity of the hepatitis delta antigen.Journal of virology · 2013Article
- Control of ADAR1 editing of hepatitis delta virus RNAs.Current topics in microbiology and immunology · 2012Review
- Article
- Multimerization of hepatitis delta antigen is a critical determinant of RNA binding specificity.Journal of virology · 2010Article
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Hepatitis delta virus (HDV) is a subviral pathogen that increases the severity of liver disease caused by hepatitis B virus. Both the small circular RNA genome and its complement, the antigenome, form a characteristic unbranched rod structure in which approximately 70% of the nucleotides are base paired. These RNAs are associated with the sole virally encoded protein, hepatitis delta antigen (HDAg), in infected cells; however, the nature of the ribonucleoprotein complexes (RNPs) is not well understood. Previous analyses of binding in vitro using native, bacterially expressed HDAg have been hampered by a lack of specificity for HDV RNA. Here, we show that removal of the C-terminal 35 amino acids of HDAg yields a native, bacterially expressed protein, HDAg-160, that specifically binds HDV unbranched rod RNA with high affinity. In an electrophoretic mobility shift assay, this protein produced a discrete, micrococcal nuclease-resistant complex with an approximately 400-nucleotide (nt) segment of HDV unbranched rod RNA. Binding occurred with several segments of HDV RNA, although with various affinities and efficiencies. Analysis of the effects of deleting segments of the unbranched rod indicated that binding did not require one or two specific binding sites within these RNA segments. Rather, a minimum-length HDV RNA unbranched rod approximately 311 nt was essential for RNP formation. The results are consistent with a model in which HDAg binds HDV unbranched rod RNA as multimers of fixed size rather than as individual subunits.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.