ArticleJournal of virology2008
Structural determinant of human La protein critical for internal initiation of translation of hepatitis C virus RNA.
Article in Journal of virology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
What it found
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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.
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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.
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Who cites it
14 citing papers in PubMed, 30 citations in OpenAlex.
- Noncanonical RNA binding of human La-related protein 6.Nucleic acids research · 2025Article
- RNA-Binding Macrocyclic Peptides.Frontiers in molecular biosciences · 2022Review
- N6-methyladenosine modification of HCV RNA genome regulates cap-independent IRES-mediated translation via YTHDC2 recognition.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Designed Metal-ATCUN Derivatives: Redox- and Non-redox-Based Applications Relevant for Chemistry, Biology, and Medicine.iScience · 2020Review
- Catalytic metallodrugs based on the LaR2C peptide target HCV SLIV IRES RNA.Dalton transactions (Cambridge, England : 2003) · 2015Article
- Specific sequence of a Beta turn in human la protein may contribute to species specificity of hepatitis C virus.Journal of virology · 2014Article
- Human La protein interaction with GCAC near the initiator AUG enhances hepatitis C Virus RNA replication by promoting linkage between 5' and 3' untranslated regions.Journal of virology · 2013Article
- Inhibition of the interaction between NS3 protease and HCV IRES with a small peptide: a novel therapeutic strategy.Molecular therapy : the journal of the American Society of Gene Therapy · 2013Article
- RNA structural elements of hepatitis C virus controlling viral RNA translation and the implications for viral pathogenesis.Viruses · 2012Review
- MicroRNA-122 antagonism against hepatitis C virus genotypes 1-6 and reduced efficacy by host RNA insertion or mutations in the HCV 5' UTR.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Interplay between NS3 protease and human La protein regulates translation-replication switch of Hepatitis C virus.Scientific reports · 2011Article
- Insights into the biology of IRES elements through riboproteomic approaches.Journal of biomedicine & biotechnology · 2010Review
- A cell-permeable peptide inhibits hepatitis C virus replication by sequestering IRES transacting factors.Virology · 2009Article
- Conserved and divergent features of the structure and function of La and La-related proteins (LARPs).Biochimica et biophysica actaReview
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human La protein has been implicated in facilitating internal ribosome entry site (IRES)-mediated translation of hepatitis C virus (HCV). Earlier, we demonstrated that the RNA recognition motif (RRM) encompassing residues 112 to 184 of La protein [La (112-184)] interacts with the HCV IRES near the initiator AUG codon. A synthetic peptide, LaR2C (24-mer), derived from La RRM (112-184), retains RNA binding ability, competes with La protein binding to the HCV IRES, and inhibits translation. The peptide interferes with the assembly of 48S complexes, resulting in the accumulation of preinitiation complexes that are incompetent for the 60S ribosomal subunit joining. Here, nuclear magnetic resonance spectroscopy of the HCV IRES-bound peptide complex revealed putative contact points, mutations that showed reduced RNA binding and translation inhibitory activity. The residues responsible for RNA recognition were found to form a turn in the RRM (112-184) structure. A 7-mer peptide comprising this turn showed significant translation inhibitory activity. The bound structure of the peptide inferred from transferred nuclear Overhauser effect experiments suggests that it is a beta turn. This conformation is significantly different from that observed in the free RRM (112-184) NMR structure, suggesting paths toward a better-stabilized mimetic peptide. Interestingly, addition of hexa-arginine tag enabled the peptide to enter Huh7 cells and showed inhibition of HCV IRES function. More importantly, the peptide significantly inhibited replication of the HCV monocistronic replicon. Elucidation of the structural determinant of the peptide provides a basis for developing small peptidomimetic structures as potent anti-HCV therapeutics.
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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.