ArticleCell host & microbe2024
Viral hijacking of hnRNPH1 unveils a G-quadruplex-driven mechanism of stress control.
Article in Cell host & microbe, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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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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Who cites it
10 citing papers in PubMed.
- DHX36 is a regulatory switch in the interferon-mediated antiviral response.Science advances · 2026Article
- RNA G-Quadruplexes in the Porcine Deltacoronavirus Genome: Structural Regulation and Therapeutic Targeting for Antiviral Strategies.Transboundary and emerging diseases · 2026Article
- Transfer RNA regulation during herpesvirus infection: Wielding a sword or raising a shield?PLoS pathogens · 2025Article
- Review
- HNRNPH1-mediated splicing events regulatebioRxiv : the preprint server for biology · 2025Article
- Viral hijacking of host DDX60 promotes Crimean-Congo haemorrhagic fever virus replication via G-quadruplex unwinding.PLoS pathogens · 2025Article
- G-quadruplex-forming small RNA inhibits coronavirus and influenza A virus replication.Communications biology · 2025Article
- Exploring the regulatory role of small RNAs in modulating host-pathogen interactions: implications for bacterial and viral infections.Molecular biology reports · 2025Review
- Conserved Sequences from Dengue Virus Genomes Form Stable G-Quadruplexes.ACS infectious diseases · 2025Article
- hnRNPH1 Inhibits Influenza Virus Replication by Binding Viral RNA.Microorganisms · 2024Article
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4 authors.
Funding
Abstract
Viral genomes are enriched with G-quadruplexes (G4s), non-canonical structures formed in DNA or RNA upon assembly of four guanine stretches into stacked quartets. Because of their critical roles, G4s are potential antiviral targets, yet their function remains largely unknown. Here, we characterize the formation and functions of a conserved G4 within the polymerase coding region of orthoflaviviruses of the Flaviviridae family. Using yellow fever virus, we determine that this G4 promotes viral replication and suppresses host stress responses via interactions with hnRNPH1, a host nuclear protein involved in RNA processing. G4 binding to hnRNPH1 causes its cytoplasmic retention with subsequent impacts on G4-containing tRNA fragments (tiRNAs) involved in stress-mediated reductions in translation. As a result, these host stress responses and associated antiviral effects are impaired. These data reveal that the interplay between hnRNPH1 and both host and viral G4 targets controls the integrated stress response and viral replication.
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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.