ArticleCell reports2026
RNase L regulates the antiviral proteome by accelerating mRNA decay, inhibiting nuclear mRNA export, and repressing transcription.
Article in Cell reports, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 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
3 citing papers in PubMed.
- PKR engages viral RNA and intron-retained host transcripts during poxvirus infection.Cell reports · 2026Article
- Lost in translation: interferon-stimulated genes targeting flavivirus protein synthesis.Journal of virology · 2026Review
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Abstract
Ribonuclease L (RNase L) is an antiviral endoribonuclease that triggers widespread degradation of cellular mRNAs. Here, we show that RNase L-mediated decay of cellular mRNA is a conserved response to flaviviruses, including Zika virus (ZIKV), dengue virus serotype 2 (DENV-2), and West Nile virus (WNV). Quantitative mass spectrometry shows that RNase L downregulates proteins with short half-lives involved in cell-cycle progression, cellular metabolism, and protein synthesis. However, mRNAs encoding antiviral proteins that are induced by interferon-stimulated genes (ISGs) initially evade degradation by RNase L, allowing for the synthesis of critical antiviral proteins. At later times during the antiviral response, RNase L dampens ISG protein synthesis by triggering a block in nuclear mRNA export and repressing transcription. These findings show that RNase L regulates the antiviral proteome through an intricate balance of mRNA decay and nuclear RNA biogenesis, which is crucial for preventing overproduction of pro-inflammatory proteins.
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