ArticleNature microbiology2020
Inhibition of the integrated stress response by viral proteins that block p-eIF2-eIF2B association.
Article in Nature microbiology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 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.
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.
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Who cites it
33 citing papers in PubMed, 49 citations in OpenAlex.
- Allosteric disordering of eIF2B regulates the integrated stress response.Nature chemical biology · 2026Article
- Glutamine-Linked Cellular Stress Responses in Viral Infection: Mechanisms, Crosstalk, and Future Perspectives.International journal of molecular sciences · 2026Review
- Cetacean coronavirus spikes highlight S glycoprotein structural plasticity.PLoS pathogens · 2026Article
- The Translation Initiation Factor eIF2Bα Regulates Development, Stress Response, Amylase Production, and Kojic Acid Synthesis in the Fungus Aspergillus oryzae.Current microbiology · 2025Review
- TOLLIP inhibits lipid accumulation and the integrated stress response in alveolar macrophages to control Mycobacterium tuberculosis infection.Nature microbiology · 2024Article
- Turnip mosaic virus NIb weakens the function of eukaryotic translation initiation factor 6 facilitating viral infection in Nicotiana benthamiana.Molecular plant pathology · 2024Article
- SARS-CoV-2 variant-specific differences in inhibiting the effects of the PKR-activated integrated stress response.Virus research · 2024Article
- SARS-CoV-2 nucleocapsid protein inhibits the PKR-mediated integrated stress response through RNA-binding domain N2b.PLoS pathogens · 2023Article
- Biomolecular phase separation in stress granule assembly and virus infection.Acta biochimica et biophysica Sinica · 2023Article
- An old model with new insights: endogenous retroviruses drive the evolvement toward ASD susceptibility and hijack transcription machinery during development.Molecular psychiatry · 2023Article
- Dysregulation of Stress-Induced Translational Control byMicroorganisms · 2023Article
- A little less aggregation a little more replication: Viral manipulation of stress granules.Wiley interdisciplinary reviews. RNA · 2023Review
- Move and countermove: the integrated stress response in picorna- and coronavirus-infected cells.Current opinion in immunology · 2022Review
- A common epigenetic mechanism across different cellular origins underlies systemic immune dysregulation in an idiopathic autism mouse model.Molecular psychiatry · 2022Article
- Regulation and function of elF2B in neurological and metabolic disorders.Bioscience reports · 2022Review
- Immunogenic cell stress and death.Nature immunology · 2022Review
- Glycosite-deleted mRNA of SARS-CoV-2 spike protein as a broad-spectrum vaccine.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Minding the message: tactics controlling RNA decay, modification, and translation in virus-infected cells.Genes & development · 2022Review
- Schweinfurthin induces ICD without ER stress and caspase activation.Oncoimmunology · 2022Article
- Viral evasion of the integrated stress response through antagonism of eIF2-P binding to eIF2B.Nature communications · 2021Article
Corrections and comments
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Authors and funding
17 authors at 2 institutions in 3 countries.
Funding
Abstract
Eukaryotic cells, when exposed to environmental or internal stress, activate the integrated stress response (ISR) to restore homeostasis and promote cell survival. Specific stress stimuli prompt dedicated stress kinases to phosphorylate eukaryotic initiation factor 2 (eIF2). Phosphorylated eIF2 (p-eIF2) in turn sequesters the eIF2-specific guanine exchange factor eIF2B to block eIF2 recycling, thereby halting translation initiation and reducing global protein synthesis. To circumvent stress-induced translational shutdown, viruses encode ISR antagonists. Those identified so far prevent or reverse eIF2 phosphorylation. We now describe two viral proteins-one from a coronavirus and the other from a picornavirus-that have independently acquired the ability to counteract the ISR at its very core by acting as a competitive inhibitor of p-eIF2-eIF2B interaction. This allows continued formation of the eIF2-GTP-Met-tRNAi ternary complex and unabated global translation at high p-eIF2 levels that would otherwise cause translational arrest. We conclude that eIF2 and p-eIF2 differ in their interaction with eIF2B to such effect that p-eIF2-eIF2B association can be selectively inhibited.
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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.