ArticleJournal of virology2017
Disruption of Stress Granule Formation by the Multifunctional Cricket Paralysis Virus 1A Protein.
Article in Journal of virology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
10 citing papers in PubMed, 30 citations in OpenAlex.
- Article
- An emerging role for the endoplasmic reticulum in stress granule biogenesis.Seminars in cell & developmental biology · 2024Review
- Targeting Nup358/RanBP2 by a viral protein disrupts stress granule formation.PLoS pathogens · 2022Article
- Stressful steps: Progress and challenges in understanding stress-induced mRNA condensation and accumulation in stress granules.Molecular cell · 2022Review
- Pathophysiology of stress granules: An emerging link to diseases (Review).International journal of molecular medicine · 2022Review
- The multi-functional RNA-binding protein G3BP1 and its potential implication in neurodegenerative disease.Journal of neurochemistry · 2021Review
- Translational Control in Virus-Infected Cells.Cold Spring Harbor perspectives in biology · 2019Review
- Strategies for Success. Viral Infections and Membraneless Organelles.Frontiers in cellular and infection microbiology · 2019Review
- Rotavirus Induces Formation of Remodeled Stress Granules and P Bodies and Their Sequestration in Viroplasms To Promote Progeny Virus Production.Journal of virology · 2018Article
- A Viral Protein Restricts Drosophila RNAi Immunity by Regulating Argonaute Activity and Stability.Cell host & microbe · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
Stress granules (SGs) are cytosolic ribonucleoprotein aggregates that are induced during cellular stress. Several viruses modulate SG formation, suggesting that SGs have an impact on virus infection. However, the mechanisms and impact of modulating SG assembly in infected cells are not completely understood. In this study, we identify the dicistrovirus cricket paralysis virus 1A (CrPV-1A) protein that functions to inhibit SG assembly during infection. Moreover, besides inhibiting RNA interference, CrPV-1A also inhibits host transcription, which indirectly modulates SG assembly. Thus, CrPV-1A is a multifunctional protein. We identify a key R146A residue that is responsible for these effects, and mutant CrPV(R146A) virus infection is attenuated in
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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.