ArticleNature communications2019
A viral expression factor behaves as a prion.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
20 citing papers in PubMed, 40 citations in OpenAlex.
- The prion-like characteristic of ORF3 contributes to virion release and pathogenesis of hepatitis E virus.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- A Prion-Like Domain in EBV EBNA1 Promotes Phase Separation and Enables SRRM1 Splicing.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Nuclear Accumulation of Bm65 Aggregate Is Blocked by Mutations in the Nuclear Export Sequence of Bm65.Viruses · 2025Article
- Investigating the Aggregation and Prionogenic Properties of Human Cancer-Related Proteins.Molecular and cellular biology · 2025Article
- IE1 of Autographa californica Multiple Nucleopolyhedrovirus Activates Low Levels of Late Gene Expression in the Absence of Virus RNA Polymerase.Microbiology spectrum · 2023Article
- Trans-seeding of Alzheimer-related tau protein by a yeast prion.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2022Article
- Structural Bases of Prion Variation in Yeast.International journal of molecular sciences · 2022Review
- Biochemical Principles in Prion-Based Inheritance.Epigenomes · 2022Review
- Prion-like proteins: from computational approaches to proteome-wide analysis.FEBS open bio · 2021Review
- The Way forward for the Origin of Life: Prions and Prion-Like Molecules First Hypothesis.Life (Basel, Switzerland) · 2021Article
- Generalizable Compositional Features Influencing the Proteostatic Fates of Polar Low-Complexity Domains.International journal of molecular sciences · 2021Article
- The Hunt for Ancient Prions: Archaeal Prion-Like Domains Form Amyloid-Based Epigenetic Elements.Molecular biology and evolution · 2021Article
- Review
- Structures of Pathological and Functional Amyloids and Prions, a Solid-State NMR Perspective.Frontiers in molecular neuroscience · 2021Review
- Elucidating the regulatory mechanism of Swi1 prion in global transcription and stress responses.Scientific reports · 2020Article
- Prions: Roles in Development and Adaptive Evolution.Journal of molecular evolution · 2020Review
- Protein assembly systems in natural and synthetic biology.BMC biology · 2020Review
- Update of the list of QPS-recommended biological agents intentionally added to food or feed as notified to EFSA 11: suitability of taxonomic units notified to EFSA until September 2019.EFSA journal. European Food Safety Authority · 2020Article
- Scientific Opinion on the update of the list of QPS-recommended biological agents intentionally added to food or feed as notified to EFSA (2017-2019).EFSA journal. European Food Safety Authority · 2020Article
- Natural and pathogenic protein sequence variation affecting prion-like domains within and across human proteomes.BMC genomics · 2020Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
Abstract
Prions are proteins that can fold into multiple conformations some of which are self-propagating. Such prion-forming proteins have been found in animal, plant, fungal and bacterial species, but have not yet been identified in viruses. Here we report that LEF-10, a baculovirus-encoded protein, behaves as a prion. Full-length LEF-10 or its candidate prion-forming domain (cPrD) can functionally replace the PrD of Sup35, a widely studied prion-forming protein from yeast, displaying a [PSI
Indexed as
Identifiers
What OpenQuestion holds
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.