ArticleMolecular and cellular biology2018
Prion Replication in the Mammalian Cytosol: Functional Regions within a Prion Domain Driving Induction, Propagation, and Inheritance.
Article in Molecular and cellular biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 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
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Who cites it
12 citing papers in PubMed, 15 citations in OpenAlex.
- Deletion Analysis of Phase Separation, Amyloid Formation and Prion Propagation by the Intrinsically Disordered Region of Yeast Sup35 Protein.International journal of molecular sciences · 2026Article
- Structural Bases of Prion Variation in Yeast.International journal of molecular sciences · 2022Review
- Prion-like proteins: from computational approaches to proteome-wide analysis.FEBS open bio · 2021Review
- Membrane composition and lipid to protein ratio modulate amyloid kinetics of yeast prion protein.RSC chemical biology · 2021Article
- MED15 prion-like domain forms a coiled-coil responsible for its amyloid conversion and propagation.Communications biology · 2021Article
- Review
- Intercellular Transmission of a Synthetic Bacterial Cytotoxic Prion-Like Protein in Mammalian Cells.mBio · 2020Article
- Entropic Bristles Tune the Seeding Efficiency of Prion-Nucleating Fragments.Cell reports · 2020Article
- Application of yeast to studying amyloid and prion diseases.Advances in genetics · 2020Review
- Fibril-induced glutamine-/asparagine-rich prions recruit stress granule proteins in mammalian cells.Life science alliance · 2019Article
- Article
- Discovering Putative Prion-Like Proteins inFrontiers in microbiology · 2018Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Prions of lower eukaryotes are transmissible protein particles that propagate by converting homotypic soluble proteins into growing protein assemblies. Prion activity is conferred by so-called prion domains, regions of low complexity that are often enriched in glutamines and asparagines (Q/N). The compositional similarity of fungal prion domains with intrinsically disordered domains found in many mammalian proteins raises the question of whether similar sequence elements can drive prion-like phenomena in mammals. Here, we define sequence features of the prototype
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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.