ReviewInternational journal of molecular sciences2021
From Prions to Stress Granules: Defining the Compositional Features of Prion-Like Domains That Promote Different Types of Assemblies.
Review in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 31 citations in OpenAlex.
- Prion-Like Protein LENG8-Mediated Nucleation Drives Stress Granule Assembly.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Evolving concepts of the protein universe.iScience · 2025Review
- On the Significance of the Terminal Location of Prion-Forming Regions of Yeast Proteins.International journal of molecular sciences · 2025Article
- Oxidative stress-induced stress granules: a central link to protein aggregation in neurodegenerative diseases.Frontiers in neuroscience · 2025Article
- Prion-like Proteins in Plants: Key Regulators of Development and Environmental Adaptation via Phase Separation.Plants (Basel, Switzerland) · 2024Review
- Evolution of Transcript Abundance is Influenced by Indels in Protein Low Complexity Regions.Journal of molecular evolution · 2024Article
- Heterotypic interactions can drive selective co-condensation of prion-like low-complexity domains of FET proteins and mammalian SWI/SNF complex.Nature communications · 2024Article
- Heterotypic interactions in the dilute phase can drive co-condensation of prion-like low-complexity domains of FET proteins and mammalian SWI/SNF complex.bioRxiv : the preprint server for biology · 2023Article
- Advanced imaging techniques for studying protein phase separation in living cells and at single-molecule level.Current opinion in chemical biology · 2023Review
- The Properties and Domain Requirements for Phase Separation of the Sup35 Prion Protein In Vivo.Biomolecules · 2023Article
- Phase separation of protein mixtures is driven by the interplay of homotypic and heterotypic interactions.Nature communications · 2023Article
- How Big Is the Yeast Prion Universe?International journal of molecular sciences · 2023Review
- Phase Separation in Mixtures of Prion-Like Low Complexity Domains is Driven by the Interplay of Homotypic and Heterotypic Interactions.Research square · 2023Article
- Liquid Droplet Aging and Seeded Fibril Formation of the Cytotoxic Granule Associated RNA Binding Protein TIA1 Low Complexity Domain.Journal of the American Chemical Society · 2023Article
- Phase separation by the SARS-CoV-2 nucleocapsid protein: Consensus and open questions.The Journal of biological chemistry · 2022Review
- Deciphering how naturally occurring sequence features impact the phase behaviours of disordered prion-like domains.Nature chemistry · 2022Article
- Protein conformation and biomolecular condensates.Current research in structural biology · 2022Review
- The prion-like transmission of tau oligomersFrontiers in aging neuroscience · 2022Review
- Polyanion order controls liquid-to-solid phase transition in peptide/nucleic acid co-assembly.Frontiers in molecular biosciences · 2022Article
- Regulation of spatially restricted gene expression: linking RNA localization and phase separation.Biochemical Society transactions · 2021Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Stress granules are ribonucleoprotein assemblies that form in response to cellular stress. Many of the RNA-binding proteins found in stress granule proteomes contain prion-like domains (PrLDs), which are low-complexity sequences that compositionally resemble yeast prion domains. Mutations in some of these PrLDs have been implicated in neurodegenerative diseases, including amyotrophic lateral sclerosis and frontotemporal dementia, and are associated with persistent stress granule accumulation. While both stress granules and prions are macromolecular assemblies, they differ in both their physical properties and complexity. Prion aggregates are highly stable homopolymeric solids, while stress granules are complex dynamic biomolecular condensates driven by multivalent homotypic and heterotypic interactions. Here, we use stress granules and yeast prions as a paradigm to examine how distinct sequence and compositional features of PrLDs contribute to different types of PrLD-containing assemblies.
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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.