ReviewFEBS open bio2021
Prion-like proteins: from computational approaches to proteome-wide analysis.
Review in FEBS open bio, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Exogenous prion-like proteins and their potential to trigger cognitive dysfunction.Molecular systems biology · 2025Article
- Aggregating amyloid resources: A comprehensive review of databases on amyloid-like aggregation.Computational and structural biotechnology journal · 2024Review
- Tracing the Evolutionary History of the Temperature-Sensing Prion-like Domain in EARLY FLOWERING 3 Highlights the Uniqueness of AtELF3.Molecular biology and evolution · 2024Article
- Prion-like Proteins in Plants: Key Regulators of Development and Environmental Adaptation via Phase Separation.Plants (Basel, Switzerland) · 2024Review
- A Protein Misfolding Shaking Amplification-based method for the spontaneous generation of hundreds of bona fide prions.Nature communications · 2024Article
- N-terminal region of Drosophila melanogaster Argonaute2 forms amyloid-like aggregates.BMC biology · 2023Article
- AmyloGraph: a comprehensive database of amyloid-amyloid interactions.Nucleic acids research · 2023Article
- Intrinsic determinants of prion protein neurotoxicity inFrontiers in molecular neuroscience · 2023Review
- Expression of Huntingtin and TDP-43 Derivatives in Fission Yeast Can Cause Both Beneficial and Toxic Effects.International journal of molecular sciences · 2022Article
- Prion-like Domains in Spike Protein of SARS-CoV-2 Differ across Its Variants and Enable Changes in Affinity to ACE2.Microorganisms · 2022Article
- Exploring cryptic amyloidogenic regions in prion-like proteins from plants.Frontiers in plant science · 2022Article
- Entering the second decade: FEBS Open Bio in 2022.FEBS open bio · 2022Article
- Review
- Membraneless organelles: a smart design for metabolic control.FEBS open bio · 2021Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Prions are self-perpetuating proteins able to switch between a soluble state and an aggregated-and-transmissible conformation. These proteinaceous entities have been widely studied in yeast, where they are involved in hereditable phenotypic adaptations. The notion that such proteins could play functional roles and be positively selected by evolution has triggered the development of computational tools to identify prion-like proteins in different kingdoms of life. These algorithms have succeeded in screening multiple proteomes, allowing the identification of prion-like proteins in a diversity of unrelated organisms, evidencing that the prion phenomenon is well conserved among species. Interestingly enough, prion-like proteins are not only connected with the formation of functional membraneless protein-nucleic acid coacervates, but are also linked to human diseases. This review addresses state-of-the-art computational approaches to identify prion-like proteins, describes proteome-wide analysis efforts, discusses these unique proteins' functional role, and illustrates recently validated examples in different domains of life.
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Registered trials
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