Treatment of Prion Disease with Heterologous Prion Proteins. [PDF]
PLoS ONE, 2015 Prion diseases such as Creutzfeldt-Jakob disease in humans, bovine spongiform encephalopathy in cattle, and scrapie in sheep are fatal neurodegenerative diseases for which there is no effective treatment.
Pamela J Skinner +9 more
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Interaction networks of prion, prionogenic and prion-like proteins in budding yeast, and their role in gene regulation. [PDF]
PLoS ONE, 2014 Prions are transmissible, propagating alternative states of proteins. Prions in budding yeast propagate heritable phenotypes and can function in large-scale gene regulation, or in some cases occur as diseases of yeast.
Djamel Harbi, Paul M Harrison
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Structural Variations of Prions and Prion-like Proteins Associated with Neurodegeneration
Current Issues in Molecular BiologyNeurodegeneration is becoming one of the leading causes of death worldwide as the population expands and grows older. There is a growing desire to understand the mechanisms behind prion proteins as well as the prion-like proteins that make up ...
Carter Sky Christensen +4 more
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Nutrient and heat stress induce changes to the solubility of predicted prion-like proteins in Dictyostelium discoideum [PDF]
BMC Molecular and Cell BiologyBackground Dictyostelium discoideum has a unique proteome among sequenced organisms that encodes nearly 10,000 homopolymeric amino acid tracts longer than 10 amino acids long.
Felicia N. Williams +4 more
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Spontaneous variants of the [RNQ+] prion in yeast demonstrate the extensive conformational diversity possible with prion proteins. [PDF]
PLoS ONE, 2013 Prion strains (or variants) are structurally distinct amyloid conformations arising from a single polypeptide sequence. The existence of prion strains has been well documented in mammalian prion diseases.
Vincent J Huang +2 more
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A Census of Human Methionine-Rich Prion-like Domain-Containing Proteins
Antioxidants, 2022 Methionine-rich prion-like proteins can regulate liquid–liquid phase separation processes in response to stresses. To date, however, very few proteins have been identified as methionine-rich prion-like. Herein, we have performed a computational survey of
Juan Carlos Aledo
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Prion‐like proteins: from computational approaches to proteome‐wide analysis
FEBS Open Bio, 2021 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 ...
Marcos Gil‐Garcia +3 more
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Cell & Bioscience, 2023 Background Aberrant stress granules (SGs) are emerging as prime suspects in the nucleation of toxic protein aggregates. Understanding the molecular networks linked with aggregation-prone proteins (prion protein, synuclein, and tau) under stressful ...
Neelam Younas +6 more
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Distinct type of transmission barrier revealed by study of multiple prion determinants of Rnq1. [PDF]
PLoS Genetics, 2010 Prions are self-propagating protein conformations. Transmission of the prion state between non-identical proteins, e.g. between homologous proteins from different species, is frequently inefficient.
Michele L Kadnar +2 more
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Anti-Prion Systems in Saccharomyces cerevisiae Turn an Avalanche of Prions into a Flurry
Viruses, 2022 Prions are infectious proteins, mostly having a self-propagating amyloid (filamentous protein polymer) structure consisting of an abnormal form of a normally soluble protein.
Moonil Son, Reed B. Wickner
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