Trends in Genetics
Review Yeast review seriesMaintenance and inheritance of yeast prions
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The interactions that shape amyloid fibrils in disease
2022, StructurePrion Protein Biology Through the Lens of Liquid-Liquid Phase Separation: Liquid-liquid phase separation of prion protein
2022, Journal of Molecular BiologyCitation Excerpt :The identification of beneficial prion-like proteins in yeast and other fungi also hinted at a much broader role of self-perpetuating protein conformational changes. These studies revealed the generic nature of the conformation-based biological information transfer in both normal biology and pathology.21,22 A growing number of neurodegenerative diseases including Alzheimer’s, Parkinson’s, amyotrophic lateral sclerosis, and cancer have now been linked to protein misfolding, aggregation, and amyloid formation.23
Prions and Prion-like assemblies in neurodegeneration and immunity: The emergence of universal mechanisms across health and disease
2020, Seminars in Cell and Developmental BiologyMore than Just a Phase: Prions at the Crossroads of Epigenetic Inheritance and Evolutionary Change
2018, Journal of Molecular BiologyCitation Excerpt :These elements were also inherited by all meiotic progeny in genetic crosses, in contrast to mutations, which are inherited by half (Fig. 2). These properties give rise to the distinctive nomenclature of [PSI+], [URE3], and other [PRION+] elements: upper case letters indicate dominance in genetic crosses and square brackets indicate their non-Mendelian behavior [83, 91]. A flurry of discoveries in the mid-1990s established that infectious conformational conversion of the Ure2 and Sup35 proteins could explain the [URE3] and [PSI+] phenotypes [18, 28, 54, 82, 83, 85, 91–98].
Effect of charged residues in the N-domain of Sup35 protein on prion [PSI<sup>+</sup>] stability and propagation
2013, Journal of Biological ChemistryCitation Excerpt :In the non-prion state, Sup35p is essential for robust translation termination. Cells bearing [PSI+] have a reduced pool of soluble Sup35p, which leads to increased read through of stop codons during translation (5, 6). The Sup35 protein consists of three distinct functional domains (Fig. 1A).
Role of chromatin states in transcriptional memory
2009, Biochimica et Biophysica Acta - General Subjects