Yeast Models for Amyloids and Prions: Environmental Modulation and Drug Discovery
Molecules, 2019 Amyloids are self-perpetuating protein aggregates causing neurodegenerative diseases in mammals. Prions are transmissible protein isoforms (usually of amyloid nature).
Tatiana A. Chernova +2 more
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C. elegans Models to Study the Propagation of Prions and Prion-Like Proteins
Biomolecules, 2020 A hallmark common to many age-related neurodegenerative diseases, such as Alzheimer’s disease (AD), Parkinson’s disease (PD), and amyotrophic lateral sclerosis (ALS), is that patients develop proteinaceous deposits in their central nervous system (CNS ...
Carl Alexander Sandhof +3 more
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Antihypertensive drug guanabenz is active in vivo against both yeast and mammalian prions. [PDF]
PLoS ONE, 2008 BackgroundPrion-based diseases are incurable transmissible neurodegenerative disorders affecting animals and humans.Methodology/principal findingsHere we report the discovery of the in vivo antiprion activity of Guanabenz (GA), an agonist of alpha2 ...
Déborah Tribouillard-Tanvier +9 more
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Identification of Prion Disease-Related Somatic Mutations in the Prion Protein Gene (PRNP) in Cancer Patients [PDF]
Cells, 2020 Prion diseases are caused by misfolded prion protein (PrPSc) and are accompanied by spongiform vacuolation of brain lesions. Approximately three centuries have passed since prion diseases were first discovered around the world; however, the exact role of certain factors affecting the causative agent of prion diseases is still debatable.
Yong-Chan Kim +2 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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Glycosylation-related Gene Expression in Prion Diseases [PDF]
Journal of Biological Chemistry, 2005 International ...
Barret, Agnès +4 more
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Chronic Wasting Disease Prion Strain Emergence and Host Range Expansion
Emerging Infectious Diseases, 2017 Human and mouse prion proteins share a structural motif that regulates resistance to common chronic wasting disease (CWD) prion strains. Successful transmission of an emergent strain of CWD prion, H95+, into mice resulted in infection. Thus, emergent CWD
Allen Herbst +4 more
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Stability and Cu(II) Binding of Prion Protein Variants Related to Inherited Human Prion Diseases [PDF]
Biophysical Journal, 2003 All inherited forms of human prion diseases are linked with mutations in the prion protein (PrP) gene. Here we have investigated the stability and Cu(II) binding properties of three recombinant variants of murine full-length PrP(23-231)-containing destabilizing point mutations that are associated with human Gerstmann-Sträussler-Scheinker disease (F198S)
Cereghetti, G. +4 more
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Assessing Prion Infectivity of Human Urine in Sporadic Creutzfeldt-Jakob Disease
Emerging Infectious Diseases, 2012 Prion diseases are neurodegenerative conditions associated with a misfolded and infectious protein, scrapie prion protein (PrPSc). PrPSc propagate prion diseases within and between species and thus pose risks to public health.
Silvio Notari +12 more
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Curing of the [URE3] prion by Btn2p, a Batten disease‐related protein [PDF]
The EMBO Journal, 2008 [URE3] is a prion (infectious protein), a self-propagating amyloid form of Ure2p, a regulator of yeast nitrogen catabolism. We find that overproduction of Btn2p, or its homologue Ypr158 (Cur1p), cures [URE3]. Btn2p is reported to be associated with late endosomes and to affect sorting of several proteins.
Dmitry S, Kryndushkin +2 more
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