Prion strains: shining new light on old concepts

AJ Block, JC Bartz - Cell and Tissue Research, 2023 - Springer
Prion diseases are a group of inevitably fatal neurodegenerative disorders affecting
numerous mammalian species, including humans. The existence of heritable phenotypes of …

Prion strain diversity

JC Bartz - Cold Spring Harbor perspectives in …, 2016 - perspectivesinmedicine.cshlp.org
Prion diseases affect a wide range of mammal species and are caused by a misfolded self-
propagating isoform (PrPSc) of the normal prion protein (PrPC). Distinct strains of prions …

Isolation of phosphatidylethanolamine as a solitary cofactor for prion formation in the absence of nucleic acids

NR Deleault, JR Piro, DJ Walsh… - Proceedings of the …, 2012 - National Acad Sciences
Infectious prions containing the pathogenic conformer of the mammalian prion protein
(PrPSc) can be produced de novo from a mixture of the normal conformer (PrPC) with RNA …

Understanding the key features of the spontaneous formation of bona fide prions through a novel methodology that enables their swift and consistent generation

H Eraña, CM Díaz-Domínguez, JM Charco… - Acta neuropathologica …, 2023 - Springer
Among transmissible spongiform encephalopathies or prion diseases affecting humans,
sporadic forms such as sporadic Creutzfeldt–Jakob disease are the vast majority. Unlike …

The degree of astrocyte activation is predictive of the incubation time to prion disease

N Makarava, O Mychko, JCY Chang… - Acta Neuropathologica …, 2021 - Springer
In neurodegenerative diseases including Alzheimer's, Parkinson's and prion diseases,
astrocytes acquire disease-associated reactive phenotypes. With growing appreciation of …

Sialylation of Prion Protein Controls the Rate of Prion Amplification, the Cross-Species Barrier, the Ratio of PrPSc Glycoform and Prion Infectivity

E Katorcha, N Makarava, R Savtchenko… - PLoS …, 2014 - journals.plos.org
The central event underlying prion diseases involves conformational change of the cellular
form of the prion protein (PrPC) into the disease-associated, transmissible form (PrPSc) …

Sialylation of the prion protein glycans controls prion replication rate and glycoform ratio

E Katorcha, N Makarava, R Savtchenko, IV Baskakov - Scientific reports, 2015 - nature.com
Prion or PrPSc is a proteinaceous infectious agent that consists of a misfolded and
aggregated form of a sialoglycoprotein called prion protein or PrPC. PrPC has two sialylated …

Prion protein misfolding, strains, and neurotoxicity: an update from studies on mammalian prions

I Poggiolini, D Saverioni… - International journal of cell …, 2013 - Wiley Online Library
Prion diseases, also known as transmissible spongiform encephalopathies (TSEs), are a
group of fatal neurodegenerative disorders affecting humans and other mammalian species …

Prion protein amplification techniques

AJE Green, G Zanusso - Handbook of clinical neurology, 2018 - Elsevier
Protein amplification techniques exploit the ability of PrP TSE to induce a conformational
change in prion protein (PrP) in a continuous fashion, so that the small amount of PrP TSE …

Multifaceted role of sialylation in prion diseases

IV Baskakov, E Katorcha - Frontiers in Neuroscience, 2016 - frontiersin.org
Mammalian prion or PrPSc is a proteinaceous infectious agent that consists of a misfolded,
self-replicating state of a sialoglycoprotein called the prion protein, or PrPC. Sialylation of …