Results 41 to 50 of about 48,246 (290)
MSA prions exhibit remarkable stability and resistance to inactivation
Acta Neuropathologica, 2017 In multiple system atrophy (MSA), progressive neurodegeneration results from the protein α-synuclein misfolding into a self-templating prion conformation that spreads throughout the brain.
A. Woerman +11 more
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Efficient interspecies transmission of synthetic prions.
PLoS Pathogens, 2021 Prions are comprised solely of PrPSc, the misfolded self-propagating conformation of the cellular protein, PrPC. Synthetic prions are generated in vitro from minimal components and cause bona fide prion disease in animals.
Alyssa J Block +6 more
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Human stem cell–derived astrocytes replicate human prions in a PRNP genotype–dependent manner
Journal of Experimental Medicine, 2017 Prions are infectious agents that cause neurodegenerative diseases such as Creutzfeldt–Jakob disease (CJD). The absence of a human cell culture model that replicates human prions has hampered prion disease research for decades.
Zuzana Krejciova +9 more
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Transboundary and Emerging Diseases, 2018 A number of prion diseases affect humans, including Creutzfeldt-Jakob disease; most of these are due to genetic mutations in the affected individual and occur sporadically, but some result from transmission of prion proteins from external sources. Of the
L. Waddell +5 more
semanticscholar +1 more source
Neurobiology of Disease, 2012 With an estimated life-time prevalence of 15 to 17% and an incapacitating illness in 50% of cases, depressive spectrum disorders represent a heavy public health burden.
Sophie Mouillet-Richard +3 more
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Cofactors influence the biological properties of infectious recombinant prions
Acta Neuropathologica, 2018 Prion diseases are caused by a misfolding of the cellular prion protein (PrP) to a pathogenic isoform named PrPSc. Prions exist as strains, which are characterized by specific pathological and biochemical properties likely encoded in the three ...
Natalia Fernández-Borges +19 more
semanticscholar +1 more source
Prions and Prion-like Proteins [PDF]
Journal of Biological Chemistry, 2014 Prions are self-replicating protein aggregates and are the primary causative factor in a number of neurological diseases in mammals. The prion protein (PrP) undergoes a conformational transformation leading to aggregation into an infectious cellular pathogen.
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BiomoleculesSlow-onset neurodegenerative disease in a low-expresser 2N4R P301L transgenic (Tg) mouse model is marked by neuroinflammation and by differing patterns of CNS deposition and accumulation of tau conformers, with such heterogeneities present even within ...
Nathalie Daude +4 more
doaj +1 more source
A systematic survey identifies prions and illuminates sequence features of prionogenic proteins
Cell, 2009 SUMMARY Prions are proteins that convert between structurally and functionally distinct states, one or more of which is transmissible. In yeast, this ability allows them to act as non-Mendelian elements of phenotypic inheritance.
S. Alberti +4 more
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Immunomodulation for prion and prion-related diseases [PDF]
Expert Review of Vaccines, 2010 Prion diseases are a unique category of illness, affecting both animals and humans, where the underlying pathogenesis is related to a conformational change of a normal self protein called cellular prion protein to a pathological and infectious conformer known as scrapie prion protein (PrP(Sc)). Currently, all prion diseases lack effective treatment and
Thomas, Wisniewski, Fernando, Goñi
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