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
Synthetic prions generated in vitro are similar to a newly identified subpopulation of PrPSc from sporadic Creutzfeldt-Jakob disease [PDF]
, 2005 In recent studies, the amyloid form of recombinant prion protein (PrP) encompassing residues 89–230 (rPrP 89-230) produced in vitro induced transmissible prion disease in mice.
Adler +66 more
core +2 more sources
Heterologous prion-forming proteins interact to cross-seed aggregation in Saccharomyces cerevisiae [PDF]
, 2017 The early stages of protein misfolding remain incompletely understood, as most mammalian proteinopathies are only detected after irreversible protein aggregates have formed.
Keefer, Kathryn M +2 more
core +2 more sources
Plants as vectors for environmental prion transmission
iScience, 2023 Summary: Prions cause fatal neurodegenerative diseases and exhibit remarkable durability, which engenders a wide array of potential exposure scenarios. In chronic wasting disease of deer, elk, moose, and reindeer and in scrapie of sheep and goats, prions
Christina M. Carlson +11 more
doaj +1 more source
Helices 2 and 3 are the initiation sites in the PrPc -> PrPsc transition
, 2012 It is established that prion protein is the sole causative agent in a number of diseases in humans and animals. However, the nature of conformational changes that the normal cellular form PrPC undergoes in the conversion process to a self-replicating ...
Chen, Jie, Thirumalai, Devarajan
core +1 more source
Computational Studies of the Structural Stability of Rabbit Prion Protein Compared to Human and Mouse Prion Proteins [PDF]
, 2011 Prion diseases are invariably fatal and highly infectious neurodegenerative diseases affecting humans and animals. The neurodegenerative diseases such as Creutzfeldt-Jakob disease, variant Creutzfeldt-Jakob diseases, Gerstmann-Str$\ddot{a}$ussler ...
Zhang, Jiapu
core +2 more sources
Mitigation of prion infectivity and conversion capacity by a simulated natural process--repeated cycles of drying and wetting. [PDF]
PLoS Pathogens, 2015 Prions enter the environment from infected hosts, bind to a wide range of soil and soil minerals, and remain highly infectious. Environmental sources of prions almost certainly contribute to the transmission of chronic wasting disease in cervids and ...
Qi Yuan +4 more
doaj +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.
openaire +2 more sources
Adult‐Onset Subacute Sclerosing Panencephalitis Presenting With Subacute Cognitive Deficits
Annals of Clinical and Translational Neurology, EarlyView.ABSTRACT We describe the case of a 41‐year‐old man diagnosed with adult‐onset subacute sclerosing panencephalitis (SSPE). The patient presented with subacute progressive cognitive deficits and a neuropsychological profile indicating predominant frontoparietal dysfunction. MRI showed only mild parietal‐predominant cerebral atrophy.
Dennis Yeow +4 more
wiley +1 more source
Targeted Mutagenesis of the Oligopeptide Repeat Domain of the Yeast Prion Sup35 [PDF]
, 2014 The formation of prions in the baker’s yeast Saccharomyces cerevisiae is determined by amino acid composition rather than the primary sequence of amino acids.
Davis, Emily, Knox, James D.
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