منابع مشابه
Prion Neurotoxicity 51 Prion Neurotoxicity: Insights from Prion Protein Mutants
The chemical nature of prions and the mechanism by which they propagate are now reasonably well understood. In contrast, much less is known about the identity of the toxic prion protein (PrP) species that are responsible for neuronal death, and the cellular pathways that these forms activate. In addition, the normal, physiological function of cellular PrP (PrPC) has remained mysterious, hamperi...
متن کاملPrion neurotoxicity: insights from prion protein mutants.
The chemical nature of prions and the mechanism by which they propagate are now reasonably well understood. In contrast, much less is known about the identity of the toxic prion protein (PrP) species that are responsible for neuronal death, and the cellular pathways that these forms activate. In addition, the normal, physiological function of cellular PrP (PrP(C)) has remained mysterious, hampe...
متن کاملRole of Prion Protein Aggregation in Neurotoxicity
In several neurodegenerative diseases, such as Parkinson, Alzheimer's, Huntington, and prion diseases, the deposition of aggregated misfolded proteins is believed to be responsible for the neurotoxicity that characterizes these diseases. Prion protein (PrP), the protein responsible of prion diseases, has been deeply studied for the peculiar feature of its misfolded oligomers that are able to pr...
متن کاملNeurotoxicity of Prion Peptides Mimicking the Central Domain of the Cellular Prion Protein
The physiological functions of PrP(C) remain enigmatic, but the central domain, comprising highly conserved regions of the protein may play an important role. Indeed, a large number of studies indicate that synthetic peptides containing residues 106-126 (CR) located in the central domain (CD, 95-133) of PrP(C) are neurotoxic. The central domain comprises two chemically distinct subdomains, the ...
متن کاملIn Vitro and In Vivo Neurotoxicity of Prion Protein Oligomers
The mechanisms underlying prion-linked neurodegeneration remain to be elucidated, despite several recent advances in this field. Herein, we show that soluble, low molecular weight oligomers of the full-length prion protein (PrP), which possess characteristics of PrP to PrPsc conversion intermediates such as partial protease resistance, are neurotoxic in vitro on primary cultures of neurons and ...
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ژورنال
عنوان ژورنال: Brain Pathology
سال: 2019
ISSN: 1015-6305
DOI: 10.1111/bpa.12694