Mutations in the PRNP gene, which encodes the prion protein (PrP), cause genetic prion disease. However, how PRNP mutations lead to spontaneous prion formation remains poorly understood. Building off the observation that expression of mutant bank vole PrP (BVPrP) in mice causes spontaneous prion disease, we sought to i...
Genki Amano, H. Arshad, Surabhi Mehra et al.· bioRxiv· 0 citations
Abstract Conformationally distinct “strains” of α‐synuclein aggregates are believed to contribute to the clinical and pathological diversity observed among synucleinopathies such as multiple system atrophy (MSA) and Parkinson's disease. Cases of MSA can be classified into two distinct subtypes: the cerebellar variant,...
Heather H. C. Lau, N. R. G. Silver, Surabhi Mehra et al.· Brain Pathology· 0 citations
Different conformations, or strains, of α-synuclein (α-syn) aggregates are believed to be responsible for the distinct seeding propensities, propagation profiles, and clinical presentations in Lewy body diseases (LBD) and multiple system atrophy (MSA). While biochemical properties and strain differences of insoluble de...
S. Zampar, Y. Mei, F. Samuel et al.· bioRxiv· 0 citations
It is shown that stable knock-down of the protein disulfide isomerase P4HB in prion-susceptible CAD5 cells reduces PrPC levels and hinders the generation of protease-resistant PrP (PrPres) following infection with two different prion strains.
Genki Amano, H. Arshad, Zeel Patel et al.· PLoS Pathogens· 0 citations
We use cookies to run the site and, with your consent, for analytics and to show ads.
See our Cookie Policy.
