Results 161 to 170 of about 1,549,882 (213)

AI-designed prion-capping proteins provide evidence that prion fibril ends are replication-competent surfaces that contribute to prion seeding activity and infectivity. [PDF]

open access: yesmBio
Slota JA   +10 more
europepmc   +1 more source

Prion shedding is reduced by chronic wasting disease vaccination. [PDF]

open access: yesPLoS Pathog
Ahmed-Hassan H   +10 more
europepmc   +1 more source

D178N prion protein mutation endows RML prions with new strain properties that do not mimic human genetic prion diseases. [PDF]

open access: yesActa Neuropathol
Masone A   +15 more
europepmc   +1 more source

Spontaneous generation of diverse recombinant prion strains: sulfated glycan cofactors facilitate strain emergence but do not determine specific strain properties. [PDF]

open access: yesActa Neuropathol Commun
Lorenzo NL   +11 more
europepmc   +1 more source

Prions and protein aggregates as pathogens, self-propagating structures, biomarkers, and therapeutic targets. [PDF]

open access: yesMicrobiol Mol Biol Rev
Caughey B   +9 more
europepmc   +1 more source

Pathological and Functional Brain Amyloids: A New Concept Explaining the Differences. [PDF]

open access: yesInt J Mol Sci
Galkin AP   +4 more
europepmc   +1 more source

Methamphetamine increases Prion Protein and induces dopamine-dependent expression of protease resistant PrPsc

open access: yesArchives Italiennes de Biologie, 2017
The cellular prion protein (PrPc) is physiologically expressed within selective brain areas of mammals. Alterations in the secondary structure of this protein lead to scrapie-like prion protein (PrPsc), which precipitates in the cell. PrPsc has been detected in infectious, inherited or sporadic neurodegenerative disorders.
FERRUCCI, MICHELA   +7 more
openaire   +4 more sources

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