Full atomistic model of prion structure and conversion.
Prions are unusual protein assemblies that propagate their conformationally-encoded information in absence of nucleic acids. The first prion identified, the scrapie isoform (PrPSc) of the cellular prion protein (PrPC), caused epidemic and epizootic ...
Giovanni Spagnolli +7 more
doaj +1 more source
A receptor for infectious and cellular prion protein
Prions are an unconventional form of infectious agents composed only of protein and involved in transmissible spongiform encephalopathies in humans and animals.
V.R. Martins
doaj +1 more source
Anti-prion drug mPPIg5 inhibits PrP(C) conversion to PrP(Sc). [PDF]
Prion diseases, also known as transmissible spongiform encephalopathies, are a group of fatal neurodegenerative diseases that include scrapie in sheep, bovine spongiform encephalopathy (BSE) in cattle and Creutzfeldt-Jakob disease (CJD) in humans.
Jeremy C. Simpson (29225) +31 more
core +2 more sources
Body-first Parkinson’s disease and variant Creutzfeldt–Jakob disease – similar or different?
In several neurodegenerative disorders, proteins that typically exhibit an α-helical structure misfold into an amyloid conformation rich in β-sheet content.
Amanda L. Woerman, Gültekin Tamgüney
doaj +1 more source
Sodium hydroxide renders the prion protein PrPSc sensitive to proteinase K
Sodium hydroxide (NaOH) solutions are widely used for the purification of contaminated equipment, as they are known to inactivate a variety of pathogens. However, information about their effect on agents causing transmissible spongiform encephalopathy (TSE) is sparse and contradictory. Scrapie hamster brain homogenate, containing the disease-associated
Käsermann F, Kempf C
openaire +3 more sources
The crystal structure of the globular domain of sheep prion protein [PDF]
The prion protein PrP is a naturally occurring polypeptide that becomes transformed from a normal conformation to that of an aggregated form, characteristic of pathological states in fatal transmissible spongiform conditions such as Creutzfeld–Jacob ...
Vasisht N +28 more
core +1 more source
Change in the characteristics of ferritin induces iron imbalance in prion disease affected brains
Prion disease associated neurotoxicity is mainly attributed to PrP-scrapie (PrPSc), the disease associated isoform of a normal protein, the prion protein (PrPC).
Ajay Singh +3 more
doaj +1 more source
Prion Strain Differences in Accumulation of PrPSc on Neurons and Glia Are Associated with Similar Expression Profiles of Neuroinflammatory Genes: Comparison of Three Prion Strains. [PDF]
Misfolding and aggregation of host proteins are important features of the pathogenesis of neurodegenerative diseases including Alzheimer's disease, Parkinson's disease, frontotemporal dementia and prion diseases.
James A Carroll +7 more
doaj +1 more source
Strain Traits of Intracranially Administered L-Type Bovine Spongiform Encephalopathy Prions Are not Significantly Modified During Intraspecies Transmission in Cynomolgus Monkeys. [PDF]
ABSTRACT Among the three prion strains of bovine spongiform encephalopathy (BSE), classical BSE (C‐BSE) prions are known causative agents of variant Creutzfeldt–Jakob disease. By contrast, human infections with L‐type (L‐) or H‐type (H‐) BSE prions have not been reported.
Hagiwara K +8 more
europepmc +2 more sources
Early Generation of New PrPSc on Blood Vessels after Brain Microinjection of Scrapie in Mice
Aggregation of misfolded host proteins in the central nervous system is believed to be important in the pathogenic process in several neurodegenerative diseases of humans, including prion diseases, Alzheimer's disease, and Parkinson's disease.
Bruce Chesebro +6 more
doaj +1 more source

