Distinct Structures of Scrapie Prion Protein (PrPSc)-seeded Versus Spontaneous Recombinant Prion Protein Fibrils Revealed by Hydrogen/Deuterium Exchange [PDF]
Journal of Biological Chemistry, 2009 The detailed structures of prion disease-associated, partially protease-resistant forms of prion protein (e.g. PrP(Sc)) are largely unknown. PrP(Sc) appears to propagate itself by autocatalyzing the conformational conversion and oligomerization of normal prion protein (PrP(C)). One manifestation of PrP(Sc) templating activity is its ability, in protein
Vytautas, Smirnovas +5 more
openaire +2 more sources
Glycosylphosphatidylinositols: More than just an anchor?
Communicative & Integrative Biology, 2016 There is increasing interest in the role of glycosylphosphatidylinositol (GPI) anchors that attach some proteins to cell membranes. Far from being biologically inert, GPIs influence the targeting, intracellular trafficking and function of the attached ...
Clive Bate, William Nolan, Alun Williams
doaj +1 more source
Sodium hydroxide renders the prion protein PrPSc sensitive to proteinase K
Journal of General Virology, 2003 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
Fabian, Käsermann, Christoph, Kempf
openaire +2 more sources
Heterogeneity of the Abnormal Prion Protein (PrPSc) of the Chandler Scrapie Strain [PDF]
Pathogens, 2013 The pathological prion protein, PrPSc, displays various sizes of aggregates. In this study, we investigated the conformation, aggregation stability and proteinase K (PK)-sensitivity of small and large PrPSc aggregates of mouse-adapted prion strains.
Kasai, Kazuo +5 more
openaire +3 more sources
Prion Protein Misfolding, Strains, and Neurotoxicity: An Update from Studies on Mammalian Prions
International Journal of Cell Biology, 2013 Prion diseases, also known as transmissible spongiform encephalopathies (TSEs), are a group of fatal neurodegenerative disorders affecting humans and other mammalian species.
Ilaria Poggiolini +2 more
doaj +1 more source
Full atomistic model of prion structure and conversion.
PLoS Pathogens, 2019 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
Brazilian Journal of Medical and Biological Research, 1999 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
Body-first Parkinson’s disease and variant Creutzfeldt–Jakob disease – similar or different?
Neurobiology of Disease, 2022 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
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]
PLoS Pathogens, 2016 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
Charged bipolar suramin derivatives induce aggregation of the prion protein at the cell surface and inhibit PrPSc replication [PDF]
Journal of Cell Science, 2005 The conversion of the cellular prion protein (PrPc) into a pathogenic isoform (PrPSc) is one of the underlying events in the pathogenesis of the fatal transmissible spongiform encephalopathies (TSEs). Numerous compounds have been described to inhibit prion replication and PrPSc accumulation in cell culture.
Max, Nunziante +5 more
openaire +2 more sources