Results 131 to 140 of about 7,097 (179)

The N-terminal cleavage site of PrPSc from BSE differs from that of PrPSc from scrapie

Biochemical and Biophysical Research Communications, 2005
Heterogeneity in transmissible spongiform encephalopathy is thought to have derived from conformational variation in an abnormal isoform of the prion protein (PrPSc). To characterize PrPSc in bovine spongiform encephalopathy (BSE) and scrapie, we analyzed the newly generated N-terminus of PrPSc isoforms by digestion with proteinase K (PK). With a lower
Hiroko K, Hayashi, Takashi, Yokoyama, Masuhiro, Takata, Yoshifumi, Iwamaru, Morikazu, Imamura, Yuko K, Ushiki, Morikazu, Shinagawa   +6 more
openaire   +2 more sources

Prion inhibition with multivalent PrPSc binding compounds

Biomaterials, 2012
Quinacrine and related heterocyclic compounds have antiprion activity. Since the infectious pathogen of prion diseases is composed of multimeric PrP(Sc) assemblies, we hypothesized that this antiprion property could be enhanced by attaching multiple quinacrine-derived chloroquinoline or acridine moieties to a scaffold.
Charles E, Mays, Shaon, Joy, Lei, Li, Linghui, Yu, Sacha, Genovesi, Frederick G, West, David, Westaway   +6 more
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Bovine macrophage degradation of scrapie and BSE PrPSc

Veterinary Immunology and Immunopathology, 2010
Transmissible spongiform encephalopathies (TSEs), such as bovine spongiform encephalopathy (BSE) and scrapie, display long incubation periods before PrP(Sc) accumulates in the central neuronal system (CNS). The precise role that phagocytic cells, such as macrophages, play in prion pathogenesis is uncertain.
Yukiko, Sassa, Yasuo, Inoshima, Naotaka, Ishiguro   +2 more
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Efficient detection of PrPSc (263K) in human plasma

Biologicals, 2006
The potential contamination of human blood or plasma with prions, such as variant Creuftzfelt-Jacob disease (vCJD), is becoming a serious problem. In this study, we established a Western blot-based detection method for PrP(Sc) (263K) spiked in plasma.
Ryo, Fujita, Takeru, Urayama, Akimasa, Ohmizu, Mikihiro, Yunoki, Shoutaro, Tsuji, Kazuyoshi, Ikuta   +5 more
openaire   +2 more sources

Species variation in PrPSc protofibril models

Journal of Materials Science, 2008
The misfolding and aggregation of the prion protein (PrP) is the primary cause of a group of infectious neurodegenerative diseases including Creutzfeldt-Jacob disease in humans and Bovine Spongiform Encephalopathy in cows. A single disease can exhibit different infectious strains distinguishable by incubation time and morphology or distribution of the ...
Alexander D. Scouras, Valerie Daggett
openaire   +1 more source

Immunodetection of PrPSc Using Western Immunoblotting Techniques

2017
Western immunoblotting is a workhorse technique used in the prion field to analyze disease-associated forms of the prion protein, termed PrPSc. The biochemical stability of PrPSc aggregates combined with the increased resistance of prion infectivity to inactivation by various treatments that inactivate most other pathogens complicates the use of ...
Gerald S, Baron, Gregory J, Raymond
openaire   +2 more sources

PrPSc Immunohistochemistry

2004
Historically, diagnosis of transmissible spongiform encephalopathies (TSEs) has been a matter for pathologists. For decades, the only available diagnostic tool in this field was the identification of spongiform changes and gnosis in CNS sections, and conventional histopathology still remains the method of choice for the confirmation of clinically ...
openaire   +1 more source

Prion-Protein-Specific Aptamer Reduces PrPSc Formation

ChemBioChem, 2002
The critical initial event in the pathophysiology of transmissible spongiform encephalopathies (TSEs) appears to be the conversion of the cellular prion protein (PrP(C)) into the abnormal isoform PrP(Sc). This isoform forms high-molecular-weight protease K (PK) resistant aggregates that accumulate in the central nervous system of affected individuals ...
Daniela, Proske, Sabine, Gilch, Franziska, Wopfner, Hermann M, Schätzl, Ernst-L, Winnacker, Michael, Famulok   +5 more
openaire   +2 more sources

Prion (PrPSc)-specific epitope defined by a monoclonal antibody

Nature, 1997
Prions are infectious particles causing transmissible spongiform encephalopathies (TSEs). They consist, at least in part, of an isoform (PrPSc) of the ubiquitous cellular prion protein (PrPC). Conformational differences between PrPC and PrPSc are evident from increased beta-sheet content and protease resistance in PrPSc.
Korth, C, Stierli, B, Streit, P, Moser, M, Schaller, O, Fischer, R, Schulz-Schaeffer, W, Kretzschmar, H, Raeber, A, Braun, Ueli, Ehrensperger, F, Hornemann, S, Glockshuber, R, Riek, R, Billeter, M, Wüthrich, K, Oesch, B   +16 more
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Prions and exosomes: From PrPc trafficking to PrPsc propagation

Blood Cells, Molecules, and Diseases, 2005
Exosomes are membrane vesicles released into the extracellular environment upon exocytic fusion of multivesicular endosomes with the cell surface. Exosome secretion can be used by cells to eject molecules targeted to intraluminal vesicles of multivesicular bodies, but particular cell types may exploit exosomes as intercellular communication devices for
Porto-Carreiro, Isabel, Février, Benoit, Paquet, Sophie, Vilette, Didier, Raposo, Graça   +4 more
openaire   +3 more sources