about
Scrapie Agent (Strain 263K) can transmit disease via the oral route after persistence in soil over yearsReversible off and on switching of prion infectivity via removing and reinstalling prion sialylation.Presence and seeding activity of pathological prion protein (PrP(TSE)) in skeletal muscles of white-tailed deer infected with chronic wasting diseaseIn situ identification of protein structural changes in prion-infected tissue.Scrapie-infected cells, isolated prions, and recombinant prion protein: a comparative study.FTIR-microspectroscopy of prion-infected nervous tissue.Changes in protein structure and distribution observed at pre-clinical stages of scrapie pathogenesis.Accumulation of pathological prion protein PrPSc in the skin of animals with experimental and natural scrapie.Relevance of the regional lymph node in scrapie pathogenesis after peripheral infection of hamsters.Preclinical deposition of pathological prion protein PrPSc in muscles of hamsters orally exposed to scrapie.Quantitative detection and biological propagation of scrapie seeding activity in vitro facilitate use of prions as model pathogens for disinfectionIs there a risk of prion-like disease transmission by Alzheimer- or Parkinson-associated protein particles?Widespread PrPSc accumulation in muscles of hamsters orally infected with scrapie.Autocatalytic self-propagation of misfolded prion proteinSequential appearance and accumulation of pathognomonic markers in the central nervous system of hamsters orally infected with scrapie.Synthetic scrapie infectivity: interaction between recombinant PrP and scrapie brain-derived RNA.Cell-free formation of misfolded prion protein with authentic prion infectivity.Aspects of risk assessment and risk management of nosocomial transmission of classical and variant Creutzfeldt-Jakob disease with special attention to German regulations.Harnessing prions as test agents for the development of broad-range disinfectantsThe spread of prions through the body in naturally acquired transmissible spongiform encephalopathies.Analytical applications of Fourier transform-infrared (FT-IR) spectroscopy in microbiology and prion research.Infrared microspectroscopy detects protein misfolding cyclic amplification (PMCA)-induced conformational alterations in hamster scrapie progeny seedsChronic wasting disease: fingerprinting the culprit in risk assessments.Early spread of scrapie from the gastrointestinal tract to the central nervous system involves autonomic fibers of the splanchnic and vagus nerves.Sialylation Controls Prion Fate in Vivo.Foodborne transmission of bovine spongiform encephalopathy to nonhuman primates.The nature of the scrapie agent: the virus theory.Transmissible spongiform encephalopathies: virally transmitted amyloidoses.Faecal shedding, alimentary clearance and intestinal spread of prions in hamsters fed with scrapie.Decontamination of medical devices from pathological amyloid-β-, tau- and α-synuclein aggregates.BSE-associated prion-amyloid cardiomyopathy in primates.Towards further reduction and replacement of animal bioassays in prion research by cell and protein misfolding cyclic amplification assays.Codon 129 polymorphism and the E200K mutation do not affect the cellular prion protein isoform composition in the cerebrospinal fluid from patients with Creutzfeldt-Jakob disease.Fast, broad-range disinfection of bacteria, fungi, viruses and prions.Association of prion protein genotype and scrapie prion protein type with cellular prion protein charge isoform profiles in cerebrospinal fluid of humans with sporadic or familial prion diseases.Detection of preclinical scrapie from serum by infrared spectroscopy and chemometrics.Decontamination of surgical instruments from prion proteins: in vitro studies on the detachment, destabilization and degradation of PrPSc bound to steel surfaces.Detection of prion particles in samples of BSE and scrapie by fluorescence correlation spectroscopy without proteinase K digestion.Discriminating scrapie and bovine spongiform encephalopathy isolates by infrared spectroscopy of pathological prion protein.Generation of genuine prion infectivity by serial PMCA.
P50
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P50
description
hulumtues
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researcher
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հետազոտող
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name
Michael Beekes
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Michael Beekes
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Michael Beekes
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Michael Beekes
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Michael Beekes
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type
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Michael Beekes
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Michael Beekes
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Michael Beekes
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Michael Beekes
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Michael Beekes
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Beekes M
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Michael Beekes
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Michael Beekes
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Michael Beekes
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Michael Beekes
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Michael Beekes
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P1053
S-1975-2018
P106
P1153
6701537872
P21
P31
P496
0000-0002-6454-6657