Cell-free formation of misfolded prion protein with authentic prion infectivity.
about
Presence and seeding activity of pathological prion protein (PrP(TSE)) in skeletal muscles of white-tailed deer infected with chronic wasting diseaseRecombinant prion protein refolded with lipid and RNA has the biochemical hallmarks of a prion but lacks in vivo infectivityGetting a grip on prions: oligomers, amyloids, and pathological membrane interactions.Anle138b: a novel oligomer modulator for disease-modifying therapy of neurodegenerative diseases such as prion and Parkinson's disease.Highly potent soluble amyloid-β seeds in human Alzheimer brain but not cerebrospinal fluidFrom high-throughput cell culture screening to mouse model: identification of new inhibitor classes against prion disease.Accelerated high fidelity prion amplification within and across prion species barriers.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?Lower specific infectivity of protease-resistant prion protein generated in cell-free reactions.Increased infectivity of anchorless mouse scrapie prions in transgenic mice overexpressing human prion proteinHarnessing prions as test agents for the development of broad-range disinfectantsThe reconstitution of mammalian prion infectivity de novo.Branched chain mechanism of polymerization and ultrastructure of prion protein amyloid fibrils.Chemical and biophysical insights into the propagation of prion strains.Analyses of protease resistance and aggregation state of abnormal prion protein across the spectrum of human prionsA specific population of abnormal prion protein aggregates is preferentially taken up by cells and disaggregated in a strain-dependent manner.Infrared microspectroscopy detects protein misfolding cyclic amplification (PMCA)-induced conformational alterations in hamster scrapie progeny seedsHighly infectious prions generated by a single round of microplate-based protein misfolding cyclic amplification.Modelling neurodegeneration in prion disease - applications for drug development.Vaccination with prion peptide-displaying papillomavirus-like particles induces autoantibodies to normal prion protein that interfere with pathologic prion protein production in infected cells.Glycoform-independent prion conversion by highly efficient, cell-based, protein misfolding cyclic amplification.Peroxymonosulfate Rapidly Inactivates the Disease-Associated Prion Protein.Shedding light on prion disease.
P2860
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P2860
Cell-free formation of misfolded prion protein with authentic prion infectivity.
description
2006 nî lūn-bûn
@nan
2006 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
Cell-free formation of misfolded prion protein with authentic prion infectivity.
@ast
Cell-free formation of misfolded prion protein with authentic prion infectivity.
@en
type
label
Cell-free formation of misfolded prion protein with authentic prion infectivity.
@ast
Cell-free formation of misfolded prion protein with authentic prion infectivity.
@en
prefLabel
Cell-free formation of misfolded prion protein with authentic prion infectivity.
@ast
Cell-free formation of misfolded prion protein with authentic prion infectivity.
@en
P2093
P2860
P356
P1476
Cell-free formation of misfolded prion protein with authentic prion infectivity.
@en
P2093
Achim Thomzig
Gerda Mitteregger
Hans A Kretzschmar
Niklas Piening
Petra Weber
P2860
P304
15818-15823
P356
10.1073/PNAS.0605608103
P407
P577
2006-10-09T00:00:00Z