Rapid acquisition of beta-sheet structure in the prion protein prior to multimer formation.
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Intracellular re-routing of prion protein prevents propagation of PrP(Sc) and delays onset of prion diseaseUltra-sensitive detection of prion protein fibrils by flow cytometry in blood from cattle affected with bovine spongiform encephalopathyKosmotropic anions promote conversion of recombinant prion protein into a PrPSc-like misfolded formMeasuring Size Distribution in Highly Heterogeneous Systems with Fluorescence Correlation SpectroscopySystematic identification of antiprion drugs by high-throughput screening based on scanning for intensely fluorescent targets.Highly conserved and disease-specific patterns of carboxyterminally truncated Abeta peptides 1-37/38/39 in addition to 1-40/42 in Alzheimer's disease and in patients with chronic neuroinflammation.Detection of prion protein particles in blood plasma of scrapie infected sheep.Protein misfolding occurs by slow diffusion across multiple barriers in a rough energy landscape.Mechanisms of prion protein assembly into amyloidConformational propagation with prion-like characteristics in a simple model of protein foldingSingle-molecule approaches to prion protein misfoldingUltrasensitive detection of pathological prion protein aggregates by dual-color scanning for intensely fluorescent targetsPharmacological chaperone reshapes the energy landscape for folding and aggregation of the prion proteinComparing the energy landscapes for native folding and aggregation of PrP.Design of anti- and pro-aggregation variants to assess the effects of methionine oxidation in human prion protein.Prion infection: seeded fibrillization or more?Hyperphosphorylation-induced tau oligomersPrion rods contain an inert polysaccharide scaffold.Single-molecule assays for investigating protein misfolding and aggregation.Assembly of natural and recombinant prion protein into fibrils.Detection of prion particles in samples of BSE and scrapie by fluorescence correlation spectroscopy without proteinase K digestion.Substitutions of PrP N-terminal histidine residues modulate scrapie disease pathogenesis and incubation time in transgenic mice.Channels formed with a mutant prion protein PrP(82-146) homologous to a 7-kDa fragment in diseased brain of GSS patients.Photo-induced crosslinking of prion protein oligomers and prions.Interaction of the cellular prion protein with raft-like lipid membranes.Structural intermediates in the putative pathway from the cellular prion protein to the pathogenic form.
P2860
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P2860
Rapid acquisition of beta-sheet structure in the prion protein prior to multimer formation.
description
1998 nî lūn-bûn
@nan
1998 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
Rapid acquisition of beta-shee ...... n prior to multimer formation.
@ast
Rapid acquisition of beta-shee ...... n prior to multimer formation.
@en
type
label
Rapid acquisition of beta-shee ...... n prior to multimer formation.
@ast
Rapid acquisition of beta-shee ...... n prior to multimer formation.
@en
prefLabel
Rapid acquisition of beta-shee ...... n prior to multimer formation.
@ast
Rapid acquisition of beta-shee ...... n prior to multimer formation.
@en
P2093
P2860
P1433
P1476
Rapid acquisition of beta-shee ...... n prior to multimer formation.
@en
P2093
Mehlhorn I
Pitschke M
P2860
P304
P356
10.1515/BCHM.1998.379.11.1307
P577
1998-11-01T00:00:00Z