Structural intermediates in the putative pathway from the cellular prion protein to the pathogenic form.
about
Prion protein structure is affected by pH-dependent interaction with membranes: a study in a model system.Progress towards structural understanding of infectious sheep PrP-amyloid.Isolation and characterization of a polymerized prion protein.In vitro and in vivo neurotoxicity of prion protein oligomers.Molecular interactions between prions as seeds and recombinant prion proteins as substrates resemble the biological interspecies barrier in vitroDistinct synthetic Aβ prion strains producing different amyloid deposits in bigenic mice.N-terminal domain of prion protein directs its oligomeric association.Highly neurotoxic monomeric α-helical prion protein.Rare large scale subdomain motions in prion protein can initiate aggregation.Mechanisms of prion protein assembly into amyloidSingle-molecule approaches to prion protein misfoldingProtease-sensitive prions with 144-bp insertion mutationsStructural changes of membrane-anchored native PrP(C)Toxic effects of intracerebral PrP antibody administration during the course of BSE infection in mice.Prion infection: seeded fibrillization or more?2-Aminothiazoles with improved pharmacotherapeutic properties for treatment of prion diseaseRegulation of PrP(C) signaling and processing by dimerization.An Account of Amyloid Oligomers: Facts and Figures Obtained from Experiments and Simulations.Pathogenic mechanisms of prion protein, amyloid-β and α-synuclein misfolding: the prion concept and neurotoxicity of protein oligomers.Homodimerization as a molecular switch between low and high efficiency PrP C cell surface delivery and neuroprotective activity.Subclinical prion disease induced by oral inoculation.Acidic pH and detergents enhance in vitro conversion of human brain PrPC to a PrPSc-like form.Assembly of natural and recombinant prion protein into fibrils.Protein misfolding cyclic amplification induces the conversion of recombinant prion protein to PrP oligomers causing neuronal apoptosis.Curcumin binds to the alpha-helical intermediate and to the amyloid form of prion protein - a new mechanism for the inhibition of PrP(Sc) accumulation.Substitutions of PrP N-terminal histidine residues modulate scrapie disease pathogenesis and incubation time in transgenic mice.Putative aggregation initiation sites in prion protein.Photo-induced crosslinking of prion protein oligomers and prions.Interaction of the cellular prion protein with raft-like lipid membranes.In vitro conversion and seeded fibrillization of posttranslationally modified prion protein.
P2860
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P2860
Structural intermediates in the putative pathway from the cellular prion protein to the pathogenic form.
description
2001 nî lūn-bûn
@nan
2001年の論文
@ja
2001年学术文章
@wuu
2001年学术文章
@zh-cn
2001年学术文章
@zh-hans
2001年学术文章
@zh-my
2001年学术文章
@zh-sg
2001年學術文章
@yue
2001年學術文章
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2001年學術文章
@zh-hant
name
Structural intermediates in th ...... rotein to the pathogenic form.
@en
Structural intermediates in th ...... rotein to the pathogenic form.
@nl
type
label
Structural intermediates in th ...... rotein to the pathogenic form.
@en
Structural intermediates in th ...... rotein to the pathogenic form.
@nl
prefLabel
Structural intermediates in th ...... rotein to the pathogenic form.
@en
Structural intermediates in th ...... rotein to the pathogenic form.
@nl
P2093
P2860
P356
P1433
P1476
Structural intermediates in th ...... rotein to the pathogenic form.
@en
P2093
P2860
P304
P356
10.1515/BC.2001.081
P577
2001-04-01T00:00:00Z