Octapeptide repeat insertions increase the rate of protease-resistant prion protein formation
about
Probing the role of PrP repeats in conformational conversion and amyloid assembly of chimeric yeast prionsPotential roles for prions and protein-only inheritance in cancerStructure of the Flexible Amino-Terminal Domain of Prion Protein Bound to a Sulfated GlycanThe octarepeat region of the prion protein is conformationally altered in PrP(Sc)Early onset prion disease from octarepeat expansion correlates with copper binding propertiesPrion fragment peptides are digested with membrane type matrix metalloproteinases and acquire enzyme resistance through Cu²⁺-bindingGenotype-phenotype analysis in inherited prion disease with eight octapeptide repeat insertional mutation.Prion protein insertional mutations increase aggregation propensity but not fiber stability.Glycosaminoglycan sulphation affects the seeded misfolding of a mutant prion proteinConformational flexibility of Y145Stop human prion protein amyloid fibrils probed by solid-state nuclear magnetic resonance spectroscopyManganese upregulates cellular prion protein and contributes to altered stabilization and proteolysis: relevance to role of metals in pathogenesis of prion diseaseInstability of the octarepeat region of the human prion protein gene.Identifying critical sites of PrP(c)-PrP(Sc) interaction in prion-infected cells by dominant-negative inhibition.Characterization of four new monoclonal antibodies against the distal N-terminal region of PrP(c).Structural polymorphism in amyloids: new insights from studies with Y145Stop prion protein fibrils.Prion protein repeat expansion results in increased aggregation and reveals phenotypic variability.Copper-induced structural conversion templates prion protein oligomerization and neurotoxicity.Molecular conformation and dynamics of the Y145Stop variant of human prion protein in amyloid fibrilsInsights into intragenic and extragenic effectors of prion propagation using chimeric prion proteins.Prion protein misfolding and disease.Thermodynamic characterization of the unfolding of the prion protein.Genetic prion disease: Experience of a rapidly progressive dementia center in the United States and a review of the literature.Prion protein with an octapeptide insertion has impaired neuroprotective activity in transgenic mice.Aggregation of prion protein with insertion mutations is proportional to the number of inserts.Characterization of mutations in (prion) gene and their possible roles in neurodegenerative diseases
P2860
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P2860
Octapeptide repeat insertions increase the rate of protease-resistant prion protein formation
description
2006 nî lūn-bûn
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2006年の論文
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2006年学术文章
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name
Octapeptide repeat insertions ...... istant prion protein formation
@ast
Octapeptide repeat insertions ...... istant prion protein formation
@en
type
label
Octapeptide repeat insertions ...... istant prion protein formation
@ast
Octapeptide repeat insertions ...... istant prion protein formation
@en
prefLabel
Octapeptide repeat insertions ...... istant prion protein formation
@ast
Octapeptide repeat insertions ...... istant prion protein formation
@en
P2093
P2860
P356
P1433
P1476
Octapeptide repeat insertions ...... istant prion protein formation
@en
P2093
Christian Herzog
David A Kocisko
John Errett
Kevin M Arnold
Roger A Moore
Stanley F Hayes
Suzette A Priola
P2860
P304
P356
10.1110/PS.051822606
P577
2006-02-01T00:00:00Z