Recombinant prion protein induces a new transmissible prion disease in wild-type animals. - Wikidata - wikimedia - TriplyDB

Recombinant prion protein induces a new transmissible prion disease in wild-type animals.

Recombinant prion protein induces a new transmissible prion disease in wild-type animals.

http://www.wikidata.org/entity/Q24645106

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Prion hypothesis: the end of the controversy?Cofactor molecules maintain infectious conformation and restrict strain properties in purified prions Insights into Mechanisms of Chronic Neurodegeneration The strain-encoded relationship between PrP replication, stability and processing in neurons is predictive of the incubation period of disease Highly efficient protein misfolding cyclic amplification Intraperitoneal Infection of Wild-Type Mice with Synthetically Generated Mammalian Prion Sialylation of prion protein controls the rate of prion amplification, the cross-species barrier, the ratio of PrPSc glycoform and prion infectivity Genesis of mammalian prions: from non-infectious amyloid fibrils to a transmissible prion disease Reversible off and on switching of prion infectivity via removing and reinstalling prion sialylation.Thermodynamic Stabilization of the Folded Domain of Prion Protein Inhibits Prion Infection in Vivo De novo generation of prion strains Ultra-efficient PrP(Sc) amplification highlights potentialities and pitfalls of PMCA technology Biochemical properties of highly neuroinvasive prion strains Kosmotropic anions promote conversion of recombinant prion protein into a PrPSc-like misfolded form Prion seeding activities of mouse scrapie strains with divergent PrPSc protease sensitivities and amyloid plaque content using RT-QuIC and eQuIC The effect of β2-α2 loop mutation on amyloidogenic properties of the prion protein Recombinant prion protein refolded with lipid and RNA has the biochemical hallmarks of a prion but lacks in vivo infectivity Parallel in-register intermolecular β-sheet architectures for prion-seeded prion protein (PrP) amyloids.Charge neutralization of the central lysine cluster in prion protein (PrP) promotes PrP(Sc)-like folding of recombinant PrP amyloids.Progress towards structural understanding of infectious sheep PrP-amyloid.Prion amyloid structure explains templating: how proteins can be genes.NLRP3 inflammasome activation in macrophage cell lines by prion protein fibrils as the source of IL-1β and neuronal toxicity.Proper calibration of ultrasonic power enabled the quantitative analysis of the ultrasonication-induced amyloid formation process.Globular domain of the prion protein needs to be unlocked by domain swapping to support prion protein conversion Effect of hydrophobic mutations in the H2-H3 subdomain of prion protein on stability and conversion in vitro and in vivo.Two amyloid States of the prion protein display significantly different folding patterns Spontaneous generation of rapidly transmissible prions in transgenic mice expressing wild-type bank vole prion protein.PrPC Governs Susceptibility to Prion Strains in Bank Vole, While Other Host Factors Modulate Strain Features.Biology and genetics of prions causing neurodegeneration Oxidation of Helix-3 methionines precedes the formation of PK resistant PrP.High-resolution structure of infectious prion protein: the final frontier Low density subcellular fractions enhance disease-specific prion protein misfolding.Mammalian prions generated from bacterially expressed prion protein in the absence of any mammalian cofactors The core of Ure2p prion fibrils is formed by the N-terminal segment in a parallel cross-β structure: evidence from solid-state NMR.Coinfecting prion strains compete for a limiting cellular resource.Dynamic diagnosis of familial prion diseases supports the β2-α2 loop as a universal interference target.Molecular structure of amyloid fibrils controls the relationship between fibrillar size and toxicity.Synthesis of high titer infectious prions with cofactor molecules.Seeding specificity and ultrastructural characteristics of infectious recombinant prions.Relationship between conformational stability and amplification efficiency of prions.

P2860

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P2860

Recombinant prion protein induces a new transmissible prion disease in wild-type animals.

http://www.wikidata.org/entity/Q24645106

description

2010 nî lūn-bûn

@nan

2010 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի հունվարին հրատարակված գիտական հոդված

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2010年の論文

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2010年論文

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2010年論文

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2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

name

Recombinant prion protein induces a new transmissible prion disease in wild-type animals

@nl

Recombinant prion protein induces a new transmissible prion disease in wild-type animals.

@ast

Recombinant prion protein induces a new transmissible prion disease in wild-type animals.

@en

type

label

Recombinant prion protein induces a new transmissible prion disease in wild-type animals

@nl

Recombinant prion protein induces a new transmissible prion disease in wild-type animals.

@ast

Recombinant prion protein induces a new transmissible prion disease in wild-type animals.

@en

prefLabel

Recombinant prion protein induces a new transmissible prion disease in wild-type animals

@nl

Recombinant prion protein induces a new transmissible prion disease in wild-type animals.

@ast

Recombinant prion protein induces a new transmissible prion disease in wild-type animals.

@en

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S00401-009-0633-X

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Acta Neuropathologica

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Recombinant prion protein induces a new transmissible prion disease in wild-type animals.

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Ilia V Baskakov

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Irina Alexeeva

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Natallia Makarava

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Olga Bocharova

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Regina Savtchenko

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Robert G Rohwer

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P2860

Formation of native prions from minimal components in vitro

De novo generation of infectious prions in vitro produces a new disease phenotype

Adapting proteostasis for disease intervention

Novel proteinaceous infectious particles cause scrapie

Eight prion strains have PrP(Sc) molecules with different conformations

Conformational switching within individual amyloid fibrils.

Scrapie pathogenesis in subclinically infected B-cell-deficient mice.

Strain-specified characteristics of mouse synthetic prions.

Synthetic mammalian prions.

In vitro generation of infectious scrapie prions.

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10.1007/S00401-009-0633-X

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119

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1046895462

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20052481

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Prion protein family

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2808531

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