Epigenetic dominance of prion conformers. - Wikidata - awgldk - TriplyDB

Epigenetic dominance of prion conformers.

Epigenetic dominance of prion conformers.

http://www.wikidata.org/entity/Q35034201

about

Structural effects of PrP polymorphisms on intra- and interspecies prion transmission.Prion formation, but not clearance, is supported by protein misfolding cyclic amplification.Prion replication without host adaptation during interspecies transmissions.Mouse models for studying the formation and propagation of prions.Mouse-hamster chimeric prion protein (PrP) devoid of N-terminal residues 23-88 restores susceptibility to 22L prions, but not to RML prions in PrP-knockout mice Comparative Susceptibility of Sheep of Different Origins, Breeds and PRNP Genotypes to Challenge with Bovine Spongiform Encephalopathy and Scrapie PrPSc-Specific Antibody Reveals C-Terminal Conformational Differences between Prion Strains.Quinacrine promotes replication and conformational mutation of chronic wasting disease prions.Regulation of histone methylation by noncoding RNAs.Insights into Mechanisms of Transmission and Pathogenesis from Transgenic Mouse Models of Prion Diseases.Prion Protein Devoid of the Octapeptide Repeat Region Delays Bovine Spongiform Encephalopathy Pathogenesis in Mice.

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P2860

Epigenetic dominance of prion conformers.

http://www.wikidata.org/entity/Q35034201

description

2013 nî lūn-bûn

@nan

2013 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2013 թվականի հոտեմբերին հրատարակված գիտական հոդված

@hy

2013年の論文

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2013年論文

@yue

2013年論文

@zh-hant

2013年論文

@zh-hk

2013年論文

@zh-mo

2013年論文

@zh-tw

2013年论文

@wuu

name

Epigenetic dominance of prion conformers.

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Epigenetic dominance of prion conformers.

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type

label

Epigenetic dominance of prion conformers.

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Epigenetic dominance of prion conformers.

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prefLabel

Epigenetic dominance of prion conformers.

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Epigenetic dominance of prion conformers.

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Epigenetic dominance of prion conformers.

@en

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Eri Saijo

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Glenn C Telling

http://www.w3.org/2001/XMLSchema#string

Hae-Eun Kang

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Jifeng Bian

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Kristi G Bowling

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Nora Hunter

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Sehun Kim

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Shawn Browning

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P2860

Cofactor molecules maintain infectious conformation and restrict strain properties in purified prions

The strain-encoded relationship between PrP replication, stability and processing in neurons is predictive of the incubation period of disease

A general model of prion strains and their pathogenicity

Florid plaques in ovine PrP transgenic mice infected with an experimental ovine BSE.

Distinct PrP properties suggest the molecular basis of strain variation in transmissible mink encephalopathy.

Accelerated high fidelity prion amplification within and across prion species barriers.

Transmission of scrapie and sheep-passaged bovine spongiform encephalopathy prions to transgenic mice expressing elk prion protein.

Markedly increased susceptibility to natural sheep scrapie of transgenic mice expressing ovine prp.

Coinfecting prion strains compete for a limiting cellular resource.

Prion strain mutation determined by prion protein conformational compatibility and primary structure.

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10.1371/JOURNAL.PPAT.1003692

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Prion protein family

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