Prion interference is due to a reduction in strain-specific PrPSc levels. - Wikidata - wikimedia - TriplyDB

Prion interference is due to a reduction in strain-specific PrPSc levels.

Prion interference is due to a reduction in strain-specific PrPSc levels.

http://www.wikidata.org/entity/Q35635053

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Multifaceted Role of Sialylation in Prion Diseases Evidence that bank vole PrP is a universal acceptor for prions Prion formation, but not clearance, is supported by protein misfolding cyclic amplification.Coinfecting prion strains compete for a limiting cellular resource.Effects of solution chemistry and aging time on prion protein adsorption and replication of soil-bound prions.Enzymatic digestion of chronic wasting disease prions bound to soil.Prion strain interactions are highly selective.Resistance of soil-bound prions to rumen digestion.Replication efficiency of soil-bound prions varies with soil type.Mitigation of prion infectivity and conversion capacity by a simulated natural process--repeated cycles of drying and wetting.Tracking protein aggregate interactions.In vitro generation of high-titer prions Change in the characteristics of ferritin induces iron imbalance in prion disease affected brains.Environmentally-relevant forms of the prion protein.Host Determinants of Prion Strain Diversity Independent of Prion Protein Genotype.Disease-associated prion protein in neural and lymphoid tissues of mink (Mustela vison) inoculated with transmissible mink encephalopathy.Deer Prion Proteins Modulate the Emergence and Adaptation of Chronic Wasting Disease Strains.Prion strain targeting independent of strain-specific neuronal tropism.Prion interference with multiple prion isolates Heterozygous inhibition in prion infection: the stone fence model Rapid, high-throughput detection of PrPSc by 96-well immunoassay.Co-existence of distinct prion types enables conformational evolution of human PrPSc by competitive selection Influence of prion strain on prion protein adsorption to soil in a competitive matrix.Implications of prion adaptation and evolution paradigm for human neurodegenerative diseases.Treatment with a non-toxic, self-replicating anti-prion delays or prevents prion disease in vivo.Incongruity between Prion Conversion and Incubation Period following Coinfection.Evidence for distinct chronic wasting disease (CWD) strains in experimental CWD in ferrets.Human prion protein (PrP) 219K is converted to PrPSc but shows heterozygous inhibition in variant Creutzfeldt-Jakob disease infection.Prion Strains and Transmission Barrier Phenomena.Dehydration of prions on environmentally relevant surfaces protects them from inactivation by freezing and thawing.New Molecular Insight into Mechanism of Evolution of Mammalian Synthetic Prions.Sporadic Creutzfeldt-Jakob Disease MM1+2C and MM1 are Identical in Transmission Properties.Independent amplification of co-infected long incubation period low conversion efficiency prion strains

P2860

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P2860

Prion interference is due to a reduction in strain-specific PrPSc levels.

http://www.wikidata.org/entity/Q35635053

description

2006 nî lūn-bûn

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2006年の論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年论文

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2006年论文

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2006年论文

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name

Prion interference is due to a reduction in strain-specific PrPSc levels.

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Prion interference is due to a reduction in strain-specific PrPSc levels.

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type

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Prion interference is due to a reduction in strain-specific PrPSc levels.

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Prion interference is due to a reduction in strain-specific PrPSc levels.

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Prion interference is due to a reduction in strain-specific PrPSc levels.

@ast

Prion interference is due to a reduction in strain-specific PrPSc levels.

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P1433

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P1433

Journal of Virology

P1476

Prion interference is due to a reduction in strain-specific PrPSc levels.

@en

P2093

Jessica A L Hutter

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

Meghan H Sheehan

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Michelle L Kramer

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Richard A Bessen

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P2860

Novel proteinaceous infectious particles cause scrapie

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

Biochemical and physical properties of the prion protein from two strains of the transmissible mink encephalopathy agent.

Synthetic mammalian prions.

Preclinical vCJD after blood transfusion in a PRNP codon 129 heterozygous patient.

Retrograde transport of transmissible mink encephalopathy within descending motor tracts.

In vitro generation of infectious scrapie prions.

Rapid prion neuroinvasion following tongue infection.

Vaccination with an attenuated Creutzfeldt-Jakob disease strain prevents expression of a virulent agent.

Normal and scrapie-associated forms of prion protein differ in their sensitivities to phospholipase and proteases in intact neuroblastoma cells.

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689-697

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10.1128/JVI.01751-06

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81

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Anthony E Kincaid

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2006-11-01T00:00:00Z

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6717874

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17079313

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Prion protein family

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1797475

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