The physical relationship between infectivity and prion protein aggregates is strain-dependent - Test2 - elhamkhani - TriplyDB

The physical relationship between infectivity and prion protein aggregates is strain-dependent

The physical relationship between infectivity and prion protein aggregates is strain-dependent

http://www.wikidata.org/entity/Q27315010

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The strain-encoded relationship between PrP replication, stability and processing in neurons is predictive of the incubation period of disease Prion pathogenesis in the absence of NLRP3/ASC inflammasomes Transgenic Rabbits Expressing Ovine PrP Are Susceptible to Scrapie Ex vivo mammalian prions are formed of paired double helical prion protein fibrils.Biochemical properties of highly neuroinvasive prion strains Prion seeding activities of mouse scrapie strains with divergent PrPSc protease sensitivities and amyloid plaque content using RT-QuIC and eQuIC Defining the conformational features of anchorless, poorly neuroinvasive prions Isolation of proteinase K-sensitive prions using pronase E and phosphotungstic acid Analysis of Conformational Stability of Abnormal Prion Protein Aggregates across the Spectrum of Creutzfeldt-Jakob Disease Prions NLRP3 Inflammasome in Neurological Diseases, from Functions to Therapies NLRP3 inflammasome activation in macrophage cell lines by prion protein fibrils as the source of IL-1β and neuronal toxicity.Enhanced neuroinvasion by smaller, soluble prions.High-resolution structure of infectious prion protein: the final frontier Atypical/Nor98 scrapie infectivity in sheep peripheral tissues.A simple, versatile and sensitive cell-based assay for prions from various species Accelerated, spleen-based titration of variant Creutzfeldt-Jakob disease infectivity in transgenic mice expressing human prion protein with sensitivity comparable to that of survival time bioassay.Prions in the urine of patients with variant Creutzfeldt-Jakob disease.Transmissibility of caprine scrapie in ovine transgenic mice.Assessment of strain-specific PrP(Sc) elongation rates revealed a transformation of PrP(Sc) properties during protein misfolding cyclic amplification Structure-based drug design identifies polythiophenes as antiprion compounds.Heterogeneity of the Abnormal Prion Protein (PrPSc) of the Chandler Scrapie Strain.Recovery of small infectious PrP(res) aggregates from prion-infected cultured cells.Sheep and goat BSE propagate more efficiently than cattle BSE in human PrP transgenic mice Plasminogen-based capture combined with amplification technology for the detection of PrP(TSE) in the pre-clinical phase of infection Quaternary structure of pathological prion protein as a determining factor of strain-specific prion replication dynamics.Insights into prion biology: integrating a protein misfolding pathway with its cellular environment.Mammalian prions: tracking the infectious entities Interaction of prion protein with acetylcholinesterase: potential pathobiological implications in prion diseases.A novel and rapid method for obtaining high titre intact prion strains from mammalian brain.Interaction between Shadoo and PrP Affects the PrP-Folding Pathway Prion subcellular fractionation reveals infectivity spectrum, with a high titre-low PrPres level disparity.Polythiophenes inhibit prion propagation by stabilizing prion protein (PrP) aggregates.PrPSc formation and clearance as determinants of prion tropism.Prion Infectivity Plateaus and Conversion to Symptomatic Disease Originate from Falling Precursor Levels and Increased Levels of Oligomeric PrPSc Species.Use of murine bioassay to resolve ovine transmissible spongiform encephalopathy cases showing a bovine spongiform encephalopathy molecular profile.Prions, proteinase K and infectivity.Fast and ultrasensitive method for quantitating prion infectivity titre.Mutated but Not Deleted Ovine PrP(C) N-Terminal Polybasic Region Strongly Interferes with Prion Propagation in Transgenic Mice Selective amplification of classical and atypical prions using modified protein misfolding cyclic amplification.Emergence of two prion subtypes in ovine PrP transgenic mice infected with human MM2-cortical Creutzfeldt-Jakob disease prions.

P2860

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P2860

The physical relationship between infectivity and prion protein aggregates is strain-dependent

http://www.wikidata.org/entity/Q27315010

description

2010 nî lūn-bûn

@nan

2010 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի ապրիլին հրատարակված գիտական հոդված

@hy

2010年の論文

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2010年論文

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2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

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2010年論文

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2010年论文

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name

The physical relationship betw ...... aggregates is strain-dependent

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The physical relationship betw ...... aggregates is strain-dependent

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The physical relationship betw ...... aggregates is strain-dependent

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type

label

The physical relationship betw ...... aggregates is strain-dependent

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The physical relationship betw ...... aggregates is strain-dependent

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The physical relationship betw ...... aggregates is strain-dependent

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prefLabel

The physical relationship betw ...... aggregates is strain-dependent

@ast

The physical relationship betw ...... aggregates is strain-dependent

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The physical relationship betw ...... aggregates is strain-dependent

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The physical relationship betw ...... aggregates is strain-dependent

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Annick Le Dur

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Emilie Jaumain

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Fabienne Reine

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Hubert Laude

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Jérôme Chapuis

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Laëtitia Herzog

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Philippe Tixador

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Vincent Béringue

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P2860

Prion diseases of humans and animals: their causes and molecular basis

A general model of prion strains and their pathogenicity

The state of the prion

Isolation from cattle of a prion strain distinct from that causing bovine spongiform encephalopathy

Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface

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

Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders

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

Prominent and persistent extraneural infection in human PrP transgenic mice infected with variant CJD.

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e1000859

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200465

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10.1371/JOURNAL.PPAT.1000859

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43343488

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20419156

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Prion protein family

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2855332

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