Biochemical properties of highly neuroinvasive prion strains - Wikidata - wikimedia - TriplyDB

Biochemical properties of highly neuroinvasive prion strains

Biochemical properties of highly neuroinvasive prion strains

http://www.wikidata.org/entity/Q28480480

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Crystal Structure of a Human Prion Protein Fragment Reveals a Motif for Oligomer Formation Relationships between PrPSc stability and incubation time for United States scrapie isolates in a natural host system Defining the conformational features of anchorless, poorly neuroinvasive prions Analysis of Conformational Stability of Abnormal Prion Protein Aggregates across the Spectrum of Creutzfeldt-Jakob Disease Prions Post-translational modifications in PrP expand the conformational diversity of prions in vivo Biochemical characterization of prion strains in bank voles Enhanced neuroinvasion by smaller, soluble prions.Assessment of strain-specific PrP(Sc) elongation rates revealed a transformation of PrP(Sc) properties during protein misfolding cyclic amplification Heterogeneity of the Abnormal Prion Protein (PrPSc) of the Chandler Scrapie Strain.Quaternary structure of pathological prion protein as a determining factor of strain-specific prion replication dynamics.Structural and kinetic analysis of protein-aggregate strains in vivo using binary epitope mapping Structural determinants of phenotypic diversity and replication rate of human prions.Structure of the β2-α2 loop and interspecies prion transmission Isolation of novel synthetic prion strains by amplification in transgenic mice coexpressing wild-type and anchorless prion proteins.Selective amplification of classical and atypical prions using modified protein misfolding cyclic amplification.Getting to the core of prion superstructural variability.Prion protein misfolding, strains, and neurotoxicity: an update from studies on Mammalian prions.Amyloid fibrils from the N-terminal prion protein fragment are infectious.Conformational stability of mammalian prion protein amyloid fibrils is dictated by a packing polymorphism within the core region.Pathogenic mutations within the hydrophobic domain of the prion protein lead to the formation of protease-sensitive prion species with increased lethality.A closer look at prion strains: characterization and important implications.Destabilizing polymorphism in cervid prion protein hydrophobic core determines prion conformation and conversion efficiency.Asparagine and glutamine ladders promote cross-species prion conversion.Species-dependent structural polymorphism of Y145Stop prion protein amyloid revealed by solid-state NMR spectroscopy.Amyloid fibril polymorphism - a challenge for molecular imaging and therapy.Generation of novel neuroinvasive prions following intravenous challenge.Pathologic and biochemical characterization of PrPSc from elk with PRNP polymorphisms at codon 132 after experimental infection with the chronic wasting disease agent.Measurement of Tau Filament Fragmentation Provides Insights into Prion-like Spreading.

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P2860

Biochemical properties of highly neuroinvasive prion strains

http://www.wikidata.org/entity/Q28480480

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2012 nî lūn-bûn

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2012 թուականի Փետրուարին հրատարակուած գիտական յօդուած

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2012 թվականի փետրվարին հրատարակված գիտական հոդված

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2012年の論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年论文

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name

Biochemical properties of highly neuroinvasive prion strains

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Biochemical properties of highly neuroinvasive prion strains

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Biochemical properties of highly neuroinvasive prion strains

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Biochemical properties of highly neuroinvasive prion strains

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Biochemical properties of highly neuroinvasive prion strains

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Biochemical properties of highly neuroinvasive prion strains

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Biochemical properties of highly neuroinvasive prion strains

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Biochemical properties of highly neuroinvasive prion strains

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Biochemical properties of highly neuroinvasive prion strains

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JOURNAL.PPAT.1002522

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Biochemical properties of highly neuroinvasive prion strains

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Christina J Sigurdson

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Cyrus Bett

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Margarita Trejo

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Melanie Lucero

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

Pawel Liberski

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Shivanjali Joshi-Barr

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P2860

Generating a prion with bacterially expressed recombinant prion protein.

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

Formation of native prions from minimal components in vitro

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

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

The amyloid-Congo red interface at atomic resolution

Impaired prion replication in spleens of mice lacking functional follicular dendritic cells

A general model of prion strains and their pathogenicity

Strain-specified relative conformational stability of the scrapie prion protein

Novel proteinaceous infectious particles cause scrapie

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e1002522

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scholarly article

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10.1371/JOURNAL.PPAT.1002522

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2

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8

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Eliezer Masliah

Jeffery W. Kelly

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2012-02-01T00:00:00Z

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221818307

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22319450

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Prion protein family

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3271082

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