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PrP polymorphisms tightly control sheep prion replication in cultured cells

PrP polymorphisms tightly control sheep prion replication in cultured cells

http://www.wikidata.org/entity/Q34471219

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Selection of ovine housekeeping genes for normalisation by real-time RT-PCR; analysis of PrP gene expression and genetic susceptibility to scrapie Cellular aspects of prion replication in vitro Insight into the PrPC-->PrPSc conversion from the structures of antibody-bound ovine prion scrapie-susceptibility variants Prion protein self-peptides modulate prion interactions and conversion.Mapping of possible prion protein self-interaction domains using peptide arrays Conversion efficiency of bank vole prion protein in vitro is determined by residues 155 and 170, but does not correlate with the high susceptibility of bank voles to sheep scrapie in vivo.Inhibition of protease-resistant prion protein formation in a transformed deer cell line infected with chronic wasting disease Prion infection of epithelial Rov cells is a polarized event.Microsecond unfolding kinetics of sheep prion protein reveals an intermediate that correlates with susceptibility to classical scrapie.PrPc does not mediate internalization of PrPSc but is required at an early stage for de novo prion infection of Rov cells.Human tonsil-derived follicular dendritic-like cells are refractory to human prion infection in vitro and traffic disease-associated prion protein to lysosomes.In vitro studies of the transmission barrier.Prion protein self-interaction in prion disease therapy approaches.The standard scrapie cell assay: development, utility and prospects.Generation of Infectious Prions and Detection with the Prion-Infected Cell Assay.Mechanisms of prion-induced neurodegeneration.Glycan-controlled epitopes of prion protein include a major determinant of susceptibility to sheep scrapie.Scrapie infection of prion protein-deficient cell line upon ectopic expression of mutant prion proteins.PrPSc binding antibodies are potent inhibitors of prion replication in cell lines.Dominant-negative effects in prion diseases: insights from molecular dynamics simulations on mouse prion protein chimeras.

P2860

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P2860

PrP polymorphisms tightly control sheep prion replication in cultured cells

http://www.wikidata.org/entity/Q34471219

description

2003 nî lūn-bûn

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2003 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2003 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

2003年の論文

@ja

2003年論文

@yue

2003年論文

@zh-hant

2003年論文

@zh-hk

2003年論文

@zh-mo

2003年論文

@zh-tw

2003年论文

@wuu

name

PrP polymorphisms tightly control sheep prion replication in cultured cells

@ast

PrP polymorphisms tightly control sheep prion replication in cultured cells

@en

PrP polymorphisms tightly control sheep prion replication in cultured cells

@nl

type

label

PrP polymorphisms tightly control sheep prion replication in cultured cells

@ast

PrP polymorphisms tightly control sheep prion replication in cultured cells

@en

PrP polymorphisms tightly control sheep prion replication in cultured cells

@nl

prefLabel

PrP polymorphisms tightly control sheep prion replication in cultured cells

@ast

PrP polymorphisms tightly control sheep prion replication in cultured cells

@en

PrP polymorphisms tightly control sheep prion replication in cultured cells

@nl

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JVI.77.4.2696-2700.2003

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Journal of Virology

P1476

PrP polymorphisms tightly control sheep prion replication in cultured cells

@en

P2093

Annick Le Dur

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

Didier Vilette

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

Hubert Laude

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

Jean-Luc Vilotte

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

Stéphanie Petit

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

Thanh Lan Lai

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

P2860

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

High yield purification and physico-chemical properties of full-length recombinant allelic variants of sheep prion protein linked to scrapie susceptibility.

Cellular biology of prion diseases.

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

Scrapie prion protein accumulation by scrapie-infected neuroblastoma cells abrogated by exposure to a prion protein antibody.

Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein.

Ex vivo propagation of infectious sheep scrapie agent in heterologous epithelial cells expressing ovine prion protein

A hypothalamic neuronal cell line persistently infected with scrapie prions exhibits apoptosis.

Ectopic expression of prion protein (PrP) in T lymphocytes or hepatocytes of PrP knockout mice is insufficient to sustain prion replication.

Scrapie susceptibility-linked polymorphisms modulate the in vitro conversion of sheep prion protein to protease-resistant forms.

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2696-2700

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scholarly article

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10.1128/JVI.77.4.2696-2700.2003

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Prion protein family

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