Seeding specificity and ultrastructural characteristics of infectious recombinant prions. - Wikidata - wikimedia - TriplyDB

Seeding specificity and ultrastructural characteristics of infectious recombinant prions.

Seeding specificity and ultrastructural characteristics of infectious recombinant prions.

http://www.wikidata.org/entity/Q33967156

about

Cofactor molecules maintain infectious conformation and restrict strain properties in purified prions Genesis of mammalian prions: from non-infectious amyloid fibrils to a transmissible prion disease Defining the conformational features of anchorless, poorly neuroinvasive prions Recombinant prion protein refolded with lipid and RNA has the biochemical hallmarks of a prion but lacks in vivo infectivity Role of polysaccharide and lipid in lipopolysaccharide induced prion protein conversion Parallel in-register intermolecular β-sheet architectures for prion-seeded prion protein (PrP) amyloids.Progress towards structural understanding of infectious sheep PrP-amyloid.Biology and genetics of prions causing neurodegeneration High-resolution structure of infectious prion protein: the final frontier Synthesis of high titer infectious prions with cofactor molecules.The tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease.Lower specific infectivity of protease-resistant prion protein generated in cell-free reactions.Prion subcellular fractionation reveals infectivity spectrum, with a high titre-low PrPres level disparity.A new mechanism for transmissible prion diseases Two alternative pathways for generating transmissible prion disease de novo.Isolation of novel synthetic prion strains by amplification in transgenic mice coexpressing wild-type and anchorless prion proteins.Convergent replication of mouse synthetic prion strains.Interaction of human laminin receptor with Sup35, the [PSI⁺] prion-forming protein from S. cerevisiae: a yeast model for studies of LamR interactions with amyloidogenic proteins Prion nucleation site unmasked by transient interaction with phospholipid cofactor.Treatment with a non-toxic, self-replicating anti-prion delays or prevents prion disease in vivo.Generation of a new infectious recombinant prion: a model to understand Gerstmann-Sträussler-Scheinker syndrome.Glycosaminoglycan sulfation determines the biochemical properties of prion protein aggregates.

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P2860

Seeding specificity and ultrastructural characteristics of infectious recombinant prions.

http://www.wikidata.org/entity/Q33967156

description

2011 nî lūn-bûn

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2011 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի հուլիսին հրատարակված գիտական հոդված

@hy

2011年の論文

@ja

2011年論文

@yue

2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

@wuu

name

Seeding specificity and ultrastructural characteristics of infectious recombinant prions.

@ast

Seeding specificity and ultrastructural characteristics of infectious recombinant prions.

@en

type

label

Seeding specificity and ultrastructural characteristics of infectious recombinant prions.

@ast

Seeding specificity and ultrastructural characteristics of infectious recombinant prions.

@en

prefLabel

Seeding specificity and ultrastructural characteristics of infectious recombinant prions.

@ast

Seeding specificity and ultrastructural characteristics of infectious recombinant prions.

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Seeding specificity and ultrastructural characteristics of infectious recombinant prions

@en

P2093

Daniel J Walsh

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

Fei Wang

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

Jiyan Ma

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

Judy R Rees

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

Surachai Supattapone

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

P2860

Structure of the cross-beta spine of amyloid-like fibrils

Generating a prion with bacterially expressed recombinant prion protein.

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

Amyloid of Rnq1p, the basis of the [PIN+] prion, has a parallel in-register beta-sheet structure

Formation of native prions from minimal components in vitro

Amyloid of the prion domain of Sup35p has an in-register parallel beta-sheet structure

Strain-specified relative conformational stability of the scrapie prion protein

Novel proteinaceous infectious particles cause scrapie

Protease-sensitive synthetic prions.

Mammalian prions generated from bacterially expressed prion protein in the absence of any mammalian cofactors

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7111-7116

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scholarly article

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10.1021/BI200786P

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33

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51509504

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21776987

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Prion protein family

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3319715

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