Cofactor molecules maintain infectious conformation and restrict strain properties in purified prions - Wikidata - wikimedia - TriplyDB

Cofactor molecules maintain infectious conformation and restrict strain properties in purified prions

Cofactor molecules maintain infectious conformation and restrict strain properties in purified prions

http://www.wikidata.org/entity/Q24632206

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Neurodegenerative diseases: expanding the prion concept Intraperitoneal Infection of Wild-Type Mice with Synthetically Generated Mammalian Prion Efficient uptake and dissemination of scrapie prion protein by astrocytes and fibroblasts from adult hamster brain Reversible off and on switching of prion infectivity via removing and reinstalling prion sialylation.Introducing a rigid loop structure from deer into mouse prion protein increases its propensity for misfolding in vitro Critical significance of the region between Helix 1 and 2 for efficient dominant-negative inhibition by conversion-incompetent prion protein Recombinant prion protein refolded with lipid and RNA has the biochemical hallmarks of a prion but lacks in vivo infectivity Shaking alone induces de novo conversion of recombinant prion proteins to β-sheet rich oligomers and fibrils 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.Charge neutralization of the central lysine cluster in prion protein (PrP) promotes PrP(Sc)-like folding of recombinant PrP amyloids.Lipid-dependent generation of dual topology for a membrane protein.Prion formation, but not clearance, is supported by protein misfolding cyclic amplification.Gene expression profiling of brains from bovine spongiform encephalopathy (BSE)-infected cynomolgus macaques.Synthesis of high titer infectious prions with cofactor molecules.Comparison of 2 synthetically generated recombinant prions.Lipopolysaccharide induced conversion of recombinant prion protein.The importance of prions.Infectious particles, stress, and induced prion amyloids: a unifying perspective.Quaternary structure of pathological prion protein as a determining factor of strain-specific prion replication dynamics.Epigenetic dominance of prion conformers.Interaction of prion protein with acetylcholinesterase: potential pathobiological implications in prion diseases.Titration of biologically active amyloid-β seeds in a transgenic mouse model of Alzheimer's disease.Contrasting Effects of Two Lipid Cofactors of Prion Replication on the Conformation of the Prion Protein A Structural and Functional Comparison Between Infectious and Non-Infectious Autocatalytic Recombinant PrP Conformers.Interaction between Shadoo and PrP Affects the PrP-Folding Pathway Requirements for mutant and wild-type prion protein misfolding in vitro.The Volumetric Diversity of Misfolded Prion Protein Oligomers Revealed by Pressure Dissociation.Interallelic Transcriptional Enhancement as an in Vivo Measure of Transvection in Drosophila melanogaster.Expanding the prion disease repertoire.Pre-amyloid oligomers of the proteotoxic RepA-WH1 prionoid assemble at the bacterial nucleoid W8, a new Sup35 prion strain, transmits distinctive information with a conserved assembly scheme.Stabilization of a prion strain of synthetic origin requires multiple serial passages Two alternative pathways for generating transmissible prion disease de novo.PrPSc formation and clearance as determinants of prion tropism.A systematic investigation of production of synthetic prions from recombinant prion protein Selective amplification of classical and atypical prions using modified protein misfolding cyclic amplification.Stimulating the Release of Exosomes Increases the Intercellular Transfer of Prions Prions and the potential transmissibility of protein misfolding diseases Role of Prion Replication in the Strain-dependent Brain Regional Distribution of Prions

P2860

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P2860

Cofactor molecules maintain infectious conformation and restrict strain properties in purified prions

http://www.wikidata.org/entity/Q24632206

description

2012 nî lūn-bûn

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2012 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2012 թվականի հուլիսին 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

Cofactor molecules maintain in ...... properties in purified prions

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Cofactor molecules maintain in ...... properties in purified prions

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Cofactor molecules maintain in ...... properties in purified prions

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Cofactor molecules maintain in ...... properties in purified prions

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Cofactor molecules maintain in ...... properties in purified prions

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Cofactor molecules maintain in ...... properties in purified prions

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Cofactor molecules maintain in ...... properties in purified prions

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PNAS.1206999109

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Cofactor molecules maintain in ...... properties in purified 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

Justin R Piro

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

Nathan R Deleault

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

Surachai Supattapone

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Xinhe Wang

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

P2860

Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications

Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins

Darwinian evolution of prions in cell culture

Isolation of phosphatidylethanolamine as a solitary cofactor for prion formation in the absence of nucleic acids

Generating a prion with bacterially expressed recombinant prion protein.

Prion induction involves an ancient system for the sequestration of aggregated proteins and heritable changes in prion fragmentation

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

The kinetics of formation of native ribonuclease during oxidation of the reduced polypeptide chain

Formation of native prions from minimal components in vitro

Pathogenic protein seeding in Alzheimer disease and other neurodegenerative disorders

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E1938-46

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scholarly article

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200470

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P356

10.1073/PNAS.1206999109

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P407

P433

28

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P478

109

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P577

2012-07-10T00:00:00Z

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P5875

227343703

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P698

22711839

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P921

Prion protein family

P932

3396481

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