Trans-dominant inhibition of prion propagation in vitro is not mediated by an accessory cofactor - sprookjes - yvandenbroek - TriplyDB

Trans-dominant inhibition of prion propagation in vitro is not mediated by an accessory cofactor

Trans-dominant inhibition of prion propagation in vitro is not mediated by an accessory cofactor

http://www.wikidata.org/entity/Q27316451

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Prions in variably protease-sensitive prionopathy: an update Structural basis for the protective effect of the human prion protein carrying the dominant-negative E219K polymorphism Critical significance of the region between Helix 1 and 2 for efficient dominant-negative inhibition by conversion-incompetent prion protein Human prion protein sequence elements impede cross-species chronic wasting disease transmission.A proposed mechanism for the promotion of prion conversion involving a strictly conserved tyrosine residue in the β2-α2 loop of PrPC.Molecular interactions between prions as seeds and recombinant prion proteins as substrates resemble the biological interspecies barrier in vitro Mammalian prions generated from bacterially expressed prion protein in the absence of any mammalian cofactors In vitro amplification of misfolded prion protein using lysate of cultured cells.Molecular structure of amyloid fibrils controls the relationship between fibrillar size and toxicity.Dissociation of infectivity from seeding ability in prions with alternate docking mechanism.Comparison of 2 synthetically generated recombinant prions.Identifying critical sites of PrP(c)-PrP(Sc) interaction in prion-infected cells by dominant-negative inhibition.The prion hypothesis: from biological anomaly to basic regulatory mechanism.Species-dependent differences in cofactor utilization for formation of the protease-resistant prion protein in vitro.Immunomodulation for prion and prion-related diseases.Effects of polymorphisms in ovine and caprine prion protein alleles on cell-free conversion Glycoform-selective prion formation in sporadic and familial forms of prion disease.Dominant prion mutants induce curing through pathways that promote chaperone-mediated disaggregation.Insights into prion biology: integrating a protein misfolding pathway with its cellular environment.A naturally occurring C-terminal fragment of the prion protein (PrP) delays disease and acts as a dominant-negative inhibitor of PrPSc formation.Requirements for mutant and wild-type prion protein misfolding in vitro.Interallelic Transcriptional Enhancement as an in Vivo Measure of Transvection in Drosophila melanogaster.Recombinant human prion protein inhibits prion propagation in vitro.De novo generation of infectious prions with bacterially expressed recombinant prion protein.Prion transmission prevented by modifying the β2-α2 loop structure of host PrPC Structural requirements for efficient prion protein conversion: cofactors may promote a conversion-competent structure for PrP(C).Elucidating the role of cofactors in mammalian prion propagation.Implications of prion adaptation and evolution paradigm for human neurodegenerative diseases.Insights into Mechanisms of Transmission and Pathogenesis from Transgenic Mouse Models of Prion Diseases.The roles of the conserved tyrosine in the β2-α2 loop of the prion protein.Dominant-negative effects in prion diseases: insights from molecular dynamics simulations on mouse prion protein chimeras.A dominant-negative mutant inhibits multiple prion variants through a common mechanism.An Amino Acid Substitution Found in Animals with Low Susceptibility to Prion Diseases Confers a Protective Dominant-Negative Effect in Prion-Infected Transgenic Mice.Protein Misfolding in Prion and Prion-Like Diseases: Reconsidering a Required Role for Protein Loss-of-Function.

P2860

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P2860

Trans-dominant inhibition of prion propagation in vitro is not mediated by an accessory cofactor

http://www.wikidata.org/entity/Q27316451

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2009 nî lūn-bûn

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2009 թուականի Յուլիսին հրատարակուած գիտական յօդուած

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2009 թվականի հուլիսին հրատարակված գիտական հոդված

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2009年の論文

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2009年学术文章

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2009年学术文章

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Trans-dominant inhibition of p ...... iated by an accessory cofactor

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Trans-dominant inhibition of p ...... iated by an accessory cofactor

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Trans-dominant inhibition of p ...... iated by an accessory cofactor

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Aimee H Kwak

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

Brent T Harris

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James C Geoghegan

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Michael B Miller

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Surachai Supattapone

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P2860

Selective incorporation of polyanionic molecules into hamster prions.

Formation of native prions from minimal components in vitro

NMR structure of the mouse prion protein domain PrP(121-231)

Solution structure of a 142-residue recombinant prion protein corresponding to the infectious fragment of the scrapie isoform

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

Novel proteinaceous infectious particles cause scrapie

De novo generation of a transmissible spongiform encephalopathy by mouse transgenesis

The dominant-negative effect of the Q218K variant of the prion protein does not require protein X.

Solution structure of Syrian hamster prion protein rPrP(90-231).

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e1000535

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4323608

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10.1371/JOURNAL.PPAT.1000535

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19649330

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Prion protein family

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