Prion generation in vitro: amyloid of Ure2p is infectious. - Wikidata - wikimedia - TriplyDB

Prion generation in vitro: amyloid of Ure2p is infectious.

Prion generation in vitro: amyloid of Ure2p is infectious.

http://www.wikidata.org/entity/Q33947121

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Prions, protein homeostasis, and phenotypic diversity Amyloids: friend or foe?A heritable switch in carbon source utilization driven by an unusual yeast prion A systematic survey identifies prions and illuminates sequence features of prionogenic proteins More than just trash bins? Potential roles for extracellular vesicles in the vertical and horizontal transmission of yeast prions Potential roles for prions and protein-only inheritance in cancer Modulation and elimination of yeast prions by protein chaperones and co-chaperones Yeast prions: structure, biology, and prion-handling systems Hsp104-dependent remodeling of prion complexes mediates protein-only inheritance Curing of the [URE3] prion by Btn2p, a Batten disease-related protein.Btn3 is a negative regulator of Btn2-mediated endosomal protein trafficking and prion curing in yeast.A yeast prion, Mod5, promotes acquired drug resistance and cell survival under environmental stress Protein folding activity of ribosomal RNA is a selective target of two unrelated antiprion drugs Screening for toxic amyloid in yeast exemplifies the role of alternative pathway responsible for cytotoxicity Prion amyloid structure explains templating: how proteins can be genes.Function of SSA subfamily of Hsp70 within and across species varies widely in complementing Saccharomyces cerevisiae cell growth and prion propagation.Distinct type of transmission barrier revealed by study of multiple prion determinants of Rnq1.Structure and assembly properties of the N-terminal domain of the prion Ure2p in isolation and in its natural context Yeast prions assembly and propagation: contributions of the prion and non-prion moieties and the nature of assemblies.Influence of prion variant and yeast strain variation on prion-molecular chaperone requirements Amyloid structure and assembly: insights from scanning transmission electron microscopy.Prion dynamics and the quest for the genetic determinant in protein-only inheritance Investigating the interactions of yeast prions: [SWI+], [PSI+], and [PIN+].Analyzing the birth and propagation of two distinct prions, [PSI+] and [Het-s](y), in yeast.Normal levels of the antiprion proteins Btn2 and Cur1 cure most newly formed [URE3] prion variants The core of Ure2p prion fibrils is formed by the N-terminal segment in a parallel cross-β structure: evidence from solid-state NMR.Beta arcades: recurring motifs in naturally occurring and disease-related amyloid fibrils Dissociation of infectivity from seeding ability in prions with alternate docking mechanism.Polymorphism in Alzheimer Abeta amyloid organization reflects conformational selection in a rugged energy landscape.Distinct subregions of Swi1 manifest striking differences in prion transmission and SWI/SNF function The tip of the iceberg: RNA-binding proteins with prion-like domains in neurodegenerative disease.Sporadic distribution of prion-forming ability of Sup35p from yeasts and fungi.Hsp40s specify functions of Hsp104 and Hsp90 protein chaperone machines.Prions.Locating folds of the in-register parallel β-sheet of the Sup35p prion domain infectious amyloid.Molecular pathology of human prion disease.Heterologous gln/asn-rich proteins impede the propagation of yeast prions by altering chaperone availability Structural dependence of HET-s amyloid fibril infectivity assessed by cryoelectron microscopy Suicidal [PSI+] is a lethal yeast prion.Protein inheritance (prions) based on parallel in-register beta-sheet amyloid structures.

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P2860

Prion generation in vitro: amyloid of Ure2p is infectious.

http://www.wikidata.org/entity/Q33947121

description

2005 nî lūn-bûn

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2005 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

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2005 թվականի օգոստոսին հրատարակված գիտական հոդված

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2005年の論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年论文

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name

Prion generation in vitro: amyloid of Ure2p is infectious.

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Prion generation in vitro: amyloid of Ure2p is infectious.

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Prion generation in vitro: amyloid of Ure2p is infectious.

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Prion generation in vitro: amyloid of Ure2p is infectious.

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Prion generation in vitro: amyloid of Ure2p is infectious.

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Prion generation in vitro: amyloid of Ure2p is infectious.

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SJ.EMBOJ.7600772

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The EMBO Journal

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Prion generation in vitro: amyloid of Ure2p is infectious.

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P2093

Andreas Brachmann

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

Reed Brendon Wickner

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Ulrich Baxa

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P2860

Amyloid aggregates of the HET-s prion protein are infectious.

Non-Mendelian mutation allowing ureidosuccinic acid uptake in yeast

The protein product of the het-s heterokaryon incompatibility gene of the fungus Podospora anserina behaves as a prion analog

Global analysis of protein expression in yeast

[URE3] as an altered URE2 protein: evidence for a prion analog in Saccharomyces cerevisiae

A structural model for Alzheimer's beta -amyloid fibrils based on experimental constraints from solid state NMR

Novel proteinaceous infectious particles cause scrapie

Self-propagating, molecular-level polymorphism in Alzheimer's beta-amyloid fibrils

Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders

Structural characterization of the fibrillar form of the yeast Saccharomyces cerevisiae prion Ure2p.

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