In vivo evidence for the fibrillar structures of Sup35 prions in yeast cells. - Wikidata - thesis-toulmin - TriplyDB

In vivo evidence for the fibrillar structures of Sup35 prions in yeast cells.

In vivo evidence for the fibrillar structures of Sup35 prions in yeast cells.

http://www.wikidata.org/entity/Q34092434

about

Prion Aggregates Are Recruited to the Insoluble Protein Deposit (IPOD) via Myosin 2-Based Vesicular Transport Single-molecule analyses of the dynamics of heat shock protein 104 (Hsp104) and protein aggregates.Heritable yeast prions have a highly organized three-dimensional architecture with interfiber structures.Glycosylphosphatidylinositol anchoring directs the assembly of Sup35NM protein into non-fibrillar, membrane-bound aggregates Yeast prions assembly and propagation: contributions of the prion and non-prion moieties and the nature of assemblies.Use of yeast as a system to study amyloid toxicity Investigating the interactions of yeast prions: [SWI+], [PSI+], and [PIN+].[SWI], the prion formed by the chromatin remodeling factor Swi1, is highly sensitive to alterations in Hsp70 chaperone system activity.Opposing effects of glutamine and asparagine govern prion formation by intrinsically disordered proteins.Analytical model for macromolecular partitioning during yeast cell division Prion aggregate structure in yeast cells is determined by the Hsp104-Hsp110 disaggregase machinery.Prions in yeast.Study of amyloids using yeast Patterns of [PSI (+) ] aggregation allow insights into cellular organization of yeast prion aggregates.Self-propagating amyloid as a critical regulator for diverse cellular functions.Live correlative light-electron microscopy to observe molecular dynamics in high resolution.Analysis of [SWI+ ] formation and propagation events.Electron microscopy for ultrastructural analysis and protein localization in Saccharomyces cerevisiae.The self-interaction of native TDP-43 C terminus inhibits its degradation and contributes to early proteinopathies.Oxidative stress conditions increase the frequency of de novo formation of the yeast [PSI+] prion.A protein polymerization cascade mediates toxicity of non-pathological human huntingtin in yeast.Mapping the Broad Structural and Mechanical Properties of Amyloid Fibrils.Peptide sequences converting polyglutamine into a prion in yeast.A bipolar functionality of Q/N-rich proteins: Lsm4 amyloid causes clearance of yeast prions.Heterogeneous interaction network of yeast prions and remodeling factors detected in live cells.Direct assessment in bacteria of prionoid propagation and phenotype selection by Hsp70 chaperone.[PSI(+)] aggregate enlargement in rnq1 nonprion domain mutants, leading to a loss of prion in yeast.Molecular and structural architecture of polyQ aggregates in yeast.A Liquid to Solid Phase Transition Underlying Pathological Huntingtin Exon1 Aggregation.

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P2860

In vivo evidence for the fibrillar structures of Sup35 prions in yeast cells.

http://www.wikidata.org/entity/Q34092434

description

2010 nî lūn-bûn

@nan

2010 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի հուլիսին հրատարակված գիտական հոդված

@hy

2010年の論文

@ja

2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

name

In vivo evidence for the fibrillar structures of Sup35 prions in yeast cells.

@ast

In vivo evidence for the fibrillar structures of Sup35 prions in yeast cells.

@en

In vivo evidence for the fibrillar structures of Sup35 prions in yeast cells.

@nl

type

label

In vivo evidence for the fibrillar structures of Sup35 prions in yeast cells.

@ast

In vivo evidence for the fibrillar structures of Sup35 prions in yeast cells.

@en

In vivo evidence for the fibrillar structures of Sup35 prions in yeast cells.

@nl

prefLabel

In vivo evidence for the fibrillar structures of Sup35 prions in yeast cells.

@ast

In vivo evidence for the fibrillar structures of Sup35 prions in yeast cells.

@en

In vivo evidence for the fibrillar structures of Sup35 prions in yeast cells.

@nl

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P356

P1433

Journal of Cell Biology

P1476

In vivo evidence for the fibrillar structures of Sup35 prions in yeast cells.

@en

P2093

Aiko Hirata

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

Chan-Gi Pack

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

Shigeko Kawai-Noma

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

Tokuko Haraguchi

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

Tomoko Kojidani

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

P2860

The use of lead citrate at high pH as an electron-opaque stain in electron microscopy

Protein misfolding, functional amyloid, and human disease

Live cell imaging and electron microscopy reveal dynamic processes of BAF-directed nuclear envelope assembly

Getting started with yeast

Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+]

Self-seeded fibers formed by Sup35, the protein determinant of [PSI+], a heritable prion-like factor of S. cerevisiae.

Studying protein dynamics in living cells.

The relationship between visible intracellular aggregates that appear after overexpression of Sup35 and the yeast prion-like elements [PSI(+)] and [PIN(+)].

Role for Hsp70 chaperone in Saccharomyces cerevisiae prion seed replication.

Yeast [PSI+] prion aggregates are formed by small Sup35 polymers fragmented by Hsp104.

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223-231

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scholarly article

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10.1083/JCB.201002149

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P433

2

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P478

190

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Yasushi Hiraoka

Haruhiko Asakawa

P577

2010-07-19T00:00:00Z

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45275047

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20643880

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P921

Prion protein family

P932

2930275

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