Variant-specific [PSI+] infection is transmitted by Sup35 polymers within [PSI+] aggregates with heterogeneous protein composition - Wikidata - wikimedia - TriplyDB

Variant-specific [PSI+] infection is transmitted by Sup35 polymers within [PSI+] aggregates with heterogeneous protein composition

Variant-specific [PSI+] infection is transmitted by Sup35 polymers within [PSI+] aggregates with heterogeneous protein composition

http://www.wikidata.org/entity/Q36678054

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Amyloid-mediated sequestration of essential proteins contributes to mutant huntingtin toxicity in yeast Modulation and elimination of yeast prions by protein chaperones and co-chaperones Amyloid cannot resist identification Differences in the curing of [PSI+] prion by various methods of Hsp104 inactivation Prion Aggregates Are Recruited to the Insoluble Protein Deposit (IPOD) via Myosin 2-Based Vesicular Transport Molecular chaperones and stress-inducible protein-sorting factors coordinate the spatiotemporal distribution of protein aggregates.Hsp104, Hsp70 and Hsp40 interplay regulates formation, growth and elimination of Sup35 prions.The Hsp70 homolog Ssb is essential for glucose sensing via the SNF1 kinase network Yeast prions are useful for studying protein chaperones and protein quality control Amyloid-associated activity contributes to the severity and toxicity of a prion phenotype Heterologous cross-seeding mimics cross-species prion conversion in a yeast model.Sensitivity-enhanced NMR reveals alterations in protein structure by cellular milieus GPI anchoring facilitates propagation and spread of misfolded Sup35 aggregates in mammalian cells.Heritable yeast prions have a highly organized three-dimensional architecture with interfiber structures.Disease-associated mutant ubiquitin causes proteasomal impairment and enhances the toxicity of protein aggregates.Prion dynamics and the quest for the genetic determinant in protein-only inheritance Overexpression of the essential Sis1 chaperone reduces TDP-43 effects on toxicity and proteolysis.Interdependence of amyloid formation in yeast: implications for polyglutamine disorders and biological functions.Analyzing the birth and propagation of two distinct prions, [PSI+] and [Het-s](y), in yeast.[SWI], the prion formed by the chromatin remodeling factor Swi1, is highly sensitive to alterations in Hsp70 chaperone system activity.In vivo monitoring of the prion replication cycle reveals a critical role for Sis1 in delivering substrates to Hsp104 The effect of red pigment on the amyloidization of yeast proteins.Prion formation and polyglutamine aggregation are controlled by two classes of genes.In vivo evidence for the fibrillar structures of Sup35 prions in yeast cells.Prion-promoted phosphorylation of heterologous amyloid is coupled with ubiquitin-proteasome system inhibition and toxicity.Small heat shock proteins potentiate amyloid dissolution by protein disaggregases from yeast and humans Hsp40s specify functions of Hsp104 and Hsp90 protein chaperone machines.Defining the limits: Protein aggregation and toxicity in vivo Heterologous gln/asn-rich proteins impede the propagation of yeast prions by altering chaperone availability Trans-species activity of a nonself recognition domain.Spatial quality control bypasses cell-based limitations on proteostasis to promote prion curing.Suicidal [PSI+] is a lethal yeast prion.Dominant prion mutants induce curing through pathways that promote chaperone-mediated disaggregation.Destabilization and recovery of a yeast prion after mild heat shock.Functional diversification of hsp40: distinct j-protein functional requirements for two prions allow for chaperone-dependent prion selection Heterologous aggregates promote de novo prion appearance via more than one mechanism.Prion aggregate structure in yeast cells is determined by the Hsp104-Hsp110 disaggregase machinery.Prions in yeast.Prion-Associated Toxicity is Rescued by Elimination of Cotranslational Chaperones.Study of amyloids using yeast

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Variant-specific [PSI+] infection is transmitted by Sup35 polymers within [PSI+] aggregates with heterogeneous protein composition

http://www.wikidata.org/entity/Q36678054

description

2008 nî lūn-bûn

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2008年の論文

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2008年論文

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2008年论文

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2008年论文

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2008年论文

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name

Variant-specific [PSI+] infect ...... erogeneous protein composition

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Variant-specific [PSI+] infect ...... erogeneous protein composition

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Variant-specific [PSI+] infect ...... erogeneous protein composition

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Variant-specific [PSI+] infect ...... erogeneous protein composition

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MBC.E08-01-0078

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Molecular Biology of the Cell

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Variant-specific [PSI+] infect ...... erogeneous protein composition

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Janet E Richmond

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Susan W Liebman

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P2860

Eukaryotic release factors (eRFs) history

Genetic and environmental factors affecting the de novo appearance of the [PSI+] prion in Saccharomyces cerevisiae

Propagation of the yeast prion-like [psi+] determinant is mediated by oligomerization of the SUP35-encoded polypeptide chain release factor

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

Mechanism of prion propagation: amyloid growth occurs by monomer addition

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

Global analysis of protein expression in yeast

Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins.

Increased expression of Hsp40 chaperones, transcriptional factors, and ribosomal protein Rpp0 can cure yeast prions.

Prions affect the appearance of other prions: the story of [PIN(+)].

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2433-2443

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scholarly article

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10.1091/MBC.E08-01-0078

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6

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19

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Sviatoslav N Bagriantsev

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2008-03-19T00:00:00Z

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5498431

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18353968

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2397312

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