Modulation of prion formation, aggregation, and toxicity by the actin cytoskeleton in yeast. - Wikidata - awgldk - TriplyDB

Modulation of prion formation, aggregation, and toxicity by the actin cytoskeleton in yeast.

Modulation of prion formation, aggregation, and toxicity by the actin cytoskeleton in yeast.

http://www.wikidata.org/entity/Q42119762

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Prion induction involves an ancient system for the sequestration of aggregated proteins and heritable changes in prion fragmentation A systematic survey identifies prions and illuminates sequence features of prionogenic proteins Actin, Membrane Trafficking and the Control of Prion Induction, Propagation and Transmission in Yeast Yeast studies reveal moonlighting functions of the ancient actin cytoskeleton Potential roles for prions and protein-only inheritance in cancer Modulation and elimination of yeast prions by protein chaperones and co-chaperones Prion Aggregates Are Recruited to the Insoluble Protein Deposit (IPOD) via Myosin 2-Based Vesicular Transport Cytoplasmic dynein is required for the spatial organization of protein aggregates in filamentous fungi Curing of the [URE3] prion by Btn2p, a Batten disease-related protein.A novel single-cell screening platform reveals proteome plasticity during yeast stress responses Accelerated aging and failure to segregate damaged proteins in Sir2 mutants can be suppressed by overproducing the protein aggregation-remodeling factor Hsp104p Yeast prions are useful for studying protein chaperones and protein quality control The NatA acetyltransferase couples Sup35 prion complexes to the [PSI+] phenotype Screening for toxic amyloid in yeast exemplifies the role of alternative pathway responsible for cytotoxicity Heritable yeast prions have a highly organized three-dimensional architecture with interfiber structures.De novo [PSI +] prion formation involves multiple pathways to form infectious oligomers.A novel mutant of the Sup35 protein of Saccharomyces cerevisiae defective in translation termination and in GTPase activity still supports cell viability.The number and transmission of [PSI] prion seeds (Propagons) in the yeast Saccharomyces cerevisiae.Distinct type of transmission barrier revealed by study of multiple prion determinants of Rnq1.Yeast prions assembly and propagation: contributions of the prion and non-prion moieties and the nature of assemblies.Modeling Huntington disease in yeast: perspectives and future directions.Low density subcellular fractions enhance disease-specific prion protein misfolding.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.Prion formation and polyglutamine aggregation are controlled by two classes of genes.Sti1 regulation of Hsp70 and Hsp90 is critical for curing of Saccharomyces cerevisiae [PSI+] prions by Hsp104.In vivo evidence for the fibrillar structures of Sup35 prions in yeast cells.Distinct subregions of Swi1 manifest striking differences in prion transmission and SWI/SNF function Stress-dependent proteolytic processing of the actin assembly protein Lsb1 modulates a yeast prion Environmental regulation of prions in yeast.Protein inheritance (prions) based on parallel in-register beta-sheet amyloid structures.Prion induction by the short-lived, stress-induced protein Lsb2 is regulated by ubiquitination and association with the actin cytoskeleton.Heterologous aggregates promote de novo prion appearance via more than one mechanism.Prion species barrier between the closely related yeast proteins is detected despite coaggregation.Proteomic consequences of expression and pathological conversion of the prion protein in inducible neuroblastoma N2a cells.An intrinsically disordered yeast prion arrests the cell cycle by sequestering a spindle pole body component.Sequestration of Sup35 by aggregates of huntingtin fragments causes toxicity of [PSI+] yeast.Modulation of efficiency of translation termination in Saccharomyces cerevisiae.An insight into the complex prion-prion interaction network in the budding yeast Saccharomyces cerevisiae Prions in yeast.

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P2860

Modulation of prion formation, aggregation, and toxicity by the actin cytoskeleton in yeast.

http://www.wikidata.org/entity/Q42119762

description

2006 nî lūn-bûn

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Modulation of prion formation, ...... e actin cytoskeleton in yeast.

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Modulation of prion formation, ...... e actin cytoskeleton in yeast.

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Modulation of prion formation, ...... e actin cytoskeleton in yeast.

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Modulation of prion formation, ...... e actin cytoskeleton in yeast.

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Modulation of prion formation, ...... e actin cytoskeleton in yeast.

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Modulation of prion formation, ...... e actin cytoskeleton in yeast.

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MCB.26.2.617-629.2006

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Molecular and Cellular Biology

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Modulation of prion formation, ...... e actin cytoskeleton in yeast.

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Elena E Ganusova

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Gary P Newnam

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Laura N Ozolins

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Michael Y Sherman

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Renee D Wegrzyn

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Srishti Bhagat

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P2860

HIP1, a human homologue of S. cerevisiae Sla2p, interacts with membrane-associated huntingtin in the brain

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

A census of glutamine/asparagine-rich regions: implications for their conserved function and the prediction of novel prions

Dissection and design of yeast prions

A comprehensive analysis of protein-protein interactions in Saccharomyces cerevisiae

Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae

Sla1p is a functionally modular component of the yeast cortical actin cytoskeleton required for correct localization of both Rho1p-GTPase and Sla2p, a protein with talin homology.

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

Sla2p is associated with the yeast cortical actin cytoskeleton via redundant localization signals.

Genomic libraries and a host strain designed for highly efficient two-hybrid selection in yeast

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10.1128/MCB.26.2.617-629.2006

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2

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Yury O. Chernoff

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7389590

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16382152

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Prion protein family

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1346895

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