Huntington toxicity in yeast model depends on polyglutamine aggregation mediated by a prion-like protein Rnq1 - Wikidata - awgldk - TriplyDB

Huntington toxicity in yeast model depends on polyglutamine aggregation mediated by a prion-like protein Rnq1

Huntington toxicity in yeast model depends on polyglutamine aggregation mediated by a prion-like protein Rnq1

http://www.wikidata.org/entity/Q36325681

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Amyloid-mediated sequestration of essential proteins contributes to mutant huntingtin toxicity in yeast Appearance and propagation of polyglutamine-based amyloids in yeast: tyrosine residues enable polymer fragmentation Amyloid of Rnq1p, the basis of the [PIN+] prion, has a parallel in-register beta-sheet structure Dissection and design of yeast prions Yeast prions: protein aggregation is not enough Cell-autonomous death of cerebellar purkinje neurons with autophagy in Niemann-Pick type C disease The stress response against denatured proteins in the deletion of cytosolic chaperones SSA1/2 is different from heat-shock response in Saccharomyces cerevisiae Model systems of protein-misfolding diseases reveal chaperone modifiers of proteotoxicity Disaggregases, molecular chaperones that resolubilize protein aggregates The [RNQ+] prion: a model of both functional and pathological amyloid Probing the role of structural features of mouse PrP in yeast by expression as Sup35-PrP fusions Curing of the [URE3] prion by Btn2p, a Batten disease-related protein.The Hsp70/90 cochaperone, Sti1, suppresses proteotoxicity by regulating spatial quality control of amyloid-like proteins.A genomic screen in yeast implicates kynurenine 3-monooxygenase as a therapeutic target for Huntington disease.Engineering enhanced protein disaggregases for neurodegenerative disease Off-target effects of psychoactive drugs revealed by genome-wide assays in yeast Screening for toxic amyloid in yeast exemplifies the role of alternative pathway responsible for cytotoxicity Aggregation of polyQ proteins is increased upon yeast aging and affected by Sir2 and Hsf1: novel quantitative biochemical and microscopic assays Aggregation of human S100A8 and S100A9 amyloidogenic proteins perturbs proteostasis in a yeast model RuvbL1 and RuvbL2 enhance aggresome formation and disaggregate amyloid fibrils.Assessment of human Nter and Cter BRCA1 mutations using growth and localization assays in yeast.Ubiquitin conjugation triggers misfolded protein sequestration into quality control foci when Hsp70 chaperone levels are limiting.Spatial sequestration of misfolded proteins by a dynamic chaperone pathway enhances cellular fitness during stress.Distinct type of transmission barrier revealed by study of multiple prion determinants of Rnq1.Pathogenic polyglutamine tracts are potent inducers of spontaneous Sup35 and Rnq1 amyloidogenesis.Probing the metabolic aberrations underlying mutant huntingtin toxicity in yeast and assessing their degree of preservation in humans and mice.Modeling Huntington disease in yeast: perspectives and future directions.Potent inhibition of huntingtin aggregation and cytotoxicity by a disulfide bond-free single-domain intracellular antibody.Polyglutamine-rich suppressors of huntingtin toxicity act upstream of Hsp70 and Sti1 in spatial quality control of amyloid-like proteins.A potent small molecule inhibits polyglutamine aggregation in Huntington's disease neurons and suppresses neurodegeneration in vivo.Use of yeast as a system to study amyloid toxicity 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.Hsc70 rapidly engages tau after microtubule destabilization Prion formation and polyglutamine aggregation are controlled by two classes of genes.An aggregation sensing reporter identifies leflunomide and teriflunomide as polyglutamine aggregate inhibitors.Prion-promoted phosphorylation of heterologous amyloid is coupled with ubiquitin-proteasome system inhibition and toxicity.Polyglutamine toxicity is controlled by prion composition and gene dosage in yeast.Identification of PrP sequences essential for the interaction between the PrP polymers and Aβ peptide in a yeast-based assay Defining the limits: Protein aggregation and toxicity in vivo

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P2860

Huntington toxicity in yeast model depends on polyglutamine aggregation mediated by a prion-like protein Rnq1

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Huntington toxicity in yeast m ...... d by a prion-like protein Rnq1

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Anatoli B Meriin

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Gary P Newnam

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Michael Y Sherman

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Xiangwei He

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Xiaoqian Zhang

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Yury O Chernoff

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P2860

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

Functional characterization of the S. cerevisiae genome by gene deletion and parallel analysis

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

Shattuck lecture--neurodegenerative diseases and prions

Mutation processes at the protein level: is Lamarck back?

Formation of neuronal intranuclear inclusions underlies the neurological dysfunction in mice transgenic for the HD mutation

Aggresomes: a cellular response to misfolded proteins

Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain

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

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6

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157

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11316166

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12058016

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Huntington disease

Prion protein family

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2174031

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