Hsp104, Hsp70 and Hsp40 interplay regulates formation, growth and elimination of Sup35 prions.
about
Prion switching in response to environmental stressPrions, protein homeostasis, and phenotypic diversityThe Brichos domain of prosurfactant protein C can hold and fold a transmembrane segmentA systematic survey identifies prions and illuminates sequence features of prionogenic proteinsEngineering and Evolution of Molecular Chaperones and Protein Disaggregases with Enhanced ActivityPrion-like domains as epigenetic regulators, scaffolds for subcellular organization, and drivers of neurodegenerative diseaseMolecular chaperones: guardians of the proteome in normal and disease statesYeast prions and human prion-like proteins: sequence features and prediction methodsRebels with a cause: molecular features and physiological consequences of yeast prionsEngineering enhanced protein disaggregases for neurodegenerative diseaseThe proteome response to amyloid protein expression in vivoAggregation of human S100A8 and S100A9 amyloidogenic proteins perturbs proteostasis in a yeast modelQualitative and quantitative multiplexed proteomic analysis of complex yeast protein fractions that modulate the assembly of the yeast prion Sup35pGPI 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.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.The Schizosaccharomyces pombe Hsp104 disaggregase is unable to propagate the [PSI] prion.Transgenerational epigenetic inheritance: how important is it?In vivo monitoring of the prion replication cycle reveals a critical role for Sis1 in delivering substrates to Hsp104Sti1 regulation of Hsp70 and Hsp90 is critical for curing of Saccharomyces cerevisiae [PSI+] prions by Hsp104.The mammalian disaggregase machinery: Hsp110 synergizes with Hsp70 and Hsp40 to catalyze protein disaggregation and reactivation in a cell-free systemPrion propagation can occur in a prokaryote and requires the ClpB chaperone.Potentiated Hsp104 variants suppress toxicity of diverse neurodegenerative disease-linked proteins.Small heat shock proteins potentiate amyloid dissolution by protein disaggregases from yeast and humansStable alpha-synuclein oligomers strongly inhibit chaperone activity of the Hsp70 system by weak interactions with J-domain co-chaperonesPrions.Meta-analysis of heat- and chemically upregulated chaperone genes in plant and human cells.The Type II Hsp40 Sis1 cooperates with Hsp70 and the E3 ligase Ubr1 to promote degradation of terminally misfolded cytosolic protein.Spatial quality control bypasses cell-based limitations on proteostasis to promote prion curing.Hsp104 suppresses polyglutamine-induced degeneration post onset in a drosophila MJD/SCA3 model.Molecular chaperone Hsp104 can promote yeast prion generationSingle particle fluorescence burst analysis of epsin induced membrane fission.Hsp70 clears misfolded kinases that partitioned into distinct quality-control compartments.Insight into molecular basis of curing of [PSI+] prion by overexpression of 104-kDa heat shock protein (Hsp104).Hsp90-Associated Immunophilin Homolog Cpr7 Is Required for the Mitotic Stability of [URE3] Prion in Saccharomyces cerevisiae.Suppression of protein aggregation by chaperone modification of high molecular weight complexesChaperones divide yeast proteins into classes of expression level and evolutionary rateThe ribosome-associated complex antagonizes prion formation in yeast.Prion-Associated Toxicity is Rescued by Elimination of Cotranslational Chaperones.
P2860
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P2860
Hsp104, Hsp70 and Hsp40 interplay regulates formation, growth and elimination of Sup35 prions.
description
2008 nî lūn-bûn
@nan
2008 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
Hsp104, Hsp70 and Hsp40 interp ...... d elimination of Sup35 prions.
@ast
Hsp104, Hsp70 and Hsp40 interp ...... d elimination of Sup35 prions.
@en
Hsp104, Hsp70 and Hsp40 interp ...... d elimination of Sup35 prions.
@nl
type
label
Hsp104, Hsp70 and Hsp40 interp ...... d elimination of Sup35 prions.
@ast
Hsp104, Hsp70 and Hsp40 interp ...... d elimination of Sup35 prions.
@en
Hsp104, Hsp70 and Hsp40 interp ...... d elimination of Sup35 prions.
@nl
altLabel
Hsp104, Hsp70 and Hsp40 interp ...... nd elimination of Sup35 prions
@en
prefLabel
Hsp104, Hsp70 and Hsp40 interp ...... d elimination of Sup35 prions.
@ast
Hsp104, Hsp70 and Hsp40 interp ...... d elimination of Sup35 prions.
@en
Hsp104, Hsp70 and Hsp40 interp ...... d elimination of Sup35 prions.
@nl
P2860
P3181
P356
P1433
P1476
Hsp104, Hsp70 and Hsp40 interp ...... d elimination of Sup35 prions.
@en
P2860
P304
P3181
P356
10.1038/EMBOJ.2008.194
P407
P577
2008-10-22T00:00:00Z