Increased expression of Hsp40 chaperones, transcriptional factors, and ribosomal protein Rpp0 can cure yeast prions.
about
Nucleophosmin interacts with and inhibits the catalytic function of eukaryotic initiation factor 2 kinase PKRStress granule assembly is mediated by prion-like aggregation of TIA-1Metabolic and chaperone gene loss marks the origin of animals: evidence for Hsp104 and Hsp78 chaperones sharing mitochondrial enzymes as clientsHsp104-dependent remodeling of prion complexes mediates protein-only inheritanceCuring of the [URE3] prion by Btn2p, a Batten disease-related protein.Hsp104, Hsp70 and Hsp40 interplay regulates formation, growth and elimination of Sup35 prions.The Hsp70/90 cochaperone, Sti1, suppresses proteotoxicity by regulating spatial quality control of amyloid-like proteins.Prion-impairing mutations in Hsp70 chaperone Ssa1: effects on ATPase and chaperone activities.The J-protein family: modulating protein assembly, disassembly and translocation.Dissection of Swa2p/auxilin domain requirements for cochaperoning Hsp70 clathrin-uncoating activity in vivo.The NatA acetyltransferase couples Sup35 prion complexes to the [PSI+] phenotype[SWI], the prion formed by the chromatin remodeling factor Swi1, is highly sensitive to alterations in Hsp70 chaperone system activity.Hsp70 chaperones as modulators of prion life cycle: novel effects of Ssa and Ssb on the Saccharomyces cerevisiae prion [PSI+]Saccharomyces cerevisiae Hsp70 mutations affect [PSI+] prion propagation and cell growth differently and implicate Hsp40 and tetratricopeptide repeat cochaperones in impairment of [PSI+]Protein inheritance (prions) based on parallel in-register beta-sheet amyloid structures.Molecular chaperone Hsp104 can promote yeast prion generationPropagation of yeast prions.Importance of the Hsp70 ATPase domain in yeast prion propagationLocalization of HET-S to the cell periphery, not to [Het-s] aggregates, is associated with [Het-s]-HET-S toxicity.Nucleotide exchange factors for Hsp70s are required for [URE3] prion propagation in Saccharomyces cerevisiae.Diversify or die: generation of diversity in response to stress.Variant-specific [PSI+] infection is transmitted by Sup35 polymers within [PSI+] aggregates with heterogeneous protein compositionFunctionally redundant isoforms of a yeast Hsp70 chaperone subfamily have different antiprion effects.The yeast Sup35NM domain propagates as a prion in mammalian cells.Chaperone effects on prion and nonprion aggregates.Prion propagation by Hsp40 molecular chaperones.Influence of Hsp70s and their regulators on yeast prion propagationHsp70 structure, function, regulation and influence on yeast prions.Prion proteostasis: Hsp104 meets its supporting castPropagation of Saccharomyces cerevisiae [PSI+] prion is impaired by factors that regulate Hsp70 substrate bindingYeast and Fungal Prions.A cytosolic network suppressing mitochondria-mediated proteostatic stress and cell deathCOPII machinery cooperates with ER-localized Hsp40 to sequester misfolded membrane proteins into ER-associated compartmentsRegulation of the Hsp104 middle domain activity is critical for yeast prion propagation.A novel high-throughput screen reveals yeast genes that increase secretion of heterologous proteinsThe β6/β7 region of the Hsp70 substrate-binding domain mediates heat-shock response and prion propagation.Multiplication of Ribosomal P-Stalk Proteins Contributes to the Fidelity of Translation.Variant-specific and reciprocal Hsp40 functions in Hsp104-mediated prion elimination.[PIN+]ing down the mechanism of prion appearance.A brief overview of the Swi1 prion-[SWI+]
P2860
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P2860
Increased expression of Hsp40 chaperones, transcriptional factors, and ribosomal protein Rpp0 can cure yeast prions.
description
2002 nî lūn-bûn
@nan
2002 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
Increased expression of Hsp40 ...... in Rpp0 can cure yeast prions.
@ast
Increased expression of Hsp40 ...... in Rpp0 can cure yeast prions.
@en
Increased expression of Hsp40 ...... in Rpp0 can cure yeast prions.
@nl
type
label
Increased expression of Hsp40 ...... in Rpp0 can cure yeast prions.
@ast
Increased expression of Hsp40 ...... in Rpp0 can cure yeast prions.
@en
Increased expression of Hsp40 ...... in Rpp0 can cure yeast prions.
@nl
prefLabel
Increased expression of Hsp40 ...... in Rpp0 can cure yeast prions.
@ast
Increased expression of Hsp40 ...... in Rpp0 can cure yeast prions.
@en
Increased expression of Hsp40 ...... in Rpp0 can cure yeast prions.
@nl
P2093
P2860
P356
P1476
Increased expression of Hsp40 ...... in Rpp0 can cure yeast prions.
@en
P2093
Dmitry S Kryndushkin
Michael D Ter-Avanesyan
Vitaly V Kushnirov
Vladimir N Smirnov
P2860
P304
P356
10.1074/JBC.M111547200
P407
P577
2002-06-28T00:00:00Z