A role for cytosolic hsp70 in yeast [PSI(+)] prion propagation and [PSI(+)] as a cellular stress.
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Yeast prions [URE3] and [PSI+] are diseasesInterplay between GCN2 and GCN4 expression, translation elongation factor 1 mutations and translational fidelity in yeast.The yeast prions [PSI+] and [URE3] are molecular degenerative diseasesModulation and elimination of yeast prions by protein chaperones and co-chaperonesYeast prions: structure, biology, and prion-handling systemsDifferences in the curing of [PSI+] prion by various methods of Hsp104 inactivationHsp104-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.Prion-impairing mutations in Hsp70 chaperone Ssa1: effects on ATPase and chaperone activities.Dissection of Swa2p/auxilin domain requirements for cochaperoning Hsp70 clathrin-uncoating activity in vivo.Yeast prions are useful for studying protein chaperones and protein quality controlThe NatA acetyltransferase couples Sup35 prion complexes to the [PSI+] phenotypeCooperative kinetics of both Hsp104 ATPase domains and interdomain communication revealed by AAA sensor-1 mutants.Using steered molecular dynamics to predict and assess Hsp70 substrate-binding domain mutants that alter prion propagationOsmostress-induced cell volume loss delays yeast Hog1 signaling by limiting diffusion processes and by Hog1-specific effectsHsp110 chaperones regulate prion formation and propagation in S. cerevisiae by two discrete activities.Function of SSA subfamily of Hsp70 within and across species varies widely in complementing Saccharomyces cerevisiae cell growth and prion propagation.Global transcript and phenotypic analysis of yeast cells expressing Ssa1, Ssa2, Ssa3 or Ssa4 as sole source of cytosolic Hsp70-Ssa chaperone activity[SWI], the prion formed by the chromatin remodeling factor Swi1, is highly sensitive to alterations in Hsp70 chaperone system activity.Role for Hsp70 chaperone in Saccharomyces cerevisiae prion seed replication.Curing of yeast [PSI+] prion by guanidine inactivation of Hsp104 does not require cell division.Sti1 regulation of Hsp70 and Hsp90 is critical for curing of Saccharomyces cerevisiae [PSI+] prions by Hsp104.[URE3] prion propagation in Saccharomyces cerevisiae: requirement for chaperone Hsp104 and curing by overexpressed chaperone Ydj1p.Viruses and prions of Saccharomyces cerevisiaeAmino acid residue 184 of yeast Hsp104 chaperone is critical for prion-curing by guanidine, prion propagation, and thermotoleranceAssessment of inactivating stop codon mutations in forty Saccharomyces cerevisiae strains: implications for [PSI] prion- mediated phenotypes.Antagonistic interactions between yeast [PSI(+)] and [URE3] prions and curing of [URE3] by Hsp70 protein chaperone Ssa1p but not by Ssa2p.Independent regulation of Hsp70 and Hsp90 chaperones by Hsp70/Hsp90-organizing protein Sti1 (Hop1).Hsp40s specify functions of Hsp104 and Hsp90 protein chaperone machines.Molecular chaperones and the assembly of the prion Sup35p, an in vitro study.Interactions among prions and prion "strains" in yeast.Changes in the middle region of Sup35 profoundly alter the nature of epigenetic inheritance for the yeast prion [PSI+]Hsp70 chaperones as modulators of prion life cycle: novel effects of Ssa and Ssb on the Saccharomyces cerevisiae prion [PSI+]Primate chaperones Hsc70 (constitutive) and Hsp70 (induced) differ functionally in supporting growth and prion propagation in Saccharomyces cerevisiae.De novo appearance and "strain" formation of yeast prion [PSI+] are regulated by the heat-shock transcription factor.Saccharomyces cerevisiae Hsp70 mutations affect [PSI+] prion propagation and cell growth differently and implicate Hsp40 and tetratricopeptide repeat cochaperones in impairment of [PSI+]Destabilizing interactions among [PSI(+)] and [PIN(+)] yeast prion variants.Spatial quality control bypasses cell-based limitations on proteostasis to promote prion curing.Suicidal [PSI+] is a lethal yeast prion.
P2860
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P2860
A role for cytosolic hsp70 in yeast [PSI(+)] prion propagation and [PSI(+)] as a cellular stress.
description
2000 nî lūn-bûn
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2000 թվականի հոտեմբերին հրատարակված գիտական հոդված
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A role for cytosolic hsp70 in yeast [PSI
@nl
A role for cytosolic hsp70 in ...... [PSI(+)] as a cellular stress.
@ast
A role for cytosolic hsp70 in ...... [PSI(+)] as a cellular stress.
@en
type
label
A role for cytosolic hsp70 in yeast [PSI
@nl
A role for cytosolic hsp70 in ...... [PSI(+)] as a cellular stress.
@ast
A role for cytosolic hsp70 in ...... [PSI(+)] as a cellular stress.
@en
prefLabel
A role for cytosolic hsp70 in yeast [PSI
@nl
A role for cytosolic hsp70 in ...... [PSI(+)] as a cellular stress.
@ast
A role for cytosolic hsp70 in ...... [PSI(+)] as a cellular stress.
@en
P2093
P2860
P1433
P1476
A role for cytosolic hsp70 in ...... [PSI(+)] as a cellular stress
@en
P2093
P2860
P304
P407
P50
P577
2000-10-01T00:00:00Z