Antagonistic interactions between yeast [PSI(+)] and [URE3] prions and curing of [URE3] by Hsp70 protein chaperone Ssa1p but not by Ssa2p.
about
Yeast prions [URE3] and [PSI+] are diseasesStress granule assembly is mediated by prion-like aggregation of TIA-1Prions, protein homeostasis, and phenotypic diversityDisaggregases, molecular chaperones that resolubilize protein aggregatesThe 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 systemsThe [RNQ+] prion: a model of both functional and pathological amyloidHsp104-dependent remodeling of prion complexes mediates protein-only inheritanceCDK-dependent Hsp70 Phosphorylation controls G1 cyclin abundance and cell-cycle progressionYeast prions are useful for studying protein chaperones and protein quality controlInteraction of Prions Causes Heritable Traits in Saccharomyces cerevisiaeUsing steered molecular dynamics to predict and assess Hsp70 substrate-binding domain mutants that alter prion propagationAggregation of human S100A8 and S100A9 amyloidogenic proteins perturbs proteostasis in a yeast modelMolecular characterization of an adaptive response to alkylating agents in the opportunistic pathogen Aspergillus fumigatusFunction of SSA subfamily of Hsp70 within and across species varies widely in complementing Saccharomyces cerevisiae cell growth and prion propagation.Structure and assembly properties of the N-terminal domain of the prion Ure2p in isolation and in its natural contextRequirements of Hsp104p activity and Sis1p binding for propagation of the [RNQ(+)] prionSelf-protection against gliotoxin--a component of the gliotoxin biosynthetic cluster, GliT, completely protects Aspergillus fumigatus against exogenous gliotoxinGlobal transcript and phenotypic analysis of yeast cells expressing Ssa1, Ssa2, Ssa3 or Ssa4 as sole source of cytosolic Hsp70-Ssa chaperone activityA region within the C-terminal domain of Ure2p is shown to interact with the molecular chaperone Ssa1p by the use of cross-linkers and mass spectrometry.Investigating the interactions of yeast prions: [SWI+], [PSI+], and [PIN+].Normal levels of the antiprion proteins Btn2 and Cur1 cure most newly formed [URE3] prion variantsSti1 regulation of Hsp70 and Hsp90 is critical for curing of Saccharomyces cerevisiae [PSI+] prions by Hsp104.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.Hsp40s specify functions of Hsp104 and Hsp90 protein chaperone machines.Environmental regulation of prions in yeast.Heterologous gln/asn-rich proteins impede the propagation of yeast prions by altering chaperone availabilityHsp70 chaperones as modulators of prion life cycle: novel effects of Ssa and Ssb on the Saccharomyces cerevisiae prion [PSI+]Loss of Hsp70 in Drosophila is pleiotropic, with effects on thermotolerance, recovery from heat shock and neurodegeneration.Primate chaperones Hsc70 (constitutive) and Hsp70 (induced) differ functionally in supporting growth and prion propagation in Saccharomyces cerevisiae.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.Suicidal [PSI+] is a lethal yeast prion.N-terminal domain of yeast Hsp104 chaperone is dispensable for thermotolerance and prion propagation but necessary for curing prions by Hsp104 overexpressionDestabilization and recovery of a yeast prion after mild heat shock.Prion diseases of yeast: amyloid structure and biology.Prion-forming ability of Ure2 of yeasts is not evolutionarily conserved.
P2860
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P2860
Antagonistic interactions between yeast [PSI(+)] and [URE3] prions and curing of [URE3] by Hsp70 protein chaperone Ssa1p but not by Ssa2p.
description
2002 nî lūn-bûn
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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
Antagonistic interactions between yeast [PSI
@nl
Antagonistic interactions betw ...... perone Ssa1p but not by Ssa2p.
@ast
Antagonistic interactions betw ...... perone Ssa1p but not by Ssa2p.
@en
type
label
Antagonistic interactions between yeast [PSI
@nl
Antagonistic interactions betw ...... perone Ssa1p but not by Ssa2p.
@ast
Antagonistic interactions betw ...... perone Ssa1p but not by Ssa2p.
@en
prefLabel
Antagonistic interactions between yeast [PSI
@nl
Antagonistic interactions betw ...... perone Ssa1p but not by Ssa2p.
@ast
Antagonistic interactions betw ...... perone Ssa1p but not by Ssa2p.
@en
P2860
P1476
Antagonistic interactions betw ...... perone Ssa1p but not by Ssa2p.
@en
P2093
Christine Schwimmer
Daniel C Masison
P2860
P304
P356
10.1128/MCB.22.11.3590-3598.2002
P407
P577
2002-06-01T00:00:00Z