Antagonistic interactions between yeast chaperones Hsp104 and Hsp70 in prion curing. - Wikidata - wikimedia - TriplyDB

Antagonistic interactions between yeast chaperones Hsp104 and Hsp70 in prion curing.

Antagonistic interactions between yeast chaperones Hsp104 and Hsp70 in prion curing.

http://www.wikidata.org/entity/Q33368981

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Stress granule assembly is mediated by prion-like aggregation of TIA-1 Disaggregases, molecular chaperones that resolubilize protein aggregates Modulation and elimination of yeast prions by protein chaperones and co-chaperones Differences in the curing of [PSI+] prion by various methods of Hsp104 inactivation Hsp104-dependent remodeling of prion complexes mediates protein-only inheritance Curing of the [URE3] prion by Btn2p, a Batten disease-related protein.Hsp104, Hsp70 and Hsp40 interplay regulates formation, growth and elimination of Sup35 prions.Increased expression of Hsp40 chaperones, transcriptional factors, and ribosomal protein Rpp0 can cure yeast prions.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 control Loss of amino-terminal acetylation suppresses a prion phenotype by modulating global protein folding The NatA acetyltransferase couples Sup35 prion complexes to the [PSI+] phenotype The requirement for Cdc48/p97 in nuclear protein quality control degradation depends on the substrate and correlates with substrate insolubility Cooperative kinetics of both Hsp104 ATPase domains and interdomain communication revealed by AAA sensor-1 mutants.Interaction of Prions Causes Heritable Traits in Saccharomyces cerevisiae Prions in Saccharomyces and Podospora spp.: protein-based inheritance.Hsp110 chaperones regulate prion formation and propagation in S. cerevisiae by two discrete activities.Requirements of Hsp104p activity and Sis1p binding for propagation of the [RNQ(+)] prion Heat shock protein 104 (Hsp104)-mediated curing of [PSI+] yeast prions depends on both [PSI+] conformation and the properties of the Hsp104 homologs.Hsp104 overexpression cures Saccharomyces cerevisiae [PSI+] by causing dissolution of the prion seeds Role for Hsp70 chaperone in Saccharomyces cerevisiae prion seed replication.Evidence for a protein mutator in yeast: role of the Hsp70-related chaperone ssb in formation, stability, and toxicity of the [PSI] prion.Sti1 regulation of Hsp70 and Hsp90 is critical for curing of Saccharomyces cerevisiae [PSI+] prions by Hsp104.Prion-dependent switching between respiratory competence and deficiency in the yeast nam9-1 mutant.Induction of distinct [URE3] yeast prion strains.Low activity of select Hsp104 mutants is sufficient to propagate unstable prion variants Viruses and prions of Saccharomyces cerevisiae Yeast prion protein derivative defective in aggregate shearing and production of new 'seeds'Amino acid residue 184 of yeast Hsp104 chaperone is critical for prion-curing by guanidine, prion propagation, and thermotolerance Assessment of inactivating stop codon mutations in forty Saccharomyces cerevisiae strains: implications for [PSI] prion- mediated phenotypes.Prions are a common mechanism for phenotypic inheritance in wild yeasts.Poly(A)-binding protein acts in translation termination via eukaryotic release factor 3 interaction and does not influence [PSI(+)] propagation.Antagonistic interactions between yeast [PSI(+)] and [URE3] prions and curing of [URE3] by Hsp70 protein chaperone Ssa1p but not by Ssa2p.Stress-dependent proteolytic processing of the actin assembly protein Lsb1 modulates a yeast prion Reassembly and protection of small nuclear ribonucleoprotein particles by heat shock proteins in yeast cells.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+]Genetic study of interactions between the cytoskeletal assembly protein sla1 and prion-forming domain of the release factor Sup35 (eRF3) in Saccharomyces cerevisiae.

P2860

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P2860

Antagonistic interactions between yeast chaperones Hsp104 and Hsp70 in prion curing.

http://www.wikidata.org/entity/Q33368981

description

1999 nî lūn-bûn

@nan

1999 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

1999 թվականի փետրվարին հրատարակված գիտական հոդված

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1999年の論文

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1999年論文

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1999年論文

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1999年論文

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1999年論文

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1999年論文

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1999年论文

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name

Antagonistic interactions between yeast chaperones Hsp104 and Hsp70 in prion curing.

@ast

Antagonistic interactions between yeast chaperones Hsp104 and Hsp70 in prion curing.

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type

label

Antagonistic interactions between yeast chaperones Hsp104 and Hsp70 in prion curing.

@ast

Antagonistic interactions between yeast chaperones Hsp104 and Hsp70 in prion curing.

@en

prefLabel

Antagonistic interactions between yeast chaperones Hsp104 and Hsp70 in prion curing.

@ast

Antagonistic interactions between yeast chaperones Hsp104 and Hsp70 in prion curing.

@en

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Molecular and Cellular Biology

P1476

Antagonistic interactions between yeast chaperones Hsp104 and Hsp70 in prion curing.

@en

P2093

G P Newnam

http://www.w3.org/2001/XMLSchema#string

R D Wegrzyn

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S L Lindquist

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Y 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

The protein product of the het-s heterokaryon incompatibility gene of the fungus Podospora anserina behaves as a prion analog

Transformation of intact yeast cells treated with alkali cations

A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae

hsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperatures.

Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins.

Role of Hsp70 subfamily, Ssa, in protein folding in yeast cells, seen in luciferase-transformed ssa mutants.

HSP104 required for induced thermotolerance.

Complex interactions among members of an essential subfamily of hsp70 genes in Saccharomyces cerevisiae.

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1325-1333

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10.1128/MCB.19.2.1325

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2

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19

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13398181

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9891066

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P921

Prion protein family

molecular chaperones

P932

116061

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