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Sti1 regulation of Hsp70 and Hsp90 is critical for curing of Saccharomyces cerevisiae [PSI+] prions by Hsp104.
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Europe PubMed Central
PMCID
2897543
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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:20479121%20AND%20SRC:MED&resulttype=core&format=json
retrieved
2 February 2020
title
Sti1 regulation of Hsp70 and Hsp90 is critical for curing of Saccharomyces cerevisiae [PSI+] prions by Hsp104
(English)
1 reference
stated in
Europe PubMed Central
PMCID
2897543
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:20479121%20AND%20SRC:MED&resulttype=core&format=json
retrieved
2 February 2020
main subject
prion protein family
0 references
Saccharomyces cerevisiae
1 reference
based on heuristic
inferred from title
author
Michael Reidy
series ordinal
1
1 reference
stated in
Europe PubMed Central
PMCID
2897543
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:20479121%20AND%20SRC:MED&resulttype=core&format=json
retrieved
2 February 2020
author name string
Daniel C Masison
series ordinal
2
1 reference
stated in
Europe PubMed Central
PMCID
2897543
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:20479121%20AND%20SRC:MED&resulttype=core&format=json
retrieved
2 February 2020
language of work or name
English
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publication date
17 May 2010
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Europe PubMed Central
PMCID
2897543
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:20479121%20AND%20SRC:MED&resulttype=core&format=json
retrieved
2 February 2020
published in
Molecular and Cellular Biology
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stated in
Europe PubMed Central
PMCID
2897543
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:20479121%20AND%20SRC:MED&resulttype=core&format=json
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2 February 2020
volume
30
1 reference
stated in
Europe PubMed Central
PMCID
2897543
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:20479121%20AND%20SRC:MED&resulttype=core&format=json
retrieved
2 February 2020
issue
14
1 reference
stated in
Europe PubMed Central
PMCID
2897543
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:20479121%20AND%20SRC:MED&resulttype=core&format=json
retrieved
2 February 2020
page(s)
3542-3552
1 reference
stated in
Europe PubMed Central
PMCID
2897543
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:20479121%20AND%20SRC:MED&resulttype=core&format=json
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2 February 2020
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The yeast global transcriptional co-repressor protein Cyc8 can propagate as a prion
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Curing of the [URE3] prion by Btn2p, a Batten disease-related protein
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Newly identified prion linked to the chromatin-remodeling factor Swi1 in Saccharomyces cerevisiae
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Hsp110 chaperones regulate prion formation and propagation in S. cerevisiae by two discrete activities
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HSP90/70 chaperones are required for rapid nucleosome removal upon induction of the GAL genes of yeast
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The role of Sse1 in the de novo formation and variant determination of the [PSI+] prion
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Accelerated aging and failure to segregate damaged proteins in Sir2 mutants can be suppressed by overproducing the protein aggregation-remodeling factor Hsp104p
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The Hsp110 molecular chaperone stabilizes apolipoprotein B from endoplasmic reticulum-associated degradation (ERAD)
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Definition of the minimal fragments of Sti1 required for dimerization, interaction with Hsp70 and Hsp90 and in vivo functions
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N-terminal domain of yeast Hsp104 chaperone is dispensable for thermotolerance and prion propagation but necessary for curing prions by Hsp104 overexpression
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5 July 2018
Effect of mutation of the tetratricopeptide repeat and asparatate-proline 2 domains of Sti1 on Hsp90 signaling and interaction in Saccharomyces cerevisiae
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Hsp70 chaperones as modulators of prion life cycle: novel effects of Ssa and Ssb on the Saccharomyces cerevisiae prion [PSI+]
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5 July 2018
Propagation of Saccharomyces cerevisiae [PSI+] prion is impaired by factors that regulate Hsp70 substrate binding
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Dissection and design of yeast prions
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Dominant gain-of-function mutations in Hsp104p reveal crucial roles for the middle region
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Aggregation of expanded polyglutamine domain in yeast leads to defects in endocytosis
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5 July 2018
Yeast [PSI+] Prion Aggregates Are Formed by Small Sup35 Polymers Fragmented by Hsp104
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5 July 2018
Amino acid residue 184 of yeast Hsp104 chaperone is critical for prion-curing by guanidine, prion propagation, and thermotolerance
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Guanidine hydrochloride inhibits the generation of prion "seeds" but not prion protein aggregation in yeast.
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5 July 2018
Antagonistic interactions between yeast [PSI(+)] and [URE3] prions and curing of [URE3] by Hsp70 protein chaperone Ssa1p but not by Ssa2p
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5 July 2018
Cooperative kinetics of both Hsp104 ATPase domains and interdomain communication revealed by AAA sensor-1 mutants
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5 July 2018
Hsp104 interacts with Hsp90 cochaperones in respiring yeast
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5 July 2018
Strong growth polarity of yeast prion fiber revealed by single fiber imaging
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5 July 2018
Mechanism of prion loss after Hsp104 inactivation in yeast
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5 July 2018
Guanidine hydrochloride inhibits Hsp104 activity in vivo: a possible explanation for its effect in curing yeast prions
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The role of Sis1 in the maintenance of the [RNQ+] prion
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5 July 2018
The truncated form of the bacterial heat shock protein ClpB/HSP100 contributes to development of thermotolerance in the cyanobacterium Synechococcus sp. strain PCC 7942.
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[URE3] prion propagation in Saccharomyces cerevisiae: requirement for chaperone Hsp104 and curing by overexpressed chaperone Ydj1p
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5 July 2018
A role for cytosolic hsp70 in yeast [PSI(+)] prion propagation and [PSI(+)] as a cellular stress.
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5 July 2018
Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine
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5 July 2018
Guanidine hydrochloride blocks a critical step in the propagation of the prion-like determinant [PSI(+)] of Saccharomyces cerevisiae.
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5 July 2018
Evidence for a protein mutator in yeast: role of the Hsp70-related chaperone ssb in formation, stability, and toxicity of the [PSI] prion
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5 July 2018
Genetic study of interactions between the cytoskeletal assembly protein sla1 and prion-forming domain of the release factor Sup35 (eRF3) in Saccharomyces cerevisiae
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5 July 2018
Antagonistic interactions between yeast chaperones Hsp104 and Hsp70 in prion curing
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5 July 2018
Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins
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5 July 2018
Genetic and environmental factors affecting the de novo appearance of the [PSI+] prion in Saccharomyces cerevisiae
1 reference
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5 July 2018
Propagation of the yeast prion-like [psi+] determinant is mediated by oligomerization of the SUP35-encoded polypeptide chain release factor
1 reference
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PubMed Central
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5 July 2018
Protein disaggregation mediated by heat-shock protein Hsp104.
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5 July 2018
Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+]
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5 July 2018
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5 July 2018
hsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperatures
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5 July 2018
A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
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5 July 2018
The polarisome is required for segregation and retrograde transport of protein aggregates.
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29 October 2018
Hsp70/Hsp90 co-chaperones are required for efficient Hsp104-mediated elimination of the yeast [PSI(+)] prion but not for prion propagation
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29 October 2018
Substrate threading through the central pore of the Hsp104 chaperone as a common mechanism for protein disaggregation and prion propagation
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29 October 2018
Diverse cellular functions of the Hsp90 molecular chaperone uncovered using systems approaches.
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29 October 2018
Hsp70 chaperone machine remodels protein aggregates at the initial step of Hsp70-Hsp100-dependent disaggregation.
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29 October 2018
Modulation of prion formation, aggregation, and toxicity by the actin cytoskeleton in yeast
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29 October 2018
Prion protein remodelling confers an immediate phenotypic switch.
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29 October 2018
Successive and synergistic action of the Hsp70 and Hsp100 chaperones in protein disaggregation
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29 October 2018
Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers
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PubMed Central
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29 October 2018
Evidence for an unfolding/threading mechanism for protein disaggregation by Saccharomyces cerevisiae Hsp104.
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29 October 2018
The prion curing agent guanidinium chloride specifically inhibits ATP hydrolysis by Hsp104.
1 reference
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PubMed Central
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29 October 2018
Pleiotropic effects of Ubp6 loss on drug sensitivities and yeast prion are due to depletion of the free ubiquitin pool
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PubMed Central
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29 October 2018
The N terminus of ClpB from Thermus thermophilus is not essential for the chaperone activity
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29 October 2018
Bidirectional amyloid fiber growth for a yeast prion determinant.
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29 October 2018
An antiprion effect of the anticytoskeletal drug latrunculin A in yeast.
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29 October 2018
Effects of ubiquitin system alterations on the formation and loss of a yeast prion
1 reference
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https://pubmed.ncbi.nlm.nih.gov/20479121
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12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Channel mutations in Hsp104 hexamer distinctively affect thermotolerance and prion-specific propagation
1 reference
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PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/20479121
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Expressed as the sole Hsp90 of yeast, the alpha and beta isoforms of human Hsp90 differ with regard to their capacities for activation of certain client proteins, whereas only Hsp90beta generates sensitivity to the Hsp90 inhibitor radicicol
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/20479121
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
DnaK-mediated association of ClpB to protein aggregates. A bichaperone network at the aggregate surface
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/20479121
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Interactions of p60, a mediator of progesterone receptor assembly, with heat shock proteins hsp90 and hsp70
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/20479121
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Identifiers
DOI
10.1128/MCB.01292-09
1 reference
stated in
Europe PubMed Central
PMCID
2897543
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:20479121%20AND%20SRC:MED&resulttype=core&format=json
retrieved
2 February 2020
PMCID
2897543
1 reference
stated in
Europe PubMed Central
PMCID
2897543
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:20479121%20AND%20SRC:MED&resulttype=core&format=json
retrieved
2 February 2020
PubMed ID
20479121
1 reference
stated in
Europe PubMed Central
PMCID
2897543
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:20479121%20AND%20SRC:MED&resulttype=core&format=json
retrieved
2 February 2020
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