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Regulatory circuits of the AAA+ disaggregase Hsp104.
scientific article published on 23 March 2011
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Europe PubMed Central
PMCID
3093873
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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:21454552%20AND%20SRC:MED&resulttype=core&format=json
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27 January 2020
title
Regulatory circuits of the AAA+ disaggregase Hsp104
(English)
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stated in
Europe PubMed Central
PMCID
3093873
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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:21454552%20AND%20SRC:MED&resulttype=core&format=json
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27 January 2020
author
Titus M Franzmann
series ordinal
1
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Europe PubMed Central
PMCID
3093873
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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:21454552%20AND%20SRC:MED&resulttype=core&format=json
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27 January 2020
author name string
Anna Czekalla
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2
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PMCID
3093873
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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:21454552%20AND%20SRC:MED&resulttype=core&format=json
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27 January 2020
Stefan G Walter
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3
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3093873
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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:21454552%20AND%20SRC:MED&resulttype=core&format=json
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27 January 2020
language of work or name
English
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publication date
23 March 2011
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Europe PubMed Central
PMCID
3093873
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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:21454552%20AND%20SRC:MED&resulttype=core&format=json
retrieved
27 January 2020
published in
Journal of Biological Chemistry
1 reference
stated in
Europe PubMed Central
PMCID
3093873
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:21454552%20AND%20SRC:MED&resulttype=core&format=json
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27 January 2020
volume
286
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Europe PubMed Central
PMCID
3093873
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:21454552%20AND%20SRC:MED&resulttype=core&format=json
retrieved
27 January 2020
issue
20
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PMCID
3093873
reference URL
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retrieved
27 January 2020
page(s)
17992-18001
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3093873
reference URL
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27 January 2020
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Structures of asymmetric ClpX hexamers reveal nucleotide-dependent motions in a AAA+ protein-unfolding machine
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Atypical AAA+ subunit packing creates an expanded cavity for disaggregation by the protein-remodeling factor Hsp104.
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Human heat shock protein 70 enhances tumor antigen presentation through complex formation and intracellular antigen delivery without innate immune signaling.
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Asymmetric deceleration of ClpB or Hsp104 ATPase activity unleashes protein-remodeling activity
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The molecular chaperone Hsp104--a molecular machine for protein disaggregation
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27 May 2018
Substrate binding to the molecular chaperone Hsp104 and its regulation by nucleotides
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27 May 2018
Thermotolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB.
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The structure of ClpB: a molecular chaperone that rescues proteins from an aggregated state
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Conformational changes of the multifunction p97 AAA ATPase during its ATPase cycle
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Cooperative kinetics of both Hsp104 ATPase domains and interdomain communication revealed by AAA sensor-1 mutants
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27 May 2018
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27 May 2018
Subunit interactions influence the biochemical and biological properties of Hsp104
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27 May 2018
Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network
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Global unfolding of a substrate protein by the Hsp100 chaperone ClpA.
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Heat-inactivated proteins are rescued by the DnaK.J-GrpE set and ClpB chaperones
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27 May 2018
Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins
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Protein disaggregation mediated by heat-shock protein Hsp104.
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27 May 2018
HSP104 required for induced thermotolerance
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27 May 2018
Hsp104 is a highly conserved protein with two essential nucleotide-binding sites.
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27 May 2018
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16 August 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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16 August 2018
Rebuilt AAA + motors reveal operating principles for ATP-fuelled machines
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16 August 2018
Asymmetric interactions of ATP with the AAA+ ClpX6 unfoldase: allosteric control of a protein machine.
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16 August 2018
Solubilization of aggregated proteins by ClpB/DnaK relies on the continuous extraction of unfolded polypeptides
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16 August 2018
Mechanisms of conformational change for a replicative hexameric helicase of SV40 large tumor antigen
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16 August 2018
Evidence for an unfolding/threading mechanism for protein disaggregation by Saccharomyces cerevisiae Hsp104.
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16 August 2018
The prion curing agent guanidinium chloride specifically inhibits ATP hydrolysis by Hsp104.
1 reference
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PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3093873
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16 August 2018
Linkage between ATP consumption and mechanical unfolding during the protein processing reactions of an AAA+ degradation machine.
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16 August 2018
H2O2, but not menadione, provokes a decrease in the ATP and an increase in the inosine levels in Saccharomyces cerevisiae. An experimental and theoretical approach
1 reference
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reference URL
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16 August 2018
The N terminus of ClpB from Thermus thermophilus is not essential for the chaperone activity
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3093873
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16 August 2018
Proteins are unfolded on the surface of the ATPase ring before transport into the proteasome
1 reference
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PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3093873
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16 August 2018
Roles of the two ATP binding sites of ClpB from Thermus thermophilus
1 reference
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PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3093873
retrieved
16 August 2018
The ATPase activity of Hsp104, effects of environmental conditions and mutations.
1 reference
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PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3093873
retrieved
16 August 2018
Processing of proteins by the molecular chaperone Hsp104
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/21454552
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
PAN, the proteasome-activating nucleotidase from archaebacteria, is a protein-unfolding molecular chaperone
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/21454552
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Biochemical coupling of the two nucleotide binding domains of ClpB: covalent linkage is not a prerequisite for chaperone activity
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/21454552
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Identifiers
DOI
10.1074/JBC.M110.216176
1 reference
stated in
Europe PubMed Central
PMCID
3093873
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:21454552%20AND%20SRC:MED&resulttype=core&format=json
retrieved
27 January 2020
PMCID
3093873
1 reference
stated in
Europe PubMed Central
PMCID
3093873
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:21454552%20AND%20SRC:MED&resulttype=core&format=json
retrieved
27 January 2020
PubMed ID
21454552
1 reference
stated in
Europe PubMed Central
PMCID
3093873
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:21454552%20AND%20SRC:MED&resulttype=core&format=json
retrieved
27 January 2020
ResearchGate publication ID
50939780
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