(Q46895785)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:16415353%20AND%20SRC:MED&resulttype=core&format=json

15 January 2020

title

Hsp70 chaperone machine remodels protein aggregates at the initial step of Hsp70-Hsp100-dependent disaggregation (English)

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:16415353%20AND%20SRC:MED&resulttype=core&format=json

15 January 2020

0 references

1

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:16415353%20AND%20SRC:MED&resulttype=core&format=json

15 January 2020

Agnieszka Lewandowska

series ordinal

2

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:16415353%20AND%20SRC:MED&resulttype=core&format=json

15 January 2020

Krzysztof Liberek

series ordinal

4

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:16415353%20AND%20SRC:MED&resulttype=core&format=json

15 January 2020

author name string

Pawel Stocki

series ordinal

3

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:16415353%20AND%20SRC:MED&resulttype=core&format=json

15 January 2020

language of work or name

English

0 references

publication date

16 January 2006

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:16415353%20AND%20SRC:MED&resulttype=core&format=json

Journal of Biological Chemistry

15 January 2020

published in

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:16415353%20AND%20SRC:MED&resulttype=core&format=json

15 January 2020

volume

281

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:16415353%20AND%20SRC:MED&resulttype=core&format=json

15 January 2020

issue

11

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:16415353%20AND%20SRC:MED&resulttype=core&format=json

15 January 2020

page(s)

7022-7029

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:16415353%20AND%20SRC:MED&resulttype=core&format=json

Posttranslational quality control: folding, refolding, and degrading proteins.

15 January 2020

cites work

1 reference

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Getting newly synthesized proteins into shape.

21 January 2018

1 reference

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Molecular chaperones in the cytosol: from nascent chain to folded protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M507893200

Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpB.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M507893200

Degradation by proteases Lon, Clp and HtrA, of Escherichia coli proteins aggregated in vivo by heat shock; HtrA protease action in vivo and in vitro.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M507893200

ClpB is the Escherichia coli heat shock protein F84.1.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M507893200

Expression of ClpB, an analog of the ATP-dependent protease regulatory subunit in Escherichia coli, is controlled by a heat shock sigma factor (sigma 32).

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M507893200

HSP104 required for induced thermotolerance

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M507893200

Mitotic transcription repression in vivo in the absence of nucleosomal chromatin condensation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M507893200

Importance of two ATP-binding sites for oligomerization, ATPase activity and chaperone function of mitochondrial Hsp78 protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M507893200

Characterization of a trap mutant of the AAA+ chaperone ClpB.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M507893200

Subunit interactions influence the biochemical and biological properties of Hsp104

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M507893200

Roles of the two ATP binding sites of ClpB from Thermus thermophilus

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M507893200

Roles of individual domains and conserved motifs of the AAA+ chaperone ClpB in oligomerization, ATP hydrolysis, and chaperone activity

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M507893200

HSP100/Clp proteins: a common mechanism explains diverse functions

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M507893200

Unfolding and internalization of proteins by the ATP-dependent proteases ClpXP and ClpAP.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M507893200

Global unfolding of a substrate protein by the Hsp100 chaperone ClpA.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M507893200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M507893200

Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M507893200

Heat-inactivated proteins are rescued by the DnaK.J-GrpE set and ClpB chaperones

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M507893200

Regulated cycling of mitochondrial Hsp70 at the protein import channel

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M507893200

Role of the Escherichia coli DnaK and DnaJ heat shock proteins in the initiation of bacteriophage lambda DNA replication

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M507893200

Autoregulation of the Escherichia coli heat shock response by the DnaK and DnaJ heat shock proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M507893200

The E. coli dnaK gene product, the hsp70 homolog, can reactivate heat-inactivated RNA polymerase in an ATP hydrolysis-dependent manner

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M507893200

Size-dependent disaggregation of stable protein aggregates by the DnaK chaperone machinery.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M507893200

Review: mechanisms of disaggregation and refolding of stable protein aggregates by molecular chaperones

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M507893200

Successive and synergistic action of the Hsp70 and Hsp100 chaperones in protein disaggregation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M507893200

Thermotolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M507893200

The structure of ClpB: a molecular chaperone that rescues proteins from an aggregated state

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M507893200

Substrate recognition by the AAA+ chaperone ClpB.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M507893200

Evidence for an unfolding/threading mechanism for protein disaggregation by Saccharomyces cerevisiae Hsp104.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M507893200

Navigating the ClpB channel to solution.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M507893200

Residues in chaperonin GroEL required for polypeptide binding and release

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M507893200

The DnaJ chaperone catalytically activates the DnaK chaperone to preferentially bind the sigma 32 heat shock transcriptional regulator

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M507893200

A chaperone network for the resolubilization of protein aggregates: direct interaction of ClpB and DnaK.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M507893200

Solubilization of aggregated proteins by ClpB/DnaK relies on the continuous extraction of unfolded polypeptides

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M507893200

Active solubilization and refolding of stable protein aggregates by cooperative unfolding action of individual hsp70 chaperones

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M507893200

21 January 2018

Identifiers

DOI

10.1074/JBC.M507893200

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:16415353%20AND%20SRC:MED&resulttype=core&format=json

15 January 2020

1 reference