Successive and synergistic action of the Hsp70 and Hsp100 chaperones in protein disaggregation (Q45012676)

8 December 2017

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

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8 December 2017

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3

Krzysztof Liberek

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8 December 2017

1

Szymon Zietkiewicz

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8 December 2017

Joanna Krzewska

2

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PubMed ID

15302880

8 December 2017

language of work or name

English

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publication date

9 August 2004

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Journal of Biological Chemistry

8 December 2017

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8 December 2017

279

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8 December 2017

43

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8 December 2017

44376-44383

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

8 December 2017

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M402405200

Getting newly synthesized proteins into shape.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M402405200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M402405200

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.M402405200

HSP104 required for induced thermotolerance

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M402405200

The molecular chaperone Hsp78 confers compartment-specific thermotolerance to mitochondria

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M402405200

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.M402405200

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.M402405200

A bichaperone (Hsp70-Hsp78) system restores mitochondrial DNA synthesis following thermal inactivation of Mip1p polymerase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M402405200

AAA proteins. Lords of the ring

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M402405200

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.M402405200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M402405200

Subunit interactions influence the biochemical and biological properties of Hsp104

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M402405200

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.M402405200

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.M402405200

HSP100/Clp proteins: a common mechanism explains diverse functions

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M402405200

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.M402405200

Trigger factor and DnaK cooperate in folding of newly synthesized proteins.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M402405200

Cooperation of GroEL/GroES and DnaK/DnaJ heat shock proteins in preventing protein misfolding in Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M402405200

Role of the DnaK and HscA homologs of Hsp70 chaperones in protein folding in E.coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M402405200

Kinetics of molecular chaperone action

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M402405200

Divergent effects of ATP on the binding of the DnaK and DnaJ chaperones to each other, or to their various native and denatured protein substrates.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M402405200

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.M402405200

Mechanism of regulation of hsp70 chaperones by DnaJ cochaperones

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M402405200

Mechanism of the targeting action of DnaJ in the DnaK molecular chaperone system

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M402405200

Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M402405200

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.M402405200

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.M402405200

Refolding of substrates bound to small Hsps relies on a disaggregation reaction mediated most efficiently by ClpB/DnaK.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M402405200

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.M402405200

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.M402405200

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.M402405200

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.M402405200

The green fluorescent protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M402405200

Chaperonin-mediated folding of green fluorescent protein.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M402405200

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.M402405200

Substrate recognition by the AAA+ chaperone ClpB.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M402405200

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.M402405200

The Hsp70 and Hsp60 chaperone machines

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M402405200

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.M402405200

Molecular chaperones: structure of a protein disaggregase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M402405200

21 January 2018

Identifiers

DOI

10.1074/JBC.M402405200

1 reference

8 December 2017

1 reference

PubMed ID

15302880