The amino-terminal domain of ClpB supports binding to strongly aggregated proteins (Q46632158)

23 December 2017

title

The amino-terminal domain of ClpB supports binding to strongly aggregated proteins (English)

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23 December 2017

author name string

Micheal E Barnett

1

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23 December 2017

Maria Nagy

2

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23 December 2017

Sabina Kedzierska

3

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23 December 2017

Michal Zolkiewski

4

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23 December 2017

language of work or name

English

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publication date

2 August 2005

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23 December 2017

Journal of Biological Chemistry

published in

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23 December 2017

volume

280

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23 December 2017

issue

41

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23 December 2017

page(s)

34940-34945

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23 December 2017

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

cites work

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M505653200

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.M505653200

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.M505653200

Heat shock protein 101 plays a crucial role in thermotolerance in Arabidopsis.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M505653200

Stability and interactions of the amino-terminal domain of ClpB from Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M505653200

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.M505653200

Nucleotide-dependent oligomerization of ClpB from Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M505653200

Nucleotide-induced switch in oligomerization of the AAA+ ATPase ClpB.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M505653200

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.M505653200

Sculpting the proteome with AAA(+) proteases and disassembly machines.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M505653200

Substrate recognition by the AAA+ chaperone ClpB.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M505653200

Conserved amino acid residues within the amino-terminal domain of ClpB are essential for the chaperone activity

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M505653200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M505653200

Structure and activity of ClpB from Escherichia coli. Role of the amino-and -carboxyl-terminal domains

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M505653200

Crystal structure of the E. coli Hsp100 ClpB N-terminal domain

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M505653200

Interaction of the N-terminal domain of Escherichia coli heat-shock protein ClpB and protein aggregates during chaperone activity

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M505653200

The truncated form of the bacterial heat shock protein ClpB/HSP100 contributes to development of thermotolerance in the cyanobacterium Synechococcus sp. strain PCC 7942.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M505653200

The N terminus of ClpB from Thermus thermophilus is not essential for the chaperone activity

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M505653200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M505653200

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M505653200

Assay of inorganic and organic phosphorus in the 0.1–5 nanomole range

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M505653200

An improved assay for nanomole amounts of inorganic phosphate

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M505653200

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.M505653200

AAA proteins. Lords of the ring

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M505653200

AAA+ superfamily ATPases: common structure--diverse function

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M505653200

Cooperative kinetics of both Hsp104 ATPase domains and interdomain communication revealed by AAA sensor-1 mutants

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M505653200

Crystallographic investigation of peptide binding sites in the N-domain of the ClpA chaperone.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M505653200

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.M505653200

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.M505653200

21 January 2018

Identifiers

DOI

10.1074/JBC.M505653200

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23 December 2017

PubMed ID

16076845

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23 December 2017