(Q43821705)

27 November 2017

title

Roles of the two ATP binding sites of ClpB from Thermus thermophilus (English)

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27 November 2017

Thermus thermophilus

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2

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27 November 2017

Yo-hei Watanabe

1

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27 November 2017

Masasuke Yoshida

series ordinal

3

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27 November 2017

language of work or name

English

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publication date

10 December 2001

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Journal of Biological Chemistry

27 November 2017

published in

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27 November 2017

volume

277

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27 November 2017

issue

8

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27 November 2017

page(s)

5804-5809

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HSP104 required for induced thermotolerance

27 November 2017

cites work

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109349200

Genetic evidence for a functional relationship between Hsp104 and Hsp70.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109349200

Protein disaggregation mediated by heat-shock protein Hsp104.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109349200

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.M109349200

Conservation of the regulatory subunit for the Clp ATP-dependent protease in prokaryotes and eukaryotes

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109349200

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.M109349200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109349200

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.M109349200

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.M109349200

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.M109349200

HSP100/Clp proteins: a common mechanism explains diverse functions

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109349200

Homology in structural organization between E. coli ClpAP protease and the eukaryotic 26 S proteasome

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109349200

Nucleotide-dependent oligomerization of ClpB from Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109349200

The structures of HsIU and the ATP-dependent protease HsIU-HsIV

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109349200

Crystal and solution structures of an HslUV protease-chaperone complex

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109349200

A molecular chaperone, ClpA, functions like DnaK and DnaJ.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109349200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109349200

Dynamics of substrate denaturation and translocation by the ClpXP degradation machine

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109349200

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.M109349200

Hsp104 is a highly conserved protein with two essential nucleotide-binding sites

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109349200

Distinctive roles of the two ATP-binding sites in ClpA, the ATPase component of protease Ti in Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109349200

The ATPase activity of Hsp104, effects of environmental conditions and mutations.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109349200

Mutational analysis of the two ATP-binding sites in ClpB, a heat shock protein with protein-activated ATPase activity in Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109349200

The chaperone function of ClpB from Thermus thermophilus depends on allosteric interactions of its two ATP-binding sites

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109349200

Subunit interactions influence the biochemical and biological properties of Hsp104

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109349200

A novel factor required for the assembly of the DnaK and DnaJ chaperones of Thermus thermophilus

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109349200

K+ is an indispensable cofactor for GrpE stimulation of ATPase activity of DnaK x DnaJ complex from Thermus thermophilus.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109349200

A malachite green procedure for orthophosphate determination and its use in alkaline phosphatase-based enzyme immunoassay

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109349200

A malachite green colorimetric assay for protein phosphatase activity

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109349200

Heat-inactivated proteins managed by DnaKJ-GrpE-ClpB chaperones are released as a chaperonin-recognizable non-native form

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109349200

ClpB cooperates with DnaK, DnaJ, and GrpE in suppressing protein aggregation. A novel multi-chaperone system from Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109349200

Mitochondrial Hsp78, a member of the Clp/Hsp100 family in Saccharomyces cerevisiae, cooperates with Hsp70 in protein refolding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109349200

Enzymatic and structural similarities between the Escherichia coli ATP-dependent proteases, ClpXP and ClpAP

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109349200

Heptameric ring structure of the heat-shock protein ClpB, a protein-activated ATPase in Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109349200

Mutational analysis of the ATP-binding site in HslU, the ATPase component of HslVU protease in Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109349200

New ribose-modified fluorescent analogs of adenine and guanine nucleotides available as subtrates for various enzymes

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M109349200

21 January 2018

Identifiers

DOI

10.1074/JBC.M109349200

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27 November 2017

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