(Q44078387)

29 November 2017

title

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

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29 November 2017

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Zhonghua Liu

1

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29 November 2017

Vekalet Tek

series ordinal

2

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29 November 2017

Vladimir Akoev

series ordinal

3

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29 November 2017

Michal Zolkiewski

series ordinal

4

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29 November 2017

language of work or name

English

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publication date

1 August 2002

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Journal of Molecular Biology

29 November 2017

published in

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29 November 2017

volume

321

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29 November 2017

issue

1

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29 November 2017

page(s)

111-120

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HSP100/Clp proteins: a common mechanism explains diverse functions

29 November 2017

cites work

1 reference

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

7 January 2021

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

7 January 2021

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Dynamics of substrate denaturation and translocation by the ClpXP degradation machine

7 January 2021

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

7 January 2021

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

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

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

7 January 2021

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

7 January 2021

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

7 January 2021

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Six-fold rotational symmetry of ClpQ, the E. coli homolog of the 20S proteasome, and its ATP-dependent activator, ClpY.

7 January 2021

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

7 January 2021

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

7 January 2021

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

7 January 2021

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

7 January 2021

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

7 January 2021

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7 January 2021

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7 January 2021

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7 January 2021

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7 January 2021

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7 January 2021

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[34] Purification and properties of Hsp104 from yeast

7 January 2021

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Environmental effects on disulfide bonding patterns of bovine kappa-casein

7 January 2021

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7 January 2021

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7 January 2021

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7 January 2021

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7 January 2021

Identifiers

DOI

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release_pwtdjiz3xfbdpepxja5jrxr44e

29 November 2017

Fatcat ID

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Fatcat

https://api.fatcat.wiki/v0/release/pwtdjiz3xfbdpepxja5jrxr44e

mapped directly with Wikidata item

24 November 2022

based on heuristic

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