Structure and function of the middle domain of ClpB from Escherichia coli (Q35678007)

9 August 2017

title

Structure and function of the middle domain of ClpB from Escherichia coli (English)

1 reference

9 August 2017

1 reference

Sabina Kedzierska

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9 August 2017

Vladimir Akoev

series ordinal

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9 August 2017

Micheal E Barnett

series ordinal

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9 August 2017

Michal Zolkiewski

series ordinal

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9 August 2017

language of work or name

English

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publication date

1 December 2003

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9 August 2017

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9 August 2017

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9 August 2017

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9 August 2017

page(s)

14242-14248

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Conformational changes of the multifunction p97 AAA ATPase during its ATPase cycle

9 August 2017

cites work

1 reference

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Site-directed mutagenesis of conserved charged amino acid residues in ClpB from Escherichia coli

27 July 2018

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Crystal structure of ClpA, an Hsp100 chaperone and regulator of ClpAP protease

27 July 2018

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Crystal structure of E. coli Hsp100 ClpB nucleotide-binding domain 1 (NBD1) and mechanistic studies on ClpB ATPase activity

27 July 2018

1 reference

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

27 July 2018

1 reference

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AAA+ superfamily ATPases: common structure--diverse function

27 July 2018

1 reference

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Effects of protein stability and structure on substrate processing by the ClpXP unfolding and degradation machine

27 July 2018

1 reference

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Characterization of the N-terminal repeat domain of Escherichia coli ClpA-A class I Clp/HSP100 ATPase

27 July 2018

1 reference

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Structure of the AAA ATPase p97

27 July 2018

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

27 July 2018

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Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin

27 July 2018

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

27 July 2018

1 reference

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Nucleotide-dependent oligomerization of ClpB from Escherichia coli

27 July 2018

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

27 July 2018

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

27 July 2018

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AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes

27 July 2018

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ClpB in a cyanobacterium: predicted structure, phylogenetic relationships, and regulation by light and temperature

27 July 2018

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

27 July 2018

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HSP100/Clp proteins: a common mechanism explains diverse functions

27 July 2018

1 reference

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Thermodynamic characterization of the structural stability of the coiled-coil region of the bZIP transcription factor GCN4.

27 July 2018

1 reference

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Structure, function and application of the coiled-coil protein folding motif

27 July 2018

1 reference

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

27 July 2018

1 reference

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The heat-shock protein ClpB in Escherichia coli is a protein-activated ATPase

27 July 2018

1 reference

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

27 July 2018

1 reference

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

25 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1821349

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

25 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1821349

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

25 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1821349

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

25 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1821349

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

25 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1821349

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

25 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1821349

Molecular properties of ClpAP protease of Escherichia coli: ATP-dependent association of ClpA and clpP.

25 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1821349

A pSC101-derived plasmid which shows no sequence homology to other commonly used cloning vectors

25 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1821349

Boundary analysis in sedimentation transport experiments: a procedure for obtaining sedimentation coefficient distributions using the time derivative of the concentration profile

25 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=1821349

ClpB and HtpG facilitate de novo protein folding in stressed Escherichia coli cells

25 September 2018

1 reference

12 December 2020

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

1 reference

12 December 2020

Partial unfolding of dodecameric glutamine synthetase from Escherichia coli: temperature-induced, reversible transitions of two domains

1 reference

12 December 2020

Two-state thermal unfolding of a long dimeric coiled-coil: the Acanthamoeba myosin II rod

1 reference

12 December 2020

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

1 reference

12 December 2020

Identifiers

DOI

10.1021/BI035573D

1 reference

release_xoqjvc26izagtfqzgcsoraj24e

9 August 2017

Fatcat ID

1 reference

Fatcat

https://api.fatcat.wiki/v0/release/xoqjvc26izagtfqzgcsoraj24e

24 November 2022

mapped directly with Wikidata item

PMC publication ID

1821349

1 reference

9 August 2017

1 reference