(Q36090078)

12 August 2017

Collaboration between the ClpB AAA+ remodeling protein and the DnaK chaperone system (English)

1 reference

12 August 2017

0 references

1 reference

3

Sue Wickner

1 reference

12 August 2017

Shannon M Doyle

1

1 reference

PMCID

2040865

12 August 2017

Joel R Hoskins

series ordinal

2

1 reference

PMCID

2040865

12 August 2017

language of work or name

English

0 references

publication date

1 June 2007

1 reference

Proceedings of the National Academy of Sciences of the United States of America

12 August 2017

1 reference

12 August 2017

104

1 reference

12 August 2017

27

1 reference

12 August 2017

11138-11144

1 reference

Asymmetric deceleration of ClpB or Hsp104 ATPase activity unleashes protein-remodeling activity

12 August 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2040865

Visualizing the ATPase cycle in a protein disaggregating machine: structural basis for substrate binding by ClpB

2 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2040865

A camel passes through the eye of a needle: protein unfolding activity of Clp ATPases

2 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2040865

Evolutionary relationships and structural mechanisms of AAA+ proteins

2 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2040865

AAA+ proteins: have engine, will work

2 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2040865

Thermotolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB.

2 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2040865

The structure of ClpB: a molecular chaperone that rescues proteins from an aggregated state

2 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2040865

Crystal Structure of ClpX Molecular Chaperone from Helicobacter pylori

2 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2040865

SWISS-MODEL: An automated protein homology-modeling server

2 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2040865

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

2 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2040865

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

2 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2040865

ClpS, a substrate modulator of the ClpAP machine

2 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2040865

Crystal and solution structures of an HslUV protease-chaperone complex

2 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2040865

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

2 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2040865

Protein binding and unfolding by the chaperone ClpA and degradation by the protease ClpAP.

2 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2040865

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

2 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2040865

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

2 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2040865

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

2 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2040865

The role of the ClpA chaperone in proteolysis by ClpAP

2 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2040865

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

2 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2040865

Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries

2 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2040865

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

2 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2040865

Protein disaggregation mediated by heat-shock protein Hsp104.

2 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2040865

HSP104 required for induced thermotolerance

2 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2040865

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

2 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2040865

Monomerization of RepA dimers by heat shock proteins activates binding to DNA replication origin

2 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2040865

Destruction or potentiation of different prions catalyzed by similar Hsp104 remodeling activities

2 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2040865

Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpB.

11 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2040865

M domains couple the ClpB threading motor with the DnaK chaperone activity.

11 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2040865

Hsp70 chaperone machine remodels protein aggregates at the initial step of Hsp70-Hsp100-dependent disaggregation.

23 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2040865

Interactions within the ClpB/DnaK bi-chaperone system from Escherichia coli

23 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2040865

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

23 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2040865

Solubilization of aggregated proteins by ClpB/DnaK relies on the continuous extraction of unfolded polypeptides

23 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2040865

Substrate recognition by the AAA+ chaperone ClpB.

23 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2040865

Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers

23 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2040865

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

23 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2040865

A chaperone network for the resolubilization of protein aggregates: direct interaction of ClpB and DnaK.

23 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2040865

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

23 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2040865

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

23 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2040865

Defining a pathway of communication from the C-terminal peptide binding domain to the N-terminal ATPase domain in a AAA protein

23 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2040865

Size-dependent disaggregation of stable protein aggregates by the DnaK chaperone machinery.

23 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2040865

The interplay of the GrpE heat shock protein and Mg2+ in RepA monomerization by DnaJ and DnaK.

23 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2040865

Organic extraction of P i with isobutanol/toluene

23 September 2018

1 reference

Crossref

https://api.crossref.org/works/10.1073%2FPNAS.0703980104

Function of DnaJ and DnaK as chaperones in origin-specific DNA binding by RepA

21 January 2018

1 reference

Crossref

https://api.crossref.org/works/10.1073%2FPNAS.0703980104

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

21 January 2018

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/17545305

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

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

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/17545305

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Substrate recognition by the ClpA chaperone component of ClpAP protease

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/17545305

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Identifiers

DOI

10.1073/PNAS.0703980104

1 reference

12 August 2017

0 references

1 reference

12 August 2017

1 reference

PMCID

2040865