(Q39501582)

English

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

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scholarly article

1 reference

Europe PubMed Central

PMC publication ID

12 September 2017

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

1 reference

Europe PubMed Central

PMC publication ID

12 September 2017

heat acclimation

1 reference

based on heuristic

inferred from title

1 reference

based on heuristic

inferred from title

thermal tolerance

1 reference

based on heuristic

inferred from title

author name string

Clarke AK

1

1 reference

Europe PubMed Central

PMC publication ID

12 September 2017

Eriksson MJ

2

1 reference

Europe PubMed Central

PMC publication ID

12 September 2017

language of work or name

0 references

publication date

1 December 2000

1 reference

Europe PubMed Central

PMC publication ID

12 September 2017

number of pages

5

1 reference

based on heuristic

inferred from page(s)

Journal of Bacteriology

1 reference

Europe PubMed Central

PMC publication ID

12 September 2017

182

1 reference

Europe PubMed Central

PMC publication ID

12 September 2017

24

1 reference

Europe PubMed Central

PMC publication ID

12 September 2017

7092-7096

1 reference

Europe PubMed Central

PMC publication ID

12 September 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=94841

12 September 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=94841

12 September 2017

Lon and Clp family proteases and chaperones share homologous substrate-recognition domains

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=94841

12 September 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=94841

12 September 2017

The molecular chaperone Hsp78 confers compartment-specific thermotolerance to mitochondria

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=94841

12 September 2017

HSP78 encodes a yeast mitochondrial heat shock protein in the Clp family of ATP-dependent proteases

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=94841

12 September 2017

Site-directed mutagenesis of the dual translational initiation sites of the clpB gene of Escherichia coli and characterization of its gene products

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=94841

12 September 2017

The function of heat-shock proteins in stress tolerance: degradation and reactivation of damaged proteins

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=94841

12 September 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=94841

12 September 2017

Protein disaggregation mediated by heat-shock protein Hsp104.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=94841

12 September 2017

Hsp78, a Clp homologue within mitochondria, can substitute for chaperone functions of mt-hsp70

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=94841

12 September 2017

Disassembly of the Mu transposase tetramer by the ClpX chaperone

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=94841

12 September 2017

The mitochondrial ClpB homolog Hsp78 cooperates with matrix Hsp70 in maintenance of mitochondrial function

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=94841

12 September 2017

HSP104 required for induced thermotolerance

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=94841

12 September 2017

The Escherichia coli heat shock protein ClpB restores acquired thermotolerance to a cyanobacterial clpB deletion mutant

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=94841

14 September 2017

Induction of the heat shock protein ClpB affects cold acclimation in the cyanobacterium Synechococcus sp. strain PCC 7942.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=94841

14 September 2017

The heat shock protein ClpB mediates the development of thermotolerance in the cyanobacterium Synechococcus sp. strain PCC 7942.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=94841

14 September 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=94841

14 September 2017

HSP100/Clp proteins: a common mechanism explains diverse functions

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=94841

25 September 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=94841

15 June 2018

Identification of dnaK multigene family in Synechococcus sp. PCC7942.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=94841

15 June 2018

Light-regulated expression of the psbD gene family in Synechococcus sp. strain PCC 7942: evidence for the role of duplicated psbD genes in cyanobacteria

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=94841

15 June 2018

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/11092876

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1128/JB.182.24.7092-7096.2000

1 reference

Europe PubMed Central

PMC publication ID

12 September 2017

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

12 September 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

12 September 2017

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