(Q45211595)

English

Dimeric trigger factor stably binds folding-competent intermediates and cooperates with the DnaK-DnaJ-GrpE chaperone system to allow refolding

scientific article published on 4 January 2005

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

10 December 2017

Dimeric trigger factor stably binds folding-competent intermediates and cooperates with the DnaK-DnaJ-GrpE chaperone system to allow refolding (English)

1 reference

Europe PubMed Central

PubMed publication ID

10 December 2017

molecular chaperones

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1 reference

based on heuristic

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author name string

Chuan-Peng Liu

1

1 reference

Europe PubMed Central

PubMed publication ID

10 December 2017

Sarah Perrett

2

1 reference

Europe PubMed Central

PubMed publication ID

10 December 2017

Jun-Mei Zhou

3

1 reference

Europe PubMed Central

PubMed publication ID

10 December 2017

language of work or name

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publication date

4 January 2005

1 reference

Europe PubMed Central

PubMed publication ID

10 December 2017

Journal of Biological Chemistry

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Europe PubMed Central

PubMed publication ID

10 December 2017

280

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Europe PubMed Central

PubMed publication ID

10 December 2017

14

1 reference

Europe PubMed Central

PubMed publication ID

10 December 2017

13315-13320

1 reference

Europe PubMed Central

PubMed publication ID

10 December 2017

Molecular chaperones in the cytosol: from nascent chain to folded protein

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M414151200

21 January 2018

sHsps and their role in the chaperone network

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M414151200

21 January 2018

Review: mechanisms of disaggregation and refolding of stable protein aggregates by molecular chaperones

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M414151200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M414151200

21 January 2018

Dynamic association of trigger factor with protein substrates

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M414151200

21 January 2018

Cooperation of enzymatic and chaperone functions of trigger factor in the catalysis of protein folding

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M414151200

21 January 2018

Modular structure of the trigger factor required for high activity in protein folding.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M414151200

21 January 2018

L23 protein functions as a chaperone docking site on the ribosome

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M414151200

21 January 2018

Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M414151200

21 January 2018

Escherichia coli trigger factor is a prolyl isomerase that associates with nascent polypeptide chains.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M414151200

21 January 2018

Trigger factor and DnaK cooperate in folding of newly synthesized proteins.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M414151200

21 January 2018

Trigger Factor and DnaK possess overlapping substrate pools and binding specificities

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M414151200

21 January 2018

The chaperone activity of trigger factor is distinct from its isomerase activity during co-expression with adenylate kinase in Escherichia coli

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M414151200

21 January 2018

Overexpression of trigger factor prevents aggregation of recombinant proteins in Escherichia coli

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M414151200

21 January 2018

Assisted folding of D-glyceraldehyde-3-phosphate dehydrogenase by trigger factor

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M414151200

21 January 2018

Binding specificity of Escherichia coli trigger factor

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M414151200

21 January 2018

Three-state equilibrium of Escherichia coli trigger factor

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M414151200

21 January 2018

Functional dissection of trigger factor and DnaK: interactions with nascent polypeptides and thermally denatured proteins

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M414151200

21 January 2018

Function of trigger factor and DnaK in multidomain protein folding: increase in yield at the expense of folding speed

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M414151200

21 January 2018

Trigger factor-assisted folding of bovine carbonic anhydrase II.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M414151200

21 January 2018

Dissociation and aggregation of D-glyceraldehyde-3-phosphate dehydrogenase during denaturation by guanidine hydrochloride

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M414151200

21 January 2018

47 A centrifuged-column procedure for the measurement of ligand binding by beef heart F1

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M414151200

21 January 2018

Escherichia coli Hsp31 functions as a holding chaperone that cooperates with the DnaK-DnaJ-GrpE system in the management of protein misfolding under severe stress conditions

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M414151200

21 January 2018

A small heat shock protein cooperates with heat shock protein 70 systems to reactivate a heat-denatured protein

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M414151200

21 January 2018

A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M414151200

21 January 2018

Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M414151200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M414151200

21 January 2018

The "trigger factor cycle" includes ribosomes, presecretory proteins, and the plasma membrane

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M414151200

21 January 2018

Functional dissection of Escherichia coli trigger factor: unraveling the function of individual domains

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M414151200

21 January 2018

On the attribution and additivity of binding energies

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M414151200

21 January 2018

Trigger factor retards protein export in Escherichia coli.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M414151200

21 January 2018

Involvement of the DnaK-DnaJ-GrpE chaperone team in protein secretion in Escherichia coli

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M414151200

21 January 2018

Identifiers

10.1074/JBC.M414151200

1 reference

Europe PubMed Central

PubMed publication ID

10 December 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

10 December 2017

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