(Q31523861)

2 July 2017

title

The molecular chaperone DnaJ is required for the degradation of a soluble abnormal protein in Escherichia coli (English)

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2 July 2017

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Huang HC

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2 July 2017

Sherman MY

series ordinal

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2 July 2017

Kandror O

series ordinal

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2 July 2017

Goldberg AL

series ordinal

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2 July 2017

language of work or name

English

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publication date

2 November 2000

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Journal of Biological Chemistry

2 July 2017

published in

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2 July 2017

volume

276

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2 July 2017

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2 July 2017

page(s)

3920-3928

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The mechanism and functions of ATP-dependent proteases in bacterial and animal cells

2 July 2017

cites work

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https://api.crossref.org/works/10.1074%2FJBC.M002937200

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M002937200

Posttranslational quality control: folding, refolding, and degrading proteins.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002937200

Escherichia coli alkaline phosphatase fails to acquire disulfide bonds when retained in the cytoplasm

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002937200

Roles of molecular chaperones in protein degradation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002937200

Protein folding in the cell

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002937200

Molecular chaperones in cellular protein folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002937200

Involvement of the molecular chaperone Ydj1 in the ubiquitin-dependent degradation of short-lived and abnormal proteins in Saccharomyces cerevisiae

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002937200

Interaction of Hsp70 chaperones with substrates

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002937200

Mechanism of regulation of hsp70 chaperones by DnaJ cochaperones

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002937200

Control of folding and membrane translocation by binding of the chaperone DnaJ to nascent polypeptides

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002937200

Role of the J-domain in the cooperation of Hsp40 with Hsp70.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002937200

Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002937200

Structure, function and evolution of DnaJ: conservation and adaptation of chaperone function

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002937200

Cooperation of GroEL/GroES and DnaK/DnaJ heat shock proteins in preventing protein misfolding in Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002937200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002937200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002937200

Protein quality control: triage by chaperones and proteases

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002937200

Role of the heat shock protein DnaJ in the lon-dependent degradation of naturally unstable proteins.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002937200

Mutations that allow disulfide bond formation in the cytoplasm of Escherichia coli.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002937200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002937200

DnaK and DnaJ heat shock proteins participate in protein export in Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002937200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002937200

Escherichia coli heat shock gene mutants are defective in proteolysis

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002937200

The conserved G/F motif of the DnaJ chaperone is necessary for the activation of the substrate binding properties of the DnaK chaperone

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002937200

Role of the mitochondrial DnaJ homologue, Mdj1p, in the prevention of heat-induced protein aggregation.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002937200

Manipulating the aggregation and oxidation of human SPARC in the cytoplasm of Escherichia coli.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002937200

A novel function of Escherichia coli chaperone DnaJ. Protein-disulfide isomerase.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002937200

The molecular chaperone Ydj1 is required for the p34CDC28-dependent phosphorylation of the cyclin Cln3 that signals its degradation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002937200

Physiological role during export for the retardation of folding by the leader peptide of maltose-binding protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002937200

Peptide-binding specificity of the molecular chaperone BiP

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002937200

Biological Sciences: The So-called Thermodynamic Compensation Law and Thermal Death

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002937200

21 January 2018

Identifiers

DOI

10.1074/JBC.M002937200

1 reference

2 July 2017

1 reference