Regulation of the heat-shock protein 70 reaction cycle by the mammalian DnaJ homolog, Hsp40. (Q38354169)

2 September 2017

title

Regulation of the heat-shock protein 70 reaction cycle by the mammalian DnaJ homolog, Hsp40. (English)

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2 September 2017

Hartl FU

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2 September 2017

Minami Y

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2 September 2017

Höhfeld J

series ordinal

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2 September 2017

Ohtsuka K

series ordinal

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2 September 2017

language of work or name

English

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publication date

1 August 1996

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Journal of Biological Chemistry

2 September 2017

published in

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2 September 2017

volume

271

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2 September 2017

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2 September 2017

page(s)

19617-19624

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Protein folding in the cell

2 September 2017

cites work

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https://api.crossref.org/works/10.1074%2FJBC.271.32.19617

Molecular chaperone functions of heat-shock proteins

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.271.32.19617

Specificity of DnaK-peptide binding

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.271.32.19617

Different conformations for the same polypeptide bound to chaperones DnaK and GroEL.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.32.19617

Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiP.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.32.19617

Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.32.19617

The peptide-binding domain of the chaperone protein Hsc70 has an unusual secondary structure topology

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.32.19617

ATP-induced protein-Hsp70 complex dissociation requires K+ but not ATP hydrolysis.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.32.19617

Kinetics of molecular chaperone action

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.271.32.19617

The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpE

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.32.19617

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.271.32.19617

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.271.32.19617

Cloning of a cDNA for heat-shock protein hsp40, a human homologue of bacterial DnaJ

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.32.19617

DnaJ-like proteins: molecular chaperones and specific regulators of Hsp70.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.32.19617

A yeast DnaJ homologue, Scj1p, can function in the endoplasmic reticulum with BiP/Kar2p via a conserved domain that specifies interactions with Hsp70s

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.32.19617

Role of auxilin in uncoating clathrin-coated vesicles

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.32.19617

Isolation of a mouse cDNA encoding MTJ1, a new murine member of the DnaJ family of proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.32.19617

Mitochondrial molecular chaperones: their role in protein translocation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.32.19617

An enzyme that removes clathrin coats: purification of an uncoating ATPase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.32.19617

Hip, a novel cochaperone involved in the eukaryotic hsc70/hsp40 reaction cycle

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.32.19617

NMR structure determination of the Escherichia coli DnaJ molecular chaperone: secondary structure and backbone fold of the N-terminal region (residues 2-108) containing the highly conserved J domain.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.32.19617

Interaction of Hsp 70 with newly synthesized proteins: implications for protein folding and assembly.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.32.19617

Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.32.19617

The dissociation of ATP from hsp70 of Saccharomyces cerevisiae is stimulated by both Ydj1p and peptide substrates

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.32.19617

Conserved ATPase and luciferase refolding activities between bacteria and yeast Hsp70 chaperones and modulators.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.32.19617

Regulation of 70-kDa heat-shock-protein ATPase activity and substrate binding by human DnaJ-like proteins, HSJ1a and HSJ1b

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.32.19617

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.271.32.19617

Cooperation of the molecular chaperone Ydj1 with specific Hsp70 homologs to suppress protein aggregation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.32.19617

Peptide-binding specificity of the molecular chaperone BiP

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.32.19617

Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.271.32.19617

21 January 2018

Identifiers

DOI

10.1074/JBC.271.32.19617

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2 September 2017

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