(Q48493458)

12 February 2018

title

Intrinsic ADP-ATP exchange activity is a novel function of the molecular chaperone, Hsp70. (English)

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12 February 2018

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Hiromura M

1

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12 February 2018

Yano M

2

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12 February 2018

Mori H

3

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12 February 2018

Inoue M

4

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12 February 2018

Kido H

5

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12 February 2018

language of work or name

English

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publication date

1 March 1998

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12 February 2018

Journal of Biological Chemistry

published in

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12 February 2018

volume

273

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12 February 2018

page(s)

5435-5438

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12 February 2018

issue

10

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12 February 2018

Molecular chaperone functions of heat-shock proteins

cites work

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.10.5435

Molecular chaperones in cellular protein folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.10.5435

Rapid purification of mammalian 70,000-dalton stress proteins: affinity of the proteins for nucleotides

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.10.5435

DnaK as a thermometer: threonine-199 is site of autophosphorylation and is critical for ATPase activity

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.10.5435

DnaK ATPase activity revisited.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.10.5435

Hsc70-binding peptides selected from a phage display peptide library that resemble organellar targeting sequences

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.10.5435

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.273.10.5435

Unfolded proteins stimulate molecular chaperone Hsc70 ATPase by accelerating ADP/ATP exchange

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.10.5435

A 16-kDa protein functions as a new regulatory protein for Hsc70 molecular chaperone and is identified as a member of the Nm23/nucleoside diphosphate kinase family

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.10.5435

Dissociation of clathrin coats coupled to the hydrolysis of ATP: role of an uncoating ATPase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.10.5435

Discrimination between acid and alkali-labile phosphorylated residues on Immobilon: phosphorylation studies of nucleoside diphosphate kinase.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.10.5435

DNA sequencing with chain-terminating inhibitors

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.10.5435

Lysine 71 of the chaperone protein Hsc70 Is essential for ATP hydrolysis

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.10.5435

Nucleosidediphosphate kinase of Escherichia coli, a periplasmic enzyme

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.10.5435

48 Nucleoside diphosphokinase from Salmonella typhimurium

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.10.5435

49 Nucleoside diphosphokinase from human erythrocytes

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.10.5435

Kinetics of molecular chaperone action

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.10.5435

Peptide-binding specificity of the molecular chaperone BiP

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.10.5435

Partner proteins determine multiple functions of Hsp70

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.10.5435

Peptide binding and release by proteins implicated as catalysts of protein assembly

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.10.5435

Phosphorylation of nucleoside diphosphate kinase at the active site studied by steady-state and time-resolved fluorescence

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.10.5435

21 January 2018

Identifiers

DOI

10.1074/JBC.273.10.5435

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12 February 2018

PubMed ID

9488662

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12 February 2018