(Q54610165)

1 June 2018

title

Calf thymus Hsc70 protein protects and reactivates prokaryotic and eukaryotic enzymes. (English)

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1 June 2018

author name string

Ziemienowicz A

1

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1 June 2018

Zylicz M

2

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1 June 2018

Floth C

3

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1 June 2018

Hübscher U

4

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1 June 2018

language of work or name

English

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publication date

1 June 1995

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1 June 2018

Journal of Biological Chemistry

published in

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1 June 2018

volume

270

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1 June 2018

page(s)

15479-15484

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1 June 2018

issue

26

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1 June 2018

cites work

The heat-shock response

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.26.15479

Protein folding in the cell: the role of molecular chaperones Hsp70 and Hsp60

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.26.15479

Molecular chaperone functions of heat-shock proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.26.15479

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.270.26.15479

The translation machinery and 70 kd heat shock protein cooperate in protein synthesis

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.26.15479

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.270.26.15479

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.270.26.15479

Reconstitution of protein translocation from solubilized yeast membranes reveals topologically distinct roles for BiP and cytosolic Hsc70.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.26.15479

Requirement for hsp70 in the mitochondrial matrix for translocation and folding of precursor proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.26.15479

70K heat shock related proteins stimulate protein translocation into microsomes.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.26.15479

A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.26.15479

Speculations on the functions of the major heat shock and glucose-regulated proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.26.15479

Uncoating ATPase is a member of the 70 kilodalton family of stress proteins.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.26.15479

DnaJ, DnaK, and GrpE heat shock proteins are required in oriP1 DNA replication solely at the RepA monomerization step

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.26.15479

The E. coli dnaK gene product, the hsp70 homolog, can reactivate heat-inactivated RNA polymerase in an ATP hydrolysis-dependent manner

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.26.15479

Procedure for the rapid, large-scale purification of Escherichia coli DNA-dependent RNA polymerase involving polymin P precipitation and DNA-cellulose chromatography

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.26.15479

Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.26.15479

Secondary structure of the mammalian 70-kilodalton heat shock cognate protein analyzed by circular dichroism spectroscopy and secondary structure prediction.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.26.15479

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.270.26.15479

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.26.15479

Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.26.15479

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.270.26.15479

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.270.26.15479

Peptide-binding specificity of the molecular chaperone BiP

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.26.15479

21 January 2018

Identifiers

DOI

10.1074/JBC.270.26.15479

1 reference

Fatcat

https://api.fatcat.wiki/v0/release/tkxvw5bj5nhylojvetbp2dtrmq

mapped directly with Wikidata item

30 July 2022

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Fatcat ID

release_tkxvw5bj5nhylojvetbp2dtrmq

1 reference

Fatcat

https://api.fatcat.wiki/v0/release/tkxvw5bj5nhylojvetbp2dtrmq

mapped directly with Wikidata item

30 July 2022

based on heuristic

1 reference

https://api.fatcat.wiki/v0/release/tkxvw5bj5nhylojvetbp2dtrmq