Divergent effects of ATP on the binding of the DnaK and DnaJ chaperones to each other, or to their various native and denatured protein substrates. (Q54606140)

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English	Divergent effects of ATP on the binding of the DnaK and DnaJ chaperones to each other, or to their various native and denatured protein substrates.	scientific article

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scholarly article

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Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7642605

Divergent effects of ATP on the binding of the DnaK and DnaJ chaperones to each other, or to their various native and denatured protein substrates. (English)

1 reference

Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7642605

molecular chaperones

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2

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Zylicz M

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Europe PubMed Central

PubMed publication ID

1 June 2018

author name string

Wawrzynów A

1

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Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7642605

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publication date

1 August 1995

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Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7642605

Journal of Biological Chemistry

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Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7642605

270

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Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7642605

33

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Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7642605

19300-19306

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Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7642605

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

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

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

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

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21 January 2018

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

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21 January 2018

Physical interaction between heat shock proteins DnaK, DnaJ, and GrpE and the bacterial heat shock transcription factor sigma 32

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21 January 2018

Protein folding in the cell

1 reference

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21 January 2018

Specificity of DnaK-peptide binding

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21 January 2018

Molecular chaperone functions of heat-shock proteins

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21 January 2018

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

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Regulation of the specific DNA binding function of p53

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

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21 January 2018

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

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21 January 2018

Autoregulation of the Escherichia coli heat shock response by the DnaK and DnaJ heat shock proteins

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21 January 2018

The DnaK chaperone modulates the heat shock response of Escherichia coli by binding to the sigma 32 transcription factor

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21 January 2018

Thermodynamic and structural analysis of the folding/unfolding transitions of the Escherichia coli molecular chaperone DnaK.

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21 January 2018

How do polypeptides cross the mitochondrial membranes?

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21 January 2018

Interaction of hsp70 with unfolded proteins: effects of temperature and nucleotides on the kinetics of binding

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21 January 2018

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

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21 January 2018

Conformational change of chaperone Hsc70 upon binding to a decapeptide: a circular dichroism study

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21 January 2018

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

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21 January 2018

Kinetics of molecular chaperone action

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21 January 2018

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

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21 January 2018

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

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

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

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

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Regulation of the heat-shock response in bacteria

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The Escherichia coli chaperones involved in DNA replication

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The dnaK protein of Escherichia coli possesses an ATPase and autophosphorylating activity and is essential in an in vitro DNA replication system

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Peptide-binding specificity of the molecular chaperone BiP

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Function of DnaJ and DnaK as chaperones in origin-specific DNA binding by RepA

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Heat shock proteins and molecular chaperones: mediators of protein conformation and turnover in the cell

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Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK

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ATP hydrolysis is required for the DnaJ-dependent activation of DnaK chaperone for binding to both native and denatured protein substrates

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21 January 2018

Identifiers

10.1074/JBC.270.33.19300

1 reference

Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7642605

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

1 June 2018

http://europepmc.org/abstract/MED/7642605

ResearchGate publication ID

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