(Q33959594)

30 July 2017

Hsc62, Hsc56, and GrpE, the third Hsp70 chaperone system of Escherichia coli (English)

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30 July 2017

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Kazuaki Yoshimune

1

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30 July 2017

Tohru Yoshimura

2

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30 July 2017

Toru Nakayama

3

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30 July 2017

Tokuzo Nishino

4

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30 July 2017

Nobuyoshi Esaki

5

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30 July 2017

language of work or name

English

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publication date

1 May 2002

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Biochemical and Biophysical Research Communications

30 July 2017

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30 July 2017

293

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30 July 2017

5

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30 July 2017

1389-1395

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30 July 2017

The heat-shock response

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https://api.crossref.org/works/10.1016%2FS0006-291X%2802%2900403-5

Trigger factor and DnaK cooperate in folding of newly synthesized proteins.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0006-291X%2802%2900403-5

Polypeptide flux through bacterial Hsp70: DnaK cooperates with trigger factor in chaperoning nascent chains

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0006-291X%2802%2900403-5

Substrate specificity of the SecB chaperone

7 January 2021

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https://api.crossref.org/works/10.1016%2FS0006-291X%2802%2900403-5

Monomerization of RepA dimers by heat shock proteins activates binding to DNA replication origin

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0006-291X%2802%2900403-5

DnaK, DnaJ, and GrpE heat shock proteins negatively regulate heat shock gene expression by controlling the synthesis and stability of sigma 32.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0006-291X%2802%2900403-5

The yeast hsp70 homologue Ssa is required for translation and interacts with Sis1 and Pab1 on translating ribosomes

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0006-291X%2802%2900403-5

Protein folding activity of Hsp70 is modified differentially by the hsp40 co-chaperones Sis1 and Ydj1.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0006-291X%2802%2900403-5

The membrane-bound DnaJ protein located at the cytosolic site of glyoxysomes specifically binds the cytosolic isoform 1 of Hsp70 but not other Hsp70 species

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0006-291X%2802%2900403-5

Dynamic interplay between antagonistic pathways controlling the sigma 32 level in Escherichia coli

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0006-291X%2802%2900403-5

Levels of DnaK and DnaJ provide tight control of heat shock gene expression and protein repair in Escherichia coli.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0006-291X%2802%2900403-5

Activity of the Hsp70 chaperone complex--DnaK, DnaJ, and GrpE--in initiating phage lambda DNA replication by sequestering and releasing lambda P protein

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0006-291X%2802%2900403-5

The requirement for molecular chaperones in lambda DNA replication is reduced by the mutation pi in lambda P gene, which weakens the interaction between lambda P protein and DnaB helicase

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0006-291X%2802%2900403-5

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0006-291X%2802%2900403-5

J proteins catalytically activate Hsp70 molecules to trap a wide range of peptide sequences

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0006-291X%2802%2900403-5

Kinetic characterization of the ATPase cycle of the DnaK molecular chaperone

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0006-291X%2802%2900403-5

Assembly of iron-sulfur clusters. Identification of an iscSUA-hscBA-fdx gene cluster from Azotobacter vinelandii

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0006-291X%2802%2900403-5

The Fe/S assembly protein IscU behaves as a substrate for the molecular chaperone Hsc66 from Escherichia coli

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0006-291X%2802%2900403-5

Hsc62, a new DnaK homologue of Escherichia coli

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0006-291X%2802%2900403-5

Pre-steady-state kinetics of Escherichia coli aspartate aminotransferase catalyzed reactions and thermodynamic aspects of its substrate specificity

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0006-291X%2802%2900403-5

Specificity of DnaK-peptide binding

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0006-291X%2802%2900403-5

A general method for introducing a series of mutations into cloned DNA using the polymerase chain reaction

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0006-291X%2802%2900403-5

Phylogenetic analysis of the third hsp70 homolog in Escherichia coli; a novel member of the Hsc66 subfamily and its possible co-chaperone.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0006-291X%2802%2900403-5

Inferences concerning the ATPase properties of DnaK and other HSP70s are affected by the ADP kinase activity of copurifying nucleoside-diphosphate kinase.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0006-291X%2802%2900403-5

The role of ATP in the functional cycle of the DnaK chaperone system

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0006-291X%2802%2900403-5

Mutations in the DnaK chaperone affecting interaction with the DnaJ cochaperone.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0006-291X%2802%2900403-5

The Hsp70 and Hsp60 chaperone machines

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0006-291X%2802%2900403-5

Mechanism of regulation of hsp70 chaperones by DnaJ cochaperones

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0006-291X%2802%2900403-5

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.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0006-291X%2802%2900403-5

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

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0006-291X%2802%2900403-5

Interaction of the Hsp70 molecular chaperone, DnaK, with its cochaperone DnaJ.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0006-291X%2802%2900403-5

Tuning of chaperone activity of Hsp70 proteins by modulation of nucleotide exchange.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0006-291X%2802%2900403-5

The Hsc66-Hsc20 chaperone system in Escherichia coli: chaperone activity and interactions with the DnaK-DnaJ-grpE system.

7 January 2021

1 reference

https://api.crossref.org/works/10.1016%2FS0006-291X%2802%2900403-5

inferred from DOI database lookup

7 January 2021

based on heuristic

Identifiers

DOI

10.1016/S0006-291X(02)00403-5

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30 July 2017

1 reference