The conserved G/F motif of the DnaJ chaperone is necessary for the activation of the substrate binding properties of the DnaK chaperone (Q38298937)

1 September 2017

title

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

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1 September 2017

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2

Zylicz M

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1 September 2017

Wall D

1

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1 September 2017

Georgopoulos C

series ordinal

3

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1 September 2017

language of work or name

English

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publication date

1 February 1995

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Journal of Biological Chemistry

1 September 2017

number of pages

6

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based on heuristic

inferred from page(s)

published in

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1 September 2017

volume

270

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1 September 2017

issue

5

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1 September 2017

page(s)

2139-2144

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

1 September 2017

cites work

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https://api.crossref.org/works/10.1074%2FJBC.270.5.2139

A module of the DnaJ heat shock proteins found in malaria parasites

21 January 2018

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

21 January 2018

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Regulation of the Escherichia coli heat-shock response.

21 January 2018

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Is hsp70 the cellular thermometer?

21 January 2018

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Topology and functional domains of Sec63p, an endoplasmic reticulum membrane protein required for secretory protein translocation

21 January 2018

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

21 January 2018

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Molecular chaperone functions of heat-shock proteins

21 January 2018

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

21 January 2018

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Regulation of the specific DNA binding function of p53

21 January 2018

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Mutations in a gene encoding a new Hsp70 suppress rapid DNA inversion and bgl activation, but not proU derepression, in hns-1 mutant Escherichia coli

21 January 2018

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

21 January 2018

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

21 January 2018

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

21 January 2018

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The Escherichia coli heat shock gene htpY: mutational analysis, cloning, sequencing, and transcriptional regulation

21 January 2018

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Improved tools for biological sequence comparison

21 January 2018

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Kinetics of molecular chaperone action

21 January 2018

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A gene encoding a DnaK/hsp70 homolog in Escherichia coli

21 January 2018

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Isolation and characterization of dnaJ null mutants of Escherichia coli

21 January 2018

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Heat shock of Escherichia coli increases binding of dnaK (the hsp70 homolog) to polypeptides by promoting its phosphorylation

21 January 2018

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Eukaryotic DnaJ homologs and the specificity of Hsp70 activity

21 January 2018

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

21 January 2018

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An analogue of the DnaJ molecular chaperone in Escherichia coli

21 January 2018

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Systematic sequencing of theEscherichia coligenome: analysis of the 0 – 2.4 min region

21 January 2018

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Regulation of the heat-shock response in bacteria

21 January 2018

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The Escherichia coli chaperones involved in DNA replication

21 January 2018

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Peptide-binding specificity of the molecular chaperone BiP

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.5.2139

The heat shock response of E. coli is regulated by changes in the concentration of σ32

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.5.2139

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.5.2139

21 January 2018

Identifiers

DOI

10.1074/JBC.270.5.2139

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1 September 2017

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