(Q30815173)

26 June 2017

title

Substrate specificity of the SecB chaperone (English)

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26 June 2017

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Knoblauch NT

1

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26 June 2017

Rüdiger S

2

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26 June 2017

Schönfeld HJ

3

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26 June 2017

Driessen AJ

4

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26 June 2017

Schneider-Mergener J

5

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26 June 2017

Bukau B

6

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26 June 2017

language of work or name

English

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publication date

1 November 1999

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Journal of Biological Chemistry

26 June 2017

published in

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26 June 2017

volume

274

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26 June 2017

issue

48

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26 June 2017

page(s)

34219-34225

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High selectivity with low specificity: how SecB has solved the paradox of chaperone binding

26 June 2017

cites work

1 reference

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Growing up in a dangerous environment: a network of multiple targeting and folding pathways for nascent polypeptides in the cytosol

21 January 2018

1 reference

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SecB protein: a cytosolic export factor that associates with nascent exported proteins

21 January 2018

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How proteins cross the bacterial cytoplasmic membrane.

21 January 2018

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Correlation of competence for export with lack of tertiary structure of the mature species: a study in vivo of maltose-binding protein in E. coli

21 January 2018

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The antifolding activity of SecB promotes the export of the E. coli maltose-binding protein

21 January 2018

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The binding cascade of SecB to SecA to SecY/E mediates preprotein targeting to the E. coli plasma membrane

21 January 2018

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Sec-dependent preprotein translocation in bacteria.

21 January 2018

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Highly selective binding of nascent polypeptides by an Escherichia coli chaperone protein in vivo

21 January 2018

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

21 January 2018

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Transient association of newly synthesized unfolded proteins with the heat-shock GroEL protein.

21 January 2018

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Involvement of the DnaK-DnaJ-GrpE chaperone team in protein secretion in Escherichia coli

21 January 2018

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SecB functions as a cytosolic signal recognition factor for protein export in E. coli.

21 January 2018

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Purified secB protein of Escherichia coli retards folding and promotes membrane translocation of the maltose-binding protein in vitro

21 January 2018

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Genetic dissection of histone function

21 January 2018

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Electrospray mass spectrometric investigation of the chaperone SecB.

21 January 2018

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A kinetic partitioning model of selective binding of nonnative proteins by the bacterial chaperone SecB.

21 January 2018

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High-affinity binding of Escherichia coli SecB to the signal sequence region of a presecretory protein

21 January 2018

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Calorimetric analyses of the interaction between SecB and its ligands

21 January 2018

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Demonstration in vivo that interaction of maltose-binding protein with SecB is determined by a kinetic partitioning

21 January 2018

1 reference

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Physiological role during export for the retardation of folding by the leader peptide of maltose-binding protein

21 January 2018

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Modulation of folding pathways of exported proteins by the leader sequence

21 January 2018

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Diffusion-limited interaction between unfolded polypeptides and the Escherichia coli chaperone SecB.

21 January 2018

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Determination of the binding frame within a physiological ligand for the chaperone SecB.

21 January 2018

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Mapping of the Binding Frame for the Chaperone SecB within a Natural Ligand, Galactose-binding Protein

21 January 2018

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Determination of the binding frame of the chaperone SecB within the physiological ligand oligopeptide-binding protein

21 January 2018

1 reference

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Cytosolic factor purified from Escherichia coli is necessary and sufficient for the export of a preprotein and is a homotetramer of SecB

21 January 2018

1 reference

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Spot synthesis: observations and optimizations

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.48.34219

Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.48.34219

Role of the DnaK and HscA homologs of Hsp70 chaperones in protein folding in E.coli

21 January 2018

1 reference

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

21 January 2018

1 reference

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Substrate shuttling between the DnaK and GroEL systems indicates a chaperone network promoting protein folding.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.48.34219

Structure of the outer membrane protein A transmembrane domain

21 January 2018

1 reference

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Regulatory region C of the E. coli heat shock transcription factor, sigma32, constitutes a DnaK binding site and is conserved among eubacteria.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.48.34219

Zinc stabilizes the SecB binding site of SecA.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.48.34219

Interaction of Hsp70 chaperones with substrates

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.48.34219

The interaction between the chaperone SecB and its ligands: evidence for multiple subsites for binding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.48.34219

Binding of SecB to ribosome-bound polypeptides has the same characteristics as binding to full-length, denatured proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.48.34219

Refined 1.8-A structure reveals the mode of binding of beta-cyclodextrin to the maltodextrin binding protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.48.34219

Spot-synthesis: an easy technique for the positionally addressable, parallel chemical synthesis on a membrane support

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.48.34219

No specific recognition of leader peptide by SecB, a chaperone involved in protein export

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.48.34219

The mature portion of Escherichia coli maltose-binding protein (MBP) determines the dependence of MBP on SecB for export.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.48.34219

Folding of barnase in the presence of the molecular chaperone SecB

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.48.34219

Peptide Binding by Chaperone SecB: Implications for Recognition of Nonnative Structure

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.48.34219

Preprotein transfer to the Escherichia coli translocase requires the co‐operative binding of SecB and the signal sequence to SecA

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.48.34219

Mapping protein-protein contact sites using cellulose-bound peptide scans

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.274.48.34219

21 January 2018

Identifiers

DOI

10.1074/JBC.274.48.34219

1 reference

26 June 2017

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