(Q38291165)

1 September 2017

title

Diverse effects of mutation on the activity of the Escherichia coli export chaperone SecB. (English)

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1 September 2017

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Kimsey HH

1

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1 September 2017

Dagarag MD

series ordinal

2

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1 September 2017

Kumamoto CA

series ordinal

3

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1 September 2017

language of work or name

English

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publication date

1 September 1995

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Journal of Biological Chemistry

1 September 2017

published in

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1 September 2017

volume

270

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1 September 2017

issue

39

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1 September 2017

page(s)

22831-22835

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

1 September 2017

cites work

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https://api.crossref.org/works/10.1074%2FJBC.270.39.22831

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.39.22831

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.39.22831

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.39.22831

Molecular chaperones and protein translocation across the Escherichia coli inner membrane

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.39.22831

Bacterial periplasmic transport systems: structure, mechanism, and evolution

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.39.22831

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.39.22831

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.39.22831

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.39.22831

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.39.22831

Characterization of the Escherichia coli protein-export gene secB.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.39.22831

Rapid and efficient site-specific mutagenesis without phenotypic selection

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.39.22831

The use of native T7 DNA polymerase for site-directed mutagenesis

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.39.22831

Mutations which alter the function of the signal sequence of the maltose binding protein of Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.39.22831

Export of the periplasmic maltose-binding protein of Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.39.22831

Escherichia coli SecB protein associates with exported protein precursors in vivo

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.39.22831

prlA suppression of defective export of maltose-binding protein in secB mutants of Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.39.22831

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

https://api.crossref.org/works/10.1074%2FJBC.270.39.22831

The foreign antigen binding site and T cell recognition regions of class I histocompatibility antigens

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.39.22831

21 January 2018

Identifiers

DOI

10.1074/JBC.270.39.22831

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1 September 2017

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