(Q24618046)

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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

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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 (English)

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2

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author name string

M Watanabe

series ordinal

1

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language of work or name

English

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publication date

April 1989

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published in

Proceedings of the National Academy of Sciences of the United States of America

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volume

86

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page(s)

2728-32

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issue

8

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cites work

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

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PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=286991

retrieved

7 April 2017

Mutations in a new gene, secB, cause defective protein localization in Escherichia coli

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stated in

PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=286991

retrieved

27 September 2017

In vitro translocation of bacterial proteins across the plasma membrane of Escherichia coli

1 reference

stated in

PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=286991

retrieved

27 September 2017

Protein export in Escherichia coli requires a soluble activity

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stated in

PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=286991

retrieved

27 September 2017

Soluble factors stimulating secretory protein translocation in bacteria and yeast can substitute for each other

1 reference

stated in

PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=286991

retrieved

27 September 2017

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

1 reference

stated in

PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=286991

retrieved

27 September 2017

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

1 reference

stated in

PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=286991

retrieved

27 September 2017

Binding of a soluble factor of Escherichia coli to preproteins does not require ATP and appears to be the first step in protein export

1 reference

stated in

PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=286991

retrieved

27 September 2017

In vitro synthesized bacterial outer membrane protein is integrated into bacterial inner membranes but translocated across microsomal membranes.

1 reference

stated in

PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=286991

retrieved

30 May 2018

Characterization of the Escherichia coli protein-export gene secB.

1 reference

stated in

PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=286991

retrieved

30 May 2018

Cell-free translation of messenger RNA in a wheat germ system.

1 reference

stated in

PubMed Central

reference URL

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=286991

retrieved

28 November 2018

Purification of the Escherichia coli secB gene product and demonstration of its activity in an in vitro protein translocation system

1 reference

stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/2649892

retrieved

12 December 2020

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Identifiers

DOI

10.1073/PNAS.86.8.2728

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ResearchGate publication ID

20506113

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(Q24618046)

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

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