(Q36280993)

13 August 2017

Calorimetric analyses of the interaction between SecB and its ligands (English)

1 reference

13 August 2017

L L Randall

1

1 reference

13 August 2017

T B Topping

series ordinal

2

1 reference

13 August 2017

D Suciu

series ordinal

3

1 reference

13 August 2017

S J Hardy

series ordinal

4

1 reference

13 August 2017

1 May 1998

1 reference

13 August 2017

1 reference

13 August 2017

7

1 reference

13 August 2017

5

1 reference

13 August 2017

1195-1200

1 reference

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

13 August 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144013

Electrospray mass spectrometric investigation of the chaperone SecB.

30 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144013

Folding of maltose-binding protein. Evidence for the identity of the rate-determining step in vivo and in vitro

30 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144013

SecB: a molecular chaperone of Escherichia coli protein secretion pathway

30 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144013

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

30 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144013

In vivo studies of the role of SecA during protein export in Escherichia coli

30 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144013

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

30 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144013

Rapid measurement of binding constants and heats of binding using a new titration calorimeter

30 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144013

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

30 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144013

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

30 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144013

Three pure chaperone proteins of Escherichia coli--SecB, trigger factor and GroEL--form soluble complexes with precursor proteins in vitro

30 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144013

SecB-independent export of Escherichia coli ribose-binding protein (RBP): some comparisons with export of maltose-binding protein (MBP) and studies with RBP-MBP hybrid proteins

30 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144013

The folding properties of the Escherichia coli maltose-binding protein influence its interaction with SecB in vitro

30 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144013

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

30 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144013

Molecular chaperones and protein translocation across the Escherichia coli inner membrane

30 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144013

Synthesis of Exported Proteins by Membrane-Bound Polysomes from Escherichia coli

30 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144013

Chaperone SecB from Escherichia coli mediates kinetic partitioning via a dynamic equilibrium with its ligands.

30 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144013

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

29 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144013

Retardation of folding as a possible means of suppression of a mutation in the leader sequence of an exported protein.

29 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144013

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

29 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144013

Biogenesis of outer membrane protein PhoE of Escherichia coli. Evidence for multiple SecB-binding sites in the mature portion of the PhoE protein

29 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144013

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

29 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144013

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

22 September 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2144013

Influence of the signal sequence and chaperone SecB on the interaction between precursor protein prePhoE and phospholipids

22 September 2018

1 reference

12 December 2020

Purification and characterization of leader (signal) peptidase from Escherichia coli

1 reference

12 December 2020

The synthesis of export-defective proteins can interfere with normal protein export in Escherichia coli

1 reference

12 December 2020

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

1 reference

12 December 2020

Identifiers

DOI

10.1002/PRO.5560070514

1 reference

13 August 2017

1 reference

13 August 2017

PubMed publication ID

9605324

1 reference