(Q41866614)

13 October 2017

Export chaperone SecB uses one surface of interaction for diverse unfolded polypeptide ligands (English)

1 reference

13 October 2017

0 references

Angela A Lilly

1

1 reference

13 October 2017

Jennine M Crane

series ordinal

2

1 reference

13 October 2017

Linda L Randall

series ordinal

3

1 reference

13 October 2017

1 September 2009

1 reference

13 October 2017

1 reference

13 October 2017

18

1 reference

13 October 2017

9

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13 October 2017

1860-1868

1 reference

Bacterial protein secretion through the translocase nanomachine

13 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2777361

Sites of interaction of a precursor polypeptide on the export chaperone SecB mapped by site-directed spin labeling

5 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2777361

SecB, one small chaperone in the complex milieu of the cell

5 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2777361

Structure of outer membrane protein A transmembrane domain by NMR spectroscopy

5 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2777361

Crystal structure of the bacterial protein export chaperone secB

5 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2777361

Calorimetric analyses of the interaction between SecB and its ligands

5 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2777361

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

5 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2777361

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

5 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2777361

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

5 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2777361

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

5 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2777361

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

5 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2777361

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

5 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2777361

The structure of protein-protein recognition sites

5 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2777361

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

5 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2777361

Asymmetric binding between SecA and SecB two symmetric proteins: implications for function in export.

5 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2777361

SecA membrane cycling at SecYEG is driven by distinct ATP binding and hydrolysis events and is regulated by SecD and SecF.

18 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2777361

SecA promotes preprotein translocation by undergoing ATP-driven cycles of membrane insertion and deinsertion.

18 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2777361

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

18 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2777361

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

18 August 2018

1 reference

12 December 2020

Kinetic partitioning. Poising SecB to favor association with a rapidly folding ligand

1 reference

12 December 2020

Mutational alterations in the homotetrameric chaperone SecB that implicate the structure as dimer of dimers

1 reference

12 December 2020

Mapping of the docking of SecA onto the chaperone SecB by site-directed spin labeling: insight into the mechanism of ligand transfer during protein export

1 reference

12 December 2020

Reconstitution of Purified Bacterial Preprotein Translocase in Liposomes

1 reference

12 December 2020

Identifiers

DOI

10.1002/PRO.197

1 reference

release_ehpxqxllona7nik2fakylmghwa

13 October 2017

1 reference

Fatcat

https://api.fatcat.wiki/v0/release/ehpxqxllona7nik2fakylmghwa

24 November 2022

mapped directly with Wikidata item

1 reference

13 October 2017

PubMed publication ID

19569227

1 reference