(Q41904736)

13 October 2017

Characterization of three areas of interactions stabilizing complexes between SecA and SecB, two proteins involved in protein export (English)

1 reference

13 October 2017

Chetan N Patel

1

1 reference

13 October 2017

Virginia F Smith

series ordinal

2

1 reference

13 October 2017

Linda L Randall

series ordinal

3

1 reference

13 October 2017

1 June 2006

1 reference

13 October 2017

1 reference

13 October 2017

15

1 reference

13 October 2017

6

1 reference

13 October 2017

1379-1386

1 reference

SecA dimer cross-linked at its subunit interface is functional for protein translocation

13 October 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2265093

Identification of the preprotein binding domain of SecA.

5 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2265093

Dimeric SecA is essential for protein translocation

5 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2265093

A large conformational change of the translocation ATPase SecA

5 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2265093

Structural determinants of SecB recognition by SecA in bacterial protein translocation

5 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2265093

Nucleotide control of interdomain interactions in the conformational reaction cycle of SecA

5 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2265093

Dissociation of the dimeric SecA ATPase during protein translocation across the bacterial membrane

5 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2265093

Complex behavior in solution of homodimeric SecA.

5 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2265093

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=2265093

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=2265093

Topology of the integral membrane form of Escherichia coli SecA protein reveals multiple periplasmically exposed regions and modulation by ATP 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=2265093

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=2265093

Electrospray mass spectrometric investigation of 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=2265093

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=2265093

Protein-protein interactions: a review of protein dimer structures

5 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2265093

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=2265093

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=2265093

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=2265093

Principles of protein-protein recognition

5 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2265093

Covalently dimerized SecA is functional in protein translocation

5 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2265093

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

18 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2265093

The bacterial ATPase SecA functions as a monomer in protein translocation.

18 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2265093

Sites of interaction between SecA and the chaperone SecB, two proteins involved in export

18 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2265093

Allosteric communication between signal peptides and the SecA protein DEAD motor ATPase domain.

18 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2265093

Zinc stabilizes the SecB binding site of SecA.

18 August 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2265093

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=2265093

Isokinetic relationship, isoequilibrium relationship, and enthalpy-entropy compensation

18 August 2018

1 reference

12 December 2020

Identification of the zinc ligands in cobalamin-independent methionine synthase (MetE) from Escherichia coli

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

A highly mobile C-terminal tail of the Escherichia coli protein export chaperone SecB

1 reference

12 December 2020

Complexes between protein export chaperone SecB and SecA. Evidence for separate sites on SecA providing binding energy and regulatory interactions

1 reference

12 December 2020

Tyr-326 plays a critical role in controlling SecA-preprotein interaction

1 reference

12 December 2020

Determination of a region in SecA that interacts with presecretory proteins in Escherichia coli

1 reference

12 December 2020

Direct calorimetric analysis of the enzymatic activity of yeast cytochrome c oxidase

1 reference

12 December 2020

Enthalpy and heat capacity changes for the proton dissociation of various buffer components in 0.1 M potassium chloride

1 reference

12 December 2020

Identifiers

DOI

10.1110/PS.062141006

1 reference

13 October 2017

1 reference

13 October 2017

PubMed publication ID

16731972

1 reference