(Q27653763)

7

0 references

Atsushi Nakagawa

object named as

Atsushi Nakagawa

3

0 references

Kenji Inaba

object named as

Kenji Inaba

1

0 references

author name string

Hiroka Iida

4

0 references

Mai Kinjo

5

0 references

Koreaki Ito

Conformational transition of Sec machinery inferred from bacterial SecYE structures

6

0 references

language of work or name

English

0 references

publication date

18 March 2009

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published in

The EMBO Journal

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volume

28

0 references

issue

6

0 references

page(s)

779-91

0 references

cites work

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2666032

NMR solution structure of the integral membrane enzyme DsbB: functional insights into DsbB-catalyzed disulfide bond formation

20 March 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2666032

Preparation and structure of the charge-transfer intermediate of the transmembrane redox catalyst DsbB

20 March 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2666032

A pathway for disulfide bond formation in vivo

20 March 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2666032

Two cysteines in each periplasmic domain of the membrane protein DsbB are required for its function in protein disulfide bond formation

20 March 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2666032

Coot: model-building tools for molecular graphics

20 March 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2666032

The CCP4 suite: programs for protein crystallography

20 March 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2666032

Improved methods for building protein models in electron density maps and the location of errors in these models

20 March 2017

2 references

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2666032

20 March 2017

https://api.crossref.org/works/10.1038/EMBOJ.2009.21

The disulfide bond formation (Dsb) system

22 April 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2666032

Mutants in DsbB that appear to redirect oxidation through the disulfide isomerization pathway

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2666032

Structure and mechanisms of the DsbB-DsbA disulfide bond generation machine.

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2666032

The name's bond......disulfide bond

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2666032

Redox-active cysteines of a membrane electron transporter DsbD show dual compartment accessibility

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2666032

Critical role of a thiolate-quinone charge transfer complex and its adduct form in de novo disulfide bond generation by DsbB.

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2666032

Protein disulfide bond formation in prokaryotes

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2666032

Formation and transfer of disulphide bonds in living cells

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2666032

Four cysteines of the membrane protein DsbB act in concert to oxidize its substrate DsbA.

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2666032

Roles of a conserved arginine residue of DsbB in linking protein disulfide-bond-formation pathway to the respiratory chain of Escherichia coli

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2666032

Respiratory chain is required to maintain oxidized states of the DsbA-DsbB disulfide bond formation system in aerobically growing Escherichia coli cells

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2666032

Characterization of new DsbB-like thiol-oxidoreductases of Campylobacter jejuni and Helicobacter pylori and classification of the DsbB family based on phylogenomic, structural and functional criteria

29 September 2017

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2666032

Respiratory chain strongly oxidizes the CXXC motif of DsbB in the Escherichia coli disulfide bond formation pathway

2 June 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2666032

Why is DsbA such an oxidizing disulfide catalyst?

2 June 2018

1 reference

https://api.crossref.org/works/10.1038%2FEMBOJ.2009.21

Crystal structure of the DsbB-DsbA complex reveals a mechanism of disulfide bond generation.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FEMBOJ.2009.21

DsbB elicits a red-shift of bound ubiquinone during the catalysis of DsbA oxidation.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FEMBOJ.2009.21

Reactivities of quinone-free DsbB from Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FEMBOJ.2009.21

Environment of the active site region of RseP, an Escherichia coli regulated intramembrane proteolysis protease, assessed by site-directed cysteine alkylation.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FEMBOJ.2009.21

Characterization of the menaquinone-dependent disulfide bond formation pathway of Escherichia coli.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FEMBOJ.2009.21

Role of the cytosolic loop of DsbB in catalytic turnover of the ubiquinone-DsbB complex.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FEMBOJ.2009.21

Partial (13)C and (15)N chemical-shift assignments of the disulfide-bond-forming enzyme DsbB by 3D magic-angle spinning NMR spectroscopy

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FEMBOJ.2009.21

Disulfide bonds are generated by quinone reduction

21 January 2018

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/19214188

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Processing of X-ray diffraction data collected in oscillation mode

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/19214188