(Q24550637)

English

Two pairs of conserved cysteines are required for the oxidative activity of Ero1p in protein disulfide bond formation in the endoplasmic reticulum

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scholarly article

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Two pairs of conserved cysteines are required for the oxidative activity of Ero1p in protein disulfide bond formation in the endoplasmic reticulum (English)

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endoplasmic reticulum

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ER oxidoreductin YML130C

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GOA release 2020-03-11

author name string

A R Frand

1

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C A Kaiser

2

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language of work or name

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publication date

September 2000

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Molecular Biology of the Cell

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11

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9

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2833-43

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ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=14959

24 March 2017

A pathway for disulfide bond formation in vivo

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=14959

24 March 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=14959

24 March 2017

2.8-A structure of yeast serine carboxypeptidase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=14959

24 March 2017

Convergent evolution of similar function in two structurally divergent enzymes

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=14959

24 March 2017

A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=14959

24 March 2017

Ero1p: a novel and ubiquitous protein with an essential role in oxidative protein folding in the endoplasmic reticulum

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=14959

24 March 2017

The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=14959

24 March 2017

Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=14959

24 March 2017

Pathways for protein disulphide bond formation

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=14959

24 March 2017

Thioredoxin--a fold for all reasons

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=14959

7 April 2017

Yeast Saccharomyces cerevisiae selectable markers in pUC18 polylinkers

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=14959

7 April 2017

Electron avenue: pathways of disulfide bond formation and isomerization

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=14959

27 September 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=14959

27 September 2017

Mutants in disulfide bond formation that disrupt flagellar assembly in Escherichia coli

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=14959

27 September 2017

The essential function of yeast protein disulfide isomerase does not reside in its isomerase activity

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=14959

27 September 2017

Identification and characterization of the Escherichia coli gene dsbB, whose product is involved in the formation of disulfide bonds in vivo

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=14959

27 September 2017

Evidence that the pathway of disulfide bond formation in Escherichia coli involves interactions between the cysteines of DsbB and DsbA

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=14959

27 September 2017

The essential function of protein-disulfide isomerase is to unscramble non-native disulfide bonds.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=14959

27 September 2017

Recent developments in the field of iron-sulfur proteins.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=14959

27 September 2017

Efficient site-directed mutagenesis using uracil-containing DNA.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=14959

27 September 2017

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=14959

30 May 2018

Overproduction of Mpd2p suppresses the lethality of protein disulfide isomerase depletion in a CXXC sequence dependent manner.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=14959

30 May 2018

Active site mutations in yeast protein disulfide isomerase cause dithiothreitol sensitivity and a reduced rate of protein folding in the endoplasmic reticulum

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=14959

30 May 2018

Determination of the reduction-oxidation potential of the thioredoxin-like domains of protein disulfide-isomerase from the equilibrium with glutathione and thioredoxin.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=14959

30 May 2018

Determination of the sequence of the yeast YCL313 gene localized on chromosome III. Homology with the protein disulfide isomerase (PDI gene product) of other organisms

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=14959

30 May 2018

Identification of a protein required for disulfide bond formation in vivo.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=14959

30 May 2018

Identification of the three-dimensional thioredoxin motif: related structure in the ORF3 protein of the Staphylococcus aureus mer operon

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=14959

30 May 2018

Roles of cysteine residues of DsbB in its activity to reoxidize DsbA, the protein disulphide bond catalyst of Escherichia coli.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=14959

30 May 2018

The CXXC motif: a rheostat in the active site.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=14959

28 November 2018

Why is DsbA such an oxidizing disulfide catalyst?

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=14959

28 November 2018

Selective retention of secretory proteins in the yeast endoplasmic reticulum by treatment of cells with a reducing agent

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=14959

28 November 2018

Protein oxidation: prime suspect found 'not guilty'

1 reference

https://pubmed.ncbi.nlm.nih.gov/10982384

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

DsbA-DsbB interaction through their active site cysteines. Evidence from an odd cysteine mutant of DsbA

1 reference

https://pubmed.ncbi.nlm.nih.gov/10982384

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

A stable mixed disulfide between thioredoxin reductase and its substrate, thioredoxin: preparation and characterization

1 reference

https://pubmed.ncbi.nlm.nih.gov/10982384

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Scanning and escape during protein-disulfide isomerase-assisted protein folding

1 reference

https://pubmed.ncbi.nlm.nih.gov/10982384

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Competition between glutathione and protein thiols for disulphide-bond formation

1 reference

https://pubmed.ncbi.nlm.nih.gov/10982384

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Reconstitution of a protein disulfide catalytic system

1 reference

https://pubmed.ncbi.nlm.nih.gov/10982384

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Biochemistry, cell biology and molecular biology of lipids of Saccharomyces cerevisiae

1 reference

https://pubmed.ncbi.nlm.nih.gov/10982384

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Oxidative protein folding is driven by the electron transport system

1 reference

https://pubmed.ncbi.nlm.nih.gov/10982384

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Ero1p oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulum

1 reference

https://pubmed.ncbi.nlm.nih.gov/10982384

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1091/MBC.11.9.2833

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