Molecular analysis of human Ero1 reveals novel regulatory mechanisms for oxidative protein folding (Q93229413)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:30456358%20AND%20SRC:MED&resulttype=core&format=json

4 May 2020

title

Molecular analysis of human Ero1 reveals novel regulatory mechanisms for oxidative protein folding (English)

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4 May 2020

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4 May 2020

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4 May 2020

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4 May 2020

Kati Korhonen

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4 May 2020

publication date

26 June 2018

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4 May 2020

published in

Life Science Alliance

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4 May 2020

volume

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issue

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4 May 2020

page(s)

e201800090

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Creative Commons Attribution 4.0 International

4 May 2020

start time

1 June 2018

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April 2022 Public Data File from Crossref

copyrighted

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cites work

Biochemical evidence that regulation of Ero1β activity in human cells does not involve the isoform-specific cysteine 262.

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Human ER Oxidoreductin-1α (Ero1α) Undergoes Dual Regulation through Complementary Redox Interactions with Protein-Disulfide Isomerase.

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A PDI-catalyzed thiol-disulfide switch regulates the production of hydrogen peroxide by human Ero1.

11 February 2021

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Different interaction modes for protein-disulfide isomerase (PDI) as an efficient regulator and a specific substrate of endoplasmic reticulum oxidoreductin-1α (Ero1α).

11 February 2021

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Ero1-α and PDIs constitute a hierarchical electron transfer network of endoplasmic reticulum oxidoreductases

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Topological plasticity of enzymes involved in disulfide bond formation allows catalysis in either the periplasm or the cytoplasm

11 February 2021

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Order-disorder transitions govern kinetic cooperativity and allostery of monomeric human glucokinase

11 February 2021

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Hyperactivity of the Ero1α oxidase elicits endoplasmic reticulum stress but no broad antioxidant response

11 February 2021

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Functional in Vitro Analysis of the ERO1 Protein and Protein-disulfide Isomerase Pathway

11 February 2021

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Simple defined autoinduction medium for high-level recombinant protein production using T7-based Escherichia coli expression systems.

11 February 2021

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Reexamination of the Role of Interplay between Glutathione and Protein Disulfide Isomerase

11 February 2021

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Molecular bases of cyclic and specific disulfide interchange between human ERO1alpha protein and protein-disulfide isomerase (PDI).

11 February 2021

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Two endoplasmic reticulum PDI peroxidases increase the efficiency of the use of peroxide during disulfide bond formation

11 February 2021

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Pre-expression of a sulfhydryl oxidase significantly increases the yields of eukaryotic disulfide bond containing proteins expressed in the cytoplasm of E.coli

11 February 2021

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The endoplasmic reticulum sulfhydryl oxidase Ero1β drives efficient oxidative protein folding with loose regulation

11 February 2021

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Disruption of reducing pathways is not essential for efficient disulfide bond formation in the cytoplasm of E. coli

11 February 2021

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Crystal structures of human Ero1α reveal the mechanisms of regulated and targeted oxidation of PDI

11 February 2021

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11 February 2021

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The reduction potential of the active site disulfides of human protein disulfide isomerase limits oxidation of the enzyme by Ero1α.

11 February 2021

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11 February 2021

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Reconstitution of human Ero1-Lalpha/protein-disulfide isomerase oxidative folding pathway in vitro. Position-dependent differences in role between the a and a' domains of protein-disulfide isomerase

11 February 2021

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11 February 2021

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A novel disulphide switch mechanism in Ero1alpha balances ER oxidation in human cells

11 February 2021

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11 February 2021

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11 February 2021

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11 February 2021

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11 February 2021

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Modulation of Cellular Disulfide-Bond Formation and the ER Redox Environment by Feedback Regulation of Ero1

11 February 2021

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11 February 2021

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11 February 2021

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11 February 2021

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Glutathione is required to regulate the formation of native disulfide bonds within proteins entering the secretory pathway

11 February 2021

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A major fraction of endoplasmic reticulum-located glutathione is present as mixed disulfides with protein

11 February 2021

1 reference

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Defining the domain boundaries of the human protein disulfide isomerases.

11 February 2021

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=6238587

Manipulation of oxidative protein folding and PDI redox state in mammalian cells

11 February 2021

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=6238587

The CXXCXXC motif determines the folding, structure and stability of human Ero1-Lalpha

11 February 2021

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=6238587

Endoplasmic reticulum oxidoreductin 1-lbeta (ERO1-Lbeta), a human gene induced in the course of the unfolded protein response

11 February 2021

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=6238587

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

11 February 2021

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=6238587

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

11 February 2021

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=6238587

Spontaneous α-N-6-Phosphogluconoylation of a “His Tag” inEscherichia coli:The Cause of Extra Mass of 258 or 178 Da in Fusion Proteins

11 February 2021

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=6238587

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

11 February 2021

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=6238587

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

11 February 2021

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=6238587

Gene disruption in Escherichia coli: TcR and KmR cassettes with the option of Flp-catalyzed excision of the antibiotic-resistance determinant

11 February 2021

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=6238587

Oxidized redox state of glutathione in the endoplasmic reticulum

11 February 2021

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=6238587

11 February 2021

Identifiers

DOI

10.26508/LSA.201800090

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4 May 2020

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4 May 2020

PubMed publication ID

30456358

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:30456358%20AND%20SRC:MED&resulttype=core&format=json