(Q34467548)

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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).

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Europe PubMed Central

PubMed publication ID

2 August 2017

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

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

endoplasmic reticulum

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object named as

Lei Wang

6

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author name string

Lihui Zhang

1

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

Yingbo Niu

2

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

Li Zhu

3

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

Jingqi Fang

4

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

Xi'e Wang

5

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Europe PubMed Central

PubMed publication ID

2 August 2017

Chih-chen Wang

7

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Europe PubMed Central

PubMed publication ID

2 August 2017

language of work or name

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publication date

25 September 2014

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Europe PubMed Central

PubMed publication ID

2 August 2017

number of pages

12

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Journal of Biological Chemistry

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Europe PubMed Central

PubMed publication ID

2 August 2017

289

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

45

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

31188-31199

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

Redox controls UPR to control redox

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4223321

6 July 2018

Inactivation of mammalian Ero1α is catalysed by specific protein disulfide-isomerases

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4223321

6 July 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4223321

6 July 2018

Glutathione peroxidase 7 utilizes hydrogen peroxide generated by Ero1α to promote oxidative protein folding

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4223321

6 July 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4223321

6 July 2018

Balanced Ero1 activation and inactivation establishes ER redox homeostasis

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4223321

6 July 2018

Structure, mechanism, and evolution of Ero1 family enzymes.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4223321

6 July 2018

Multiple ways to make disulfides

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4223321

6 July 2018

Functional in vitro analysis of the ERO1 protein and protein-disulfide isomerase pathway

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4223321

6 July 2018

The sarcoplasmic reticulum luminal thiol oxidase ERO1 regulates cardiomyocyte excitation-coupled calcium release and response to hemodynamic load

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4223321

6 July 2018

Inhibitors of protein disulfide isomerase suppress apoptosis induced by misfolded proteins

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4223321

6 July 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4223321

6 July 2018

Disulphide production by Ero1α-PDI relay is rapid and effectively regulated

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4223321

6 July 2018

Vitamin K epoxide reductase prefers ER membrane-anchored thioredoxin-like redox partners

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4223321

6 July 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4223321

6 July 2018

Plasticity of human protein disulfide isomerase: evidence for mobility around the X-linker region and its functional significance

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4223321

6 July 2018

Oxidative activity of yeast Ero1p on protein disulfide isomerase and related oxidoreductases of the endoplasmic reticulum

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4223321

6 July 2018

Domain a' of protein disulfide isomerase plays key role in inhibiting alpha-synuclein fibril formation

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4223321

6 July 2018

Protein disulphide isomerase family members show distinct substrate specificity: P5 is targeted to BiP client proteins.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4223321

6 July 2018

Protein disulfide isomerase: a critical evaluation of its function in disulfide bond formation

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4223321

6 July 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4223321

6 July 2018

Alternative conformations of the x region of human protein disulphide-isomerase modulate exposure of the substrate binding b' domain

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4223321

6 July 2018

Ero1 and redox homeostasis 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=4223321

6 July 2018

In vivo reduction-oxidation state of protein disulfide isomerase: the two active sites independently occur in the reduced and oxidized forms

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4223321

6 July 2018

Dynamic retention of Ero1alpha and Ero1beta in the endoplasmic reticulum by interactions with PDI and ERp44.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4223321

6 July 2018

Role of protein disulfide isomerase and other thiol-reactive proteins in HIV-1 envelope protein-mediated fusion.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4223321

6 July 2018

Annular arrangement and collaborative actions of four domains of protein-disulfide isomerase: a small angle X-ray scattering study in solution

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4223321

6 July 2018

The contributions of protein disulfide isomerase and its homologues to oxidative protein folding in the yeast endoplasmic reticulum

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4223321

6 July 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4223321

6 July 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4223321

6 July 2018

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=4223321

6 July 2018

Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: dependence of the rate on the composition of the redox buffer

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4223321

6 July 2018

Reexamination of the folding of BPTI: predominance of native intermediates.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=4223321

6 July 2018

Manipulating disulfide bond formation and 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=4223321

6 July 2018

Low reduction potential of Ero1alpha regulatory disulphides ensures tight control of substrate oxidation.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M114.602961

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M114.602961

21 January 2018

Molecular characterization of the principal substrate binding site of the ubiquitous folding catalyst protein disulfide isomerase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M114.602961

21 January 2018

Sulfhydryl oxidation, not disulfide isomerization, is the principal function of protein disulfide isomerase in yeast Saccharomyces cerevisiae

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M114.602961

21 January 2018

Formation and isomerization of disulfide bonds in proteins: protein disulfide-isomerase

1 reference

https://pubmed.ncbi.nlm.nih.gov/25258311

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Structure-function analysis of human protein Ero1-Lalpha

1 reference

https://pubmed.ncbi.nlm.nih.gov/25258311

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/25258311

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1074/JBC.M114.602961

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

PMC publication ID

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

2 August 2017

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