(Q46253049)

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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

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scholarly article

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Europe PubMed Central

PubMed publication ID

20 December 2017

http://europepmc.org/abstract/MED/19001419

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 (English)

1 reference

Europe PubMed Central

PubMed publication ID

20 December 2017

http://europepmc.org/abstract/MED/19001419

protein folding

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object named as

Lei Wang

1

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object named as

Yi Liang

5

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author name string

Sheng-jian Li

2

1 reference

Europe PubMed Central

PubMed publication ID

20 December 2017

http://europepmc.org/abstract/MED/19001419

Ateesh Sidhu

3

1 reference

Europe PubMed Central

PubMed publication ID

20 December 2017

http://europepmc.org/abstract/MED/19001419

Li Zhu

4

1 reference

Europe PubMed Central

PubMed publication ID

20 December 2017

http://europepmc.org/abstract/MED/19001419

Robert B Freedman

6

1 reference

Europe PubMed Central

PubMed publication ID

20 December 2017

http://europepmc.org/abstract/MED/19001419

Chih-chen Wang

7

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Europe PubMed Central

PubMed publication ID

20 December 2017

http://europepmc.org/abstract/MED/19001419

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publication date

11 November 2008

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Europe PubMed Central

PubMed publication ID

20 December 2017

http://europepmc.org/abstract/MED/19001419

Journal of Biological Chemistry

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Europe PubMed Central

PubMed publication ID

20 December 2017

http://europepmc.org/abstract/MED/19001419

284

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Europe PubMed Central

PubMed publication ID

20 December 2017

http://europepmc.org/abstract/MED/19001419

1

1 reference

Europe PubMed Central

PubMed publication ID

20 December 2017

http://europepmc.org/abstract/MED/19001419

199-206

1 reference

Europe PubMed Central

PubMed publication ID

20 December 2017

http://europepmc.org/abstract/MED/19001419

Conservation and diversity of the cellular disulfide bond formation pathways.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M806645200

21 January 2018

Protein disulfide isomerases exploit synergy between catalytic and specific binding domains

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M806645200

21 January 2018

The human protein disulphide isomerase family: substrate interactions and functional properties

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M806645200

21 January 2018

The crystal structure of yeast protein disulfide isomerase suggests cooperativity between its active sites

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M806645200

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.M806645200

21 January 2018

Both the isomerase and chaperone activities of protein disulfide isomerase are required for the reactivation of reduced and denatured acidic phospholipase A2.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M806645200

21 January 2018

S-nitrosylated protein-disulphide isomerase links protein misfolding to neurodegeneration

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M806645200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M806645200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M806645200

21 January 2018

Ero1 and redox homeostasis in the endoplasmic reticulum.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M806645200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M806645200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M806645200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M806645200

21 January 2018

Two conserved cysteine triads in human Ero1alpha cooperate for efficient disulfide bond formation in the endoplasmic reticulum

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M806645200

21 January 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://api.crossref.org/works/10.1074%2FJBC.M806645200

21 January 2018

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M806645200

21 January 2018

Generating disulfides enzymatically: reaction products and electron acceptors of the endoplasmic reticulum thiol oxidase Ero1p

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M806645200

21 January 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://api.crossref.org/works/10.1074%2FJBC.M806645200

21 January 2018

Crystal structure of human ERp44 shows a dynamic functional modulation by its carboxy-terminal tail

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M806645200

21 January 2018

The FAD- and O(2)-dependent reaction cycle of Ero1-mediated oxidative protein folding in the endoplasmic reticulum

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M806645200

21 January 2018

Biochemical basis of oxidative protein folding in the endoplasmic reticulum

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M806645200

21 January 2018

Crystal structure of the bb' domains of the protein disulfide isomerase ERp57

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M806645200

21 January 2018

Protein disulfide isomerase: the structure of oxidative folding

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M806645200

21 January 2018

TROSY-NMR reveals interaction between ERp57 and the tip of the calreticulin P-domain

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M806645200

21 January 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://api.crossref.org/works/10.1074%2FJBC.M806645200

21 January 2018

Domain architecture of protein-disulfide isomerase facilitates its dual role as an oxidase and an isomerase in Ero1p-mediated disulfide formation.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M806645200

21 January 2018

The b' domain provides the principal peptide-binding site of protein disulfide isomerase but all domains contribute to binding of misfolded proteins

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M806645200

21 January 2018

Domains b' and a' of protein disulfide isomerase fulfill the minimum requirement for function as a subunit of prolyl 4-hydroxylase. The N-terminal domains a and b enhances this function and can be substituted in part by those of ERp57.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M806645200

21 January 2018

Catalysis of disulfide bond formation and isomerization in the Escherichia coli periplasm

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M806645200

21 January 2018

The role of glutathione in disulphide bond formation and endoplasmic-reticulum-generated oxidative stress.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M806645200

21 January 2018

Oxidized redox state of glutathione in the endoplasmic reticulum

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M806645200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M806645200

21 January 2018

Protein Disulfide Isomerase Acts as a Redox-Dependent Chaperone to Unfold Cholera Toxin

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M806645200

21 January 2018

Identifiers

10.1074/JBC.M806645200

1 reference

Europe PubMed Central

PubMed publication ID

20 December 2017

http://europepmc.org/abstract/MED/19001419

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

20 December 2017

http://europepmc.org/abstract/MED/19001419

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