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

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

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http://www.wikidata.org/entity/Q43142090

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2016 nî lūn-bûn

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2016年の論文

@ja

2016年学术文章

@wuu

2016年学术文章

@zh

2016年学术文章

@zh-cn

2016年学术文章

@zh-hans

2016年学术文章

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2016年学术文章

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2016年學術文章

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2016年學術文章

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name

Human ER Oxidoreductin-1α (Ero ...... h Protein-Disulfide Isomerase.

@en

Human ER Oxidoreductin-1α

@nl

type

Item

label

Human ER Oxidoreductin-1α (Ero ...... h Protein-Disulfide Isomerase.

@en

Human ER Oxidoreductin-1α

@nl

prefLabel

Human ER Oxidoreductin-1α (Ero ...... h Protein-Disulfide Isomerase.

@en

Human ER Oxidoreductin-1α

@nl

P1476

Human ER Oxidoreductin-1α (Ero ...... th Protein-Disulfide Isomerase

@en

P2093

Katsuhide Yutani

http://www.w3.org/2001/XMLSchema#string

Masaki Okumura

http://www.w3.org/2001/XMLSchema#string

Shingo Kanemura

http://www.w3.org/2001/XMLSchema#string

Takaaki Hikima

http://www.w3.org/2001/XMLSchema#string

Thomas Ramming

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P2860

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

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

Recycling of peroxiredoxin IV provides a novel pathway for disulphide formation in the endoplasmic reticulum

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

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

Insights into MHC Class I Peptide Loading from the Structure of the Tapasin-ERp57 Thiol Oxidoreductase Heterodimer

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

Synergistic cooperation of PDI family members in peroxiredoxin 4-driven oxidative protein folding

Radically different thioredoxin domain arrangement of ERp46, an efficient disulfide bond introducer of the mammalian PDI family

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

P304

23952-23964

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P31

scholarly article

P356

10.1074/JBC.M116.735662

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P407

English

P433

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P478

291

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P50

Christian Appenzeller-Herzog

Kenji Inaba

Shuji Akiyama

P577

2016-10-04T00:00:00Z

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P698

27703014

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P932

5104921

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