Cysteines 208 and 241 in Ero1α are required for maximal catalytic turnover

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Structural basis of pH-dependent client binding by ERp44, a key regulator of protein secretion at the ER-Golgi interface.Human ER Oxidoreductin-1α (Ero1α) Undergoes Dual Regulation through Complementary Redox Interactions with Protein-Disulfide Isomerase.

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Q42290711-FA7B6DF3-259F-4D0F-B105-DB6B374E8AC3 Q43142090-051EF7A9-39C6-401B-BDF4-26BCD220FE6F

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Cysteines 208 and 241 in Ero1α are required for maximal catalytic turnover

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Cysteines 208 and 241 in Ero1α are required for maximal catalytic turnover

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Cysteines 208 and 241 in Ero1α are required for maximal catalytic turnover

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Cysteines 208 and 241 in Ero1α are required for maximal catalytic turnover

@ast

Cysteines 208 and 241 in Ero1α are required for maximal catalytic turnover

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Cysteines 208 and 241 in Ero1α are required for maximal catalytic turnover

@ast

Cysteines 208 and 241 in Ero1α are required for maximal catalytic turnover

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P1476

Cysteines 208 and 241 in Ero1α are required for maximal catalytic turnover

@en

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Masaki Okumura

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

Shingo Kanemura

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

Thomas Ramming

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

P2860

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

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

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

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

Green fluorescent protein-based monitoring of endoplasmic reticulum redox poise

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

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

Lack of an efficient endoplasmic reticulum-localized recycling system protects peroxiredoxin IV from hyperoxidation.

Structure, mechanism, and evolution of Ero1 family enzymes.

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14-20

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

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scholarly article

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10.1016/J.REDOX.2015.11.004

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

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

P50

Christian Appenzeller-Herzog

Kenji Inaba

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2015-11-14T00:00:00Z

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

P5875

284137044

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

P698

26609561

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

P932

4683387

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

Cysteines 208 and 241 in Ero1α are required for maximal catalytic turnover

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P2860

P2860

Cysteines 208 and 241 in Ero1α are required for maximal catalytic turnover

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type

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P1433

P1476

P2093

P2860

P304

P31

P356

P478

P50

P577

P5875

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P478

P50

P577

P5875

P698

P932