ERO1-like protein alpha
Definition:
References:
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[1]. A Mezghrani, et al. Manipulation of oxidative protein folding and PDI redox state in mammalian cells. EMBO J. 2001 Nov 15;20(22):6288-96. [Content Brief]
[2]. A M Benham, et al. The CXXCXXC motif determines the folding, structure and stability of human Ero1-Lalpha. EMBO J. 2000 Sep 1;19(17):4493-502. [Content Brief]
[3]. A Cabibbo, et al. ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum. J Biol Chem. 2000 Feb 18;275(7):4827-33. [Content Brief]
[4]. Jianchao Zhang, et al. Secretory kinase Fam20C tunes endoplasmic reticulum redox state via phosphorylation of Ero1α. EMBO J. 2018 Jul 13;37(14):e98699. [Content Brief]
[5]. Christian Appenzeller-Herzog, et al. A novel disulphide switch mechanism in Ero1alpha balances ER oxidation in human cells. EMBO J. 2008 Nov 19;27(22):2977-87. [Content Brief]
[6]. Karl M Baker, et al. Low reduction potential of Ero1alpha regulatory disulphides ensures tight control of substrate oxidation. EMBO J. 2008 Nov 19;27(22):2988-97. [Content Brief]
[7]. Henning Gram Hansen, et al. Hyperactivity of the Ero1α oxidase elicits endoplasmic reticulum stress but no broad antioxidant response. J Biol Chem. 2012 Nov 16;287(47):39513-23. [Content Brief]
[8]. Billy Tsai, et al. Unfolded cholera toxin is transferred to the ER membrane and released from protein disulfide isomerase upon oxidation by Ero1. J Cell Biol. 2002 Oct 28;159(2):207-16. [Content Brief]
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