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Items: 1 to 20 of 116

1.

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

Cabibbo A, Pagani M, Fabbri M, Rocchi M, Farmery MR, Bulleid NJ, Sitia R.

J Biol Chem. 2000 Feb 18;275(7):4827-33.

2.

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

Pagani M, Fabbri M, Benedetti C, Fassio A, Pilati S, Bulleid NJ, Cabibbo A, Sitia R.

J Biol Chem. 2000 Aug 4;275(31):23685-92.

4.
5.

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

Bertoli G, Simmen T, Anelli T, Molteni SN, Fesce R, Sitia R.

J Biol Chem. 2004 Jul 16;279(29):30047-52.

6.

Structure, mechanism, and evolution of Ero1 family enzymes.

Araki K, Inaba K.

Antioxid Redox Signal. 2012 Apr 15;16(8):790-9. doi: 10.1089/ars.2011.4418. Review.

PMID:
22145624
7.

Ero1-PDI interactions, the response to redox flux and the implications for disulfide bond formation in the mammalian endoplasmic reticulum.

Benham AM, van Lith M, Sitia R, Braakman I.

Philos Trans R Soc Lond B Biol Sci. 2013 Mar 25;368(1617):20110403. doi: 10.1098/rstb.2011.0403.

9.

A PDI-catalyzed thiol-disulfide switch regulates the production of hydrogen peroxide by human Ero1.

Ramming T, Okumura M, Kanemura S, Baday S, Birk J, Moes S, Spiess M, Jenö P, Bernèche S, Inaba K, Appenzeller-Herzog C.

Free Radic Biol Med. 2015 Jun;83:361-72. doi: 10.1016/j.freeradbiomed.2015.02.011.

PMID:
25697776
10.

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

Araki K, Nagata K.

J Biol Chem. 2011 Sep 16;286(37):32705-12. doi: 10.1074/jbc.M111.227181.

11.

Vitamin K epoxide reductase contributes to protein disulfide formation and redox homeostasis within the endoplasmic reticulum.

Rutkevich LA, Williams DB.

Mol Biol Cell. 2012 Jun;23(11):2017-27. doi: 10.1091/mbc.E12-02-0102.

12.

Biochemical basis of oxidative protein folding in the endoplasmic reticulum.

Tu BP, Ho-Schleyer SC, Travers KJ, Weissman JS.

Science. 2000 Nov 24;290(5496):1571-4.

13.

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

Mezghrani A, Fassio A, Benham A, Simmen T, Braakman I, Sitia R.

EMBO J. 2001 Nov 15;20(22):6288-96.

14.

The physiological functions of mammalian endoplasmic oxidoreductin 1: on disulfides and more.

Ramming T, Appenzeller-Herzog C.

Antioxid Redox Signal. 2012 May 15;16(10):1109-18. doi: 10.1089/ars.2011.4475. Review.

PMID:
22220984
16.

Intracellular catalysis of disulfide bond formation by the human sulfhydryl oxidase, QSOX1.

Chakravarthi S, Jessop CE, Willer M, Stirling CJ, Bulleid NJ.

Biochem J. 2007 Jun 15;404(3):403-11.

17.

Ero1 and redox homeostasis in the endoplasmic reticulum.

Sevier CS, Kaiser CA.

Biochim Biophys Acta. 2008 Apr;1783(4):549-56. doi: 10.1016/j.bbamcr.2007.12.011. Review.

18.

Novel Roles of the Non-catalytic Elements of Yeast Protein-disulfide Isomerase in Its Interplay with Endoplasmic Reticulum Oxidoreductin 1.

Niu Y, Zhang L, Yu J, Wang CC, Wang L.

J Biol Chem. 2016 Apr 8;291(15):8283-94. doi: 10.1074/jbc.M115.694257.

PMID:
26846856
19.

Glutathione limits Ero1-dependent oxidation in the endoplasmic reticulum.

Molteni SN, Fassio A, Ciriolo MR, Filomeni G, Pasqualetto E, Fagioli C, Sitia R.

J Biol Chem. 2004 Jul 30;279(31):32667-73.

20.

A flavoprotein oxidase defines a new endoplasmic reticulum pathway for biosynthetic disulphide bond formation.

Sevier CS, Cuozzo JW, Vala A, Aslund F, Kaiser CA.

Nat Cell Biol. 2001 Oct;3(10):874-82.

PMID:
11584268
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