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Items: 18

1.

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.

2.

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. Epub 2012 Jan 25. Review.

PMID:
22145624
3.

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. Epub 2012 Feb 15. Review.

PMID:
22220984
4.

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. Epub 2007 Dec 23. Review.

5.

Molecular mechanisms regulating oxidative activity of the Ero1 family in the endoplasmic reticulum.

Tavender TJ, Bulleid NJ.

Antioxid Redox Signal. 2010 Oct;13(8):1177-87. doi: 10.1089/ars.2010.3230. Review.

PMID:
20486761
6.

Protein folding: a missing redox link in the endoplasmic reticulum.

Freedman RB, Dunn AD, Ruddock LW.

Curr Biol. 1998 Jun 18;8(13):R468-70. Review.

7.

ERO1: A protein disulfide oxidase and H2O2 producer.

Zito E.

Free Radic Biol Med. 2015 Jun;83:299-304. doi: 10.1016/j.freeradbiomed.2015.01.011. Epub 2015 Jan 31. Review.

PMID:
25651816
8.

PRDX4, an endoplasmic reticulum-localized peroxiredoxin at the crossroads between enzymatic oxidative protein folding and nonenzymatic protein oxidation.

Zito E.

Antioxid Redox Signal. 2013 May 1;18(13):1666-74. doi: 10.1089/ars.2012.4966. Epub 2012 Nov 6. Review.

PMID:
23025503
9.

Redox signaling loops in the unfolded protein response.

Higa A, Chevet E.

Cell Signal. 2012 Aug;24(8):1548-55. doi: 10.1016/j.cellsig.2012.03.011. Epub 2012 Mar 28. Review.

PMID:
22481091
10.

Oxidative folding in the endoplasmic reticulum: towards a multiple oxidant hypothesis?

Margittai E, Bánhegyi G.

FEBS Lett. 2010 Jul 16;584(14):2995-8. doi: 10.1016/j.febslet.2010.05.055. Epub 2010 May 31. Review.

11.

Role of ascorbate in oxidative protein folding.

Bánhegyi G, Csala M, Szarka A, Varsányi M, Benedetti A, Mandl J.

Biofactors. 2003;17(1-4):37-46. Review.

PMID:
12897427
12.

Protein folding in the endoplasmic reticulum and the unfolded protein response.

Zhang K, Kaufman RJ.

Handb Exp Pharmacol. 2006;(172):69-91. Review.

PMID:
16610355
13.

Multiple ways to make disulfides.

Bulleid NJ, Ellgaard L.

Trends Biochem Sci. 2011 Sep;36(9):485-92. doi: 10.1016/j.tibs.2011.05.004. Epub 2011 Jul 19. Review.

PMID:
21778060
14.

The endoplasmic reticulum: folding, calcium homeostasis, signaling, and redox control.

Görlach A, Klappa P, Kietzmann T.

Antioxid Redox Signal. 2006 Sep-Oct;8(9-10):1391-418. Review.

PMID:
16986999
15.

Peroxides and peroxidases in the endoplasmic reticulum: integrating redox homeostasis and oxidative folding.

Kakihana T, Nagata K, Sitia R.

Antioxid Redox Signal. 2012 Apr 15;16(8):763-71. doi: 10.1089/ars.2011.4238. Epub 2012 Jan 25. Review.

PMID:
22146055
16.

Oxidative protein folding and the Quiescin-sulfhydryl oxidase family of flavoproteins.

Kodali VK, Thorpe C.

Antioxid Redox Signal. 2010 Oct;13(8):1217-30. doi: 10.1089/ars.2010.3098. Review.

17.

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

Chakravarthi S, Jessop CE, Bulleid NJ.

EMBO Rep. 2006 Mar;7(3):271-5. Review.

18.

Oxidative protein folding in the secretory pathway and redox signaling across compartments and cells.

Margittai E, Sitia R.

Traffic. 2011 Jan;12(1):1-8. doi: 10.1111/j.1600-0854.2010.01108.x. Epub 2010 Sep 20. Review.

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