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Items: 1 to 20 of 43

1.

Oxidative protein folding in eukaryotes: mechanisms and consequences.

Tu BP, Weissman JS.

J Cell Biol. 2004 Feb 2;164(3):341-6. Review.

2.

Pathways for protein disulphide bond formation.

Frand AR, Cuozzo JW, Kaiser CA.

Trends Cell Biol. 2000 May;10(5):203-10. Review.

PMID:
10754564
3.

Oxidative protein folding: from thiol-disulfide exchange reactions to the redox poise of the endoplasmic reticulum.

Hudson DA, Gannon SA, Thorpe C.

Free Radic Biol Med. 2015 Mar;80:171-82. doi: 10.1016/j.freeradbiomed.2014.07.037. Epub 2014 Aug 1. Review.

4.

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
5.

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
6.

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
7.

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.

8.

Protein disulfide isomerase: the structure of oxidative folding.

Gruber CW, Cemazar M, Heras B, Martin JL, Craik DJ.

Trends Biochem Sci. 2006 Aug;31(8):455-64. Epub 2006 Jul 11. Review.

PMID:
16815710
9.

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.

10.

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
11.

Oxidative protein folding in the mammalian endoplasmic reticulum.

Jessop CE, Chakravarthi S, Watkins RH, Bulleid NJ.

Biochem Soc Trans. 2004 Nov;32(Pt 5):655-8. Review.

PMID:
15493980
12.

Enzymatic catalysis of disulfide formation.

Noiva R.

Protein Expr Purif. 1994 Feb;5(1):1-13. Review.

PMID:
7909462
13.

The thioredoxin superfamily in oxidative protein folding.

Lu J, Holmgren A.

Antioxid Redox Signal. 2014 Jul 20;21(3):457-70. doi: 10.1089/ars.2014.5849. Epub 2014 Mar 6. Review.

PMID:
24483600
14.

Participation of low molecular weight electron carriers in oxidative protein folding.

Margittai E, Csala M, Mandl J, Bánhegyi G.

Int J Mol Sci. 2009 Mar;10(3):1346-59. doi: 10.3390/ijms10031346. Epub 2009 Mar 20. Review.

15.

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
16.

Disulfide bond formation, a race between FAD and oxygen.

Bardwell JC.

Dev Cell. 2002 Dec;3(6):758-60. Review.

17.

Formation, isomerisation and reduction of disulphide bonds during protein quality control in the endoplasmic reticulum.

Fassio A, Sitia R.

Histochem Cell Biol. 2002 Feb;117(2):151-7. Epub 2002 Jan 19. Review.

PMID:
11935291
18.

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
19.

Catalysis of protein folding by protein disulfide isomerase and small-molecule mimics.

Kersteen EA, Raines RT.

Antioxid Redox Signal. 2003 Aug;5(4):413-24. Review.

20.

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.

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