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Items: 1 to 20 of 90

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.

Conservation and diversity of the cellular disulfide bond formation pathways.

Sevier CS, Kaiser CA.

Antioxid Redox Signal. 2006 May-Jun;8(5-6):797-811. Review.

PMID:
16771671
5.

Oxidative protein folding in eukaryotes: mechanisms and consequences.

Tu BP, Weissman JS.

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

6.

Enzymatic catalysis of disulfide formation.

Noiva R.

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

PMID:
7909462
7.

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
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.

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.

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.

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
12.

Pathways of disulfide bond formation in Escherichia coli.

Messens J, Collet JF.

Int J Biochem Cell Biol. 2006;38(7):1050-62. Epub 2006 Jan 11. Review.

PMID:
16446111
13.
14.

Protein disulfide isomerase assists protein folding as both an isomerase and a chaperone.

Wang CC.

Ann N Y Acad Sci. 1998 Dec 13;864:9-13. Review.

PMID:
9928079
15.

Defining the protein-protein interactions of the mammalian endoplasmic reticulum oxidoreductases (EROs).

Dias-Gunasekara S, Benham AM.

Biochem Soc Trans. 2005 Dec;33(Pt 6):1382-4. Review.

PMID:
16246124
16.

Substrate recognition by the protein disulfide isomerases.

Hatahet F, Ruddock LW.

FEBS J. 2007 Oct;274(20):5223-34. Epub 2007 Sep 24. Review.

17.

Protein disulfide isomerase: the multifunctional redox chaperone of the endoplasmic reticulum.

Noiva R.

Semin Cell Dev Biol. 1999 Oct;10(5):481-93. Review.

PMID:
10597631
18.

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.

19.

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
20.

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

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