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Items: 17

1.

Functional characterization of 3 thioredoxin homology domains of ERp72.

Satoh M, Shimada A, Keino H, Kashiwai A, Nagai N, Saga S, Hosokawa M.

Cell Stress Chaperones. 2005 Winter;10(4):278-84.

2.

ERp57 and PDI: multifunctional protein disulfide isomerases with similar domain architectures but differing substrate-partner associations.

Maattanen P, Kozlov G, Gehring K, Thomas DY.

Biochem Cell Biol. 2006 Dec;84(6):881-9. Review.

PMID:
17215875
3.

Similarities and differences in the thioredoxin superfamily.

Carvalho AP, Fernandes PA, Ramos MJ.

Prog Biophys Mol Biol. 2006 Jul;91(3):229-48. Epub 2005 Jul 26. Review.

PMID:
16098567
4.

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
5.

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
6.

Protein disulfides and protein disulfide oxidoreductases in hyperthermophiles.

Ladenstein R, Ren B.

FEBS J. 2006 Sep;273(18):4170-85. Epub 2006 Aug 23. Review.

7.

The protein disulphide-isomerase family: unravelling a string of folds.

Ferrari DM, Söling HD.

Biochem J. 1999 Apr 1;339 ( Pt 1):1-10. Review.

8.

Reconsideration of an early dogma, saying "there is no evidence for disulfide bonds in proteins from archaea".

Ladenstein R, Ren B.

Extremophiles. 2008 Jan;12(1):29-38. Epub 2007 May 17. Review.

PMID:
17508126
9.

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
10.

The human PDI family: versatility packed into a single fold.

Appenzeller-Herzog C, Ellgaard L.

Biochim Biophys Acta. 2008 Apr;1783(4):535-48. Epub 2007 Dec 3. Review.

11.

The machinery for oxidative protein folding in thermophiles.

Pedone E, Limauro D, Bartolucci S.

Antioxid Redox Signal. 2008 Jan;10(1):157-69. Review.

PMID:
17956189
12.

Substrate recognition by the protein disulfide isomerases.

Hatahet F, Ruddock LW.

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

13.

Protein disulfide isomerases exploit synergy between catalytic and specific binding domains.

Freedman RB, Klappa P, Ruddock LW.

EMBO Rep. 2002 Feb;3(2):136-40. Review.

14.

Electron avenue: pathways of disulfide bond formation and isomerization.

Debarbieux L, Beckwith J.

Cell. 1999 Oct 15;99(2):117-9. Review. No abstract available.

15.

Thioredoxins and glutaredoxins as facilitators of protein folding.

Berndt C, Lillig CH, Holmgren A.

Biochim Biophys Acta. 2008 Apr;1783(4):641-50. doi: 10.1016/j.bbamcr.2008.02.003. Epub 2008 Feb 19. Review.

16.

ERp29, an unusual redox-inactive member of the thioredoxin family.

Mkrtchian S, Sandalova T.

Antioxid Redox Signal. 2006 Mar-Apr;8(3-4):325-37. Review.

PMID:
16677078
17.

TXNDC5, a newly discovered disulfide isomerase with a key role in cell physiology and pathology.

Horna-Terrón E, Pradilla-Dieste A, Sánchez-de-Diego C, Osada J.

Int J Mol Sci. 2014 Dec 17;15(12):23501-18. doi: 10.3390/ijms151223501. Review.

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