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Items: 1 to 20 of 26

1.

Generating an unfoldase from thioredoxin-like domains.

Forster ML, Mahn JJ, Tsai B.

J Biol Chem. 2009 May 8;284(19):13045-56. doi: 10.1074/jbc.M808352200. Epub 2009 Mar 16.

2.

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.

3.

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
4.

Protein disulfide-isomerase, a folding catalyst and a redox-regulated chaperone.

Wang L, Wang X, Wang CC.

Free Radic Biol Med. 2015 Jun;83:305-13. doi: 10.1016/j.freeradbiomed.2015.02.007. Epub 2015 Feb 17. Review.

PMID:
25697778
5.

Enzymatic catalysis of disulfide formation.

Noiva R.

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

PMID:
7909462
6.

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
7.

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
8.

AGR2, ERp57/GRP58, and some other human protein disulfide isomerases.

Shishkin SS, Eremina LS, Kovalev LI, Kovaleva MA.

Biochemistry (Mosc). 2013 Dec;78(13):1415-30. doi: 10.1134/S000629791313004X. Review.

9.

Oxidative protein folding in eukaryotes: mechanisms and consequences.

Tu BP, Weissman JS.

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

10.

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.

11.

Extracellular Thiol Isomerases and Their Role in Thrombus Formation.

Schulman S, Bendapudi P, Sharda A, Chen V, Bellido-Martin L, Jasuja R, Furie BC, Flaumenhaft R, Furie B.

Antioxid Redox Signal. 2016 Jan 1;24(1):1-15. doi: 10.1089/ars.2015.6530. Epub 2015 Nov 18. Review.

12.

Endoplasmic reticulum-dependent redox reactions control endoplasmic reticulum-associated degradation and pathogen entry.

Walczak CP, Bernardi KM, Tsai B.

Antioxid Redox Signal. 2012 Apr 15;16(8):809-18. doi: 10.1089/ars.2011.4425. Epub 2012 Jan 30. Review.

13.

Protein disulfide isomerases: Redox connections in and out of the endoplasmic reticulum.

Soares Moretti AI, Martins Laurindo FR.

Arch Biochem Biophys. 2017 Mar 1;617:106-119. doi: 10.1016/j.abb.2016.11.007. Epub 2016 Nov 24. Review.

PMID:
27889386
14.

Protein disulfide isomerase and Nox: new partners in redox signaling.

Trevelin SC, Lopes LR.

Curr Pharm Des. 2015;21(41):5951-63. Review.

PMID:
26510433
15.

Protein Disulphide Isomerases: emerging roles of PDI and ERp57 in the nervous system and as therapeutic targets for ALS.

Perri E, Parakh S, Atkin J.

Expert Opin Ther Targets. 2017 Jan;21(1):37-49. Epub 2016 Nov 25. Review.

PMID:
27786579
16.

Role of PDI in regulating tissue factor: FVIIa activity.

Popescu NI, Lupu C, Lupu F.

Thromb Res. 2010 Apr;125 Suppl 1:S38-41. doi: 10.1016/j.thromres.2010.01.034. Epub 2010 Feb 16. Review.

17.

Protein disulfide isomerase and host-pathogen interaction.

Stolf BS, Smyrnias I, Lopes LR, Vendramin A, Goto H, Laurindo FR, Shah AM, Santos CX.

ScientificWorldJournal. 2011;11:1749-61. doi: 10.1100/2011/289182. Epub 2011 Oct 18. Review.

18.

Protein disulphide isomerase: building bridges in protein folding.

Freedman RB, Hirst TR, Tuite MF.

Trends Biochem Sci. 1994 Aug;19(8):331-6. Review.

PMID:
7940678
19.

Dual protein trafficking to secretory and non-secretory cell compartments: clear or double vision?

Porter BW, Yuen CY, Christopher DA.

Plant Sci. 2015 May;234:174-9. doi: 10.1016/j.plantsci.2015.02.013. Epub 2015 Feb 26. Review.

PMID:
25804820
20.

Assisting oxidative protein folding: how do protein disulphide-isomerases couple conformational and chemical processes in protein folding?

Wallis AK, Freedman RB.

Top Curr Chem. 2013;328:1-34. doi: 10.1007/128_2011_171. Review.

PMID:
21630134

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