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Items: 1 to 20 of 72

1.

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. Review.

2.

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. Review.

PMID:
25697778
3.

Redox-dependent protein quality control in the endoplasmic reticulum: folding to degradation.

Hagiwara M, Nagata K.

Antioxid Redox Signal. 2012 May 15;16(10):1119-28. doi: 10.1089/ars.2011.4495. Review.

PMID:
22229892
4.

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. Review.

5.

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. Review.

6.

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
7.

Structures and functions of protein disulfide isomerase family members involved in proteostasis in the endoplasmic reticulum.

Okumura M, Kadokura H, Inaba K.

Free Radic Biol Med. 2015 Jun;83:314-22. doi: 10.1016/j.freeradbiomed.2015.02.010. Review.

PMID:
25697777
8.

A bacterial toxin and a nonenveloped virus hijack ER-to-cytosol membrane translocation pathways to cause disease.

He K, Ravindran MS, Tsai B.

Crit Rev Biochem Mol Biol. 2015;50(6):477-88. doi: 10.3109/10409238.2015.1085826. Review.

9.

Redox diversity in ERAD-mediated protein retrotranslocation from the endoplasmic reticulum: a complex puzzle.

Suzuki Y, Schmitt MJ.

Biol Chem. 2015 May;396(5):539-54. doi: 10.1515/hsz-2014-0299. Review.

PMID:
25741737
10.

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
11.

Three approaches to one problem: protein folding in the periplasm, the endoplasmic reticulum, and the intermembrane space.

Herrmann JM, Riemer J.

Antioxid Redox Signal. 2014 Jul 20;21(3):438-56. doi: 10.1089/ars.2014.5841. Review.

PMID:
24483706
12.

Proteins of the PDI family: unpredicted non-ER locations and functions.

Turano C, Coppari S, Altieri F, Ferraro A.

J Cell Physiol. 2002 Nov;193(2):154-63. Review.

PMID:
12384992
13.

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. Review.

PMID:
16815710
14.

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. Review.

PMID:
22220984
15.

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
16.
17.

Forming disulfides in the endoplasmic reticulum.

Oka OB, Bulleid NJ.

Biochim Biophys Acta. 2013 Nov;1833(11):2425-9. doi: 10.1016/j.bbamcr.2013.02.007. Review.

18.

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. Review.

PMID:
24483600
19.

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
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