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Items: 1 to 20 of 160

1.

Oxidative protein folding in eukaryotes: mechanisms and consequences.

Tu BP, Weissman JS.

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

3.
5.

Glutathione limits Ero1-dependent oxidation in the endoplasmic reticulum.

Molteni SN, Fassio A, Ciriolo MR, Filomeni G, Pasqualetto E, Fagioli C, Sitia R.

J Biol Chem. 2004 Jul 30;279(31):32667-73.

6.

Pathways for protein disulphide bond formation.

Frand AR, Cuozzo JW, Kaiser CA.

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

PMID:
10754564
7.

FAD oxidizes the ERO1-PDI electron transfer chain: the role of membrane integrity.

Papp E, Nardai G, Mandl J, Bánhegyi G, Csermely P.

Biochem Biophys Res Commun. 2005 Dec 16;338(2):938-45.

PMID:
16246310
8.

Biochemical basis of oxidative protein folding in the endoplasmic reticulum.

Tu BP, Ho-Schleyer SC, Travers KJ, Weissman JS.

Science. 2000 Nov 24;290(5496):1571-4.

9.

Oxidative activity of yeast Ero1p on protein disulfide isomerase and related oxidoreductases of the endoplasmic reticulum.

Vitu E, Kim S, Sevier CS, Lutzky O, Heldman N, Bentzur M, Unger T, Yona M, Kaiser CA, Fass D.

J Biol Chem. 2010 Jun 11;285(24):18155-65. doi: 10.1074/jbc.M109.064931.

10.

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.

12.

Novel Roles of the Non-catalytic Elements of Yeast Protein-disulfide Isomerase in Its Interplay with Endoplasmic Reticulum Oxidoreductin 1.

Niu Y, Zhang L, Yu J, Wang CC, Wang L.

J Biol Chem. 2016 Apr 8;291(15):8283-94. doi: 10.1074/jbc.M115.694257.

PMID:
26846856
13.
14.

Functional in vitro analysis of the ERO1 protein and protein-disulfide isomerase pathway.

Araki K, Nagata K.

J Biol Chem. 2011 Sep 16;286(37):32705-12. doi: 10.1074/jbc.M111.227181.

15.

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
17.

Ero1-PDI interactions, the response to redox flux and the implications for disulfide bond formation in the mammalian endoplasmic reticulum.

Benham AM, van Lith M, Sitia R, Braakman I.

Philos Trans R Soc Lond B Biol Sci. 2013 Mar 25;368(1617):20110403. doi: 10.1098/rstb.2011.0403.

18.

The endoplasmic reticulum sulfhydryl oxidase Ero1β drives efficient oxidative protein folding with loose regulation.

Wang L, Zhu L, Wang CC.

Biochem J. 2011 Feb 15;434(1):113-21. doi: 10.1042/BJ20101357.

PMID:
21091435
19.

Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells.

Molinari M, Helenius A.

Nature. 1999 Nov 4;402(6757):90-3.

PMID:
10573423
20.

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. Review.

PMID:
25651816

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