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Items: 1 to 20 of 103

1.

Yeast flavin-containing monooxygenase generates oxidizing equivalents that control protein folding in the endoplasmic reticulum.

Suh JK, Poulsen LL, Ziegler DM, Robertus JD.

Proc Natl Acad Sci U S A. 1999 Mar 16;96(6):2687-91.

2.

Redox regulation of yeast flavin-containing monooxygenase.

Suh JK, Poulsen LL, Ziegler DM, Robertus JD.

Arch Biochem Biophys. 2000 Sep 15;381(2):317-22.

PMID:
11032421
3.

Yeast flavin-containing monooxygenase is induced by the unfolded protein response.

Suh JK, Robertus JD.

Proc Natl Acad Sci U S A. 2000 Jan 4;97(1):121-6.

4.

Competition between glutathione and protein thiols for disulphide-bond formation.

Cuozzo JW, Kaiser CA.

Nat Cell Biol. 1999 Jul;1(3):130-5.

PMID:
10559898
5.

Oxidative protein folding and unfolded protein response elicit differing redox regulation in endoplasmic reticulum and cytosol of yeast.

Delic M, Rebnegger C, Wanka F, Puxbaum V, Haberhauer-Troyer C, Hann S, Köllensperger G, Mattanovich D, Gasser B.

Free Radic Biol Med. 2012 May 1;52(9):2000-12. doi: 10.1016/j.freeradbiomed.2012.02.048. Epub 2012 Mar 8.

PMID:
22406321
6.

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.

8.
10.

Lysine 219 participates in NADPH specificity in a flavin-containing monooxygenase from Saccharomyces cerevisiae.

Suh JK, Poulsen LL, Ziegler DM, Robertus JD.

Arch Biochem Biophys. 1999 Dec 15;372(2):360-6.

PMID:
10600176
11.

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
12.
13.

Balanced Ero1 activation and inactivation establishes ER redox homeostasis.

Kim S, Sideris DP, Sevier CS, Kaiser CA.

J Cell Biol. 2012 Mar 19;196(6):713-25. doi: 10.1083/jcb.201110090. Epub 2012 Mar 12.

14.
15.

Ubiquitin ligase Hul5 is required for fragment-specific substrate degradation in endoplasmic reticulum-associated degradation.

Kohlmann S, Schäfer A, Wolf DH.

J Biol Chem. 2008 Jun 13;283(24):16374-83. doi: 10.1074/jbc.M801702200. Epub 2008 Apr 24.

16.

Glutathione- and non-glutathione-based oxidant control in the endoplasmic reticulum.

Appenzeller-Herzog C.

J Cell Sci. 2011 Mar 15;124(Pt 6):847-55. doi: 10.1242/jcs.080895.

17.

The contributions of protein disulfide isomerase and its homologues to oxidative protein folding in the yeast endoplasmic reticulum.

Xiao R, Wilkinson B, Solovyov A, Winther JR, Holmgren A, Lundström-Ljung J, Gilbert HF.

J Biol Chem. 2004 Nov 26;279(48):49780-6. Epub 2004 Sep 17.

18.

Oxidized redox state of glutathione in the endoplasmic reticulum.

Hwang C, Sinskey AJ, Lodish HF.

Science. 1992 Sep 11;257(5076):1496-502.

PMID:
1523409
19.

The KKXX signal mediates retrieval of membrane proteins from the Golgi to the ER in yeast.

Townsley FM, Pelham HR.

Eur J Cell Biol. 1994 Jun;64(1):211-6. No abstract available.

PMID:
7957309
20.

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. Epub 2004 May 25.

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