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Items: 1 to 20 of 172

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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
7.

Stress-induced transcription of the endoplasmic reticulum oxidoreductin gene ERO1 in the yeast Saccharomyces cerevisiae.

Takemori Y, Sakaguchi A, Matsuda S, Mizukami Y, Sakurai H.

Mol Genet Genomics. 2006 Jan;275(1):89-96.

PMID:
16292667
8.

A flavoprotein oxidase defines a new endoplasmic reticulum pathway for biosynthetic disulphide bond formation.

Sevier CS, Cuozzo JW, Vala A, Aslund F, Kaiser CA.

Nat Cell Biol. 2001 Oct;3(10):874-82.

PMID:
11584268
9.

Endoplasmic reticulum oxidoreductin 1-lbeta (ERO1-Lbeta), a human gene induced in the course of the unfolded protein response.

Pagani M, Fabbri M, Benedetti C, Fassio A, Pilati S, Bulleid NJ, Cabibbo A, Sitia R.

J Biol Chem. 2000 Aug 4;275(31):23685-92.

11.

MCD4 encodes a conserved endoplasmic reticulum membrane protein essential for glycosylphosphatidylinositol anchor synthesis in yeast.

Gaynor EC, Mondésert G, Grimme SJ, Reed SI, Orlean P, Emr SD.

Mol Biol Cell. 1999 Mar;10(3):627-48.

12.

The thiol oxidant dipyridyl disulfide can supply the PDI-Ero1p pathway with additional oxidative equivalents.

López-Mirabal HR, Winther JR.

Antonie Van Leeuwenhoek. 2007 Nov;92(4):463-72.

PMID:
17564811
13.

The CXXCXXC motif determines the folding, structure and stability of human Ero1-Lalpha.

Benham AM, Cabibbo A, Fassio A, Bulleid N, Sitia R, Braakman I.

EMBO J. 2000 Sep 1;19(17):4493-502.

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ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum.

Cabibbo A, Pagani M, Fabbri M, Rocchi M, Farmery MR, Bulleid NJ, Sitia R.

J Biol Chem. 2000 Feb 18;275(7):4827-33.

17.

Structure of Ero1p, source of disulfide bonds for oxidative protein folding in the cell.

Gross E, Kastner DB, Kaiser CA, Fass D.

Cell. 2004 May 28;117(5):601-10.

18.

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.

19.

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
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