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Items: 1 to 20 of 157

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. Epub 2012 Jan 30. Review.

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ERdj5 Reductase Cooperates with Protein Disulfide Isomerase To Promote Simian Virus 40 Endoplasmic Reticulum Membrane Translocation.

Inoue T, Dosey A, Herbstman JF, Ravindran MS, Skiniotis G, Tsai B.

J Virol. 2015 Sep;89(17):8897-908. doi: 10.1128/JVI.00941-15. Epub 2015 Jun 17.

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.

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. Epub 2012 Feb 23. Review.

PMID:
22229892
6.

The crystal structure of the protein-disulfide isomerase family member ERp27 provides insights into its substrate binding capabilities.

Kober FX, Koelmel W, Kuper J, Drechsler J, Mais C, Hermanns HM, Schindelin H.

J Biol Chem. 2013 Jan 18;288(3):2029-39. doi: 10.1074/jbc.M112.410522. Epub 2012 Nov 28.

7.

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. Epub 2014 Aug 1. Review.

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9.

Different interaction modes for protein-disulfide isomerase (PDI) as an efficient regulator and a specific substrate of endoplasmic reticulum oxidoreductin-1α (Ero1α).

Zhang L, Niu Y, Zhu L, Fang J, Wang X, Wang L, Wang CC.

J Biol Chem. 2014 Nov 7;289(45):31188-99. doi: 10.1074/jbc.M114.602961. Epub 2014 Sep 25.

10.

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.

11.

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. Print 2013 May 5.

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13.

Protein disulfide isomerase acts as a redox-dependent chaperone to unfold cholera toxin.

Tsai B, Rodighiero C, Lencer WI, Rapoport TA.

Cell. 2001 Mar 23;104(6):937-48.

15.

Is protein disulfide isomerase a redox-dependent molecular chaperone?

Lumb RA, Bulleid NJ.

EMBO J. 2002 Dec 16;21(24):6763-70.

16.

Protein disulfide isomerases contribute differentially to the endoplasmic reticulum-associated degradation of apolipoprotein B and other substrates.

Grubb S, Guo L, Fisher EA, Brodsky JL.

Mol Biol Cell. 2012 Feb;23(4):520-32. doi: 10.1091/mbc.E11-08-0704. Epub 2011 Dec 21.

17.

ERdj5 is required as a disulfide reductase for degradation of misfolded proteins in the ER.

Ushioda R, Hoseki J, Araki K, Jansen G, Thomas DY, Nagata K.

Science. 2008 Jul 25;321(5888):569-72. doi: 10.1126/science.1159293.

18.

Protein disulfide isomerase-like proteins play opposing roles during retrotranslocation.

Forster ML, Sivick K, Park YN, Arvan P, Lencer WI, Tsai B.

J Cell Biol. 2006 Jun 19;173(6):853-9.

19.

Retarded PDI diffusion and a reductive shift in poise of the calcium depleted endoplasmic reticulum.

Avezov E, Konno T, Zyryanova A, Chen W, Laine R, Crespillo-Casado A, Melo EP, Ushioda R, Nagata K, Kaminski CF, Harding HP, Ron D.

BMC Biol. 2015 Jan 10;13:2. doi: 10.1186/s12915-014-0112-2.

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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