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Deglutathionylation of 2-Cys peroxiredoxin is specifically catalyzed by sulfiredoxin.

Park JW, Mieyal JJ, Rhee SG, Chock PB.

J Biol Chem. 2009 Aug 28;284(35):23364-74. doi: 10.1074/jbc.M109.021394. Epub 2009 Jun 27.


Role of sulfiredoxin as a regulator of peroxiredoxin function and regulation of its expression.

Jeong W, Bae SH, Toledano MB, Rhee SG.

Free Radic Biol Med. 2012 Aug 1;53(3):447-56. doi: 10.1016/j.freeradbiomed.2012.05.020. Epub 2012 May 24. Review.


Reduction of cysteine sulfinic acid by sulfiredoxin is specific to 2-cys peroxiredoxins.

Woo HA, Jeong W, Chang TS, Park KJ, Park SJ, Yang JS, Rhee SG.

J Biol Chem. 2005 Feb 4;280(5):3125-8. Epub 2004 Dec 8.


Sulfiredoxin Translocation into Mitochondria Plays a Crucial Role in Reducing Hyperoxidized Peroxiredoxin III.

Noh YH, Baek JY, Jeong W, Rhee SG, Chang TS.

J Biol Chem. 2009 Mar 27;284(13):8470-7. doi: 10.1074/jbc.M808981200. Epub 2009 Jan 28.


Reduction of cysteine sulfinic acid in eukaryotic, typical 2-Cys peroxiredoxins by sulfiredoxin.

Lowther WT, Haynes AC.

Antioxid Redox Signal. 2011 Jul 1;15(1):99-109. doi: 10.1089/ars.2010.3564. Epub 2010 Dec 17. Review.


The sulfiredoxin-peroxiredoxin (Srx-Prx) axis in cell signal transduction and cancer development.

Mishra M, Jiang H, Wu L, Chawsheen HA, Wei Q.

Cancer Lett. 2015 Oct 1;366(2):150-9. doi: 10.1016/j.canlet.2015.07.002. Epub 2015 Jul 10. Review.


Identification of intact protein thiosulfinate intermediate in the reduction of cysteine sulfinic acid in peroxiredoxin by human sulfiredoxin.

Jönsson TJ, Tsang AW, Lowther WT, Furdui CM.

J Biol Chem. 2008 Aug 22;283(34):22890-4. doi: 10.1074/jbc.C800124200. Epub 2008 Jun 30.


Evidence that glutathione and the glutathione system efficiently recycle 1-cys sulfiredoxin in vivo.

Boukhenouna S, Mazon H, Branlant G, Jacob C, Toledano MB, Rahuel-Clermont S.

Antioxid Redox Signal. 2015 Mar 20;22(9):731-43. doi: 10.1089/ars.2014.5998. Epub 2015 Jan 8.


Concerted action of sulfiredoxin and peroxiredoxin I protects against alcohol-induced oxidative injury in mouse liver.

Bae SH, Sung SH, Cho EJ, Lee SK, Lee HE, Woo HA, Yu DY, Kil IS, Rhee SG.

Hepatology. 2011 Mar;53(3):945-53. doi: 10.1002/hep.24104. Epub 2011 Feb 11.


Characterization of plant sulfiredoxin and role of sulphinic form of 2-Cys peroxiredoxin.

Iglesias-Baena I, Barranco-Medina S, Lázaro-Payo A, López-Jaramillo FJ, Sevilla F, Lázaro JJ.

J Exp Bot. 2010 Mar;61(5):1509-21. doi: 10.1093/jxb/erq016. Epub 2010 Feb 22.


Reduction of cysteine sulfinic acid in peroxiredoxin by sulfiredoxin proceeds directly through a sulfinic phosphoryl ester intermediate.

Jönsson TJ, Murray MS, Johnson LC, Lowther WT.

J Biol Chem. 2008 Aug 29;283(35):23846-51. doi: 10.1074/jbc.M803244200. Epub 2008 Jun 24.


Protein engineering of the quaternary sulfiredoxin.peroxiredoxin enzyme.substrate complex reveals the molecular basis for cysteine sulfinic acid phosphorylation.

Jönsson TJ, Johnson LC, Lowther WT.

J Biol Chem. 2009 Nov 27;284(48):33305-10. doi: 10.1074/jbc.M109.036400. Epub 2009 Oct 6.


Sestrin 2 is not a reductase for cysteine sulfinic acid of peroxiredoxins.

Woo HA, Bae SH, Park S, Rhee SG.

Antioxid Redox Signal. 2009 Apr;11(4):739-45. doi: 10.1089/ARS.2008.2360.


Sulfiredoxin protein is critical for redox balance and survival of cells exposed to low steady-state levels of H2O2.

Baek JY, Han SH, Sung SH, Lee HE, Kim YM, Noh YH, Bae SH, Rhee SG, Chang TS.

J Biol Chem. 2012 Jan 2;287(1):81-9. doi: 10.1074/jbc.M111.316711. Epub 2011 Nov 15.


The contribution of NADPH thioredoxin reductase C (NTRC) and sulfiredoxin to 2-Cys peroxiredoxin overoxidation in Arabidopsis thaliana chloroplasts.

Puerto-Galán L, Pérez-Ruiz JM, Guinea M, Cejudo FJ.

J Exp Bot. 2015 May;66(10):2957-66. doi: 10.1093/jxb/eru512. Epub 2015 Jan 5.


The dual-targeted plant sulfiredoxin retroreduces the sulfinic form of atypical mitochondrial peroxiredoxin.

Iglesias-Baena I, Barranco-Medina S, Sevilla F, Lázaro JJ.

Plant Physiol. 2011 Feb;155(2):944-55. doi: 10.1104/pp.110.166504. Epub 2010 Dec 7.


Protein glutathionylation in the regulation of peroxiredoxins: a family of thiol-specific peroxidases that function as antioxidants, molecular chaperones, and signal modulators.

Chae HZ, Oubrahim H, Park JW, Rhee SG, Chock PB.

Antioxid Redox Signal. 2012 Mar 15;16(6):506-23. doi: 10.1089/ars.2011.4260. Review.


Nuclear factor E2-related factor 2 dependent overexpression of sulfiredoxin and peroxiredoxin III in human lung cancer.

Kim YS, Lee HL, Lee KB, Park JH, Chung WY, Lee KS, Sheen SS, Park KJ, Hwang SC.

Korean J Intern Med. 2011 Sep;26(3):304-13. doi: 10.3904/kjim.2011.26.3.304. Epub 2011 Sep 13.

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