Chang TS - Search Results

1

Characterization of mammalian sulfiredoxin and its reactivation of hyperoxidized peroxiredoxin through reduction of cysteine sulfinic acid in the active site to cysteine.

Chang TS, Jeong W, Woo HA, Lee SM, Park S, Rhee SG. Chang TS, et al. J Biol Chem. 2004 Dec 3;279(49):50994-1001. doi: 10.1074/jbc.M409482200. Epub 2004 Sep 24. J Biol Chem. 2004. PMID: 15448164 Free article.

2

Regulation of peroxiredoxin I activity by Cdc2-mediated phosphorylation.

Chang TS, Jeong W, Choi SY, Yu S, Kang SW, Rhee SG. Chang TS, et al. J Biol Chem. 2002 Jul 12;277(28):25370-6. doi: 10.1074/jbc.M110432200. Epub 2002 May 1. J Biol Chem. 2002. PMID: 11986303 Free article.

3

Cytosolic peroxiredoxin attenuates the activation of Jnk and p38 but potentiates that of Erk in Hela cells stimulated with tumor necrosis factor-alpha.

Kang SW, Chang TS, Lee TH, Kim ES, Yu DY, Rhee SG. Kang SW, et al. Among authors: chang ts. J Biol Chem. 2004 Jan 23;279(4):2535-43. doi: 10.1074/jbc.M307698200. Epub 2003 Nov 3. J Biol Chem. 2004. PMID: 14597634 Free article.

4

Roles of TRP14, a thioredoxin-related protein in tumor necrosis factor-alpha signaling pathways.

Jeong W, Chang TS, Boja ES, Fales HM, Rhee SG. Jeong W, et al. Among authors: chang ts. J Biol Chem. 2004 Jan 30;279(5):3151-9. doi: 10.1074/jbc.M307959200. Epub 2003 Nov 7. J Biol Chem. 2004. PMID: 14607843 Free article.

5

Peroxiredoxin III, a mitochondrion-specific peroxidase, regulates apoptotic signaling by mitochondria.

Chang TS, Cho CS, Park S, Yu S, Kang SW, Rhee SG. Chang TS, et al. J Biol Chem. 2004 Oct 1;279(40):41975-84. doi: 10.1074/jbc.M407707200. Epub 2004 Jul 27. J Biol Chem. 2004. PMID: 15280382 Free article.

6

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. Woo HA, et al. Among authors: chang ts. J Biol Chem. 2005 Feb 4;280(5):3125-8. doi: 10.1074/jbc.C400496200. Epub 2004 Dec 8. J Biol Chem. 2005. PMID: 15590625 Free article.

7

Controlled elimination of intracellular H(2)O(2): regulation of peroxiredoxin, catalase, and glutathione peroxidase via post-translational modification.

Rhee SG, Yang KS, Kang SW, Woo HA, Chang TS. Rhee SG, et al. Among authors: chang ts. Antioxid Redox Signal. 2005 May-Jun;7(5-6):619-26. doi: 10.1089/ars.2005.7.619. Antioxid Redox Signal. 2005. PMID: 15890005 Review.

8

Molecular mechanism of the reduction of cysteine sulfinic acid of peroxiredoxin to cysteine by mammalian sulfiredoxin.

Jeong W, Park SJ, Chang TS, Lee DY, Rhee SG. Jeong W, et al. Among authors: chang ts. J Biol Chem. 2006 May 19;281(20):14400-7. doi: 10.1074/jbc.M511082200. Epub 2006 Mar 24. J Biol Chem. 2006. PMID: 16565085 Free article.

9

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

Noh YH, Baek JY, Jeong W, Rhee SG, Chang TS. Noh YH, et al. Among authors: chang ts. J Biol Chem. 2009 Mar 27;284(13):8470-7. doi: 10.1074/jbc.M808981200. Epub 2009 Jan 28. J Biol Chem. 2009. PMID: 19176523 Free PMC article.

10

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. Baek JY, et al. Among authors: chang ts. J Biol Chem. 2012 Jan 2;287(1):81-89. doi: 10.1074/jbc.M111.316711. Epub 2011 Nov 15. J Biol Chem. 2012. PMID: 22086924 Free PMC article.

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