| Name | thioredoxin |
|---|---|
| Synonyms | ADF; TRX 1; TRX1; ATL derived factor; SASP; Surface associated sulphydryl protein; TRDX; TRX… |
| Name | sulfur |
|---|---|
| CAS | sulfur |
| PubMed | Abstract | RScore(About this table) | |
|---|---|---|---|
| 19714775 | Dimastrogiovanni D, Anselmi M, Miele AE, Boumis G, Petersson L, Angelucci F, Nola AD, Brunori M, Bellelli A: Combining crystallography and molecular dynamics: the case of Schistosoma mansoni phospholipid peroxidase. Proteins. 2010 Feb 1;78(2):259-70. Among these, peroxidases (Gpx) are a family of sulfur or -dependent isozymes sharing the ability to reduce peroxides using the reducing equivalents provided by or possibly small proteins such as thioredoxin. |
81(1,1,1,1) | Details |
| 19744922 | Chung JS, Noguera-Mazon V, Lancelin JM, Kim SK, Hirasawa M, Hologne M, Leustek T, Knaff DB: Interaction domain on thioredoxin for Pseudomonas aeruginosa 5'-adenylylsulfate reductase. J Biol Chem. 2009 Nov 6;284(45):31181-9. Epub 2009 Sep 10. |
5(0,0,0,5) | Details |
| 19762467 | Westrop GD, Georg I, Coombs GH: The mercaptopyruvate sulfurtransferase of Trichomonas vaginalis links catabolism to the production of thioredoxin persulfide. J Biol Chem. 2009 Nov 27;284(48):33485-94. Epub 2009 Sep 17. This consists of an aspartate aminotransferase (TvAspAT1), which transaminates to form (3-MP), and mercaptopyruvate sulfurtransferase (TvMST), which transfers the sulfur of 3-MP to a nucleophilic acceptor, generating |
4(0,0,0,4) | Details |
| 19801666 | Roussel X, Kriznik A, Richard C, Rahuel-Clermont S, Branlant G: Catalytic mechanism of Sulfiredoxin from Saccharomyces cerevisiae passes through an oxidized disulfide sulfiredoxin intermediate that is reduced by thioredoxin. J Biol Chem. 2009 Nov 27;284(48):33048-55. Epub 2009 Sep 30. |
3(0,0,0,3) | Details |
| 19908864 | Xu X, Schurmann P, Chung JS, Hass MA, Kim SK, Hirasawa M, Tripathy JN, Knaff DB, Ubbink M: Ternary protein complex of ferredoxin, ferredoxin:thioredoxin reductase, and thioredoxin studied by paramagnetic NMR spectroscopy. J Am Chem Soc. 2009 Dec 9;131(48):17576-82. |
2(0,0,0,2) | Details |
| 19733575 | Ranaivoson FM, Neiers F, Kauffmann B, Boschi-Muller S, Branlant G, Favier F: Methionine sulfoxide reductase B displays a high level of flexibility. J Mol Biol. 2009 Nov 20;394(1):83-93. Epub 2009 Sep 4. MsrB are stereospecific to R epimer on the sulfur of sulfoxide. For the subclass of MsrB whose recycling process passes through the formation of an intradisulfide bond, the recycling reducer is thioredoxin. |
2(0,0,0,2) | Details |
| 20345183 | Jan YH, Heck DE, Gray JP, Zheng H, Casillas RP, Laskin DL, Laskin JD: Selective Targeting of in Thioredoxin Reductase by the Half Mustard 2-Chloroethyl Ethyl Sulfide in Lung Epithelial Cells. Chem Res Toxicol. 2010 Mar 29. Thioredoxin reductase (TrxR) is a -containing flavoprotein that catalyzes the -dependent reduction of oxidized thioredoxin and plays a key role in regulating cellular redox homeostasis. In the present studies, we examined the effects of 2-chloroethyl ethyl sulfide (CEES), a model sulfur mustard vesicant, on TrxR in lung epithelial cells. |
1(0,0,0,1) | Details |
| 19958171 | Ugarte N, Petropoulos I, Friguet B: Oxidized Mitochondrial Protein Degradation and Repair in Aging and Oxidative Stress. Antioxid Redox Signal. 2010 Mar 8. Oxidized protein repair is limited to certain oxidation products of the sulfur-containing amino acids and Oxidized protein repair systems, thioredoxin/thioredoxin reductase or glutaredoxin//glutathione reductase that catalytically reduce disulfide bridges or sulfenic acids, and reductase that reverses back to within proteins, are present in the mitochondrial matrix. |
1(0,0,0,1) | Details |
| 20306235 | Hawkes WC, Alkan Z: Regulation of Redox Signaling by Selenoproteins. Biol Trace Elem Res. 2010 Mar 20. Thioredoxin reductases (three genes) use to reduce oxidized thioredoxin and its homologs, which regulate a plethora of redox signaling events. The sulfur amino acids, and are the main targets of reactive species in proteins. |
2(0,0,0,2) | Details |
| 20135153 | Papenbrock J, Guretzki S, Henne M: Latest news about the sulfurtransferase protein family of higher plants. Amino Acids. 2010 Feb 5. Sulfurtransferases/rhodaneses (Str) comprise a group of enzymes widely distributed in all phyla which catalyze in vitro the transfer of a from suitable sulfur donors to nucleophilic sulfur acceptors. Several studies in different organisms demonstrate a protein-protein interaction with members of the thioredoxin MPF indicating a role of Str in maintenance of the cellular redox homeostasis. |
1(0,0,0,1) | Details |
| 19954209 | Crack JC, den Hengst CD, Jakimowicz P, Subramanian S, Johnson MK, Buttner MJ, Thomson AJ, Le Brun NE: Characterization of [4Fe-4S]-containing and cluster-free forms of Streptomyces WhiD. Biochemistry. 2009 Dec 29;48(51):12252-64. WhiD, a member of the WhiB-like (Wbl) family of iron-sulfur proteins found exclusively within the actinomycetes, is required for the late stages of sporulation in Streptomyces coelicolor. Low molecular weight thiols, including a mycothiol analogue and thioredoxin, exerted a small but significant protective effect against WhiD cluster loss, an activity that could be of physiological importance. [4Fe-4S](2+) WhiD was found to react much more rapidly with than with either or peroxide, which may also be of physiological significance. |
1(0,0,0,1) | Details |
| 19825618 | Hosoya-Matsuda N, Inoue K, Hisabori T: Roles of thioredoxins in the obligate anaerobic green sulfur photosynthetic bacterium Chlorobaculum tepidum. Mol Plant. 2009 Mar;2(2):336-43. Epub 2008 Dec 4. In this study, 37 cytoplasmic proteins were captured as thioredoxin target candidates, including proteins involved in sulfur assimilation. |
120(1,2,3,5) | Details |