| Name | thioredoxin |
|---|---|
| Synonyms | ADF; TRX 1; TRX1; ATL derived factor; SASP; Surface associated sulphydryl protein; TRDX; TRX… |
| Name | phosphine |
|---|---|
| CAS | phosphine |
| PubMed | Abstract | RScore(About this table) | |
|---|---|---|---|
| 19572737 | Liang J, Fernandez JM: Mechanochemistry: One Bond at a Time. ACS Nano. 2009 Jul 2. Small nucleophiles, such as 1,4-dl- (DTT), tris (2-carboxyethyl) phosphine (TCEP), and react with the S-S bond with monotonically increasing rates under the applied force, while thioredoxin enzymes exhibit both stretching-favored and -resistant reaction-rate regimes. |
81(1,1,1,1) | Details |
| 17154358 | Schmidt AC, Koppelt J, Neustadt M, Otto M: Mass spectrometric evidence for different complexes of peptides and proteins with arsenic (III), arsenic (V), (II), and zinc (II) species. Rapid Commun Mass Spectrom. 2007;21(2):153-63. In contrast, for thioredoxin a bonding of As that depended on the concentration of the disulfide-reducing agent tris (2-carboxyethyl) phosphine was demonstrated. |
31(0,1,1,1) | Details |
| 17379716 | Orawski G, Bardischewsky F, Quentmeier A, Rother D, Friedrich CG: The periplasmic thioredoxin SoxS plays a key role in activation in vivo of chemotrophic oxidation of Paracoccus pantotrophus. Microbiology. 2007 Apr;153(Pt 4):1081-6. Chemical complementation by reductants such as DTT and tris (2-carboxyethyl) phosphine also restored the activity of strain GBOmegaS in the presence of chloramphenicol, which is an inhibitor of de novo protein synthesis. |
2(0,0,0,2) | Details |
| 14975452 | Landino LM, Iwig JS, Kennett KL, Moynihan KL: Repair of damage to tubulin by the thioredoxin reductase system. Free Radic Biol Med. 2004 Feb 15;36(4):497-506. Herein we report that -induced disulfides in porcine brain tubulin are repaired by the thioredoxin reductase system composed of rat liver thioredoxin reductase, human or Escherichia coli thioredoxin, and The extent of activity restored by thioredoxin reductase and by the nonspecific disulfide-reducing agent tris (2-carboxyethyl) phosphine hydrochloride was identical; however, activity was not restored to control levels. |
2(0,0,0,2) | Details |
| 15025511 | Waters SB, Devesa V, Del Razo LM, Styblo M, Thomas DJ: Endogenous reductants support the catalytic function of recombinant rat cyt19, an arsenic methyltransferase. Chem Res Toxicol. 2004 Mar;17(3):404-9. The reductants or tris (2-carboxylethyl) phosphine support catalysis by recombinant rat cyt19 (rrcyt19). Coupled systems containing an endogenous reductant (thioredoxin/thioredoxin reductase/ glutaredoxin//glutathione reductase/ or /thioredoxin reductase/ support inorganic As methylation by rrcyt19. |
2(0,0,0,2) | Details |
| 17697672 | Rackham O, Nichols SJ, Leedman PJ, Berners-Price SJ, Filipovska A: A gold (I) phosphine complex selectively induces apoptosis in breast cancer cells: implications for anticancer therapeutics targeted to mitochondria. Biochem Pharmacol. 2007 Oct 1;74(7):992-1002. Epub 2007 Jul 21. To address the molecular basis of the observed selectivity between the two cell lines we investigated the effect of the gold complex on the thioredoxin/thioredoxin reductase system in normal and cancer breast cells. |
2(0,0,0,2) | Details |
| 17298084 | Wang W, Winther JR, Thorpe C: Erv2p: characterization of the redox behavior of a yeast sulfhydryl oxidase. Biochemistry. 2007 Mar 20;46(11):3246-54. Epub 2007 Feb 14. Zn2+ also strongly inhibits Erv2p when assayed using tris (2-carboxyethyl) phosphine (TCEP) as the reducing substrate of the oxidase. In contrast to QSOX, Erv2p shows a comparatively low turnover with a range of small thiol substrates, with reduced Escherichia coli thioredoxin and with unfolded proteins. |
1(0,0,0,1) | Details |
| 19665452 | Gandin V, Fernandes AP, Rigobello MP, Dani B, Sorrentino F, Tisato F, Bjornstedt M, Bindoli A, Sturaro A, Rella R, Marzano C: Cancer cell death induced by phosphine gold (I) compounds targeting thioredoxin reductase. Biochem Pharmacol. 2010 Jan 15;79(2):90-101. Epub 2009 Aug 7. The thioredoxin system, composed of thioredoxin reductase (TrxR), thioredoxin (Trx), and plays a central role in regulating cellular redox homeostasis and signaling pathways. |
1(0,0,0,1) | Details |
| 16510263 | Omata Y, Folan M, Shaw M, Messer RL, Lockwood PE, Hobbs D, Bouillaguet S, Sano H, Lewis JB, Wataha JC: Sublethal concentrations of diverse gold compounds inhibit mammalian cytosolic thioredoxin reductase (TrxR1). Toxicol In Vitro. 2006 Sep;20(6):882-90. Epub 2006 Feb 28. Thioredoxin reductase (TrxR) reduces thioredoxin (Trx), thereby contributing to cellular redox balance, facilitating the synthesis of deoxy- sugars for DNA synthesis, and regulating redox-sensitive gene expression. METHODS: We exposed rat-TrxR1 to auranofin, gold thiomalate, aurothiosulfate, triphenyl phosphine gold or gold and measured TrxR activity ex vivo. |
1(0,0,0,1) | Details |
| 15568811 | Cline DJ, Redding SE, Brohawn SG, Psathas JN, Schneider JP, Thorpe C: New water-soluble phosphines as reductants of peptide and protein disulfide bonds: reactivity and membrane permeability. Biochemistry. 2004 Dec 7;43(48):15195-203. Tris (2-carboxyethyl) phosphine (TCEP) is a widely used substitute for (DTT) in the reduction of disulfide bonds in biochemical systems. The effectiveness of all four phosphines relative to DTT has been determined using model disulfides, including a fluorescent disulfide-containing peptide (H (3) N (+)-VTWCGACKM-NH (2)), and with protein disulfide bonds in thioredoxin and sulfhydryl oxidase. |
1(0,0,0,1) | Details |
| 16363808 | Imriskova-Sosova I, Andrews D, Yam K, Davidson D, Yachnin B, Hill BC: Characterization of the redox and metal binding activity of BsSco, a protein implicated in the assembly of cytochrome c oxidase. Biochemistry. 2005 Dec 27;44(51):16949-56. The soluble domain of Sco has a thioredoxin fold that is suggestive of redox activity for this protein. |
1(0,0,0,1) | Details |