the thioredoxin system, comprising thioredoxin (trx), thioredoxin reductase (trxr) and nadph, is one of the major cellular antioxidant systems, implicated in a large and growing number of biological functions. trx acts as an oxidoreductase via a highly conserved dithiol/disulfide motif located in the active site ( trp-cys-gly-pro- cys-lys-). different factors are involved in the regulation of t...

thioredoxins (trxs) are small ubiquitous oxidoreductase proteins with two redox-active cys residues in a conserved active site (wcg/ppc) that regulate numerous target proteins via thiol/disulfide exchanges in the cells of prokaryotes and eukaryotes. the isoforms ostrx23 with a typical active site (wcgpc) and ostrx20 with an atypical active site (wctpc) are two  trx h- type isoforms in rice that ...

A set of Xanthohumol derivatives were selected and molecular docking studies of these ‎compounds on thioredoxin reductase were conducted. Based on new structural patterns using in ‎silico-screening study, new potent lead compounds were designed. The results due to validated ‎docking protocols lead to find that Thr58, Gly57, Gly21, Asp334, Glu163, Ala130, IIe332, ‎Val44 and Gly132 are the main a...

Thioredoxin, thioredoxin reductase and NADPH form the thioredoxin system and are the major cellular protein disulphide reductase. We report here that Escherichia coli thioredoxin and thioredoxin reductase interact with unfolded and denatured proteins, in a manner similar to that of molecular chaperones that are involved in protein folding and protein renaturation after stress. Thioredoxin and/o...

BACKGROUND The selenoenzyme thioredoxin reductase 1 has a complex role relating to cell growth. It is induced as a component of the cellular response to potentially mutagenic oxidants, but also appears to provide growth advantages to transformed cells by inhibiting apoptosis. In addition, selenocysteine-deficient or alkylated forms of thioredoxin reductase 1 have also demonstrated oxidative, pr...

The cytosolic thioredoxin redox system composed of thioredoxin-1 and the NADPH-dependent thioredoxin reductase-1 reductase is an important regulator of cell growth and survival. Thioredoxin-1 is overexpressed in many human tumors where it is associated with increased cell proliferation, decreased apoptosis, and decreased patient survival. We hypothesized that thioredoxin reductase-1 provides a ...

Selenium compounds like selenite (SeO3(2-) may form a covalent adduct with glutathione (GSH) in the form of selenodiglutathione (GS-Se-SG), which is assumed to be important in the metabolism of selenium. We have isolated GS-Se-SG and studied its reactions with NADPH and thioredoxin reductase from calf thymus or with thioredoxin reductase and thioredoxin from Escherichia coli. Incubation of 0.1 ...

The thioredoxin system is vital in maintaining the cellular redox state and implicated various cancers other diseases. It comprises of reductase, NADPH. Various methods have been developed for detection quantification reductase enzyme. Most these suffer shortfall poor specificity, hence there need to develop more robust specific techniques. Recently, has an increased interest fluorescent probes...

Thioredoxin reductase and glutathione reductase are important enzymes of redox system that help the malaria parasite to maintain an adequate intracellular redox environment and contribute greatly to the antioxidant capacity of the cell. In the present study humoral immune response directed against thioredoxin reductase and glutathione reductase during Plasmodium berghei infection were investiga...

Plants possess two well described thioredoxin systems: a cytoplasmic system including several thioredoxins and an NADPH-dependent thioredoxin reductase and a specific chloroplastic system characterized by a ferredoxin-dependent thioredoxin reductase. On the basis of biochemical activities, plants also are supposed to have a mitochondrial thioredoxin system as described in yeast and mammals, but...