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 ...

background: targeting of cd20 antigen with monoclonal antibodies has become the mainstay in the treatment of non-hodgkin's lymphomas and immunotherapeutic depletion of malignant b cells. accessibility of antigen is one of the crucial factors in development of monoclonal antibodies against this antigen. one major problem in expression of full length cd20 is aggregation and misfolding. there...

background: thioredoxin reductase 1 (txnrd1) and thioredoxin interacting protein (txnip) also known as thioredoxin binding protein 2 or vitamin d3-upregulated protein 1 are key players in oxidative stress control. thioredoxin (trx) is one of the major components of the thiol reducing system and plays multiple roles in cellular processes. computational analyses of txnrd1, txnip and trx expressio...

Thioredoxin reductase (TrxR) is a central component in the thioredoxin system by involving catalyzing reduction of thioredoxin, which critical for organism survival. Because this essential, it promising target novel antimicrobial agents. Herein, we solved 1.9 Å high‐resolution structure TrxR from Acinetobacter baumannii ( Ab TrxR), Gram‐negative, pathogenic bacterium and drug‐resistant superbug...

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...

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 from Escherichia coli (a small hydrogen transport protein containing 108 amino acid residues and having in its oxidized form a single disulfide bond) was acylated with citraconic anhydride. Citraconylation of all amino groups resulted in total loss of enzymatic activity with thioredoxin reductase and immunoprecipitin activity with antithioredoxin antibodies; both these activities we...

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...

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...