Selenium: A trace mineral that is a cofactor for production of active antioxidant enzymes such as glutathione peroxidases and thioredoxin reductase. ❋ MEHMET C. OZ (2007)
GSSG inhibition was a problem with thioredoxin and thioredoxin reductase which were needed to keep something in the reduced state. ❋ Unknown (2002)
Instead, they possess a linked thioredoxin-glutathione system with a selenocysteine-containing enzyme thioredoxin glutathione reductase (TGR) as the single redox hub that controls the overall redox homeostasis. ❋ Unknown (2010)
Inflammasome activators such as uric acid crystals induced the dissociation of TXNIP from thioredoxin in a reactive oxygen species (ROS) - sensitive manner and allowed it to bind NLRP3. ❋ Rongbin Zhou (2010)
Spx.activates trxA (thioredoxin) and trxB (thioredoxin reductase) in response to thiol stress, and bears an N-terminal C10XXC13 redox disulfide center that is oxidized in active Spx. The structure of mutant Spx.10S showed a change in the conformation of helix α4. ❋ Michiko M. Nakano Et Al. (2010)
DUVR did not alter mRNA level of catalase, thioredoxin, glutathion peroxidase, or the transcription factor Nrf2 and its modulators Keap1 and Bach1. ❋ Claire Marionnet Et Al. (2010)
In contrast, the free-living platyhelminth Schmidtea mediterranea (Class Turbellaria) possesses conventional and linked thioredoxin and glutathione systems. ❋ Unknown (2010)
The thioredoxin and/or glutathione pathways occur in all organisms. ❋ Unknown (2010)
Our results indicate that thioredoxin and glutathione pathways differ in parasitic and free-living flatworms and that canonical enzymes were specifically lost in the parasitic lineage. ❋ Unknown (2010)
Activation of the glutathione and thioredoxin antioxidant systems and changes in the iron metabolism suggested the need for protection against oxidative stress. ❋ Unknown (2010)
Little is known regarding the genomic structure of flatworm TGRs, the expression of TGR variants and whether the absence of conventional thioredoxin and glutathione systems is a signature of the entire platyhelminth phylum. ❋ Unknown (2010)
Disulfide bond formation in the endoplasmic reticulum of eukaryotic cells is catalyzed by the protein disulfide isomerase (PDI) and other members of the thioredoxin family ❋ Virginie Renaud Et Al. (2010)
We examine platyhelminth genomes and transcriptomes and find that all platyhelminth parasites (from classes Cestoda and Trematoda) conform to a biochemical scenario involving, exclusively, a selenium-dependent linked thioredoxin-glutathione system having TGR as a central redox hub. ❋ Unknown (2010)
Here we show that NLRP3 interacted with thioredoxin (TRX) - interacting protein (TXNIP), a protein linked to insulin resistance. ❋ Unknown (2010)
In contrast to their mammalian hosts, platyhelminth (flatworm) parasites studied so far, lack conventional thioredoxin and glutathione systems. ❋ Unknown (2010)
