Mitochondrial Thioredoxin-Glutathione Reductase from Larval Taenia crassiceps (Cysticerci)
Mitochondrial thioredoxin-glutathione reductase was purified from larval Taenia crassiceps (cysticerci). The preparation showed NADPH-dependent reductase activity with either thioredoxin or GSSG, and was able to perform thiol/disulfide exchange reactions.
Alberto Guevara-Flores +5 more
doaj +2 more sources
Energetic nutrients are oxidized to sustain high intracellular NADPH/NADP+ ratios. NADPH-dependent reduction of thioredoxin-1 (Trx1) disulfide and glutathione disulfide by thioredoxin reductase-1 (TrxR1) and glutathione reductase (Gsr), respectively ...
Justin R. Prigge +16 more
doaj +2 more sources
Thioredoxin and Its Reductase Are Present on Synaptic Vesicles, and Their Inhibition Prevents the Paralysis Induced by Botulinum Neurotoxins [PDF]
Botulinum neurotoxins consist of a metalloprotease linked via a conserved interchain disulfide bond to a heavy chain responsible for neurospecific binding and translocation of the enzymatic domain in the nerve terminal cytosol.
Marco Pirazzini +10 more
doaj +2 more sources
A search of the disulfide reductase activities expressed in the adult stage of the free-living platyhelminth Dugesia dorotocephala was carried out. Using GSSG or DTNB as substrates, it was possible to obtain a purified fraction containing both GSSG and ...
Alberto Guevara-Flores +5 more
doaj +2 more sources
A Rare Case of Coexisting Mutation in Desmin and Thioredoxin Reductase 2 Genes Causing Dilated Cardiomyopathy [PDF]
Desmin (DES) maintains the overall structure of cardiomyocytes and cytoskeletal organization within striated muscle cells. Mitochondrial thioredoxin reductase 2 (TXNRD-2) is essential for mitochondrial oxygen radical scavenging.
Khatun, Nazima +3 more
core +1 more source
Structural analysis of glutaredoxin domain of Mus musculus thioredoxin glutathione reductase. [PDF]
Thioredoxin glutathione reductase (TGR) is a member of the mammalian thioredoxin reductase family that has a monothiol glutaredoxin (Grx) domain attached to the thioredoxin reductase module.
Olena Dobrovolska +3 more
doaj +1 more source
Mycobacterium tuberculosis Thioredoxin Reductase Is Essential for Thiol Redox Homeostasis but Plays a Minor Role in Antioxidant Defense. [PDF]
Mycobacterium tuberculosis (Mtb) must cope with exogenous oxidative stress imposed by the host. Unlike other antioxidant enzymes, Mtb's thioredoxin reductase TrxB2 has been predicted to be essential not only to fight host defenses but also for in vitro ...
Kan Lin +6 more
doaj +1 more source
Cell death by SecTRAPs: thioredoxin reductase as a prooxidant killer of cells. [PDF]
BackgroundSecTRAPs (selenium compromised thioredoxin reductase-derived apoptotic proteins) can be formed from the selenoprotein thioredoxin reductase (TrxR) by targeting of its selenocysteine (Sec) residue with electrophiles, or by its removal through C ...
Karin Anestål +3 more
doaj +1 more source
Thioredoxin Dependent Changes in the Redox States of FurA from Anabaena sp. PCC 7120
FurA is a multifunctional regulator in cyanobacteria that contains five cysteines, four of them arranged into two CXXC motifs. Lack of a structural zinc ion enables FurA to develop disulfide reductase activity.
Jorge Guío +6 more
doaj +1 more source
The role of thioredoxin reductases in brain development [PDF]
The thioredoxin-dependent system is an essential regulator of cellular redox balance. Since oxidative stress has been linked with neurodegenerative disease, we studied the roles of thioredoxin reductases in brain using mice with nervous system (NS ...
Jonna Soerensen +26 more
core +1 more source

