Thioredoxin and glutaredoxin systems.

By A. Holmgren. Journal of Biological Chemistry, 2019

1,450 citations recorded by the source corpus.

Subfields: Biophysics, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/d96fa56516f6247738579b3e69327b205bc1e0fd

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Citations in the corpus

Exercise-Induced Oxidative Stress: Cellular Mechanisms and Impact on Muscle Force Production (2008, background): “Indeed, while TRX and GRX have some overlapping functions, GRXs are uniquely reactive with glutathione-mixed disulfides (160).”
Salinity Tolerance in Plants: Revisiting the Role of Sulfur Metabolites (2014, background): “Thioredoxins are believed to regulate the cell redox with active disulfide bridge [82] with a conserved pair of vicinal Cys (-Trp-Cys-Gly-Pro-Cys-Lys-) [83].”
Thioredoxin and Related Molecules–From Biology to Health and Disease (2007, neutral): “The localization of Grx1 and the impairment of the Grx1 system both in inflammatory and fibrotic lung diseases suggest a prominent role of Grx1 in the primary defense of the human lung (186).”
The Response to Heat Shock and Oxidative Stress in Saccharomyces cerevisiae (2012, background): “These systems are thermodynamically linked, since each uses NADPH as a source of reducing equivalents (Holmgren 1989).”
Reactive oxygen species, antioxidants, and the mammalian thioredoxin system. (2001, background): “Thioredoxin reductase (TrxR) isoenzymes are NADPH-dependent homodimer oxidoreductases with one FAD per subunit that reduce the active site disulfide in oxidized Trx [133,134,152,173].”
Disulfide bond formation in the Escherichia coli cytoplasm: an in vivo role reversal for the thioredoxins (1998, background): “Glutathione is then able to reduce the three glutaredoxins (glutaredoxin 1, 2 and 3) (Holmgren, 1989).”
Glutaredoxins: Glutathione-Dependent Redox Enzymes with Functions Far Beyond a Simple Thioredoxin Backup System (2004, neutral): “This is likely due to redundancy, because double mutants lacking both thioredoxin reductase ( trxB ) and GR ( gor ) are nonviable unless supplemented with a reductant like dithiothreitol, which chemically will reduce the redoxins (36, 39).”
Redox homeostasis in plants under abiotic stress: role of electron carriers, energy metabolism mediators and proteinaceous thiols (2015, background): “Glutaredoxins act as redox enzymes to catalyze the reduction of disulfides by using reduced glutathione (GSH) as a cofactor (Holmgren, 1988, 1989; Holmgren and Gleason, 1988).”
Posttranslational Protein Modification in Archaea (2005, background): “In eucaryal and bacterial cells, the formation and redox states of disulfide bonds are mediated by protein disulfide oxidoreductases (168).”