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Acute Cadmium Exposure Inactivates Thioltransferase (Glutaredoxin), Inhibits Intracellular Reduction of Protein-glutathionyl-mixed Disulfides, and Initiates Apoptosis*
Oxidative stress broadly impacts cells, initiating regulatory pathways as well as apoptosis and necrosis. A key molecular event is protein S-glutathionylation, and thioltransferase (glutaredoxin) isExpand
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Mechanistic and kinetic details of catalysis of thiol-disulfide exchange by glutaredoxins and potential mechanisms of regulation.
Glutaredoxins are small, heat-stable proteins that exhibit a characteristic thioredoxin fold and a CXXC/S active-site motif. A variety of glutathione (GSH)-dependent catalytic activities have beenExpand
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Reactivity of the human thioltransferase (glutaredoxin) C7S, C25S, C78S, C82S mutant and NMR solution structure of its glutathionyl mixed disulfide intermediate reflect catalytic specificity.
Human thioltransferase (TTase) is a 12 kDa thiol-disulfide oxidoreductase that appears to play a critical role in maintaining the redox environment of the cell. TTase acts as a potent and specificExpand
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Glutathione Supplementation Potentiates Hypoxic Apoptosis by S-Glutathionylation of p65-NFκB*
In murine embryonic fibroblasts, N-acetyl-l-cysteine (NAC), a GSH generating agent, enhances hypoxic apoptosis by blocking the NFκB survival pathway (Qanungo, S., Wang, M., and Nieminen, A. L. (2004)Expand
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Kinetic and mechanistic characterization and versatile catalytic properties of mammalian glutaredoxin 2: implications for intracellular roles.
Glutaredoxin (Grx)-catalyzed deglutathionylation of protein-glutathione mixed disulfides (protein-SSG) serves important roles in redox homeostasis and signal transduction, regulating diverseExpand
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Glutathione-Thiyl Radical Scavenging and Transferase Properties of Human Glutaredoxin (Thioltransferase)
Glutaredoxin (GRx, thioltransferase) is implicated in cellular redox regulation, and it is known for specific and efficient catalysis of reduction of protein-S-S-glutathione-mixed disulfidesExpand
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Thioltransferase in human red blood cells: purification and properties.
Thioltransferase activity was identified and the enzyme purified to apparent homogeneity from human red blood cells. Activity was measured as glutathione-dependent reduction of the prototypeExpand
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Thioltransferase in human red blood cells: kinetics and equilibrium.
Thioltransferase from human red blood cells (HRBC TTase), coupled to GSSG reductase, catalyzed glutathione (GSH)-dependent reduction of prototype substrates hydroxyethyl disulfide (HEDS) and sodiumExpand
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Computational and mutational analysis of human glutaredoxin (thioltransferase): probing the molecular basis of the low pKa of cysteine 22 and its role in catalysis.
Human glutaredoxin (GRx), also known as thioltransferase, is a 12 kDa thiol-disulfide oxidoreductase that is highly selective for reduction of glutathione-containing mixed disulfides. The apparentExpand
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Thioltransferase (Glutaredoxin) Is Detected Within HIV-1 and Can Regulate the Activity of Glutathionylated HIV-1 Protease in Vitro *
Previous studies have suggested that the two conserved cysteines of the HIV-1 protease may be involved in regulating protease activity. Here, we examined diglutathionylated wild type proteaseExpand
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