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Molecular mechanisms and clinical implications of reversible protein S-glutathionylation.
Sulfhydryl chemistry plays a vital role in normal biology and in defense of cells against oxidants, free radicals, and electrophiles. Modification of critical cysteine residues is an importantExpand
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Mechanisms of reversible protein glutathionylation in redox signaling and oxidative stress.
Reversible protein S-glutathionylation (protein-SSG) is an important post-translational modification, providing protection of protein cysteines from irreversible oxidation and serving to transduceExpand
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Reversible Glutathionylation Regulates Actin Polymerization in A431 Cells*
In response to growth factor stimulation, many mammalian cells transiently generate reactive oxygen species (ROS) that lead to the elevation of tyrosine-phosphorylated and glutathionylated proteins.Expand
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Glutaredoxin: role in reversible protein s-glutathionylation and regulation of redox signal transduction and protein translocation.
Reversible posttranslational modifications on specific amino acid residues can efficiently regulate protein functions. O-Phosphorylation is the prototype and analogue to the rapidly emergingExpand
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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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Thioltransferase is a specific glutathionyl mixed disulfide oxidoreductase.
To study the substrate specificity and mechanism of thioltransferase (TTase) catalysis, we have used 14C- and 35S-radiolabeled mixed disulfides of cysteine and glutathione (GSH) with variousExpand
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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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Protein-thiol oxidation and cell death: regulatory role of glutaredoxins.
SIGNIFICANCE Glutaredoxin (Grx) is the primary enzyme responsible for catalysis of deglutathionylation of protein-mixed disulfides with glutathione (GSH) (protein-SSG). This reversibleExpand
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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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