ATP-dependent reduction of cysteine–sulphinic acid by S. cerevisiae sulphiredoxin
By B. Biteau, J. Labarre, M. Tolédano. Nature, 2003
943 citations recorded by the source corpus.
Subfields: Biochemistry, Cell Biology, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/5e99145430f223a496f1a6d73fff9c45c2b800e5
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Citations in the corpus
- Protein Disulfide Isomerase: A Critical Evaluation of Its Function in Disulfide Bond Formation (2009, background): “It is thought to be a nonfunctional product caused by the action of ROS on reactive cysteines and requires the action of sulfiredoxin to reduce back it to the free cysteine thiol (24).”
- Trends in oxidative aging theories. (2007, background): “In fact, as late as 2003, a new antioxidant protein, sulfiredoxin, was discovered [178] in yeast and mammals.”
- Oxidative modifications to cellular components in plants. (2007, background): “The further oxidation of cysteine via cysteine sulfenic acid (R-SOH) to cysteine sulfinic acid (R-SO2H) (Figure 4) is also enzymatically reversible and probably involved in signaling pathways (11).”
- The cytoprotective role of the Keap1–Nrf2 pathway (2011, background): “Intriguingly, during the reduction of their substrates, the peroxidatic Cys of the Prxs can be overoxidised to sulfinic acid (–SOOH) that, in turn, is reduced back to Cys by the ATP-dependent sulfinic acid reductase sulfiredoxin (Srx) (Biteau et al. 2003; Woo et al. 2005).”
- Chemistry and biology of reactive oxygen species in signaling or stress responses (2011, background): “Moreover, sulfinic and sulfonic acids can be formed by subsequent two- and four-electron oxidations of sulfenic acid congeners, and the discovery of Sulfiredoxin proteins, which can convert sulfinic acids back to thiols, presages an additional layer of redox regulation at this higher oxidation stat”
- Reactive Oxygen Species in Health and Disease (2012, background): “This has been well studied in bacteria where the existence of a number of different ROS and redox statusresponsive signaling pathways is well established [17], as well as in the yeast Saccharomyces cerevisiae [18].”
- The Response to Heat Shock and Oxidative Stress in Saccharomyces cerevisiae (2012, background): “Differences in the cytoplasmic Prx’s are further highlighted by the finding that in contrast to Tsa1 and Tsa2, overoxidation of Ahp1 to cysteine–sulfinic acid is not reversed by Srx1 (Biteau et al. 2003).”