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Role of sulfiredoxin as a peroxiredoxin-2 denitrosylase in human iPSC-derived dopaminergic neurons [PDF]
Proceedings of the National Academy of Sciences of the United States of America, 2016 Significance S -nitrosylation, addition of an NO group to a cysteine thiol, can regulate protein activity. Aberrant protein S -nitrosylation, however, can disrupt normal enzyme function, as is the case for S -nitrosylated peroxiredoxin (SNO-Prx), which would otherwise ...
Abdullah Sultân +2 more
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Peroxiredoxins and Sulfiredoxin at the Crossroads of the NO and H2O2 Signaling Pathways
2013Peroxiredoxins (Prxs) are a family of peroxidases that maintain thiol homeostasis by catalyzing the reduction of organic hydroperoxides, H2O2, and peroxynitrite. Eukaryotic 2-Cys-Prxs, also referred to as typical Prxs, can be inactivated by oxidation of the catalytic cysteine to sulfinic acid, which may regulate the intracellular messenger function of ...
Abbas, Kahina +2 more
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A colorimetric assay for sulfiredoxin activity using inorganic phosphate measurement
Analytical Biochemistry, 20092-Cys peroxiredoxin (Prx) is the major subgroup of a family of Prx enzymes that reduce peroxide molecules such as hydrogen peroxide (H(2)O(2)). 2-Cys Prxs are inactivated when their active site cysteine residue is hyperoxidized to sulfinic acid. Sulfiredoxin (Srx) is an enzyme that catalyzes reduction of hyperoxidized 2-Cys Prxs in the presence of ATP,
Hojin, Kim +4 more
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Role of sulfiredoxin as a regulator of peroxiredoxin function and regulation of its expression
Free Radical Biology and Medicine, 2012Peroxiredoxins (Prxs) constitute a family of peroxidases in which cysteine serves as the primary site of oxidation during the reduction of peroxides. Members of the 2-Cys Prx subfamily of Prxs (Prx I to IV in mammals) are inactivated via hyperoxidation of the active-site cysteine to sulfinic acid (Cys-SO(2)H) during catalysis and are reactivated via an
Woojin, Jeong +3 more
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Experimental Cell Research, 2017
As a direct consequence of hyperglycaemia, the excessive generation of ROS is central to the pathogenesis of diabetic cardiomyopathy. We hypothesize that stimulation of high glucose (HG) results in an increased sulfiredoxin (Srx) expression, which regulates ROS signaling through reducing the hyperoxidized peroxiredoxins (Prxs).
Sa, Shi +6 more
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As a direct consequence of hyperglycaemia, the excessive generation of ROS is central to the pathogenesis of diabetic cardiomyopathy. We hypothesize that stimulation of high glucose (HG) results in an increased sulfiredoxin (Srx) expression, which regulates ROS signaling through reducing the hyperoxidized peroxiredoxins (Prxs).
Sa, Shi +6 more
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Nitric oxide activates an Nrf2/sulfiredoxin antioxidant pathway in macrophages
Free Radical Biology and Medicine, 2011Peroxiredoxins (Prx's) are a family of peroxidases that maintain thiol homeostasis by catalyzing the reduction of organic hydroperoxides, H₂O₂, and peroxynitrite. Under conditions of oxidative stress, eukaryotic Prx's can be inactivated by the substrate-dependent oxidation of the catalytic cysteine to sulfinic acid, which may regulate the intracellular
Abbas, Kahina +8 more
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1H, 15N, and 13C Chemical Shift Assignments of the Human Sulfiredoxin (hSrx)
Journal of Biomolecular NMR, 2005Electronic supplementary material Electronic supplementary material is available for this article at http://dx.doi.org/10.1007/s10858-005-0472-6 and accessible for authorised users.
Duck-Yeon, Lee +3 more
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Journal of Molecular Graphics and Modelling, 2019
When intracellular reactive oxygen species (ROS) increase, cancer cells are more vulnerable to oxidative stress compared to normal cells; thus, the collapse of redox homeostasis can lead to selective death of cancer cells. Indeed, recent studies have shown that inhibition of sulfiredoxin (Srx), which participates in antioxidant mechanisms, induces ROS ...
Minsup, Kim +4 more
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When intracellular reactive oxygen species (ROS) increase, cancer cells are more vulnerable to oxidative stress compared to normal cells; thus, the collapse of redox homeostasis can lead to selective death of cancer cells. Indeed, recent studies have shown that inhibition of sulfiredoxin (Srx), which participates in antioxidant mechanisms, induces ROS ...
Minsup, Kim +4 more
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Effective killing of cancer cells and regression of tumor growth by K27 targeting sulfiredoxin
Free Radical Biology and Medicine, 2016Cancer cells have been suggested to be more susceptible to oxidative damages and highly dependent on antioxidant capacity in comparison with normal cells, and thus targeting antioxidant enzymes has been a strategy for effective cancer treatment. Sulfiredoxin (Srx) is an enzyme that catalyzes the reduction of sulfinylated peroxiredoxins and thereby ...
Jiwon, Kim +11 more
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ROLE OF SULFIREDOXIN INTERACTING PROTEINS IN LUNG CANCER DEVELOPMENT
2016Sulfiredoxin (Srx) is an antioxidant enzyme that can be induced by oxidative stress. It promotes oncogenic phenotypes of cell proliferation, colony formation, migration, and metastasis in lung, skin and colon cancers. Srx reduces the overoxidation of 2-cysteine peroxiredoxins in cells, in addition to its role of removing glutathione modification from ...
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