Results 21 to 30 of about 1,937 (151)
Antioxidants, 2023 Peroxiredoxin IV (Prx4), a typical two-cysteine-containing member of the peroxidase family, functions as an antioxidant to maintain cellular redox homeostasis through the reduction of reactive oxygen species (ROS) via cycles of oxidation–reduction ...
Pratik Thapa +7 more
doaj +1 more source
Circadian Oscillation of Sulfiredoxin in the Mitochondria [PDF]
Molecular Cell, 2015 Hydrogen peroxide (H2O2) released from mitochondria regulates various cell signaling pathways. Given that H2O2-eliminating enzymes such as peroxiredoxin III (PrxIII) are abundant in mitochondria, however, it has remained unknown how such release can occur.
Kil, In Sup +7 more
openaire +3 more sources
Atlas of Genetics and Cytogenetics in Oncology and Haematology, 2013 Review on SRXN1 (sulfiredoxin 1), with data on DNA, on the protein encoded, and where the gene is implicated.
Chawsheen, HA, Jiang, H, Wei, Q
openaire +2 more sources
A Novel Role for Human Sulfiredoxin in the Reversal of Glutathionylation [PDF]
Cancer Research, 2006 Abstract Modification of protein cysteine residues by disulfide formation with glutathione (glutathionylation) is a reversible posttranslational modification of critical importance in controlling cell signaling events following oxidative and/or nitrosative stress.
Victoria J, Findlay +5 more
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mLife, 2022 Cryptococcus neoformans and its sister species Cryptococcus deuterogattii are important human fungal pathogens. Despite their phylogenetically close relationship, these two Cryptococcus pathogens are greatly different in their clinical characteristics ...
Weixin Ke +11 more
doaj +1 more source
Catalytic Mechanism of Sulfiredoxin from Saccharomyces cerevisiae Passes through an Oxidized Disulfide Sulfiredoxin Intermediate That Is Reduced by Thioredoxin [PDF]
Journal of Biological Chemistry, 2009 Sulfiredoxin catalyzes the ATP-dependent reduction of overoxidized eukaryotic 2-Cys peroxiredoxin PrxSO(2) into sulfenic PrxSOH. Recent mechanistic studies on sulfiredoxins have validated a catalytic mechanism that includes formation of a phosphoryl intermediate on the sulfinyl moiety of PrxSO(2), followed by an attack of the catalytic cysteine of ...
Roussel, Xavier +4 more
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Antioxidants, 2023 The role of catechins in the epigenetic regulation of gene expression has been widely studied; however, if and how this phenomenon relates to the redox properties of these polyphenols remains unknown.
Patrycja Jakubek +8 more
doaj +1 more source
Neurobiology of Disease, 2012 In current study, we tested the hypothesis that c-Jun-dependent sulfiredoxin expression mediates protective effects of brain-derived neurotrophic factor (BDNF) against neurotoxicity induced by 3-nitropropionic acid (3-NP), a mitochondrial complex II ...
Chia-Lin Wu +5 more
doaj +1 more source
Deglutathionylation of 2-Cys Peroxiredoxin Is Specifically Catalyzed by Sulfiredoxin [PDF]
Journal of Biological Chemistry, 2009 Reversible protein glutathionylation plays a key role in cellular regulation and cell signaling and protects protein thiols from hyperoxidation. Sulfiredoxin (Srx), an enzyme that catalyzes the reduction of Cys-sulfinic acid derivatives of 2-Cys peroxiredoxins (2-Cys Prxs), has been shown to catalyze the deglutathionylation of actin.
Ji Won, Park +3 more
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Structural Basis for the Retroreduction of Inactivated Peroxiredoxins by Human Sulfiredoxin, [PDF]
Biochemistry, 2005 Sufiredoxins (Srx) repair the inactivated forms of typical two-Cys peroxiredoxins (Prx) implicated in hydrogen peroxide-mediated cell signaling. The reduction of the cysteine sulfinic acid moiety within the active site of the Prx by Srx involves novel sulfur chemistry and the use of ATP and Mg(2+).
Thomas J, Jönsson +4 more
openaire +2 more sources