Results 51 to 60 of about 1,937 (151)
Reduction of Cysteine Sulfinic Acid by Sulfiredoxin Is Specific to 2-Cys Peroxiredoxins [PDF]
Cysteine residues of certain peroxiredoxins (Prxs) undergo reversible oxidation to sulfinic acid (Cys-SO2H) and the reduction reaction is catalyzed by sulfiredoxin (Srx). Specific Cys residues of various other proteins are also oxidized to sulfinic acid, suggesting that formation of Cys-SO2H might be a novel posttranslational modification that ...
Hyun Ae, Woo +6 more
openaire +2 more sources
Abstract Triple‐negative breast cancer (TNBC) predominantly affects young and minority women, with cytotoxic chemotherapy regimens causing severe side effects, including chronic cardiac dysfunction. Obesity worsens TNBC survival. Inositol‐requiring enzyme‐1 (IRE1), a key arm of the unfolded protein response (UPR), influences tumor progression.
Yismeilin R. Feliz‐Mosquea +5 more
wiley +1 more source
Evidence for the Formation of a Covalent Thiosulfinate Intermediate with Peroxiredoxin in the Catalytic Mechanism of Sulfiredoxin [PDF]
The typical 2-Cys peroxiredoxins are thiol-peroxidases involved in the physiology of hydrogen peroxide not only as a toxic but also as a signaling molecule. Coordination of these functions depends on the sulfinylation of the catalytic Cys, a modification reversed by ATP-dependent sulfiredoxin, which specifically reduces the sulfinic acid group of ...
Roussel, Xavier +6 more
openaire +3 more sources
Oxidative Stress in Antigen Processing and Presentation
Reactive oxygen species (ROS) play a crucial role in antigen processing and presentation, essential for linking innate and adaptive immunity. While balanced ROS levels promote immune function, excess ROS can disrupt antigen recognition, resulting in immune dysfunction.
Qinxia Chang +9 more
wiley +1 more source
Balancing anti-inflammatory and anti-oxidant responses in murine bone marrow derived macrophages.
RationaleThe underlying pathophysiology of bronchopulmonary dysplasia includes a macrophage-mediated host response orchestrated by anti-inflammatory peroxisome proliferator-activated receptor gamma (PPARγ) and anti-oxidant nuclear factor (erythroid ...
Christopher R Nitkin, Tracey L Bonfield
doaj +1 more source
In this study, we show that the sulfur compound commonly found in cruciferous and allium vegetables and the main human metabolite of S‐methyl‐L‐cysteine sulfoxide, called S‐methyl methanethiosulfonate (MMTSO), alters energy metabolism in DU145 prostate cancer cells.
Gemma Beasy +8 more
wiley +1 more source
MOLECULAR MECHANISM OF THE REDUCTION OF CYSTEINE SULFINIC ACID OF PEROXIREDOXIN TO CYSTEINE BY MAMMALIAN SULFIREDOXIN [PDF]
Among many proteins with cysteine sulfinic acid (Cys–SO2H) residues, the sulfinic forms of certain peroxiredoxins (Prxs) are selectively reduced by sulfiredoxin (Srx) in the presence of ATP. All Srx enzymes contain a conserved cysteine residue. To elucidate the mechanism of the Srx‐catalyzed reaction, we generated various mutants of Srx and examined ...
Woojin, Jeong +4 more
openaire +2 more sources
Background: Fetal-to-neonatal transition is associated with oxidative stress. In preterm infants, immaturity of the antioxidant system favours supplemental oxygen-derived morbidity and mortality.
Javier Escobar +9 more
doaj +1 more source
Proteomic analysis reveals that instead of specific proteins, different tissues exhibit common dysregulated functional networks. Specifically, the integrity of the midgut barrier function is compromised during aging, which can be restored through the downregulation of the insulin receptor (InR).
Congying Zhang +10 more
wiley +1 more source
Hyperoxidation of Peroxiredoxin 6 Induces Alteration from Dimeric to Oligomeric State
Peroxiredoxins(Prdx), the family of non-selenium glutathione peroxidases, are important antioxidant enzymes that defend our system from the toxic reactive oxygen species (ROS).
Sharifun Shahnaj +8 more
doaj +1 more source

