Results 11 to 20 of about 77,092 (210)

Allopurinol and oxypurinol differ in their strength and mechanisms of inhibition of xanthine oxidoreductase [PDF]

open access: yesJournal of Biological Chemistry, 2023
Xanthine oxidoreductase is a metalloenzyme that catalyzes the final steps in purine metabolism by converting hypoxanthine to xanthine and then uric acid.
Mai Sekine, Ken Okamoto, Emil F Pai
exaly   +5 more sources

Emerging Roles of Xanthine Oxidoreductase in Chronic Kidney Disease [PDF]

open access: yesAntioxidants
Xanthine Oxidoreductase (XOR) is a ubiquitous, essential enzyme responsible for the terminal steps of purine catabolism, ultimately producing uric acid that is eliminated by the kidneys.
Hunter W. Korsmo   +2 more
doaj   +3 more sources

Inhibition of xanthine oxidoreductase with febuxostat, but not allopurinol, prevents inflammasome assembly and IL-1β release [PDF]

open access: yesLife Science Alliance
This study focuses on the underappreciated distinct effects of two clinically used xanthine oxidoreductase inhibitors: allopurinol and febuxostat. Besides reducing uric acid levels in gout treatment, febuxostat, but not allopurinol, prevents NLRP3 ...
Lauar de Brito Monteiro   +9 more
doaj   +3 more sources

Xanthine oxidoreductase activity in platelet-poor and rich plasma as a oxidative stress indicator in patients required renal replacement therapy [PDF]

open access: yesBMC Nephrology, 2022
Background Xanthine oxidoreductase (XOR) is a hydroxylase enzyme involved in the metabolism of purines. XOR activity can vary: the homodimer protein can be converted into two different isoforms XD (antioxidant) and XO (prooxidant).
Elżbieta Cecerska-Heryć   +7 more
doaj   +3 more sources

Purine-Induced IFN-γ Promotes Uric Acid Production by Upregulating Xanthine Oxidoreductase Expression [PDF]

open access: yesFrontiers in Immunology, 2022
ObjectiveLimiting purine intake, inhibiting xanthine oxidoreductase (XOR) and inhibiting urate reabsorption in proximal tubule by uricosuric drugs, to reduce serum uric acid (UA) levels, are recognized treatments for gout.
Huanhuan Wang   +9 more
doaj   +3 more sources

Xanthine oxidoreductase inhibition ameliorates high glucose-induced glomerular endothelial injury by activating AMPK through the purine salvage pathway [PDF]

open access: yesScientific Reports
Xanthine oxidoreductase (XOR) contributes to reactive oxygen species production. We investigated the cytoprotective mechanisms of XOR inhibition against high glucose (HG)-induced glomerular endothelial injury, which involves activation of the AMP ...
Keum-Jin Yang   +5 more
doaj   +3 more sources

The double faced role of xanthine oxidoreductase in cancer. [PDF]

open access: yesActa Pharmacol Sin, 2022
Xanthine oxidoreductase (XOR) is a critical, rate-limiting enzyme that controls the last two steps of purine catabolism by converting hypoxanthine to xanthine and xanthine to uric acid. It also produces reactive oxygen species (ROS) during the catalytic process.
Chen MM, Meng LH.
europepmc   +4 more sources

Xanthine Oxidoreductase Is Involved in Chondrocyte Mineralization and Expressed in Osteoarthritic Damaged Cartilage [PDF]

open access: yesFrontiers in Cell and Developmental Biology, 2021
Pathologic calcification of cartilage consists of the formation of basic calcium phosphate (BCP) and/or calcium pyrophosphate dihydrate (CPPD) containing calcium crystals in mature hyaline or articular cartilage and is associated with aging, cartilage ...
Sonia Nasi   +9 more
doaj   +3 more sources

Diurnal Variations in Serum Uric Acid, Xanthine, and Xanthine Oxidoreductase Activity in Male Patients with Coronary Artery Disease. [PDF]

open access: yesNutrients, 2023
Hyperuricemia is influenced by diet and can cause gout. Whether it is a potential risk factor for cardiovascular disease (CVD) remains controversial, and the mechanism is unclear.
Shimizu M   +14 more
europepmc   +3 more sources

The Thermodynamics of Xanthine Oxidoreductase Catalysis [PDF]

open access: yesAntioxidants & Redox Signaling, 1999
Xanthine oxidoreductase is a complex enzyme found in a wide range of organisms. Recent interest in this enzyme stems from its ability to produce reactive oxygen species under a range of conditions. It is found as a homodimer, each unit containing a molybdopterin cofactor, two iron sulfur centers, and FAD.
Sanders, Stephen A., Massey, Vincent
openaire   +4 more sources

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