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xanthine/تسوس سني

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مقالاتالتجارب السريريةبراءات الاختراع
الصفحة 1 من عند 54 النتائج

Structure-related pharmacokinetics of xanthines after direct administration into the peritoneal cavity of rats.

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The pharmacokinetic characteristics, peritoneal permeability and hydrophobicity of three xanthine derivatives, theophylline, enprofylline and 1-methyl-3-propylxanthine (MPX), were investigated in rats. Isotonic saline (30 ml) containing xanthine (2.5, 5 and 10 mg/kg) and blue dextran (0.2%) was
This work describes molecular dynamics (MD) simulations in aqueous media for the complex of the homotetrameric urate oxidase (UOX) from Aspergillus flavus with xanthine anion (5) in the presence of dioxygen (O2 ). After 196.6 ns of trajectory from unrestrained MD, a O2 molecule was observed leaving

Monodispersed gold nanoparticles entrapped in ordered mesoporous carbon/silica nanocomposites as xanthine oxidase mimic for electrochemical sensing of xanthine

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Monodispersed Au nanoparticles in ordered mesoporous carbon/silica (Au/OMCS) nanocomposites were prepared by the solvent evaporation induced self-assembly. Au/OMCS nanocomposites were characterized through XRD, BET, and TEM. The obtained nanocomposites exhibit uniform mesopores with the size of 18 ±

Hypoxanthine, xanthine, and urate in synovial fluid from patients with inflammatory arthritides.

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As nucleotide catabolism increases during tissue injury the appearance of purine metabolites in inflamed synovial fluid might be of value in understanding the joint damage in inflammatory arthritides. In this study, therefore, synovial and plasma concentrations of hypoxanthine, xanthine, and urate

Purine substrate recognition by the nucleobase-ascorbate transporter signature motif in the YgfO xanthine permease: ASN-325 binds and ALA-323 senses substrate.

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The nucleobase-ascorbate transporter (NAT) signature motif is a conserved 11-amino acid sequence of the ubiquitous NAT/NCS2 family, essential for function and selectivity of both a bacterial (YgfO) and a fungal (UapA) purine-transporting homolog. We examined the role of NAT motif in more detail,

Synthesis, characterization and xanthine oxidase inhibition of Cu(II)-chrysin complex.

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Xanthine oxidase (XO) is a key enzyme catalyzing hypoxanthine to xanthine and then uric acid causing hyperuricemia. A Cu(II) complex of chrysin was synthesized and characterized by UV-vis absorption, Fourier transform infrared, nuclear magnetic resonance (1H NMR) and mass spectroscopy studies. The

High levels of xanthine oxidoreductase in rat endothelial, epithelial and connective tissue cells. A relation between localization and function?

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The localization of xanthine oxidoreductase activity was investigated in unfixed cryostat sections of various rat tissues by an enzyme histochemical method which specifically demonstrates both the dehydrogenase and oxidase forms of xanthine oxidoreductase. High activity was found in epithelial cells

Deciphering the inhibitory mechanism of genistein on xanthine oxidase in vitro.

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Genistein (Gen), widely distributed in soybean, is proved to be important in homeostasis in the human body. Herein, the inhibitory mechanism of Gen against xanthine oxidase (XO) was studied through multispectroscopic methods and molecular simulation. The inhibition kinetics showed that Gen

Crystal structure of the hypoxanthine-guanine-xanthine phosphoribosyltransferase from the protozoan parasite Tritrichomonas foetus.

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The crystal structure of the hypoxanthine-guanine-xanthine phosphoribosyltransferase (HGXPRTase) from Tritrichomonas foetus has been determined and refined against X-ray data to 1.9 A resolution. T. foetus HGXPRTase crystallizes as an asymmetric dimer, with GMP bound to only one of the two molecules

The inhibitory kinetics and mechanism of dietary vitamins D3 and B2 on xanthine oxidase.

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Dietary guidelines to promote health are usually based on the patterns' prediction on disease risk of foods and nutrients. Overactivity of xanthine oxidase (XO) is the underlying cause of gout. Herein, the inhibitory kinetics and mechanism of dietary vitamins D3 and B2 on XO were investigated by

Inhibition of chrysin on xanthine oxidase activity and its inhibition mechanism.

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Chrysin, a bioactive flavonoid, was investigated for its potential to inhibit the activity of xanthine oxidase (XO), a key enzyme catalyzing xanthine to uric acid and finally causing gout. The kinetic analysis showed that chrysin possessed a strong inhibition on XO ability in a reversible

In silico design and synthesis of hesperitin derivatives as new xanthine oxidase inhibitors.

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Hesperitin, a naturally occurring flavonoid was hybridized with phenolic acids to evaluate its potential to inhibit the activity of xanthine oxidase (XO), a key enzyme which catalyses xanthine to uric acid which is found to be associated with gout and many life style related

Phytochemicals from Acacia confusa heartwood extracts reduce serum uric acid levels in oxonate-induced mice: their potential use as xanthine oxidase inhibitors.

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In this study, the antihyperuricemic effect of Acacia confusa heartwood extracts and their phytochemicals on potassium oxonate (PO)-induced acute hyperuricemia was investigated for the first time. All treatments at the same dosage (100 mmol/kg) were administered to the abdominal cavity of PO-induced

Recognition of Multiple Methyl Groups on Aromatic Rings by a Polyaromatic Cavity.

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The methyl group is a small substituent, usually showing relatively weak or no interactions with other functional groups and metal ions. Herein, we present the recognition of the number of methyl groups on synthetic and natural aromatic compounds (i.e., benzene and xanthine derivatives,

The C-terminal peptide plays a role in the formation of an intermediate form during the transition between xanthine dehydrogenase and xanthine oxidase.

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Mammalian xanthine oxidoreductase can exist in both dehydrogenase and oxidase forms. Conversion between the two is implicated in such diverse processes as lactation, anti-bacterial activity, reperfusion injury and a growing number of diseases. We have constructed a variant of the rat liver enzyme
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