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Role of reactive oxygen species and poly-ADP-ribose polymerase in the development of AZT-induced cardiomyopathy in rat.
TLDR
ROS-mediated oxidative damages, activated ADP-ribosylation reactions and accelerated NAD+ catabolism play basic roles in the development of AZT-induced cardiomyopathy in the animal model and indicated that these ROS-mediated processes can be important factors in theDevelopment of myopathy and cardiopathy in zidovudine-treated AIDS patients. Expand
PARP1- and CTCF-Mediated Interactions between Active and Repressed Chromatin at the Lamina Promote Oscillating Transcription.
TLDR
An inter-chromosomal network connecting active loci enriched in circadian genes to repressed lamina-associated domains (LADs) is uncovered, finding that PARP1 and CTCF-regulated contacts between circadian loci and the repressive chromatin environment at the lamina mediate circadian transcriptional plasticity. Expand
The glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase works as an arsenate reductase in human red blood cells and rat liver cytosol.
  • Z. Gregus, B. Németi
  • Biology, Medicine
  • Toxicological sciences : an official journal of…
  • 1 June 2005
TLDR
It is shown that, if supplied with glutathione (GSH), NAD, and glycolytic substrate, the mixture of purified GAPDH and PGK indeed catalyzes the reduction of AsV, which is exclusively responsible for reduction in human erythrocytes. Expand
Glutathione synthetase promotes the reduction of arsenate via arsenolysis of glutathione.
TLDR
The findings support the conclusion that GS promotes reduction of As(V) by catalyzing the arsenolysis of GSH, thus producing ADP-arsenate, which upon being released from the enzyme is readily reduced by GSH to As(III). Expand
Purine nucleoside phosphorylase as a cytosolic arsenate reductase.
  • Z. Gregus, B. Németi
  • Chemistry, Medicine
  • Toxicological sciences : an official journal of…
  • 1 November 2002
TLDR
The hypothesis that PNP is responsible for the thiol- and purine nucleoside-dependent reduction of AsV to AsIII by rat liver cytosol is tested and it is found that P NP reduces AsVto AsIII, using AsV instead of phosphate in the reaction above. Expand
Dose-dependent biotransformation of arsenite in rats--not S-adenosylmethionine depletion impairs arsenic methylation at high dose.
TLDR
It appears that exhausted elimination capacity of As III, rather than MMAsIII produced from AsIII, contributes significantly to the acute toxicity of AsIII after GSH depletion the retained AsIII can increasingly inhibit SH-enzymes, thus causing ATP depletion and energetic disorder. Expand
Arsenate reduction in human erythrocytes and rats--testing the role of purine nucleoside phosphorylase.
TLDR
PNP does not appear to play a significant role in AsV reduction in human erythrocytes and in rats in vivo, and its biochemical mechanism in mammals is incompletely understood. Expand
Mechanism of thiol-supported arsenate reduction mediated by phosphorolytic-arsenolytic enzymes: II. Enzymatic formation of arsenylated products susceptible for reduction to arsenite by thiols.
TLDR
Phosphorolytic enzymes, such as PNP, GAPDH, GPa, and PTA, promote thiol-dependent AsV reduction because they convert AsV into arsenylated products reducible by thiols more readily than AsV. Expand
Reduction of dimethylarsinic acid to the highly toxic dimethylarsinous acid by rats and rat liver cytosol.
TLDR
Reduction ofDMAs(V) to the highly toxic DMAs(III) in rats and rat liver cytosol is a GSH-dependent enzymatic process, yet its mechanism remains uncertain. Expand
Metabolism of carnitine in phenylacetic acid-treated rats and in patients with phenylketonuria.
TLDR
P phenylacetic acid (PEAA) decreased the hepatic level of glutamic acid and alpha-ketoglutaric acid (alpha-KG), suggesting a mechanism for the reduced flux through the butyrobetaine hydroxylase enzyme, because alpha-G is an obligatory co-enzyme. Expand
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