16 research outputs found
NQO2 is a reactive oxygen species generating off-target for acetaminophen
Get PDF[Image: see text] The analgesic and antipyretic compound acetaminophen (paracetamol) is one of the most used drugs worldwide. Acetaminophen overdose is also the most common cause for acute liver toxicity. Here we show that acetaminophen and many structurally related compounds bind quinone reductase 2 (NQO2) in vitro and in live cells, establishing NQO2 as a novel off-target. NQO2 modulates the levels of acetaminophen derived reactive oxygen species, more specifically superoxide anions, in cultured cells. In humans, NQO2 is highly expressed in liver and kidney, the main sites of acetaminophen toxicity. We suggest that NQO2 mediated superoxide production may function as a novel mechanism augmenting acetaminophen toxicity
Crystal and Molecular Structure of Piceatannol; Scavenging Features of Resveratrol and Piceatannol on Hydroxyl and Peroxyl Radicals and Docking with Transthyretin
No full textSynthesis of Casimiroin and Optimization of Its Quinone Reductase 2 and Aromatase Inhibitory Activities
No full textIndolequinone Inhibitors of NRH:Quinone Oxidoreductase 2. Characterization of the Mechanism of Inhibition in both Cell-Free and Cellular Systems
No full textScreening Natural Products for Inhibitors of Quinone Reductase-2 Using Ultrafiltration LC−MS
No full textQuantum Chemical Associations Ligand−Residue: Their Role to Predict Flavonoid Binding Sites in Proteins
No full textDabigatran and Dabigatran Ethyl Ester: Potent Inhibitors of Ribosyldihydronicotinamide Dehydrogenase (NQO2)
No full textBiochemical and Cellular Evidence Demonstrating AKT-1 as a Binding Partner for Resveratrol Targeting Protein NQO2
No full textResveratrol Directly Controls the Activity of Neuronal Ryanodine Receptors at the Single-Channel Level
No full textDesign, Synthesis, and Biological Evaluation of Potent Quinoline and Pyrroloquinoline Ammosamide Analogues as Inhibitors of Quinone Reductase 2
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