ArticleEvidence-based complementary and alternative medicine : eCAM2016
Evaluation of the Isoflavone Genistein as Reversible Human Monoamine Oxidase-A and -B Inhibitor.
Article in Evidence-based complementary and alternative medicine : eCAM, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
23 citing papers in PubMed, 39 citations in OpenAlex.
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- Review
- Isoflavones prevent oxidative stress and inhibit the activity of the enzyme monoamine oxidase in vitro.Molecular biology reports · 2019Article
- Genus Psoralea: A review of the traditional and modern uses, phytochemistry and pharmacology.Journal of ethnopharmacology · 2019Review
- Quercetin and Related Chromenone Derivatives as Monoamine Oxidase Inhibitors: Targeting Neurological and Mental Disorders.Molecules (Basel, Switzerland) · 2019Review
- MAO-A Inhibitory Potential of Terpene Constituents from Ginger Rhizomes-A Bioactivity Guided Fractionation.Molecules (Basel, Switzerland) · 2018Article
- Psoralea corylifolia L: Ethnobotanical, biological, and chemical aspects: A review.Phytotherapy research : PTR · 2018Review
- Inhibition of human monoamine oxidase A and B by flavonoids isolated from two Algerian medicinal plants.Phytomedicine : international journal of phytotherapy and phytopharmacology · 2018Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Monoamine oxidases inhibitors (MAOIs) are effective therapeutic drugs for managing Parkinson's disease (PD) and depression. However, their irreversibility may lead to rare but serious side effects. As finding safer and reversible MAOIs is our target, we characterized the recombinant human (h) MAO-A and MAO-B inhibition potentials of two common natural isoflavones, genistein (GST) and daidzein (DZ) using luminescence assay. The results obtained showed that DZ exhibits partial to no inhibition of the isozymes examined while GST inhibited hMAO-B (IC50 of 6.81 μM), and its hMAO-A inhibition was more potent than the standard deprenyl. Furthermore, the reversibility, mode of inhibition kinetics, and tyramine oxidation of GST were examined. GST was a time-independent reversible and competitive hMAO-A and hMAO-B inhibitor with a lower K i of hMAO-B (1.45 μM) than hMAO-A (4.31 μM). GST also inhibited hMAO-B tyramine oxidation and hydrogen peroxide production more than hMAO-A. Docking studies conducted indicated that the GST reversibility and hMAO-B selectivity of inhibition may relate to C5-OH effects on its orientation and its interactions with the threonine 201 residue of the active site. It was concluded from this study that the natural product GST has competitive and reversible MAOs inhibitions and may be recommended for further investigations as a useful therapeutic agent for Parkinson's disease.
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Registered trials
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