S
S.A.B.E. van Acker
Researcher at VU University Amsterdam
Publications - 18
Citations - 3690
S.A.B.E. van Acker is an academic researcher from VU University Amsterdam. The author has contributed to research in topics: Cardiotoxicity & Antioxidant. The author has an hindex of 11, co-authored 18 publications receiving 3552 citations.
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Structural aspects of antioxidant activity of flavonoids.
TL;DR: It can be concluded that Ep/2 values and iron chelating activity can almost completely describe the LPO inhibiting behaviour of the flavonoids.
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Structural aspects of antioxidant activity of flavonoids.
S.A.B.E. van Acker,D.-J. Van Den Berg,M. N. J. L. Tromp,D. H. Griffioen,W.P. van Bennekom,W.J.F. van der Vijgh,Aalt Bast +6 more
TL;DR: In this article, a large group of flavonoids from all major structural subclasses were tested on their ability to inhibit doxorubicin (enzymatically)-induced microsomal lipid peroxidation (LPO) and to chelate Fe2+.
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A quantum chemical explanation of the antioxidant activity of flavonoids.
S.A.B.E. van Acker,M.J. de Groot,D.-J. Van Den Berg,M. N. J. L. Tromp,G. M. Donne-Op Den Kelder,W.J.F. van der Vijgh,Aalt Bast +6 more
TL;DR: By comparing the geometries of several flavonoids, this work was able to explain the structural dependency of the antioxidant action of these compounds and investigate the spin density of the radical to determine the delocalization possibilities.
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Flavonoids as Scavengers of Nitric Oxide Radical
TL;DR: It was found that the flavonoids are very potent .NO scavengers and the anthocyanidins were found to be more effective scavengers than the hydroxyethylrutosides, which correlated with their therapeutic activity.
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A predictive model for substrates of cytochrome P450-debrisoquine (2D6).
L. Koymans,Nico P. E. Vermeulen,S.A.B.E. van Acker,J. M. Te Koppele,J. J. P. Heykants,K. Lavrijsen,W. Meuldermans,G. M. Donne-Op Den Kelder +7 more
TL;DR: The substrate specificity of P450 2D6 most likely is determined by the distance between oxidation site and basic nitrogen atom, by steric constraints near the oxidation site, and by the degree of complementarity between the MEPs of substrate and protein in the planar region adjacent to the oxidationSite.