Zobrazeno 1 - 10
of 129
pro vyhledávání: '"de Groot Mj"'
Publikováno v:
Journal of Medicinal Chemistry. 42:4062-4070
A combined protein and pharmacophore model for cytochrome P450 2D6 (CYP2D6) has been extended with a second pharmacophore in order to explain CYP2D6 catalyzed N-dealkylation reactions. A group of 14 experimentally verified N-dealkylation reactions fo
Publikováno v:
de Groot, M J, Bijlo, G J, Martens, B J, Goeptar, A R & Vermeulen, N P E 1997, ' A refined substrate model for human cytochrome P450 2D6. ', SON Discussiegroep Farmacochemie, Lunteren, 14/04/97-15/04/97 .
SON Discussiegroep Farmacochemie, Lunteren
Chemical Research in Toxicology, 10, 41-48. American Chemical Society
de Groot, M J, Bijlo, G J, Martens, B J, van Acker, F A A & Vermeulen, N P E 1997, ' A refined substrate model for human cytochrome P450 2D6. ', Chemical Research in Toxicology, vol. 10, pp. 41-48 . https://doi.org/10.1021/tx960129f
Vrije Universiteit Amsterdam
SON Discussiegroep Farmacochemie, Lunteren
Chemical Research in Toxicology, 10, 41-48. American Chemical Society
de Groot, M J, Bijlo, G J, Martens, B J, van Acker, F A A & Vermeulen, N P E 1997, ' A refined substrate model for human cytochrome P450 2D6. ', Chemical Research in Toxicology, vol. 10, pp. 41-48 . https://doi.org/10.1021/tx960129f
Vrije Universiteit Amsterdam
Cytochromes P450 (P450s) constitute a large superfamily of heme-containing enzymes, capable of oxidizing and reducing a variety of substrates. Cytochrome P450 2D6 is a polymorphic member of the P450 superfamily and is absent in 5-9% of the Caucasian
Publikováno v:
Chemical Research in Toxicology, 9, 1079-1091. American Chemical Society
de Groot, M J, Vermeulen, N P E, Kramers, J D, van Acker, F A A & Donné-Op den Kelder, G M 1996, ' A three-dimensional protein model for human cytochrome P450 2D6 based on the crystal structures of P450 101, P450 102, and P450 108. ', Chemical Research in Toxicology, vol. 9, pp. 1079-1091 . https://doi.org/10.1021/tx960003i
de Groot, M J, Vermeulen, N P E, Kramers, J D, van Acker, F A A & Donné-Op den Kelder, G M 1996, ' A three-dimensional protein model for human cytochrome P450 2D6 based on the crystal structures of P450 101, P450 102, and P450 108. ', Chemical Research in Toxicology, vol. 9, pp. 1079-1091 . https://doi.org/10.1021/tx960003i
Cytochromes P450 (P450s) constitute a superfamily of phase I enzymes capable of oxidizing and reducing various substrates. P450 2D6 is a polymorphic enzyme, which is absent in 5-9% of the Caucasian population as a result of a recessive inheritance of
Autor:
de Groot Mj, Heijnen Vv, van der Vusse Gj, Robert S. Reneman, A.H.G.J. Schrijvers, Peter M. Frederik
Publikováno v:
Journal of Molecular and Cellular Cardiology. 22:653-665
In normoxic hearts a limited number of multilamellar vesicles was found in both endothelial cells and myocytes. The total number of multilamellar vesicles observed in myocytes, particularly those extruded from mitochondria, significantly increased in
Publikováno v:
Nature biotechnology. 16(9)
Agrobacterium tumefaciens transfers part of its Ti plasmid, the T-DNA, to plant cells during tumorigenesis. It is routinely used for the genetic modification of a wide range of plant species. We report that A. tumefaciens can also transfer its T-DNA
Publikováno v:
FASEB Journal, 11(9), A778-A778. FASEB
Vermeulen, NPE, De Groot, MJ, Commandeur, JXM & Meerman, JHM 1997, ' Protein and substrate modeling as a tool to predict metabolism: The case of cytochrome P450 2D6. ', FASEB Journal, vol. 11, no. 9, pp. A778-A778 .
Vermeulen, NPE, De Groot, MJ, Commandeur, JXM & Meerman, JHM 1997, ' Protein and substrate modeling as a tool to predict metabolism: The case of cytochrome P450 2D6. ', FASEB Journal, vol. 11, no. 9, pp. A778-A778 .
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::0c53106d0972fac7fb6c428a6275fda9
https://research.vu.nl/en/publications/2ec3b14c-7a6b-4808-8ea1-4fea21c3a788
https://research.vu.nl/en/publications/2ec3b14c-7a6b-4808-8ea1-4fea21c3a788
Publikováno v:
Molecular and cellular biochemistry. 146(2)
Previous studies have shown that exogenous lactate impairs mechanical function of reperfused ischaemic hearts, while pyruvate improves post-ischaemic recovery. The aim of this study was to investigate whether the diverging influence of exogenous lact
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