ReviewProperties of cytochrome P450 isoenzymes and their substrates part 2: properties of cytochrome P450 substrates
References (20)
Biochem. Pharmacol.
(1992)Biochem. Pharmacol.
(1992)Life Sci.
(1991)J. Biol. Chem.
(1995)Med. Res. Rev.
(1996)Cancer Res.
(1990)Drug Metab. Rev.
(1986)Xenobiotica
(1996)Xenobiotica
(1996)Drug Metab. Dispos.
(1996)
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CYP2J2 Molecular Recognition: A New Axis for Therapeutic Design
2020, Pharmacology and TherapeuticsCitation Excerpt :Further information regarding CYP inhibition is reviewed in the book chapter by Correia and Hollenberg (Correia & Hollenberg, 2015). CYP epoxygenases metabolize both lipids and drugs and are able to recognize a wide variety of ligands, including those that are either polycyclic, aliphatic, or both (Correia & Hollenberg, 2015; Lewis et al., 1999; Smith, Ackland, & Jones, 1997a, 1997b). To this point, it has been postulated that some drug substrates of CYP2J2 interfere with its epoxygenase activity and contribute to cardiotoxicity (Solanki et al., 2018) (Arnold & Das, 2018).
Identification and characterization of citalopram new metabolites with the use of UHPLC-Q-TOF technique: In silico toxicity assessment of the identified transformation products
2020, Journal of Pharmaceutical and Biomedical AnalysisCitation Excerpt :Biotransformation of pharmacologically active substances is divided into two stages. During Phase I, the substance is mainly modified to more polar, hydrophilic entities generally due to the enzymatic activity of cytochrome P450 superfamily of enzymes [4–6]. On the contrary, Phase II is responsible for the conjugation of formerly formed metabolites with glutathione, glucuronic or sulfuric acid, etc.
Discovery of renin inhibitors containing a simple aspartate binding moiety that imparts reduced P450 inhibition
2017, Bioorganic and Medicinal Chemistry LettersEmerging technologies for metabolite generation and structural diversification
2013, Bioorganic and Medicinal Chemistry LettersIn silico metabolism studies of dietary flavonoids by CYP1A2 and CYP2C9
2013, Food Research InternationalCitation Excerpt :The same was observed for the Asp313, Phe226, Phe256 and Phe260 residues of the CYP1A2 isoform. The active site of CYP1A2 has been well characterized as being narrow and lined by residues on helix F and helix I (Ekins, de Groot, & Jones, 2001; Sansen et al., 2007; Smith, Ackland, & Jones, 1997a, 1997b). The active site is formed mainly by the backbone of residues Gly316, Ala317, and Asp320.
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