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- j.pharmthera.2005.01.001 author "Krueger SK, Williams DE".
- j.pharmthera.2005.01.001 date "June 2005".
- j.pharmthera.2005.01.001 doi "10.1016/j.pharmthera.2005.01.001".
- j.pharmthera.2005.01.001 isCitedBy Amphetamine.
- j.pharmthera.2005.01.001 isCitedBy Dextroamphetamine.
- j.pharmthera.2005.01.001 isCitedBy Flavin-containing_monooxygenase.
- j.pharmthera.2005.01.001 isCitedBy Methamphetamine.
- j.pharmthera.2005.01.001 isCitedBy Phenethylamine.
- j.pharmthera.2005.01.001 issue "3".
- j.pharmthera.2005.01.001 journal "Pharmacol. Ther.".
- j.pharmthera.2005.01.001 journal "Pharmacology & Therapeutics".
- j.pharmthera.2005.01.001 last2 "Williams".
- j.pharmthera.2005.01.001 pages "357–387".
- j.pharmthera.2005.01.001 pages "357– 387".
- j.pharmthera.2005.01.001 pages "357–387".
- j.pharmthera.2005.01.001 pmc "1828602".
- j.pharmthera.2005.01.001 pmid "15922018".
- j.pharmthera.2005.01.001 quote "The biogenic amines, phenethylamine and tyramine, are N-oxygenated by FMO to produce the N-hydroxy metabolite, followed by a rapid second oxygenation to produce the trans-oximes . This stereoselective N-oxygenation to the trans-oxime is also seen in the FMO-dependent N-oxygenation of amphetamine ... Interestingly, FMO2, which very efficiently N-oxygenates N-dodecylamine, is a poor catalyst of phenethylamine N-oxygenation. The most efficient human FMO in phenethylamine N-oxygenation is FMO3, the major FMO present in adult human liver; the Km is between 90 and 200 μM .".
- j.pharmthera.2005.01.001 title "Mammalian flavin-containing monooxygenases: structure/function, genetic polymorphisms and role in drug metabolism".
- j.pharmthera.2005.01.001 vauthors "Krueger SK, Williams DE".
- j.pharmthera.2005.01.001 volume "106".