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Dihydropyrimidine dehydrogenase (DPYD) catalyzes the first rate-limiting step of the NADPH-dependent catabolism of uracil and thymine to dihydrouracil and dihydrothymine; thus, a deficiency of DPYD leads to an accumulation of uracil and thymine. Abnormal concentrations of these metabolites in bodily fluids may be the cause of neurological disease and a contraindication for treatment of cancer patients with certain pyrimidine analogs. DPYD also catalyzes the anticancer agent 5-fluorouracil (

Potassium channels are present in most mammalian cells, where they participate in a wide range of physiologic responses. The protein encoded by this gene is an integral membrane protein and inward-rectifier type potassium channel. The encoded protein, which has a greater tendency to allow potassium to flow into a cell rather than out of a cell, probably participates in establishing action potential waveform and excitability of neuronal and muscle tissues. Mutations in this gene have been ass

The Eph subfamily represents the largest group of receptor protein tyrosine kinases identified to date (1–3). While the biological activities of these receptors have yet to be determined, there is increasing evidence that they are involved in central nervous system function and in development (1–3). The Eph subfamily receptors of human origin (and their murine/avian homologs) include EphA1 (Eph), EphA2 (Eck), EphA3 (Hek4), EphA4 (Hek8), EphA5 (Hek7), EphA6 (Hek12), EphA7 (Hek11/MDK1), EphA8

Syntaxins were originally thought to be docking proteins, but have more recently been categorized as anchoring proteins that anchor themselves to the cytoplasmic surfaces of cellular membranes. Syntaxins have been shown to bind to various proteins involved in exocytosis, including VAMPs (vesicle-associated membrane proteins), NSF (N-ethylmaleimide-sensitive factor), SNAP 25 (synaptosomal-associated protein of 25kDa), SNAPs (soluble NSF attachment proteins) and synaptotagmin. VAMPs (also design

The Flavin containing monooxygenase family consists of five gene products, FMO1-5, that are major enzymatic oxidants involved in the metabolism of various therapeutics. Located in the liver, FMO3 is a hepatic microsomal enzyme that oxygenates soft nucleophiles such as secondary and tertiary amines. Through its N-oxygenase capabilities, FMO3 acts on a variety of xenobiotics to catalyze oxidative digestion. Defects in the FMO3 gene are the primary cause of trimethylaminuria (TMAuria), an inborn