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Satori A. Marchitti

Researcher at United States Environmental Protection Agency

Publications -  23
Citations -  1694

Satori A. Marchitti is an academic researcher from United States Environmental Protection Agency. The author has contributed to research in topics: Aldehyde dehydrogenase & Breast milk. The author has an hindex of 15, co-authored 21 publications receiving 1426 citations. Previous affiliations of Satori A. Marchitti include University of Colorado Denver & Anschutz Medical Campus.

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Non-P450 aldehyde oxidizing enzymes: the aldehyde dehydrogenase superfamily.

TL;DR: What is currently known about each member of the human ALDH superfamily, composed of NAD(P)+-dependent enzymes that catalyze aldehyde oxidation, is presented including the pathophysiological significance of these enzymes.
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Neurotoxicity and Metabolism of the Catecholamine-Derived 3,4-Dihydroxyphenylacetaldehyde and 3,4-Dihydroxyphenylglycolaldehyde: The Role of Aldehyde Dehydrogenase

TL;DR: This article presents a comprehensive review of what is currently known of both the neurotoxicity and respective metabolism pathways of 3,4-dihydroxyphenylacetaldehyde and 3, 4-Dihydroxybutyric aciduria with an emphasis on the role that aldehyde dehydrogenase enzymes play in the detoxification of these two aldehydes.
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Environmental Chemicals in Breast Milk and Formula: Exposure and Risk Assessment Implications.

TL;DR: Better-designed studies are needed to characterize infant exposures to environmental chemicals in breast milk and infant formula as well as to improve risk assessments of chemicals found in both foods.
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Human and Rat ABC Transporter Efflux of Bisphenol A and Bisphenol A Glucuronide: Interspecies Comparison and Implications for Pharmacokinetic Assessment

TL;DR: Evaluated BPA and BPA-G as potential substrates for the human and rat ABC transporters: P-glycoprotein (MDR1), multidrug resistance-associated proteins (MRPs), and breast cancer-resistant protein (BCRP), and analysis of ABC transporter amino acid sequences revealed key differences in putative binding site composition that may explain substrate specificity.