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Karen A. Veverka

Researcher at Mayo Clinic

Publications -  5
Citations -  148

Karen A. Veverka is an academic researcher from Mayo Clinic. The author has contributed to research in topics: Aldehyde dehydrogenase & Disulfiram. The author has an hindex of 4, co-authored 5 publications receiving 138 citations.

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Journal ArticleDOI

Inhibition of aldehyde dehydrogenase by disulfiram and its metabolite methyl diethylthiocarbamoyl-sulfoxide.

TL;DR: Observations are consistent with mechanisms where inhibition of aldehyde dehydrogenase by DSF in vitro involves oxidation of the active site, whereas MeDTC-SO forms a covalent adduct with the protein in vitro resulting in cessation of enzyme activity.
Journal ArticleDOI

The Rat Neurotensin Receptor Expressed in Chinese Hamster Ovary Cells Mediates the Release of Inositol Phosphates

TL;DR: Results indicating that the expressed transfected receptor was functional and Neurotensin‐mediated inositol phosphate release is the first report of second messenger synthesis for this receptor expressed in atransfected cell line suggest that the relation between structure and function of the neurotensin receptor can be readily studied in trans infected cell lines.
Journal ArticleDOI

S-Methyl N,N-diethylthiocarbamate sulfone, a potential metabolite of disulfiram and potent inhibitor of low Km mitochondrial aldehyde dehydrogenase

TL;DR: Results of these studies indicate that MeDTC sulfone, a potential metabolite of disulfiram, is a potent, irreversible inhibitor of low Km mitochondrial ALDH.
Journal ArticleDOI

Simultaneous structure—activity determination of disulfiram photolysis products by on-line continuous-flow liquid secondary ion mass spectrometry and enzyme inhibition assay

TL;DR: A mixture of products derived photochemically from DSF with on-line microbore HPLC-continuous-flow liquid secondary ion mass spectrometry was analyzed and structurally characterize an interesting sulfine compound that inhibited ALDH.
Book ChapterDOI

Inhibition of and Interaction with Human Recombinant Mitochondrial Aldehyde Dehydrogenase by Methyl Diethylthiocarbamate Sulfoxide

TL;DR: The effect of MeDTC-sulfoxide upon the activity of human ALDH was examined and the interaction of the inhibitor with this enzyme by mass spectrometry was investigated.