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Herbert T. Nagasawa

Researcher at University of Minnesota

Publications -  168
Citations -  3999

Herbert T. Nagasawa is an academic researcher from University of Minnesota. The author has contributed to research in topics: Aldehyde dehydrogenase & Cyanamide. The author has an hindex of 32, co-authored 168 publications receiving 3864 citations. Previous affiliations of Herbert T. Nagasawa include United States Department of Veterans Affairs & Veterans Health Administration.

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Reaction between S-nitrosothiols and thiols: generation of nitroxyl (HNO) and subsequent chemistry.

TL;DR: It is found that S-nitrosothiols can react with thiols to generate nitroxyl (HNO) and the corresponding disulfide, which results in the generation of other species including NO, sulfinamide, and hydroxylamine.
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Mechanisms of Inhibition of Aldehyde Dehydrogenase by Nitroxyl, the Active Metabolite of the Alcohol Deterrent Agent Cyanamide

TL;DR: The sulfhydryl reagents dithiothreitol and reduced glutathione completely blocked the inhibition of AlDH by Angeli's salt and were able to partially restore activity to the nitroxyl-inhibited enzyme, the extent of reactivation being dependent on the pH at which the inactivation occurred.
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Reaction of nitric oxide with the free sulfhydryl group of human serum albumin yields a sulfenic acid and nitrous oxide.

TL;DR: The production of HSA-sulfenic acid by NO, as well as by other oxidizing agents such as H2O2 and peroxynitrite, followed by its reaction with circulating GSH or L-Cys may account for the mixed disulfides of H SA observed in plasma.
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Evidence for nitroxyl in the catalase-mediated bioactivation of the alcohol deterrent agent cyanamide

TL;DR: Utilisation de cyanamide marque au 15 N and au 13 C pour mettre en evidence l'intermediaire N-hydroxycyanamide donnant par decomposition le nitroxyle, inhibiteur de l'aldehyde deshydrogenase (ALDH)
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2-Substituted thiazolidine-4(R)-carboxylic acids as prodrugs of L-cysteine. Protection of mice against acetaminophen hepatotoxicity

TL;DR: It is suggested that these 2-substituted thiazolidine-4(R)-carboxylic acids are prodrugs of L-cysteine that liberate this sulfhydryl amino acid in vivo by nonenzymatic ring opening, followed by solvolysis.