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Debra J. Salmon

Researcher at University of Arizona

Publications -  11
Citations -  1052

Debra J. Salmon is an academic researcher from University of Arizona. The author has contributed to research in topics: Nitroxyl & NONOate. The author has an hindex of 7, co-authored 11 publications receiving 972 citations. Previous affiliations of Debra J. Salmon include University of Minnesota & Kansas State University.

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Building co-crystals with molecular sense and supramolecular sensibility

TL;DR: In this article, the authors provide an overview of some modular and transferable strategies for the synthesis of binary and ternary supermolecules and co-crystals based upon a hierarchy of intermolecular interactions, notably hydrogen bonds.
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Cyanophenyloximes: Reliable and Versatile Tools for Hydrogen-Bond Directed Supramolecular Synthesis of Cocrystals

TL;DR: A systematic structural and spectroscopic examination of the products resulting from cocrystallization reactions between three types of phenyloximes R−CN−OH (where R = H, Me, or CN) and a series of N-heterocyclic hydrogen-bond acceptors is presented in this paper.
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The specificity of nitroxyl chemistry is unique among nitrogen oxides in biological systems.

TL;DR: The chemical biology of HNO has been identified as related to, but unique from, that of its redox congener nitric oxide, and its pharmacological benefits have been demonstrated in several pathophysiological settings such as cardiovascular disorders, cancer, and alcoholism.
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HNO and NO Release from a Primary Amine-Based Diazeniumdiolate As a Function of pH

TL;DR: P pH is shown to also affect product formation from IPA/NO, suggesting that at or above this pH, IPA/NO is primarily an HNO donor, and primary amine NONOates may serve as a tunable class of nitrogen oxide donor.
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Dual Mechanisms of HNO Generation by a Nitroxyl Prodrug of the Diazeniumdiolate (NONOate) Class

TL;DR: A novel caged form of the highly reactive bioeffector molecule, nitroxyl (HNO), which was significantly enhanced over 1 at physiological pH, in part because the slower rate of hydrolysis for 2 generated a correspondingly lower steady-state concentration of HNO, thus, minimizing self-consumption and enhancing trapping by biological targets such as metmyoglobin and glutathione.