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Donald H. Maurice

Researcher at Queen's University

Publications -  24
Citations -  3245

Donald H. Maurice is an academic researcher from Queen's University. The author has contributed to research in topics: Phosphodiesterase & Phosphodiesterase 3. The author has an hindex of 20, co-authored 24 publications receiving 3038 citations. Previous affiliations of Donald H. Maurice include McMaster University.

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Journal ArticleDOI

Advances in targeting cyclic nucleotide phosphodiesterases

TL;DR: Pharmaceutical interest in PDEs has been reignited by the increasing understanding of the roles of individual P DEs in regulating the subcellular compartmentalization of specific cyclic nucleotide signalling pathways, by the structure-based design of novel specific inhibitors and by the development of more sophisticated strategies to target individual PDE variants.
Journal Article

Molecular basis of the synergistic inhibition of platelet function by nitrovasodilators and activators of adenylate cyclase: inhibition of cyclic AMP breakdown by cyclic GMP.

TL;DR: Although cyclic GMP may mediate the inhibition of rabbit platelet function by high concentrations of nitrovasodilators added alone, the synergistic interaction of lower concentrations with PGE1 depends on an enhanced accumulation of cyclic AMP.
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Cyclic Nucleotide Phosphodiesterase Activity, Expression, and Targeting in Cells of the Cardiovascular System

TL;DR: This review introduces the PDE families whose members are expressed in cells of the cardiovascular system including cardiomyocytes, vascular smooth muscle cells, and vascular endothelial cells and attempts to emphasize how changes in the activity, expression, and targeting of PDE influence cyclic nucleotide-mediated regulation of the behavior of these cells.
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cAMP-Specific phosphodiesterase-4 enzymes in the cardiovascular system: a molecular toolbox for generating compartmentalized cAMP signaling.

TL;DR: How cardiomyocytes and vascular smooth muscle cells selectively vary both the expression and the catalytic activities of PDE4 isoforms to regulate their various functions are described and how altered regulation of these processes can influence the development of cardiovascular pathologies, such as heart failure, as well as various vasculopathies.
Journal Article

Selective inhibition of heme oxygenase, without inhibition of nitric oxide synthase or soluble guanylyl cyclase, by metalloporphyrins at low concentrations.

TL;DR: CrMP, at a concentration of 5 microM, was a selective inhibitor of HO activity and was the most useful metalloporphyrin for the conditions tested, suggesting that CrMP would appear to be a valuable chemical probe in elucidating the physiological role of HO.