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Kirkwood A. Pritchard

Researcher at Medical College of Wisconsin

Publications -  164
Citations -  10696

Kirkwood A. Pritchard is an academic researcher from Medical College of Wisconsin. The author has contributed to research in topics: Endothelium & Nitric oxide. The author has an hindex of 52, co-authored 162 publications receiving 10186 citations. Previous affiliations of Kirkwood A. Pritchard include Yale University & Ohio State University.

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Superoxide generation by endothelial nitric oxide synthase: The influence of cofactors

TL;DR: The mechanism of superoxide generation by endothelial nitric oxide synthase (eNOS) was investigated by the electron spin resonance spin-trapping technique using 5-diethoxyphosphoryl-5-methyl-1-pyrroline N-oxide as discussed by the authors.
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Chronic exercise in dogs increases coronary vascular nitric oxide production and endothelial cell nitric oxide synthase gene expression.

TL;DR: This finding suggests that exercise can provide a stimulus for the enhanced production of EDRF/NO, thus possibly contributing to the beneficial effects of exercise on the cardiovascular system.
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Native Low-Density Lipoprotein Increases Endothelial Cell Nitric Oxide Synthase Generation of Superoxide Anion

TL;DR: In this article, low-density lipoprotein (n-LDL) perturbs endothelial cell (EC) release of superoxide anion (O2-) and nitric oxide (NO), which increases the likelihood of the formation of peroxynitrite (ONOO-), a potent oxidant.
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Endothelial nitric oxide synthase-dependent superoxide generation from adriamycin

TL;DR: It is demonstrated here that the endothelial isoform of nitric oxide synthase (eNOS) reduces adriamycin to the semiquinone radical, which enhances superoxide formation and Nitric oxide production and leads eNOS to generate peroxynitrite and hydrogen peroxide, potent oxidants implicated in several vascular pathologies.
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Heat shock protein 90 mediates the balance of nitric oxide and superoxide anion from endothelial nitric-oxide synthase.

TL;DR: Data show that Hsp 90 is essential for eNOS-dependent ·NO production and that inhibition of ATP-dependent conformational changes in Hsp90 uncouples eN OS activity and increases eNos-dependent O⨪2production.