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Ian A. McDonald

Researcher at Marion Merrell Dow

Publications -  46
Citations -  1072

Ian A. McDonald is an academic researcher from Marion Merrell Dow. The author has contributed to research in topics: Amino acid & Serotonin. The author has an hindex of 19, co-authored 46 publications receiving 1055 citations. Previous affiliations of Ian A. McDonald include University of Dundee & Merck & Co..

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Nitric oxide synthesis in the CNS endothelium and macrophages differs in its sensitivity to inhibition by arginine analogues.

TL;DR: The results suggest that distinct enzymes are responsible for nitric oxide synthesis in different cell types, and indicate that it may be possible to selectively modulateNitric oxide production in vivo.
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Enzyme-activated irreversible inhibitors of monoamine oxidase: phenylallylamine structure-activity relationships

TL;DR: Seventeen 2-aryl-3-haloallylamines derivatives were prepared and evaluated as inhibitors of monoamine oxidase and (E)-2-(3,4-dimethoxyphenyl)-3-fluoroallylamine proved to be in vitro as selective for the B form of MAO as deprenyl.
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A protective role for nitric oxide in the oxidative modification of low density lipoproteins by mouse macrophages.

TL;DR: The data indicate that the production of NO may inhibit the oxidative modification of LDL with cytokine‐stimulated macrophages and suggest that NO plays a protective role in limiting macrophage‐induced LDL modification.
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Characterization of cell selectivity of two novel inhibitors of nitric oxide synthesis.

TL;DR: Two novel inhibitors to block cytokine-induced nitric oxide (NO) synthesis by macrophages and vascular smooth muscle cells, as well as NO production by the constitutive enzyme in central nervous system tissue are assessed.
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3-(2-carboxyindol-3-yl)propionic acid derivatives: antagonists of the strychnine-insensitive glycine receptor associated with the N-methyl-D-aspartate receptor complex.

TL;DR: L'acide 3-(4,6-dichloro-2-carboxyindol-3-yl) propionique ainsi que d'autres derives ofert une nouvelle classe d'antagonistes de l'acides N-methyl-D-aspartique, agissant au niveau d'un site de liaison de la glycine insensible a la strychnine.