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David R. Gang

Researcher at Washington State University

Publications -  142
Citations -  9971

David R. Gang is an academic researcher from Washington State University. The author has contributed to research in topics: Mass spectrometry & Gene. The author has an hindex of 48, co-authored 133 publications receiving 8725 citations. Previous affiliations of David R. Gang include University of Arizona & Johns Hopkins University School of Medicine.

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Genetics and biochemistry of secondary metabolites in plants: an evolutionary perspective.

TL;DR: Repeated evolution is a special form of convergent evolution in which new enzymes with the same function evolve independently in separate plant lineages from a shared pool of related enzymes with similar but not identical functions.
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The Lycopodium alkaloids

TL;DR: The effect of HupA and other cholinesterase inhibitors (anti-AD drugs) on acetylcholine esterase activity in the rat cortex and butylCholine esters activity are compared.
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An investigation of the storage and biosynthesis of phenylpropenes in sweet basil.

TL;DR: It is demonstrated here that the volatile oil constituents eugenol and methylchavicol accumulate, respectively, in the peltate glands of basil lines SW and EMX-1, which serve as an excellent model system to study phenylpropene biosynthesis.
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Understanding in vivo benzenoid metabolism in petunia petal tissue.

TL;DR: In vivo stable isotope labeling and computer-assisted metabolic flux analysis were used to investigate the metabolic pathways in petunia (Petunia hybrida) cv Mitchell leading from Phe to benzenoid compounds, a process that requires the shortening of the side chain by a C2 unit.
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Eugenol and isoeugenol, characteristic aromatic constituents of spices, are biosynthesized via reduction of a coniferyl alcohol ester

TL;DR: It is shown that glandular trichomes of sweet basil, which synthesize and accumulate phenylpropenes, possess an enzyme that can use coniferyl acetate and NADPH to form eugenol, and that petunia and basil phenylpropene-forming enzymes belong to a structural family of NADPH-dependent reductases that also includes pinoresinol-lariciresinol reductase.