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Nina M. Gorenstein

Researcher at Purdue University

Publications -  8
Citations -  1396

Nina M. Gorenstein is an academic researcher from Purdue University. The author has contributed to research in topics: SH2 domain & Benzoic acid. The author has an hindex of 8, co-authored 8 publications receiving 1309 citations.

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(E)-β-Ocimene and Myrcene Synthase Genes of Floral Scent Biosynthesis in Snapdragon: Function and Expression of Three Terpene Synthase Genes of a New Terpene Synthase Subfamily

TL;DR: Analyses of tissue-specific, developmental, and rhythmic expression of these monoterpene synthase genes in snapdragon flowers revealed coordinated regulation of phenylpropanoid and isoprenoid scent production.
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Colinearity and its exceptions in orthologous adh regions of maize and sorghum

TL;DR: A much higher degree of diversity at a microstructural level than predicted by genetic mapping studies for closely related grass species, as well as for comparisons of monocots and dicots is revealed.
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Developmental Regulation of Methyl Benzoate Biosynthesis and Emission in Snapdragon Flowers

TL;DR: Linear regression analysis revealed that production of methyl benzoate is regulated by the amount of benzoic acid and theamount of BAMT protein, which in turn is regulated at the transcriptional level.
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Regulation of Circadian Methyl Benzoate Emission in Diurnally and Nocturnally Emitting Plants

TL;DR: The data clearly show that the total amount of substrate (benzoic acid) in the cell is involved in the regulation of the rhythmic emission of methyl benzoate, and suggest that similar molecular mechanisms are involved inThe regulation of methyl Benzoate production in diurnally (snapdragon) and noctURNally (tobacco and petunia) emitting plants.
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Molecular cloning and characterization of a candidate human growth-related and time-keeping constitutive cell surface hydroquinone (NADH) oxidase.

TL;DR: The cloning, expression, and characterization of a human candidate constitutive ENOX (CNOX or ENOX1) protein is reported, with functional motifs previously identified by site-directed mutagenesis in a cancer-associated ENOX2 as adenine nucleotide or copper binding along with essential cysteines present, but the drug-binding motif (EEMTE) sequence of ENox2 is absent.