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Natalia Kolosova
Researcher at Purdue University
Publications - 9
Citations - 1331
Natalia Kolosova is an academic researcher from Purdue University. The author has contributed to research in topics: Antirrhinum majus & Benzoic acid. The author has an hindex of 7, co-authored 8 publications receiving 1225 citations.
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Journal ArticleDOI
(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
Natalia Dudareva,Diane M. Martin,Christine M. Kish,Natalia Kolosova,Nina M. Gorenstein,Jenny Fäldt,Barbara Miller,Jörg Bohlmann +7 more
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.
Journal ArticleDOI
Developmental Regulation of Methyl Benzoate Biosynthesis and Emission in Snapdragon Flowers
Natalia Dudareva,Lisa M. Murfitt,Craig J. Mann,Nina M. Gorenstein,Natalia Kolosova,Christine M. Kish,Connie C. Bonham,Karl V. Wood +7 more
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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Cellular and subcellular localization of S-adenosyl-L-methionine:benzoic acid carboxyl methyltransferase, the enzyme responsible for biosynthesis of the volatile ester methylbenzoate in snapdragon flowers.
TL;DR: It is suggested that scent biosynthetic genes are expressed almost exclusively in the epidermal cells of floral organs and cytosolic location of methylbenzoate biosynthesis is suggested.
Journal ArticleDOI
Purification and characterization of S-adenosyl-L-methionine:benzoic acid carboxyl methyltransferase, the enzyme responsible for biosynthesis of the volatile ester methyl benzoate in flowers of Antirrhinum majus.
TL;DR: The molecular mass values for native and denatured protein were 100 and 49 kDa, respectively, suggesting that the active enzyme is a homodimer, and the addition of monovalent cations K+ and NH4+ stimulates BAMT activity by a factor of 2, whereas the added of Fe2+ and Cu2+ has a strong inhibitory effect.