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Takaaki Kusumi

Researcher at University of Tokyo

Publications -  43
Citations -  2370

Takaaki Kusumi is an academic researcher from University of Tokyo. The author has contributed to research in topics: Dandruff & Anthocyanin. The author has an hindex of 22, co-authored 43 publications receiving 2184 citations.

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Engineering of the Rose Flavonoid Biosynthetic Pathway Successfully Generated Blue-Hued Flowers Accumulating Delphinidin

TL;DR: This work down-regulated the endogenous dihydroflavonol 4-reductase (DFR) gene and overexpressed the Irisxhollandica DFR gene in addition to the viola F3'5'H gene in a rose cultivar, resulting in the accumulation of a high percentage of delphinidin and a novel bluish flower color.
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Aureusidin Synthase: A Polyphenol Oxidase Homolog Responsible for Flower Coloration

TL;DR: DNA sequence analysis revealed that aureusidin synthase belongs to the plant polyphenol oxidase family, providing an unequivocal example of the function of the polyphenl oxidase homolog in plants, i.e., flower coloration.
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Yellow flowers generated by expression of the aurone biosynthetic pathway

TL;DR: Chalcone 4'-O-glucosyltransferase (4'CGT) is essential for aurone biosynthesis and yellow coloration in vivo, and the findings herein open the way to engineering yellow flowers for major ornamental species lacking this color variant.
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Biochemical and Molecular Characterization of a Novel UDP-Glucose:Anthocyanin 3′-O-Glucosyltransferase, a Key Enzyme for Blue Anthocyanin Biosynthesis, from Gentian

TL;DR: This is the first report of the gene isolation of a B-ring-specific glucosyltransferase of anthocyanins, which paves the way to modification of flower color by production of blue anthocianins.
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cDNA cloning, gene expression and subcellular localization of anthocyanin 5-aromatic acyltransferase from Gentiana triflora.

TL;DR: Immunohistochemical analysis demonstrated that the 5AT protein is specifically expressed in the outer epidermal cells of gentian petals and that it is localized mainly in the cytosol, and this indicates that 5AT is a member of a proposed superfamily of multi-functional acyltransferases.