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Toshihiko Ashikari

Researcher at Kobe Gakuin University

Publications -  68
Citations -  3598

Toshihiko Ashikari is an academic researcher from Kobe Gakuin University. The author has contributed to research in topics: Yeast & Gene. The author has an hindex of 32, co-authored 68 publications receiving 3439 citations.

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S-phase checkpoint proteins Tof1 and Mrc1 form a stable replication-pausing complex

TL;DR: It is demonstrated that the checkpoint regulatory proteins Tof1 and Mrc1 interact directly with the DNA replication machinery in Saccharomyces cerevisiae, which forms a stable pausing structure that serves to anchor subsequent DNA repair events.
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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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Genome Sequence of the Lager Brewing Yeast, an Interspecies Hybrid

TL;DR: The genome sequence of this interspecies hybrid yeast provides a new tool for better understanding of lager brewing yeast behavior in industrial beer production.
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Pure and Mixed Genetic Lines of Saccharomyces bayanus and Saccharomyces pastorianus and Their Contribution to the Lager Brewing Strain Genome

TL;DR: This study identifies brewing strains that could be used as novel genetic sources in strain improvement programs and provides data that can be used to generate a model of how naturally occurring and industrial hybrid strains may have evolved.
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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.