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Tsunehiro Aki

Researcher at Hiroshima University

Publications -  128
Citations -  3221

Tsunehiro Aki is an academic researcher from Hiroshima University. The author has contributed to research in topics: Polyunsaturated fatty acid & Fatty acid. The author has an hindex of 30, co-authored 123 publications receiving 2940 citations. Previous affiliations of Tsunehiro Aki include National Institutes of Health & Laboratory of Molecular Biology.

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Molecular cloning and functional characterization of rat delta-6 fatty acid desaturase.

TL;DR: Results indicate that the protein encoded by the rat cDNA is Δ-6 fatty acid desaturase, and the first 17 amino acids corresponding to the coding region 97-147 of the clone are not required to function in yeast.
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Repressor induced site‐specific binding of HU for transcriptional regulation

TL;DR: It is proposed that HU, in concert with GalR, forms a specific nucleoprotein higher order complex containing a DNA loop and deforms the promoter to make the latter inactive for transcription initiation while remaining sensitive to inducer.
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Immunochemical characterization of recombinant and native tropomyosins as a new allergen from the house dust mite, Dermatophagoides farinae.

TL;DR: In this article, a new allergen complementary DNA (cDNA) clone was isolated from a D. farinae protein cDNA library, which revealed significant homology with tropomyosins conserved in a wide range of animals.
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Thraustochytrid as a potential source of carotenoids

TL;DR: It is described here that thraustochytrid strain KH105, isolated as a DHA producer, also accumulates significant levels of β-carotene and xanthophylls including canthaxanthin and astaxanthIn, which is considered to be a promising source of xanthopylls as well as DHA for use in the food industry.
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Repression and activation of transcription by Gal and Lac repressors: involvement of alpha subunit of RNA polymerase.

TL;DR: It is proposed that Gal and Lac repressors inhibit or stimulate transcription initiation by disabling or stimulating RNA polymerase activity at a post‐binding step by directly or indirectly altering the C‐terminal alpha domain to an unfavorable state at P1 or a more favorable state atP2, respectively.