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Shin-ichi Ayabe

Researcher at Nihon University

Publications -  70
Citations -  2997

Shin-ichi Ayabe is an academic researcher from Nihon University. The author has contributed to research in topics: Glycyrrhiza echinata & Lotus japonicus. The author has an hindex of 30, co-authored 69 publications receiving 2727 citations. Previous affiliations of Shin-ichi Ayabe include Tokyo Medical and Dental University.

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CYP81E1, a cytochrome P450 cDNA of licorice (Glycyrrhiza echinata L.), encodes isoflavone 2'-hydroxylase.

TL;DR: The microsome of yeast cells overexpressing CYP81E1, a cytochrome P450 cDNA recently cloned from licorice, demonstrated for the first time to be isoflavone 2'-hydroxylase involved in the biosynthesis of is oflavonoid-derived antimicrobial compounds of legumes.
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Molecular cloning and biochemical characterization of a novel cytochrome P450, flavone synthase II, that catalyzes direct conversion of flavanones to flavones.

TL;DR: Cytochrome P450 cDNAs were isolated from snapdragon and torenia petal cDNA libraries and identified to encode flavone synthase II catalyzing direct conversion of flavanones to flavones probably via 2-hydroxyflavanones.
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Suppression of root nodule formation by artificial expression of the TrEnodDR1 (coat protein of White clover cryptic virus 1) gene in Lotus japonicus.

TL;DR: TrEnodDR1 suppresses nodulation by increasing the endogenous ABA concentration, perhaps by activating the plant's innate immune response, the first report of the suppression of nodulations by the artificial expression of a virus coat protein gene.
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Functional and structural analysis of genes encoding oxidosqualene cyclases of Lotus japonicus

TL;DR: This work comprehensively analyzed the functions and structures of OSC genes of a model legume, Lotus japonicus, and compared them with those of Arabidopsis thaliana in order to elucidate the diversification process of plant cyclic triterpenoids.
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cDNA cloning and biochemical characterization of S-adenosyl-L-methionine: 2,7,4'-trihydroxyisoflavanone 4'-O-methyltransferase, a critical enzyme of the legume isoflavonoid phytoalexin pathway.

TL;DR: A cDNA encoding SAM: 2,7,4'-trihydroxyisoflavanone 4'-O-methyltransferase (HI4'OMT) is cloned through the screening of functionally expressed Glycyrrhiza echinata (Fabaceae) cDNAs, indicating that HI4' OMT is the enzyme of formononetin biosynthesis in general legumes.