S
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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Journal ArticleDOI
Genome-wide Analyses of the Structural Gene Families Involved in the Legume-specific 5-Deoxyisoflavonoid Biosynthesis of Lotus japonicus
Norimoto Shimada,Shusei Sato,Tomoyoshi Akashi,Yasukazu Nakamura,Satoshi Tabata,Shin-ichi Ayabe,Toshio Aoki +6 more
TL;DR: Analysis of genes encoding enzymes involved in the biosynthesis of the legume-specific 5-deoxyisoflavonoid of L. japonicus provides reliable annotations of the genes and genetic markers for comparative and functional genomics of leguminous plants.
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Identification of cDNAs encoding pterocarpan reductase involved in isoflavan phytoalexin biosynthesis in Lotus japonicus by EST mining
TL;DR: A search of the expressed sequence tag library of a model legume Lotus japonicus for homologs of phenylcoumaran benzylic ether reductase catalyzing the reductive cleavage of dihydrofurans yielded seven full‐length cDNAs, and the encoded proteins were analyzed in vitro.
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Multiple mutagenesis of P450 isoflavonoid synthase reveals a key active-site residue.
Yuji Sawada,Shin-ichi Ayabe +1 more
TL;DR: Molecular evolution of CYP93 enzymes is discussed and Leu 371 appeared to control the substrate accommodation in favor of hydrogen abstraction from C-3 of the flavanone molecule and contribute to the P450 fold under the presence of Lys 375, the residue responsible for aryl migration.
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Triterpenoid biosynthesis in tissue cultures of Glycyrrhiza glabra var. glandulifera.
TL;DR: The incorporation of [1-14C]acetate and [214 C]mevalonate into free and esterified triterpen-3-ols was examined in original plant organs and tissue cultures of Glycyrrhiza glabra var.
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Identification of protein–protein interactions of isoflavonoid biosynthetic enzymes with 2-hydroxyisoflavanone synthase in soybean (Glycine max (L.) Merr.)
Toshiyuki Waki,Dong Chan Yoo,Naoto Fujino,Ryo Mameda,Konstantin Denessiouk,Satoshi Yamashita,Reiko Motohashi,Tomoyoshi Akashi,Toshio Aoki,Shin-ichi Ayabe,Seiji Takahashi,Toru Nakayama +11 more
TL;DR: Binary protein-protein interactions of 2-hydroxyisoflavanone synthase 1 (GmIFS1), a P450 (CYP93C), with cytoplasmic enzymes involved in isoflavone biosynthesis in soybean are analyzed to provide strong evidence that, in planta, interaction of Gm CHS1 and GmCHIs with Gm IFS1 takes place on ER, and also provide important clues to understand how enzymes and proteins