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Your search keyword '"Shinohara, Yasuro"' showing total 8 results
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8 results on '"Shinohara, Yasuro"'

4. Exposure to brefeldin A induces unusual expression of hybrid- and complex-type free N-glycans in HepG2 cells

Author

Sugiura, Kanako, primary, Kawai, Yuho, additional, Yamamoto, Arisa, additional, Yoshioka, Hiroki, additional, Kiyohara, Yuika, additional, Iida, Ayaka, additional, Ozawa, Yurika, additional, Nishikawa, Mai, additional, Miura, Nobuaki, additional, Hanamatsu, Hisatoshi, additional, Furukawa, Jun-ichi, additional, and Shinohara, Yasuro, additional

Published
2023
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6. Evaluation of the context of downstream N- and free N-glycomic alterations induced by swainsonine in HepG2 cells

Author

Morikawa, Chie, primary, Sugiura, Kanako, additional, Kondo, Keina, additional, Yamamoto, Yurie, additional, Kojima, Yuma, additional, Ozawa, Yurika, additional, Yoshioka, Hiroki, additional, Miura, Nobuaki, additional, Piao, Jinhua, additional, Okada, Kazue, additional, Hanamatsu, Hisatoshi, additional, Tsuda, Masumi, additional, Tanaka, Shinya, additional, Furukawa, Jun-ichi, additional, and Shinohara, Yasuro, additional

Published
2022
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8. An Efficient Approach to the Discovery of Potent Inhibitors against Glycosyltransferases

Author

Hosoguchi, Kensaku, Maeda, Takahiro, Furukawa, Jun-ichi, Shinohara, Yasuro, Hinou, Hiroshi, Sekiguchi, Mitsuaki, Togame, Hiroko, Takemoto, Hiroshi, Kondo, Hirosato, and Nishimura, Shin-Ichiro

Abstract

We describe a standardized approach for searching potent and selective inhibitors of glycosyltransferases by high throughput quantitative MALDI-TOFMS-based screening of focused compound libraries constructed by 1,3-dipolar cycloaddition of the desired azidosugar nucleotides with various alkynes. An aminooxy-functionalized reagent with a stable isotope was conjugated with oligosaccharides to afford glycopeptides as acceptor substrates with improved ion sensitivity. Enhanced ionization potency of new substrates allowed for MALDI-TOFMS-based facile and quantitative analysis of enzymatic glycosylation in the presence of glycosyl donor substrates. A non-natural synthetic sugar nucleotide was identified to be the first highly specific inhibitor for rat recombinant α2,3-(N)-sialyltransferase (α2,3ST, IC50= 8.2 μM), while this compound was proved to become a favorable substrate for rat recombinant α2,6-(N)-sialyltransferase (α2,6ST, Km= 125 μM). Versatility of this strategy was demonstrated by identification of two selective inhibitors for human recombinant α1,3-fucosyltransferase V (α1,3-FucT, Ki= 293 nM) and α1,6-fucosyltransferase VIII (α1,6-FucT, Ki= 13.8 μM).

Published
2024
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