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研究業績詳細
藤平 陽彦（フジヒラ ハルヒコ）
| 研究テーマ | 細胞質における糖鎖代謝の生理学的意義解明 |
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| 研究業績（論文） | Glycans unique to the relapse-prone subset within triple-negative breast cancer as revealed by lectin array-based analysis of surgical specimens. Sakata-Matsuzawa M., Denda-Nagai K., Fujihira H., Noji M., Ishii-Schrade K.B., Matsuda A., Kuno A., Okazaki M., Nakai K., Horimoto Y., Saito M., Irimura T. PLoS One, 16(5) (2021) Bisecting-GlcNAc on Asn388 is characteristic to ERC/mesothelin expressed on epithelioid mesothelioma cells. Fujihira H., Takakura D., Matsuda A., Abe M., Miyazaki M., Nakagawa T., Kajino K., Denda-Nagai K., Noji M., Hino O., Irimura T. J. Biochem., in press (2021) JF1/B6F1 Ngly1-/- mouse as an isogenic animal model of NGLY1 deficiency. Asahina M., Fujinawa R., Fujihira H., Masahara-Negishi Y., Andou T., Tozawa R., Suzuki T. Proc. Jpn. Acad. Ser. B Phys. Biol. Sci., 97(2) (2021) Biological and Clinicopathological Implications of Beta-3-N-acetylglucosaminyltransferase 8 in Triple-negative Breast Cancer. Okazaki M., Mogushi K., Denda-Nagai K., Fujihira H., Noji M., Ishii-Schrade K., Sakata-Matsuzawa M., Nakai K., Horimoto Y., Saito M., Irimura T. Anticancer Res., 41(2) (2021) Cytosolic N-GlcNAc proteins are formed by the action of endo-β-N-acetylglucosaminidase. Maynard J.C., Fujihira H., Dolgonos G.E., Suzuki T., Burlingame A.L. Biochem. Biophys. Res. Commun., 530(4) (2020) Liver-specific deletion of Ngly1 causes abnormal nuclear morphology and lipid metabolism under food stress. Fujihira H., Masahara-Negishi Y., Akimoto Y., Hirayama H., Lee H.-C., Story A. B., Mueller F. W., Jakob P., Clauder-Münster S., Steinmetz M. L., Radhakrishnan K. S., Kawakami H., Kamada Y., Miyoshi E., Yokomizo T., Suzuki T. Biochim. Biophys. Acta Mol. Basis Dis., 1866(3), (2020) Physiological Function of the Cytosolic Peptide:N-glycanase (Ngly1) Fujihira H. Trends in Glycoscience and Glycotechnology, 31(179) (2019) N-glycanase NGLY1 regulates mitochondrial homeostasis and inflammation through NRF1. Yang K., Huang R., Fujihira H., Suzuki T., Yan N. J. Exp. Med., 215(10), 2600, (2018) A Critical Domain of Ebolavirus Envelope Glycoprotein Determines Glycoform and Infectivity Fujihira H., Usami K., Matsuno K., Takeuchi H., Denda-Nagai K., Furukawa J., Shinohara Y., Takada A., Kawaoka Y. and Irimura T. Sci. Rep., 8(1), 5495 (2018) Lethality of mice bearing a knockout of the Ngly1-gene is partially rescued by the additional deletion of the Engase gene. Fujihira H., Masahara-Negishi Y., Tamura M., Huang C., Harada Y., Wakana S., Takakura D., Kawasaki N., Taniguchi N., Kondoh G., Yamashita T., Funakoshi Y., Suzuki T. PLOS Genet., 13(4), e1006696 (2017) Occurrence of free sialyl oligosaccharides related to N-glycans (sialyl FNGs) in animal sera. Seino J., Fujihira H., Nakakita S., Masahara-Negishi Y., Miyoshi E., Hirabayashi J., Suzuki T. Glycobiology, 26(10), 1072-1085 (2016) The cytoplasmic peptide:N-glycanase (NGLY1) -Structure, expression and cellular functions. Suzuki T., Huang C., Fujihira H. Gene, 577(1), 1-7 (2015) Endo-beta-N-acetylglucosaminidase forms N-GlcNAc protein aggregates during ER-associated degradation in Ngly1-defective cells. Huang C., Harada Y., Hosomi A., Masahara-Negishi Y., Seino J., Fujihira H., Funakoshi Y., Suzuki T., Dohmae N., Suzuki T. Proc. Natl. Acad. Sci. U. S. A., 112(5), 1398-403 (2015) |
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