arrow 研究業績一覧


◇ 原著論文

  • Kuriya, K., Nishio, M.*, Ono, N., Masuda, Y., Katsuzaki, H., Kondo, S., Sono, J., Nakamura, M., Umekawa, H.: Isolation and characterization of antihyperglycemic compounds from Vigna angularis extracts. J. Food. Sci. 2019, 84, 3172–3178.
  • Ohsawa, K., Sugai, M., Zhang, L., Masuda, Y., Yoshida, M., Doi, T.*: Total synthesis and structural revision of cyclotetrapeptide asperterrestide A. J. Org. Chem. 2019, 84, 6765–6779.
  • D’Amato, A., Della Sala, G., Izzo, I., Costabile, C., Masuda, Y.*, De Riccardis, F.*: Cyclic octamer peptoids: simplified isosters of bioactive fungal cyclodepsipeptides. Molecules 201823, 1779.
  • Masuda, Y.*, Tanaka, R., Ganesan, A., Doi, T.*: Systematic analysis of relationship among 3D structure, bioactivity, and membrane permeability of PF1171F, a cyclic hexapeptide with paralyzing effects on silkworms. J. Org. Chem. 2017, 82, 11447–11463.
  • Onda, Y., Masuda, Y., Yoshida, M., Doi, T.*: Conformation-based design and synthesis of apratoxin A mimetics modified at the alpha,beta-unsaturated thiazoline moiety. J. Med. Chem., 2017, 60, 6751–6765.
  • Masuda, Y., Maruyama, C., Kawabata, K., Hamano, Y., Doi, T.*: Synthesis of (2S,3R,4R)-3,4-dihydroxyarginine and its inhibitory activity against nitric oxide synthase. Tetrahedron 2016, 72, 56025611.
  • Masuda, Y., Aoyama, K., Yoshida, M., Kobayashi, K., Ohshiro, T., Tomoda, H., Doi T.*: Design, synthesis, and biological evaluation of beauveriolide analogues bearing photoreactive amino acids. Chem. Pharm. Bull., 2016, 64, 754765. Special Collection of Papers Celebrating Professor Satoshi Ōmura's 2015 Nobel Prize in Physiology or Medicine.

  • Yoshida, M., Onda, Y., Masuda, Y., Doi, T.*: Potent oxazoline analogue of apratoxin C: synthesis, biological evaluation, and conformational analysis. Biopolymers (Peptide Science), 2016, 106, 404414. Special Issue: Emerging Peptide Science from Japan.
  • Kawahara, T., Kagaya, N., Masuda, Y., Doi, T., Izumikawa, M., Ohta, K., Hirao, A., Shin-Ya, K.*: Foxo3a inhibitors of microbial origin, JBIR-141 and JBIR-142. Org. Lett. 2015. 17, 5476-5479.

  • Masuda, Y., Tanaka, R., Ganesan, A.,* Doi, T.*: Structure revision of similanamide to PF1171C by total synthesis. J. Nat. Prod. 2015, 78, 2286-2291.

  • Masuda, Y., Suzuki, J., Onda, Y., Fujino, Y., Yoshida, M., Doi, T.*: Total synthesis and conformational analysis of apratoxin C. J. Org. Chem. 2014, 79, 8000-8009.

  • Masuda, Y., Tanaka, R., Kai, K., Ganesan, A.,* Doi, T.*: Total synthesis and biological evaluation of PF1171A, C, F, and G, cyclic hexapeptides with insecticidal activity. J. Org. Chem. 2014, 79, 7844-7853.
  • Shen, M., Liu, Q., Trébosc, J., Lafon, O., Masuda, Y., Takegoshi, K., Amoureux, J. P.,* Hu, B.,* Chen, Q.: Exploring various modulation-sideband recoupling conditions of SHA+ sequence at fast MAS. Solid State Nucl. Magn. Reson. 2013, 55-56, 42-47.

  • Sato, M., Murakami, K., Uno, M., Nakagawa, Y., Katayama, S., Akagi, K., Masuda, Y., Takegoshi, K., Irie, K.*: Site-specific inhibitory mechanism for amyloid-beta 42 aggregation by catechol-type flavonoids targeting the Lys residues. J. Biol. Chem. 2013, 288, 23212-23224.
  • Doi, T., Masuda, Y.,* Irie, K., Akagi, K., Monobe, Y., Imazawa, T., Takegoshi, K.: Solid-state NMR analysis of the beta-strand orientation of the protofibrils of amyloid beta-protein. Biochem. Biophys. Res. Commun. 2012, 428, 458-462.

  • Hu, B.,* Trébosc, J., Lafon, O., Chen, Q., Masuda, Y., Takegoshi, K., Amoureux, J. P.*: Very-long-distance correlations in proteins revealed by solid-state NMR spectroscopy. ChemPhysChem 2012, 13, 3585-3588.
  • Tsuji, F., Ishihara, A., Nakagawa, A., Okada, M., Kitamura, S., Kanamaru, K., Masuda, Y., Murakami, K., Irie, K., Sakagami, Y.*: Lack of the consensus sequence necessary for tryptophan prenylation in the ComX pheromone precursor. Biosci. Biotechnol. Biochem. 2012, 76, 1492-1496.

  • Tsuji, F., Ishihara, A., Kurata, K., Nakagawa, A., Okada, M., Kitamura, S., Kanamaru, K., Masuda, Y., Murakami, K., Irie, K., Sakagami, Y.*: Geranyl modification on the tryptophan residue of ComXRO-E-2 pheromone by a cell-free system. FEBS Lett. 2012, 586, 174-179.
  • Masuda, Y.,* Fukuchi, M., Yatagawa, T., Tada, M., Takeda, K., Irie, K., Akagi, K., Monobe, Y., Imazawa, T., Takegoshi, K.: Solid-state NMR analysis of interaction sites of curcumin and 42-residue amyloid beta -protein fibrils. Bioorg. Med. Chem. 2011, 19, 5967-5974.

  • Nakagawa, Y.*, Doi, T., Masuda, Y., Takegoshi, K., Igarashi, Y., Ito, Y.*: Mapping of the primary mannose-binding site of pradimicin A. J. Am. Chem. Soc. 2011, 133, 17485-17493.
  • Nakagawa, Y.*, Masuda, Y., Yamada, K., Doi, T., Takegoshi, K., Igarashi, Y., Ito, Y.*: Solid-state NMR spectroscopic analysis of the Ca2+-dependent mannose binding of pradimicin A. Angew. Chem. Int. Ed. 2011, 50, 6084-6088.

  • Weingarth, M., Masuda, Y., Takegoshi, K., Bodenhausen, G., Tekely, P.*: Sensitive 13C-13C correlation spectra of amyloid fibrils at very high spinning frequencies and magnetic fields. J. Biomol. NMR 2011, 50, 129-136.
  • Murakami, K., Horikoshi-Sakuraba, Y., Murata, N., Noda, Y., Masuda, Y., Kinoshita, N., Hatsuta, H., Murayama, S., Shirasawa, T., Shimizu, T.,* Irie, K.*: Monoclonal antibody against the turn of the 42-residue amyloid beta -protein at positions 22 and 23. ACS Chem. Neurosci. 2010, 1, 747-756.

  • Kondo, T., Kajita, R., Miyazaki, A., Hokoyama, M., Nakamura-Miura, T., Mizuno, S., Masuda, Y., Irie, K., Tanaka, Y., Takada, S., Kakimoto, T., Sakagami, Y.*: Stomatal density is controlled by a mesophyll-derived signaling molecule. Plant Cell Physiol. 2010, 51, 1-8.
  • Masuda, Y., Uemura, S., Ohashi, R., Nakanishi, A., Takegoshi, K., Shimizu, T., Shirasawa, T., Irie, K.*: Identification of physiological and toxic conformations in Abeta42 aggregates. ChemBioChem 2009, 10, 287-295.

  • Masuda, Y., Nakanishi, A., Ohashi, R., Takegoshi, K., Shimizu, T., Shirasawa, T., Irie, K.*: Verification of the intermolecular parallel beta-sheet in E22K-Abeta42 aggregates by solid-state NMR using rotational resonance: Implications for the supramolecular arrangement of the toxic conformer of Abeta42. Biosci. Biotechnol. Biochem. 2008, 72, 2170-2175.
  • Masuda, Y., Uemura, S., Nakanishi, A., Ohashi, R., Takegoshi, K., Shimizu, T., Shirasawa, T., Irie, K.*: Verification of the C-terminal intramolecular beta-sheet in Abeta42 aggregates using solid-state NMR: Implications for potent neurotoxicity through the formation of radicals. Bioorg. Med. Chem. Lett. 2008, 18, 3206-3210.

  • Murakami, K., Uno, M., Masuda, Y., Shimizu, T., Shirasawa, T., Irie, K.*: Isomerization and/or racemization at Asp23 of Abeta42 do not increase its aggregative ability, neurotoxicity, and radical productivity in vitro. Biochem. Biophys. Res. Commun. 2008, 366, 745-751.
  • Murakami, K., Hara, H., Masuda, Y., Ohigashi, H., Irie, K.*: Distance measurement between Tyr10 and Met35 in amyloid beta by site-directed spin-labeling ESR spectroscopy: Implications for the stronger neurotoxicity of Abeta42 than Abeta40. ChemBioChem 2007, 8, 2308-2314.

  • Masuda, Y., Irie, K.,* Murakami, K., Ohigashi, H., Ohashi, R., Takegoshi, K., Shimizu, T., Shirasawa, T.: Verification of the turn at positions 22 and 23 of the beta-amyloid fibrils with Italian mutation using solid-state NMR. Bioorg. Med. Chem. 2005, 13, 6803-6809.
  • Morimoto, A., Irie, K.,* Murakami, K., Masuda, Y., Ohigashi, H., Nagao, M., Fukuda, H., Shimizu, T., Shirasawa, T.: Analysis of the secondary structure of beta-amyloid (Abeta42) fibrils by systematic proline replacement. J. Biol. Chem. 2004, 279, 52781-52788.


◇ 総説・解説

  • Doi, T.,* Masuda, Y., Yoshida, M.: Cyclodepsipeptide Natural Products Apratoxins A and C and Their Analogs. J. Synth. Org. Chem. Jpn. 2018, 76 (11), 11701175.
  • 増田裕一: 中分子で免疫チェックポイントを制御する. ファルマシア 2018, 54 (6), 574.
  • 増田裕一*,土井隆行: 生物活性環状ペプチドPF1171類とapratoxin Cの全合成と三次元構造解析 化学工業 2016, 67, 18−25.

  • 上一馬,増田裕一,入江一浩*: 固体NMRおよびESRによるアミロイドβの立体構造解析と毒性ターン構造特異抗体の開発. 遺伝子医学MOOK2012, 21, 211-216.

  • Murakami, K., Masuda, Y., Shirasawa, T., Shimizu, T.,* Irie, K.*: The turn formation at positions 22 and 23 in the 42-mer amyloid beta peptide: The emerging role in the pathogenesis of Alzheimer’s disease. Geriatr. Gerontol. Int. 2010, 10, S169–S179.
  • 増田 裕一, 入江 一浩*: ポリフェノールによるアルツハイマー病予防の可能性.  FFIジャーナル 2010, 215, 53-59.

  • 入江 一浩,* 増田 裕一: βアミロイドの毒性コンホメーション. 化学と生物 2008, 46, 431-434.
  • Irie, K.,* Murakami, K., Masuda, Y., Morimoto, A., Ohigashi, H., Hara, H., Ohashi, R., Takegoshi, K., Fukuda, H., Nagao, M., Shimizu, T., Shirasawa, T.: The toxic conformation of the 42-residue amyloid beta peptide and its relevance to oxidative stress in Alzheimer’s disease. Mini-Rev. Med. Chem. 2007, 7, 1001-1008.

  • Irie, K.,* Murakami, K., Masuda, Y., Morimoto, A., Ohigashi, H., Ohashi, R., Takegoshi, K., Nagao, M., Shimizu, T., Shirasawa, T.: Structure of beta-amyloid fibrils and its relevance to their neurotoxicity: Implications for the pathogenesis of Alzheimer’s disease. J. Biosci. Bioeng. 2005, 99, 437-447.

◇ 招待講演

  • Yuichi Masuda: Elucidation of important 3D structures for bioactivity of naturally occurring peptides. 23rd Korean Peptide and Protein Society Symposium, Invited lecture (Daemyung Resort, Sol Beach Yangyang, South Korea) , July 1~2, 2019
  • 増田裕一: 生物活性環状ペプチドの合成と三次元構造解析. 日本薬学会東北支部 13回化学系若手研究者セミナー (仙台) 20149.

  • Masuda, Y.: Identification of Toxic Conformation in the Aggregates of 42-residue Amyloid b-Protein.  Seminar in Unité de Catalyse et de Chimie du Solide (UCCS) – UMR CNRS 8181, University of Lille, (Lille, France) Novemver 2009.

  • Masuda, Y.: Identification of Toxic Conformation in the Aggregates of 42-residue Amyloid b-Protein.  Seminar in Département de Chimie, Ecole Normale Supérieure (Paris, France) Novemver 2009.

◇ 特許

  • 土井隆行,吉田将人,増田裕一,恩田勇一: 環状デプシペプチド化合物. PCT/JP2017/005777 (2017).

  • Irie, K., Murakami, K., Masuda, Y., Shimizu, T., Shirasawa, T., Seito, T.: Antibody recognizing turn structure in amyloid beta. 特許登録US 8,710,193; CN ZL201080046483.9 (2014).



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