研究成果

原著論文（2005年以降）

  • Sakakura, M., Tanabe, M., Mori, M., Takahashi, H., Mio, K. (2023) Structural bases for the Charcot-Marie-Tooth disease induced by single amino acid substitutions of myelin protein zero. Structure 31, 1452-1462.e4. doi: 10.1016/j.str.2023.08.016

  • Argunhan, B.*, Sakakura, M.*, Afshar, N., Kurihara, M., Ito, K., Maki, T., Kanamaru, S., Murayama, Y., Tsubouchi, H., Takahashi, M., Takahashi, H., Iwasaki, H. (2020) Cooperative interactions facilitate stimulation of Rad51 by the Swi5-Sfr1 auxiliary factor complex. eLIFE 9, e52566 *These authors contributed equally to this work.

  • Sakakura, M., Ohkubo, Y., Oshima, H., Re, S., Ito, M., Sugita, Y., Takahashi, H. (2019) Structural Mechanisms Underlying Activity Changes in an AMPA-type Glutamate Receptor Induced by Substitutions in Its Ligand-Binding Domain. Structure 27, 1698-1709.e5.

  • Vanoye, C. G., Sakakura, M., Follis, R. M., Trevisan, A. J., Narayan, M., Li, J., Sanders, C. R., Carter, B. D. (2019) Peripheral myelin protein 22 modulates store operated calcium channel activity, providing insights into Charcot-Marie-Tooth disease etiology. J. Biol. Chem. 294, 12054-12065

  • Oshima, H., Re, S., Sakakura, M., Takahashi, H., and Sugita, Y. (2019) Population Shift Mechanism for Partial Agonism of AMPA Receptor. Biophys. J. 116, 57-68.

  • Suzuki, R., Sakakura, M., Mori, M., Fujii, M., Akashi, S., and Takahashi, H. (2018) Methyl-selective isotope labeling using α-ketoisovalerate for the yeast Pichia pastoris recombinant protein expression system. J. Biomol. NMR 71, 213-223.

  • Sakakura, M., Tamura, M., Fujii, N., Takeuchi, T., Hatanaka, T., Kishimoto, S., Arata, Y., and Takahashi, H. (2018) Structural mechanisms for the S-nitrosylation-derived protection of mouse galectin-2 from oxidation-induced inactivation revealed by NMR. FEBS. J. 285, 1129-45.

  • Kiyonaka, S., Kubota, R., Michibata, Y., Sakakura, M., Takahashi, H., Numata, T., Inoue, R., Yuzaki, M., and Hamachi, I. (2016) Allosteric activation of membrane-bound glutamate receptors using coordination chemistry within living cells. Nat. Chem. 8, 958-67.

  • Sakakura, M., Hadziselimovic, A., Wang, Z., Schey, K. L., and Sanders, C. R. (2011) Structural basis for the Trembler-J phenotype of Charcot-Marie-Tooth disease. Structure 19, 1160-1169.

  • Koehler, J., Sulistijo E. S., Sakakura, M., Kim, H. J., Ellis, C. D., and Sanders, C. R. (2010) Lysophospholipid micelles sustain the stability and catalytic activity of diacylglycerol kinase in the absence of lipids. Biochemistry 49, 7089-7099.

  • Beel, A. J., Sakakura, M., Barrett, P. J., and Sanders, C. R. (2010) Direct binding of cholesterol to the amyloid precursor protein: An important interaction in lipid-Alzheimer’s disease relationships? Biochim. Biophys. Acta. 1801, 975-982.

  • Nakada, S., Sakakura, M., Takahashi, H., Okuda, S., Tokuda, H. & Shimada, I. (2009) Structural investigation of the interaction between LolA and LolB using NMR. J. Biol. Chem. 284, 24634-24643.

  • Moriya, J., Sakakura, M., Tokunaga, Y., Prosser, R. S. & Shimada, I. (2009) An NMR method for the determination of protein binding interfaces using TEMPOL-induced chemical shift perturbations. Biochim. Biophys. Acta. 1790, 1368-1376.

  • Shimada, I., Ueda, T., Matsumoto, M., Sakakura, M., Osawa, M., Takeuchi, K., Nishida, N. & Takahashi, H. (2009) Cross-saturation and transferred cross-saturation experiments. Progress in Nuclear Magnetic Resonance Spectroscopy 54, 123-140.

  • Sakakura, M., Oo-puthinan, S., Moriyama, C., Kimura, T., Moriya, J., Irimura, T. & Shimada, I. (2008) Carbohydrate binding mechanism of the macrophage galactose-type C-type lectins 1 revealed by saturation transfer experiments. J. Biol. Chem. 283, 33665-33673.

  • Oo-puthinan, S., Maenuma, K., Sakakura, M., Denda-Nagai, K., Tsuiji, M., Shimada, I., Nakamura-Tsuruta, S., Hirabayashi, J., Bovin, N. V. & Irimura, T. (2008) The amino acids involved in the distinct carbohydrate specificities between macrophage galactose-type C-type lectins 1 and 2 (CD301a and b) of mice. Biochim. Biophys. Acta. 1780, 89-100.

  • Nakada, S., Sakakura, M., Takahashi, H., Tokuda, H. & Shimada, I. (2007) Backbone resonance assignment for the outer membrane lipoprotein receptor LolB from Escherichia coli. Biomolecular NMR Assignments 1, 121-123.

  • Nakada, S., Takahashi, H., Sakakura, M., Kurono, M. & Shimada, I. (2007) Backbone resonance assignments for the periplasmic chaperone LolA from Escherichia coli. Biomolecular NMR Assignments 1, 125-127.

  • Oda, M., Ito, N., Tsumuraya, T., Suzuki, K., Sakakura, M. & Fujii, I. (2007) Thermodynamic and structural basis for transition-state stabilization in antibody-catalyzed hydrolysis. J. Mol. Biol. 369, 198-209.

  • Sakakura, M., Takahashi, H., Shimba, N., Fujii, I. & Shimada, I. (2007) Structural basis of the transition-state stabilization in antibody-catalyzed hydrolysis. J. Mol. Biol. 367, 133-147.

  • Takeda, M., Ogino, S., Umemoto, R., Sakakura, M., Kajiwara, M., Sugahara, K. N., Hayasaka, H., Miyasaka, M., Terasawa, H. & Shimada, I. (2006) Ligand-induced structural changes of the CD44 hyaluronan-binding domain revealed by NMR. J. Biol. Chem. 281, 40089-40095.

  • Sakakura, M., Takahashi, H., Terasawa, H, Takeuchi, K., Fujii, I. & Shimada, I. (2005) Backbone resonance assignments for the Fv fragment of catalytic antibody 6D9 complexed with a transition state analogue. J. Biomol. NMR 33, 282.

  • Sakakura, M., Noba, S., Luchette, P. A., Shimada, I. & Prosser, R. S. (2005) An NMR method for the determination of protein binding interfaces using dioxygen-induced spin-lattice relaxation enhancement. J. Am. Chem. Soc. 127, 5826-5832.


    • 書籍

  • NMRによる有機材料分析とその試料前処理、データ解釈；第６章第６節　NMRによるペプチドの立体構造解析； 坂倉正義、高橋栄夫；技術情報協会；p566-577；2021年9月