新学術領域「動的秩序と機能」研究業績リスト

研究業績リスト

A01：動的秩序の探査	A02：動的秩序の創生	A03：動的秩序の展開
秋　山　修　志秋　山　　　良安　中　雅　彦池　谷　鉄　兵岩　田　耕　一内　橋　貴　之上久保　裕　生佐　藤　啓　文高　田　十志和立　川　仁　典田　中　良　和寺　嶋　正　秀内　藤　　　晶東　　　雅　大松　村　浩　由松　森　信　明養王田　正　文	新　井　亮　一飯　野　亮　太井　上　将　彦上　野　隆　史大　谷　　　亮片　山　　　勉神　谷　由紀子佐　田　和　己佐　藤　宗　太杉　安　和　憲鈴　木　大　介平　岡　秀　一二　井　勇　人二　木　史　朗芳　坂　貴　弘松　浦　友　亮三　宅　弘　之	稲　垣　直　之内　山　　　進老　木　成　稔岡　本　祐　幸奥　村　久　士加　藤　晃　一菊　地　和　也佐　甲　靖　志笹　井　理　生佐　藤　　　健申　　　惠　媛真行寺　千佳子杉　山　正　明茶　谷　絵　理寺　内　一　姫水　野　健　作村　田　和　義山　本　量　一
班　友
澤　田　知　久、　重　田　育　照、　塚　崎　智　也、　長　田　裕　也、濵　田　大　三、　原　野　幸　治、　前　田　大　光

公募班A01：動的秩序の探査

秋山修志 ▲班員一覧に戻る▲: 【雑誌論文】; A. Mukaiyama, Y. Furuike, J. Abe, E. Yamashita, T. Kondo, *S. Akiyama, “Conformational rearrangements of the C1 ring in KaiC measure the timing of assembly with KaiB”, Sci. Rep., 8, 8803, (2018), DOI: 10.1038/s41598-018-27131-8; *S. Akiyama, A. Mukaiyama, J. Abe, Y. Furuike “Cyanobacterial circadian clock system: how and why can it be so slow and stable?”, Biological Clocks, proceedings of the Sapporo Symposium on Biological Rhythms, 73-77 (2017).; Y. Furuike, J. Abe, A. Mukaiyama, *S. Akiyama, “Accelerating in Vitro Studies on Circadian Clock Systems Using an Automated Sampling Device”, Biophysics and Physicobiology, 13, 235-241, (2016), DOI: 10.2142/biophysico.13.0_235; *Y. Furukawa, Y. Suzuki, M.Fukuoka, K. Nagasawa, K. Nakagome, H. Shimizu, A. Mukaiyama, S. Akiyama, “A Molecular Mechanism Realizing Sequence-specific Recognition of Nucleic Acids by TDP-43”, Sci. Rep.,6, 20576, (2016), DOI: 10.1038/srep20576; *Y. Furukawa, I. Anzai, S. Akiyama, M. Imai, Cruz FJC, T. Saio, K. Nagasawa, T. Nomura, K. Ishimori, “Conformational Disorder of the Most Immature Cu,Zn-Superoxide Dismutase Leading to Amyotrophic Lateral Sclerosis”, J. Biol. Chem., 291, 4144-4155, (2016), DOI: 10.1074/jbc.M115.683763; 秋山修志*「時間生物学と放射光科学の接点」放射光 in press, (2016); 阿部淳，向山厚，秋山修志*「時計タンパク質KaiCの「遅さ」が刻み込まれた原子構造」SPring-8/SACLA利用者情報 21, 2-4 (2016); J. Abe, A. Mukaiyama, *S. Akiyama "Absolute slowness encoded in the circadian clock protein KaiC," SPring-8 Research Frontiers 2015, 24-25 (2016); 向山厚，阿部淳，孫世永，秋山修志*「タンパク質の化学反応が細胞内の時を計る」実験医学 33, 3119-3122 (2015); J. Abe, T.B. Hiyama, A. Mukaiyama, S. Son, T. Mori, S. Saito, M. Osako, J. Wolanin, E. Yamashita, T. Kondo, *S. Akiyama,“Atomic-scale Origins of Slowness in the Cyanobacterial Circadian Clock”, Science 349, 312-316, (2015),DOI: 10.1126/science.1261040; A. Mukaiyama, M. Osako, T. Hikima, T. Kondo, *S. Akiyama, “A Protocol for Preparing Nucleotide-free KaiC Monomer”, BIOPHYSICS 11, 79, (2015),DOI: 10.2142/biophysics.11.79; 【図書】; *秋山修志 "概日時計因子の構造や動態を調べる意義とは？" 生物物理 56, 266-270 (2016).
秋山良 ▲班員一覧に戻る▲: 【雑誌論文】; *Y. Nakamura, A. Yoshimori, R. Akiyama, T. Yamaguchi “Stick Boundary Condition at Large Hard Sphere Arising from Effective Attraction in Binary Hard-sphere Mixtures”, J. Chem. Phys., 148, 124502 (2018), DOI: 10.1063/1.5025202; *K. Tokunaga, *R. Akiyama “Basic Cell Size Dependence of Displacement for a Solvation Motor in a Lennard-Jones Solvent”, J. Comp. Chem. Jpn., 17, 80–84, (2018), DOI: 10.2477/jccj.2018-0004; *H. Okumura, M. Higashi, Y. Yoshida, H. Sato, R.Akiyama, “Theoretical Approaches for Dynamical Ordering of Biomolecular Systems”, Biochim. Biophys. Acta, (BBA), Gen. Subj., 1862, 212-228, (2017), DOI: 10.1016/j.bbagen.2017.10.001; *Ayano Chiba, Masanori Inui, Yukio Kajihara, Kazuhiro Fuchizaki, Ryo Akiyama “Isotactic poly(4-methyl-1-pentene) melt as a porous liquid: Reduction of compressibility due to penetration of pressure medium” J. Chem. Phys. 146 194503-1-5 (2017). DOI: 10.1063/1.4983508; *Mafumi Hishida, Yoko Nomura, Ryo Akiyama, Yasuhisa Yamamura, and *Kazuya Saito “Electrostatic double-layer interaction between stacked charged bilayers” Phys. Rev. E 96, 040601(R)-1-5 (2017) DOI: 10.1103/PhysRevE.96.040601; *A. Suematsu, A. Yoshimori, R. Akiyama, “Effects of Interactions between Depletants in Phase Diagrams of Binary Hard-sphere Systems”, EPL, 116, 38004-1-7, (2016), DOI: 10.1209/0295-5075/116/38004; S. Fujihara, *R. Akiyama, “Attractive Interaction between Macroanions Mediated by Multivalent Cations in Biological Fluids”, J. Mol. Liq., 200, 89-94 (2014), DOI: 10.1016/j.molliq.2014.06.022; *Y. Nakamura, A. Yoshimori, R. Akiyama, “Effects of Solvation Structure on Diffusion of Large Particle in Binary Mixture Studied by Perturbation Theory”, J. Mol. Liq., 200,85-88 (2014), DOI: 10.1016/j.molliq.2014.06.021; *R. Akiyama, T. Yamashita, S. Fujihara, “Hidden Peak of Radial Distribution Function and Effective Attraction between Like-charged Proteins caused by Translational Motion of Solvent Molecules”, J. Mol. Liq., 200, 72-76 (2014), DOI: 10.1016/j.molliq.2014.06.004; Y. Kawabata, *R. Akiyama, “Choice of the Center of Water Molecules in Calculations of Partial Molar Volume of Single Ions Immersed in Water: A Molecular Simulation Study”, J. Mol. Liq., 200, 67-71 (2014), DOI: 10.1016/j.molliq.2014.05.022; Y. Nakamura, *A. Yoshimori, R. Akiyama, “Perturbation Theory of Large-Particle Diffusion in a Binary Solvent Mixture”, J. Phys. Soc. Jpn., 83, 064601-1-9(2014), DOI: 10.7566/JPSJ.83.064601; 【図書】; 安池智一、秋山良“エントロピーからはじめる熱力学”, 放送大学教育振興会, 日本, p.p.1-300, 2016年3月20日. ISBN978-4-595-31643
安中雅彦 ▲班員一覧に戻る▲: 【雑誌論文】; Masahiko Annaka“ Relaxation phenomena and development of structure in a physically cross-linked telechelic polymers, Soft Matter”,in press; M. Yanagisawa, Y. Yamashita, S. Mukai, M. Annaka, M. Tokita “Phase separation in binary polymer solution: Gelatin/Poly (ethylene glycol) system”, Journal of Molecular Liquid, 200, 2-6 (2014), DOI: 10.1016/j.molliq.2013.12.035; A. Shundo, K. Hori, D. P. Penaloza Jr. K. Yoshihiro, M. Annaka, K. Tanaka,” Nonsolvents-induced swelling of poly(methylmethacrylate) nanoparticles”, Physical Chemistry Chemical Physics, 15, 16574-16578, (2014), DOI: 10.1039/c3cp52673a
池谷鉄兵 ▲班員一覧に戻る▲: 【雑誌論文】; T. Ikeya,*Y. Ito, “Protein NMR Structure Refinement Based on Bayesian Inference for Dynamical Ordering of Biomacromolecules.” J. Comput. Chem. Jpn., 7 (1), 65-75,( 2018), DOI: 10.2477/jccj.2018-0009; *Ikeya, T., Ban, D., Lee, D., Ito, Y., Kato, K., & *Griesinger, C., “Solution NMR views of dynamical ordering of biomacromolecules”, Biochim. Biophys. Acta, Gen. Subj., S0304-4165(17)30276-3 (2017) DOI: 10.1016/j.bbagen.2017.08.020; T. Ikeya, T. Hanashima, S. Hosoya, M. Shimazaki, S. Ikeda, M. Mishima, P. Güntert,*Y. Ito, “In-cell Structure Determination of Proteins at Near-physiological Concentration”, Sci. Rep., 6, 38312, (2016), DOI: 10.1038/srep38312; Y. Hikone, G. Hirai, M. Mishima, K. Inomata, T. Ikeya, S. Arai, M. Shirakawa, M. Sodeoka, *Y. Ito, “A New Carbamidemethyl-linked Lanthanide Chelating Tag for PCS NMR Spectroscopy of Proteins in Living HeLa cells” J. Biomol. NMR, 66, 99-110, (2016), DOI: 10.1007/s10858-016-0059-4; Y. Nishida, T. Ikeya, T. Mikawa, J. Inoue, Y. Ito, Y. Shintani, R. Masui, S. Kuramitsu, *S. Takashima, “A Specific Single-stranded DNA Induces a Distinct Conformational Change in the Nucleoid-associated Protein HU”, BB Reports, 8, 318–324, (2016), DOI: 10.1016/j.bbrep.2016.09.014; *T. Ikeya, S. Ikeda, T. Kigawa, Y. Ito and P. Güntert*, “Protein NMR Structure Refinement based on Bayesian Inference,” J. Phys.: Conf. Ser., 699, 012005, 1-14, (2016); Y. Shigemitsu, T. Ikeya, A.Yamamoto, Y. Tsuchie, M. Mishima, B. O. Smith, P. Güntert and *Y. Ito, “Evaluation of the reliability of the maximum entropy method for reconstructing 3D and 4D NOESY-type NMR spectra of proteins.”, Biochem. Biophys. Res. Commun., 457(2), 200-205, (2015), DOI: 10.1016/j.bbrc.2014.12.088; *Y.J.Lin, T. Ikeya, D.K. Kirchner, P. Güntert, “Influence of Incomplete NOESY Peaks of the Interface Residues on Structure Determinations of Homodimeric Proteins”, J. Chin. Chem. Soc. 61、1297-1306, (2014), DOI: 10.1002/jccs.201400095; E. Schmidt, T. Ikeya, M. Takeda, F. Löhr, L. Buchner, Y. Ito, *M. Kainosho, *P. Güntert, “Automated Resonance Assignment of the 21 kDa Stereo-array Isotope Labeled Thioldisulfide Oxidoreductase DsbA”, J. Magn. Reson. 249, 88-93 (2014), DOI: 10.1016/j.jmr.2014.10.005; 【図書】; Ikeya, T. and *Ito, Y., Advances in NMR data acquisition and processing for protein structure determination, Experimental approaches of NMR spectroscopy -Methodology and application to life science and materials science-, Springer, in press; 葛西卓磨, 池谷鉄兵, 木川隆則, “生命分子のNMR計測・解析への応用”, 電子情報通信学会誌, Vol.99, pp439-443, 2016
岩田耕一 ▲班員一覧に戻る▲: 【雑誌論文】; *T. Takaya, M. Anan, *K. Iwata, “Vibrational Relaxation Dynamics of β-carotene and its Derivatives with Substituents on Terminal Rings in Electronically Excited States as Studied by Femtosecond Time-resolved Stimulated Raman Spectroscopy in near-IR”, Phys. Chem. Chem. Phys., 20, 3320-3327, (2018), DOI: 10.1039/C7CP06343A; F. Lu, N. Kitamura, T. Takaya, K. Iwata, *T. Nakanishi, Y. Kurashige, “Experimental and Theoretical Investigation of Fluorescence Solvatochromism of Dialkoxyphenyl-pyrene Molecules”, Phys. Chem. Chem. Phys., 20, 3258-3264, (2018), DOI: 10.1039/C7CP06811E; *K. Iwata, *M. Terazima, *H. Masuhara, “Novel Physical Chemistry Approaches in Biophysical Researches with Advanced Application of Lasers: Detection and Manipulation”, Biochim. Biophys. Acta, (BBA), Gen. Subj., 1862, 335-357, DOI: 10.1016/j.bbagen.2017.11.003; *R. Ohtani, T. Tokita, T. Takaya, *K. Iwata, M. Kinoshita, N. Matsumori, M. Nakamura, L. F. Lindoy, *S. Hayami, “Morphology Controls of Hybrid Liposomes Using Metal Complex Lipids and Viscosities for Photo-chemical Reaction in Hydrophobic Fields”, Chem. Comm., 53, 13249-13252, (2017), DOI: 10.1039/C7CC07944C; B. Narayan, K. Nagura, T. Takaya, K. Iwata, A. Shinohara, H. Shinmori, H. Wang, Q. Li, X. Sun, H. Li, S. Ishihara and *T. Nakanishi, “Regioisomeric effect on photo-physical properties of alkylated-naphthalene liquids”, Phys. Chem. Chem. Phys., 20, 2970-2975, (2018), DOI: 10.1039/C7CP05584F (2017 PCCP HOT Article, Inside Front Cover); 4. N. Dwivedi, A. Verma, T. Takaya, K. Iwata, *S. Saha, *S. S. Sunkari, “NIR Luminescent Heterodinuclear [ZnII LnIII] Complexes: Synthesis, Crystal Structures and Photophysical properties”, J. Luminesc. 192, 156-165 (2017). DOI: 10.1016/j.jlumin.2017.06.045; F. Lu, *T. Takaya, K. Iwata, I. Kawamura, A. Saeki, M. Ishii, K. Nagura, *T. Nakanishi“A Guide to Design Functional Molecular Liquids with Tailorable Properties using Pyrene-Fluorescence as a Probe”, Sci. Rep. 7, 3416 (2017), DOI: 10.1038/s41598-017-03584-1; *T. Takaya, K. Iwata“Development of a Femtosecond Time-resolved Near-IR Multiplex Stimulated Raman Spectrometer in Resonance with Transitions in the 900–1550 nm Region”, Analyst 141, 4283-4292, (2016), DOI: 10.1039/c6an01051b (Cover Article, “HOT research article”に採用); S. Okino, T. Takaya, *K. Iwata, “Femtosecond Time-resolved near-infrared Spectroscopy of Oligothiophenes and Polythiophene: Energy Location and Effective Conjugation Length of their Low-lying Excited States”, Chem. Lett. 44, 1059-1061,(2015), DOI: 10.1246/cl.150330; A. Z. Samuel, S. Yabumoto, K. Kawamura, *K. Iwata, “Rapid Microstructure Characterization of Polymer Thin Films with 2D-Array Multifocus Raman Microspectroscopy”, Analyst 140, 1847 – 1851, (2015), DOI: 10.1039/C4AN01983K; *T. Takaya, K. Iwata, “Relaxation Mechanism of β-Carotene from S₂ (¹Bu⁺) State to S₁(²Ag^–) State: Femtosecond Time-Resolved Near-IR Absorption and Stimulated Resonance Raman Studies in 900–1550 nm Region”, J. Phys. Chem. A, 118(23), 4071–4078 (2014), DOI: 10.1021/jp504272h; Y. Nojima, *K. Iwata, “Viscosity Heterogeneity Inside Lipid Bilayers of Single-Component Phosphatidylcholine Liposomes Observed with Picosecond Time-Resolved Fluorescence Spectroscopy”, J. Phys. Chem. B, 118(29), 8631-8641 (2014), DOI: 10.1021/jp503921e; 【図書】; “Time-resolved Raman Spectroscopy”, Hiro-o Hamatuchi and Koichi Iwata, Encyclopedia of Spectroscopy and Spectrometry, 3rd Edition, Elsevier. 分担執筆 (in press)．; 「ラマン分光法」，日本光生物学協会光と生命の事典編集委員会編，朝倉書店（2016）．ISBN978-4-254-17161-7．「光検出器」を分担執筆．; 岩田耕一（分担執筆）, 「ラマン分光法」，日本分光学会分光法シリーズ1，濵口宏夫，岩田耕一共編，講談社（2015）．第3章「ラマン分光の実際」（51から87ページ）および付録Aから付録C（145から180ページ）; T. Yamaguchi, K. Kato “Paramagnetism-assisted nuclear magnetic resonance analysis of dynamic conformations and interactions of oligosaccharides”, Glycoscience: Biology and Medicine, N. Taniguchi, T. Endo, G.W. Hart, P. Seeberger, and C.-H. Wong ed. Springer (Japan), Vol.1, pp 137-145, 2014. DOI: 10.1007/978-4-431-54841-6_101; 岩田耕一“光化学の事典” 3-2節「さまざまな光化学反応」③「結合解離反応」, (2014)光化学の事典編集委員会編，（朝倉書店, 東京, 日本）（分担執筆）
内橋貴之 ▲班員一覧に戻る▲: 【雑誌論文】; M. Hosoyamada, *N. Yanai, K. Okumura, T. Uchihashi, N. Kimizuka, “Translating MOF Chemistry into Supramolecular Chemistry: Soluble Coordination Nanofibers Showing Efficient Photon Upconversion”, ChemComm., in press, (2018), DOI: 10.1039/C8CC01594E; N. Terahara, Y. Inoue, N. Kodera, Y. V. Morimoto, T. Uchihashi, K. Imada, T. Ando, K. Namba, *T. Minamino, “Insight into Structural Remodeling of the FlhA Ring Responsible for Bacterial Flagellar type III Protein Export”, Sci. Adv., in press.; A. Oda, S. Nagao, M. Yamanaka, H. Watanabe, T. Uchihashi, I. Ueda, N. Shibata, Y. Higuchi, *S. Hirota, “Construction of a Triangle-Shaped Trimer and a Tetrahedral Structure Using an α-Helix-Inserted Circular Permutant of Cytochrome c₅₅₅“, Chem. Asian. J., in press, DOI: 10.1002/asia.201800252; H. Tsukamoto, M. Higashi, H. Motoki, H. Watanabe, C. Ganser, K. Nakajo, Y. Kubo, T. Uchihashi, *Y. Furutani, “Structural Properties Determining Low K+ Affinity of the Selectivity Filter in the TWIK1 K⁺ Channel”, J. Biol. Chem., in press, DOI: 10.1074/jbc.RA118.001817; T. Maruno, H. Watanabe, T. Uchihashi, S. Adachi, K. Arai, T. Sawaguchi, *S. Uchiyama, “Sweeping of Adsorbed Therapeutic Proteins on Prefillable Syringe Enhances Subvisible Particles Generation” ,J. Pharm. Sci., in press, 10DOI: 10.1016/j.xphs.2018.01.021; T. Umakoshi, H. Udaka, T. Uchihashi, T. Ando, M. Suzuki, *T. Fukuda, “Quantum-dot Antibody Conjugation Visualized at the Single-molecule Scale with High-speed Atomic Force Microscopy”, Colloids Surf., B., 167, 267-274, (2018), DOI: 10.1016/j.colsurfb.2018.04.015; *内橋貴之“高速原子間力顕微鏡によるタンパク質の動態可視化と画像解析”, J. Comp. Chem., 17, 20-30, (2018), DOI: 10.2477/jccj.2018-0001; T. Haruyama, T. Uchihashi, Y. Yamada, N. Kodera, T. Ando, *H. Konno, “Negatively Charged Lipids are Essential for Functional and Structural Switch of Human 2-Cys Peroxiredoxin II”, J. Mol. Biol., 430, 602-610, (2018), DOI: 10.1016/j.jmb.2017.12.020; T. Takeda, T. Kozai, H. Yang, D. Ishikuro, K. Seyama, Y. Kumagai, T. Abe, H. Yamada, T. Uchihashi, *T. Ando, *K. Takei, “Dynamic Clustering of Dynamin-amphiphysin Helices Regulates Membrane Constriction and Fission Coupled with GTP Hydrolysis”, e-Life, 7, e3024, (2018), DOI: 10.7554/eLife.30246; M. Yagi-Utsumi, A. Sikdar, T. Kozai, R. Inoue, M. Sugiyama, T. Uchihashi, T. Satoh, *K. Kato, “Conversion of Functionally Undefined Homopentameric Protein PbaA into a Proteasome Activator by Mutational Modification of its C-terminal Segment Conformation”, Protein Eng. Des. Sel., 31, 29-36, (2018), DOI: 10.1093/protein/gzx066; A. Nakamura, T. Tasaki, Y. Okuni, C. Song, K. Murata, T. Kozai, M. Hara, H. Sugimoto, K. Suzuki, T.Watanabe, T. Uchihashi, H. Noji and *R. Iino, "Rate constants, processivity, and productive binding ratio of chitinase A revealed by single-molecule analysis", Phys. Chem. Chem. Phys., 20, 3010-3018, (2018), DOI: 10.1039/c7cp04606e; *T. Uchihashi and S. Scheuring, "Review: Applications of high-speed atomic force microscopy to real-time visualization of dynamic biomolecular processes", Biochim. Biophys. Acta, (BBA), Gen. Subj., 1862, 229-2410, (2017), DOI: 10.1016/j.bbagen.2017.07.010; T. Kozai, T. Sekiguchi, T. Satoh, H. Yagi, *K. Kato and *T. Uchihashi, "Two-step process for disassembly mechanism of proteasome α7 homo-tetradecamer by α6 revealed by high-speed atomic force microscopy", Sci. Rep. 7, 15373 (2017). DOI: 10.1038/s41598-017-15708-8; N. Terahara, N. Kodera, T. Uchihashi, T. Ando, *K. Namba and *T. Minamino, "Na+-induced structural transition of MotPS for stator assembly of Bacillus flagellar motor", Sci. Adv. 3, eaao4119 (2017) DOI: 10.1126/sciadv.aao4119; *M. Shibata, H. Watanabe, T. Uchihashi, T. Ando and R. Yasuda, "High-speed atomic force microscopy imaging of live mammalian cells", BPPB 14, 127-135 (2017) DOI: 10.2142/biophysico.14.0_127; *M. Shibata, *H. Nishimasu, N. Kodera, S. Hirano, T.Ando, T. Uchihashi and *O. Nureki, "Real-space and real-time dynamics of CRISPR-Cas9 visualized by high-speed atomic force microscopy", Nat. Commun. 8, 1430 (2017). DOI: 10.1038/s41467-017-01466-8; *T. Satoh, C. Song, T. Zhu, T. Toshimori, K. Murata, Y. Hayashi, H. Kamikubo, T. Uchihashi and *K. Kato, "Visualisation of a flexible modular structure of the ER folding-sensor enzyme UGGT", Sci. Rep. 7, 12142 (2017). DOI: 10.1038/s41598-017-12283-w; H. Harada, *A. Onoda, *T. Uchihashi, H. Watanabe, N. Sunagawa, M. Samejima, *K. Igarashi, and T. Hayashi, "Interdomain Flip-flop Motion Visualized in Flavocytochrome Cellobiose Dehydrogenase Using High-speed Atomic Force Microscopy during Catalysis", Chem. Sci. 8, 6561-6565 (2017) DOI: 10.1039/c7sc01672g; S. Matsui, T. Kureha, S. Hiroshige, M. Shibata, *T. Uchihashi, and *D. Suzuki, "Fast Adsorption of Soft Hydrogel Microspheres on Solid Surfaces in Aqueous Solution", Angew. Chem. Int. Ed. (Communication) 56, 12146-12149 (2017). DOI: 10.1002/anie.201705808; J. J. Keya, D. Inoue, Y. Suzuki, T. Kozai, D. Ishikuro, N. Kodera, T. Uchihashi, A. Md. R. Kabir, M. Endo, K. Sada, A. Kakugo, "High-Resolution Imaging of a Single Gliding Protofilament of Tubulins by HS-AFM", Sci. Rep. 7, 6166 (2017) DOI: 10.1038/s41598-017-06249-1; M. Mohamed, A. Kobayashi, A. Taoka, T. Watanabe-Nakayama, Y. Kikuchi, M. Hazawa, T. Minamoto, Y. Fukumori, N. Kodera, T. Uchihashi, T. Ando and *R. Wong, "High-Speed Atomic Force Microscopy Reveals Loss of Nuclear Pore Resilience as a Dying Code in Colorectal Cancer Cells", ACS Nano 11, 5567-5578 (2017) DOI: 10.1021/acsnano.7b00906; A. Sumino, T. Uchihashi, *S. Oiki , “Oriented Reconstitution of the Full-Length KcsA Potassium Channel in a Lipid Bilayer for AFM Imaging”, J. Phys. Chem. Lett. 8, 785-793, (2017), DOI: 10.1021/acs.jpclett.6b03058; K. Inoue, S. Ito, Y. Kato, Y. Nomura, M. Shibata, T. Uchihashi, S. P. Tsunoda, *H. Kandori, “A Natural Light-driven Inward Proton Pump”, Nat. Commun. 8, 13415, (2016), DOI: 10.1038/ncomms13415; T. Uchihashi, H. Watanabe, S. Fukuda, M. Shibata, *T. Ando“Functional Extension of High-speed Atomic Force Microscopy”, Ultramicroscopy, 160, 182-196 (2016), DOI: 10.1016/j.ultramic.2015.10.017; W. Sriwimol, A. Aroonkesorn, S. Sakdee, C. Kanchanawarin, T. Uchihashi, T. Ando, *C. Angsuthanasombat, “Potential Pre-pore Trimer Formation by the Bacillus Thuringiensis Mosquito-specific Toxin: Molecular Insights into a Critical Prerequisite of Membrane-bound Monomers”, J. Biol. Chem.,290 (34), 20793-20803,(2015), DOI: 10.1074/jbc.M114.627554; S. Fukuda, T. Uchihashi, *T. Ando, “Method of Mechanical Holding of Cantilever Chip for Tip-scan High-speed Atomic Force Microscopy”, Rev. Sci. Instrum. 86, 063703, (2015), DOI: 10.1063/1.4922381; M. Imamura, T. Uchihashi, T. Ando, A. Leifert, U. Simon, *A. D. Maly, *J. G.Heddle, "Probing Structural Dynamics of an Artificial Protein Cage Using High-Speed Atomic Fore Microscopy", Nano Letters, 15(2), 1331-1335 (2015), DOI: 10.1021/nl5045617; K. Takeda, T. Uchihashi, H. Watanabe, T. Ishida, *K. Igarashi, N. *Nakamura, H. Ohno“Real-time Dynamic Adsorption Processes of Cytochrome c on an Electrode Observed through Electrochemical High-speed Atomic Force Microscopy”, PLoS ONE 10(2), e0116685, (2015), DOI: 10.1371/journal.pone.0116685; *M. Shibata, T. Uchihashi, T. Ando, *R. Yasuda“Long-tip High-speed Atomic Force Microscopy for Nanometer-scale Imaging in Live Cells”, Sci. Rep. 5, 8724, (2015), DOI: 10.1038/srep08724; Y. Shibafuji, A. Nakamura, T. Uchihashi, N. Sugimoto, S. Fukuda, H. Watanabe, M. Samejima, T. Ando, H. Noji, A. Koivula, K. Igarashi, *R. Iino, “Single-molecule Imaging Analysis of Elementary Reaction Steps of Trichoderma Reesei cellobiohydrolase I (Cel7A) Hydrolyzing Crystalline Cell” J. Biol. Chem., 289, 14056-14065, (2014), DOI: 10.1074/jbc.M113.546085; *,**K. Igarashi,** T. Uchihashi, T. Uchiyama, H. Sugimoto, M. Wada, K. Suzuki, S. Sakuda, T. Ando, T. Watanabe, and M. Samejima, "Two-way Traffic of Glycoside Hydrolase Family 18 Processive Chitinases on Crystalline Chitin", Nat. Commun. 5, 3975 (2014), DOI: 10.1038/ncomms4975
** Co-first authors; A. Nakamura, H. Watanabe, T. Ishida, T. Uchihashi, M. Wada, T. Ando, K. Igarashi, and M. Samejima, "Trade-off between Processivity and Hydrolytic Velocity of Cellobiohydrolases at the Surface of Crystalline Cellulose", J. Am. Chem. Soc. 136, 4584-4592 (2014), DOI: 10.1021/ja4119994; 杉本華幸, 五十嵐圭日子, 内橋貴之, 鈴木一史, *渡邉剛志「キチナーゼによる結晶性キチンのプロセッシブ（連続的）な分解機構の解明」 日本応用糖質化学会誌 4（2）, 107-112 (2014); 内橋貴之「高速原子間力顕微鏡による生体試料のダイナミクス観察」膜誌 39(5), 322-328 (2014); 古寺哲幸, 内橋貴之, 安藤敏夫「高速原子間力顕微鏡による生体分子のナノ動体撮影」日本物理学会誌 69(7), 459-464 (2014); 内橋貴之, 飯野亮太, 安藤敏夫, 野地博行「高速AFMによるF₁-ATPase分子回転の直接可視化」生化学 86(2), 127-136 (2014); 【図書】; 内橋貴之, “光と生命の辞典”　第５章　「光による生命現象の計測」177節　高速原子間力顕微鏡, (20016), 真嶋哲郎, 七田芳則, 飯野盛利, 藤堂剛　編, (朝倉書店, 東京) ISBN: 978-254-17161-7 C3545; T. Uchihahshi, N. Kodera, and T. Ando、“Development of High-speed AFM and its Biological Applications”, K. Takeyasu ed., Atomic Force Microscopy in Nanobiology, Chap. 8, pp. 143-176. Pan Stanford Publishing, (2014), DOI: 10.4032/9789814411592
上久保裕生 ▲班員一覧に戻る▲: 【雑誌論文】; M. Yamaguchi, E. Ohta, T.Muto, T. Watanabe, T. Hohsaka, Y. Yamazaki, *H. Kamikubo, *M. Kataoka, “Statistical description of the denatured structure of a single protein, staphylococcal nuclease, by FRET analysis”, Biophys. Rev., 10(2), 145-152, (2018), DOI: 10.1007/s12551-017-0334-y; 上久保裕生、「連続滴定X線溶液散乱測定を志向したμ流路型自動サンプリングシステムの開発」、Journal of Computer Chemistry Japan, 17巻(2018)1号, 57-64, (2018), DOI: 10.2477/jccj.2018-0008; P. Bernadó, N. Shimizu, G. Zaccai, *H. Kamikubo, *M. Sugiyama, “Solution scattering approaches to dynamical ordering in biomolecular systems”, Biochimica et Biophysica Acta-General Subjects, 1862, 253-274, (2017), DOI: 10.1016/j.bbagen.2017.10.015; *T. Satoh, C. Song, T. Zhu, T. Toshimori, K. Murata, Y. Hayashi, H. Kamikubo, T. Uchihashi, *K. Kato, “Visualisation of a flexible modular structure of the ER folding-sensor enzyme UGGT”, Sci. Rep., 7, 12142, (2017), DOI: 10.1038/10.1038/s41598-017-12283-w; K. Yonezawa, N. Shimizu, K. Kurihara, Y. Yamazaki, *H. Kamikubo, *M. Kataoka, “Neutron crystallography of photoactive yellow protain reveals unusual protonation state of Arg52 in the crystal”, Sci. Rep., 7, 9361, (2017), DOI: 10.1038/s41598-017-09718-9; M. Nawata, H. Tsutsumi, Y Kobayashi, S. Unzai, S. Mine, T. Nakamura, K. Uegaki, H. Kamikubo, M. Kataoka, *D. Hamada, “Heat-induced native dimerization prevents amyloid formation by variable domain from immunoglobulin light-chain REI”, FEBS J., 284, 3114-3127, (2017), DOI: 10.1111/febs.14181; R. Kawatani, Y. Nishiyama, H. Kamikubo, K. Kakiuchi, H. Ajiro, “Aggregation Control by Multi-stimuli-Responsive Poly (N-vinylamide) Derivatives in Aqueous System”, Nanoscale Research Letters, 12, 461, (2017), DOI: 10.1186/s11671-017-2221-7; H. Kuramochi , S. Takeuchi ,K. Yonezawa , H. Kamikubo , M. Kataoka, *T.Tahara, “Probing the Early stages of Photoreception in Photoactive Yellow Protein with Ultrafast Time-domain Raman Spectroscopy”, Nature Chemistry, 9, 660-666, (2017), DOI: 10.1038/nchem.2717; L. Zhang, H. Kondo, H. Kamikubo, M. Kataoka, *W. Sakamoto, “VIPP1 has a Disordered C-terminal Tail Necessary for Protecting Photosynthetic Membranes against Stress in Arabidopsis”, Plant Physiology, 171, 1983-1995, (2016), DOI: 10.1104/pp.16.00532; J. K. Endow, A. G. Rocha , A. J. Baldwin , R. L. Roston , T. Yamaguchi, H. Kamikubo, *K. Inoue, “Polyglycine Acts as a Rejection Signal for Protein Transport at the Chloroplast Envelope”, PLOS ONE, 11(12), e0167802, (2016), DOI: 10.1371/journal.pone.0167802; Y. Yoshimura, N. A. Oktaviani, K. Yonezawa, H. Kamikubo, F. A. A. *Mulder, “Unambiguous Determination of the Ionization State of a Photoactive Protein Active Site Arginine in Solution by NMR Spectroscopy”, Angewandte Chemie, 56, 239-242, (2016), DOI: 10.1002/anie.201609605; Y. Kanematsu, H. Kamikubo, M. Kataoka, M. Tachikawa, “Vibrational Analysis on the Revised Potential Energy Curve of the Low-barrier Hydrogen Bond in Photoactive Yellow Protein”, Comput. Struct. Biotechnol. J., 14, 16-19, (2015), DOI: 10.1016/j.csbj.2015.10.003; S. Nagao, M. Ueda, H. Osuka, H. Komori, H. Kamikubo, M. Kataoka Y. Higuchi, *S. Hirota, “Domain-Swapped Dimer of Pseudomonas Aeruginosa Cytochrome c551: Structural Insights into Domain Wapping of Cytochrome c Family Proteins.”, PLoS One.,10(4):e0123653, (2015), DOI: 10.1371/journal.pone.0123653; M. Deshpande, P. Parui, H.Kamikubo, M. Yamanaka, S. Nagao, H. Komori, M. Kataoka, Y. Higuchi, *S. Hirota, “Formation of Domain-Swapped Oligomer of Cytochrome c from Its Molten Globule State Oligomer” Biochemistry, 53 (28), 4696–4703, (2014), DOI: 10.1021/bi500497s; Kobayashi, H. Tsutsumi, T. Abe, K. Ikeda, Y. Tashiro, S. Unzai, H. Kamikubo, M. Kataoka, H. Hiroaki, D.*Hamada, “Decreased Amyloidogenicity by Mutational Modulation of Surface Properties of the Immunoglobulin Light Chain BRE Variable Domain,” Biochemistry. 53(31), 5162-73, (2014), DOI: 10.1021/bi5007892; H. Nakagawa, Y. Yonetani, K. Nakajima, S. Ohira-Kawamura, T.Kikuchi, Y. Inamura, M. *Kataoka, *H. Kono, “Local Dynamics Coupled to Hydration Water Determines DNA-sequence Dependent Deformability”, Physical Reiew E 90, 22723, (2014), DOI: 10.1103/PhysRevE.90.022723; *D. Novitasari, H. Kamikubo, Y. Yamazaki, M. Yamaguchi, M. Kataoka, “Excited-State Proton Transfer in Fluorescent Photoactive Yellow Protein Containing 7-Hydroxycoumarin”, Adv. Mater. Res., 896, 85-88, (2014), DOI: 10.4028/www.scientific.net/AMR.896.85; P. Parui, M. Deshpande, S. Nagao, H. Kamikubo, Y. Higuchi, M. Kataoka, S. *Hirota“Formation of oligomeric cytochrome c during folding by intermolecular hydrophobic interaction between N- and C-terminal α-helices” Biochemistry, 52(48), 8732–8744, (2013), DOI: 10.1021/bi400986g; M. Hamaguchi, H. Kamikubo, K. N. Suzuki, Y. Hagihara, I. Yanagihara, I. Sakata, M. Kataoka, *D. Hamada, “Structural Basis of Alpha-Catenin Recognition by EspB from Enterohaemorrhagic E. coli Based on Hybrid Strategy Using Low-resolution Structural and Protein Dissection”, PLoS One, 8 (8), e71618, (2013), DOI: 10.1371/journal.pone.0071618; N. Inoue, D. Hamada, H. Kamikubo, K. Hirata, M. Kataoka, M. Yamamoto, M. Ikawa, M. Okabe, *Y. Hagihara, “Molecular Dissection of IZUMO1, a Sperm Protein Essential for Sperm-egg Fusion”, Development, 140, 3221-3229, (2013), DOI: 10.1242/dev.094854; Y. Kita, H. Kamikubo, M. Kataoka, *M. Tachikawa, “Theoretical Analysis of the Geometrical Isotope Effect on the Hydrogen Bonds in Photoactive Yellow Protein with Multi-component Density Functional Theory”, Chem. Phys., 419, 50-53, (2013), DOI: 10.1016/j.chemphys.2012.11.022; J. Uewaki, H. Kamikubo, J. Kurita, N. Hiroguchi, H. Moriuchi, M. Yoshida, M. Kataoka, N. Utsunomiya-Tate, *S. Tate, “Preferential Domain Orientation of HMGB2 Determined by the Weak Intramolecular Interactions Mediated by the Interdomain Linker”, Chem. Phys., 419, 212-223, (2013), DOI: 10.1016/j.chemphys.2013.02.004; *J. Yuasa, T. Ohno, H. Tsumatori, R. Shiba, H. Kamikubo, M. Kataoka, Y. Hasegawa, *T. Kawai, “Fingerprint Signatures of Lanthanide Circularly Polarized Luminescence from Proteins Covalently Labeled with a Beta-diketonate Europium(III) Chelate”, Chem. Commun., 49(41), 4604-4606, (2013), DOI: 10.1039/c3cc40331a
佐藤啓文 ▲班員一覧に戻る▲: 【雑誌論文】; Y. Matsumura, S. Iuchi, *H. Sato, “A Model Electronic Hamiltonian for the Self-assembly of an Octahedron-shaped Coordination Capsule”, Phys. Chem. Chem. Phys., 20, 1164-1172, (2018), DOI: 10.1039/c7cp06094g; Y. Matsumura, S. Hiraoka, and *H. Sato“A reaction model on the self-assembly process of octahedron-shaped coordination capsules”, Phys. Chem. Chem. Phys. 19, 20338-20342 (2017) DOI: 10.1039/c7cp03493h (2017 PCCP HOT Articles); *T. Fujita, Y. Haketa, H. Maeda, T. Yamamoto, “Relating Stacking Structures and Charge Transport in Crystal Polymorphs of the Pyrrole-Based pi-Conjugate Molecule”, Org. Electron., 49, 53, (2017), DOI: 10.1016/j.orgel.2017.06.028; T. Fujita, *T. Yamamoto, “Assessing the Accuracy of Integral Equation Theories for Nano-sized Hydrophobic Solutes in Water”, J. Chem. Phys. 147, 014110, (2017), DOI: 10.1063/1.4990502; H. Arefi, *T. Yamamoto, “Communication: Self-assembly of a Model Supramolecular Polymer Studied by Replica Exchange with Solute Tempering”, J. Chem. Phys., 147, 211102 (2017), DOI: 10.1063/1.5008275; Y. Yoshida, *H. Sato, J.W.R. Morgan, D.J. Wales“Potential Energy Landscapes of Tetragonal Pyramid Molecules”Chem.Phys.Lett., 664, 5- 9, (2016), DOI: 10.1016/j.cplett.2016.09.058(Editor’s choice, Front Coverに採用); Y. Matsumura *H. Sato, “An Integral Equation Theory for Solvation Effects on the Molecular Structural Fluctuation”, J. Chem. Phys., 143, No. 1, 014104 , (2015), 　DOI: 10.1063/1.4923038; K. Kikui, S. Hayaki, K. Kido, D. Yokogawa, K. Kasahara, Y. Matsumura, *H. Sato, S. Sakaki, “Solvent Structure of Ionic Liquid with Carbon Dioxide”　J. Mol. Liq., 217, 12-16, (2015), , DOI: 10.1016/j.molliq.2015.06.061; K. Kido, K. Kasahara, *H.Sato, S. Sakaki, “ A molecular Level Study of Selective Cation Capture by a Host–guest Mechanism for 25,26,27,28-tetramethoxycalix[4]arene in MClO ”, Mol. Simul., 41, (10-12), 881- 891, (2014), DOI: 10.1080/08927022.2014.895002; K. Kasahara, *H. Sato, “Development of Three-dimensional Site-site Smoluchowski- Vlasov Equation and Application to Electrolyte Solutions”, J. Chem. Phys., 140, 244110, (2014), DOI: 10.1063/1.4884386; T. Inagaki, S. Aono, H. Nakano, *T. Yamamoto, “Like-Charge Attraction of Molecular Cations in Water: Subtle Balance between Interionic Interactions and Ionic Solvation Effect”, J. Phys. Chem. B, 118(20), 5499-5508, (2014), DOI: 10.1021/jp501212y; T. Inagaki, *T. Yamamoto, “Critical Role of Deep Hydrogen Tunneling to Accelerate the Antioxidant Reaction of Ubiquinol and Vitamin E”, J. Phys. Chem. B, 118(4), 937-950, (2014), DOI: 10.1021/jp410263f; H. Nakano, *T. Yamamoto, “Accurate and Efficient Treatment of Continuous Solute Charge Density in the Mean-Field QM/MM Free Energy Calculation”, J. Chem. Theory Comp., 9(1), 188-203, (2013), DOI: 10.1021/ct300831t; 【図書】; 佐藤啓文, “揺らぎ・ダイナミクスと生体機能: 物理化学的視点から見た生体分子” (DOJIN BIOSCIENCE SERIES) 第7章「理論」2節「分子性液体の積分方程式理論」,(2013), 寺嶋正秀編,（化学同人,京都）ISBN:9784759815108
高田十志和 ▲班員一覧に戻る▲: 【雑誌論文】; *T. Takata, D. Aoki, “Topology-Transformable Polymer: Linear–Branched Polymer Structure Change Utilizing Mechanical Linking of Polymer Chains”, Polymer Journal, 50, 127–147, (2018), DOI: 10.1038/pj.2017.60; H. Sato, D. Aoki, *T. Takata,“Which One is Bulkier: The 3,5-Dimethylphenyl or the 2,6-Dimethylphenyl Group? Development of Size-Complementary Molecular and Macromolecular [2]Rotaxanes”, Chem. Asian J., 13 ,785 –789, (2018), DOI: 10.1002/asia.201800170; J. Sawada, D. Aoki, M. Kuzume, K. Nakazono, S. Uchida, H. Otsuka, *T. Takata, “Vinylic Rotaxane Cross-linker for Toughened Network Polymer via Radical Polymerization of Vinyl Monomers”, Polym. Chem., 8, 1878-1881, (2017), DOI: 10.1039/C7PY00193B; H. Jang, K. Iijima, Y. Koyama, S. Uchida, S. Asai, *T. Takata, “Synthesis and Properties of Rotaxane-cross-linked polymers using a double-stranded γ-CD-based inclusion complex as a supramolecular cross-linker “ Polymer (2017) in press, DOI: 10.1016/j.polymer.2017.01.062; K. Iijima, D. Aoki, H. Otsuka, *T. Takata, “Synthesis of Rotaxane Cross-Linked Polymers With Supramolecular Cross-Linkers Based on γ−CD and PTHF Macromonomers: The Effect of The Macromonomer Structure on The Polymer Properties”, Polymer, 128, 392–396, (2017), DOI: 10.1016/j.polymer.2017.01.024; K. Iijima, D. Aoki, H. Sogawa, S. Asai, *T. Takata, “Synthesis and Characterization of Supramolecular Cross-linkers Containing Cyclodextrin Dimer and Trimer,” Polym. Chem., 7, 3492–3495, (2016), DOI: 10.1039/C6PY00367B; H. Sato, D. Aoki, *T. Takata, “Synthesis and Star/Linear Topology Transformation of a Mechanically Linked ABC Terpolymer” ACS Macro Lett., 5, 699–703, (2016), DOI: 10.1021/acsmacrolett.6b00320; Z. Chen, D. Aoki, S. Uchida, H. Marubayashi, S. Nojima, *T. Takata, “Effect of Component Mobility on the Properties of Macromolecular [2]rotaxanes”, Angew. Chem. Int. Ed., 53, 2778–2781,(2016), DOI: 10.1002/anie.201510953; M. Ogawa, H. Sogawa, Y. Koyama, *T. Takata, “Synthesis of Rotaxane Cross-linked Polymers Derived from Vinyl Monomers Using a Metal-containing Supramolecular Cross-linker”, Polym. J., 47, 580-584, (2015),DOI: 10.1038/pj.2015.34; M. Ogawa, M. Nagashima, H. Sogawa, S. Kuwata, *T. Takata, “Synthesis and Cavity Size Effect of Pd-containing Macrocycle Catalyst for Efficient Intramolecular Hydroamination of Allylurethane”, Org. Lett., 17, 1664-1667, (2015), DOI: 10.1021/acs.orglett.5b00378; J. Sawada, D. Aoki, S. Uchida, H, Otsuka, *T. Takata, “Synthesis of Vinylic Macromolecular Rotaxane Cross-linkers Endowing Network Polymers with Toughness”, Acs Macro Lett., 4, 598-601, (2015), DOI: 10.1021/acsmacrolett.5b00242; D. Aoki, S. Uchida, *T. Takata, “Star/Linear Polymer Topology Transformation Facilitated by Mechanical Linking of Polymer Chains”, Angew. Chem. Int. Ed., 54, 6770-6774, (2015), DOI: 10.1002/anie.201500578; T. Ogawa, K. Nakazono, D. Aoki, S. Uchida, *T. Takata, “Effective Approach to Cyclic Polymer from Linear Polymer: Synthesis and Transformation of Macromolecular [1]Rotaxane” , ACS Macro Lett., 4, 343−347, (2015), DOI: 10.1021/acsmacrolett.5b00067; T. Ogawa, N. Usuki, K. Nakazono, Y. Koyama, *T. Takata,“Linear–cyclic Polymer Structural Transformation and its Reversible Control Using a Rational Rotaxane Strategy”,　Chem. Commun., 51, 5606—5609, (2015), DOI: 10.1039/C4CC08982K; 打田聖, 澤田隼, 飯島圭祐,青木大輔, 中薗和子, *高田十志和“新しい架橋剤：空間連結型架橋剤の合成とビニル重合系への展開”高分子論文集, 72, 93-103, (2015), DOI: DOI:10.1295/koron.2014-0075; K. Nakazono, T. Ishino, T. Takashima, D. Saeki, D. Natsui, N. Kihara, *T. Takata, “Directed One-pot Syntheses of Crown Ether Wheel-containing Main Chain-type Polyrotaxanes with Controlled Rotaxanation Ratios”, Chem. Commun., 50, 15341-15344, (2014), DOI: 10.1039/C4CC06943A; Y. Akae, Y. Koyama, S. Kuwata, *T. Takata, “Cyclodextrin-Based Size-Complementary [3]Rotaxanes: Selective Synthesis and Specific Dissociation”, Chem. Eur. J., 20, 17132 – 17136, (2014), DOI: 10.1002/chem.201405005; S. Suzuki, K. Matsuura, K. Nakazono, *T. Takata, “Effect of a Side Chain Rotaxane Structure on the Helix-Folding of Poly(m-phenylene diethynylene)”, Polym. J., 46(6), 355-365 (2014), DOI: 10.1038/pj.2014.4（Selected as a Cover Page Picture）; D. Aoki, S. Uchida, *T. Takata, “Mechanically Linked Block/Graft Copolymers: Effective Synthesis via Functional Macromolecular [2]Rotaxanes”, ACS Macro Lett., 3(4), 324-328 (2014), DOI: 10.1021/mz5001306; D. Aoki, S. Uchida, *T. Takata, “Synthesis and Characterization of A Mechanically Linked Transformable Polymer”, Polym. J., 46(9), 546-552 (2014), DOI: 10.1038/pj.2014.22; Y. Abe, H. Okamura, S. Uchida, *T. Takata, “Synthesis of Main Chain-type Liquid Crystalline Polyrotaxanes: Influence of The Wheel Components and Their Mobility on Liquid Crystalline Properties”, Polym. J., 46(9), 553-558 (2014), DOI: 10.1038/pj.2014.23; 【図書】; 新版ゲルテクノロジーハンドブック, 高田十志和、曽川洋光（架橋点可動型）, （2014）（エヌティーエス出版, 東京、日本）
立川仁典 ▲班員一覧に戻る▲: 【雑誌論文】; *R. Harada, T. Mashiko, M. Tachikawa, S. Hiraoka, and *Y. Shigeta, “Programed Dynamical Ordering in the Self-organization Processes of a Nanocube: A Molecular Dynamics Study”, Phys. Chem. Chem. Phys., 20, 9115-9122, (2018), DOI: 10.1039/C8CP00284C; N. Tanaka, Y.-Y. Zhan, Y. Ozawa, T. Kojima, T. Koide, T. Mashiko, U. Nagashima, M. Tachikawa, and *S. Hiraoka, “Semi-quantitative Evaluation of Molecular Meshing by Surface Analysis with Varying Probe Radii”, Chem. Commun., 54, 3335-3338, (2018), (selected as Back Cover), DOI: 10.1039/c8cc00695d; Y.-Y. Zhan, K. Ogata, T. Kojima, T. Koide, K. Ishii, T. Mashiko, M. Tachikawa, S. Uchiyama, and *S. Hiraoka, “Hyperthermostable Cube-shaped Assembly in Water”, Communications Chemistry, 1, 14, (2018), DOI: 10.1038/s42004-018-0014-2; *H. Kato, S. Yoshimoto, A. Ueda, S. Yamamoto, Y. Kanematsu, M. Tachikawa, H. Mori, J.Yoshinobu, I. Matsuda,“Strong Hydrogen-Bonds at the interface between Proton-Donating and Accepting Self-Assembled Monolayers on Au(111) ”, Langmuir, 34, 2189-2197, (2018), DOI: 10.1021/acs.langmuir.7b03451; *T. Udagawa, *M. Tachikawa, “Reaction Mechanism of Hydrogen-tritium Exchange Reactions between Several Organic and HTO Molecules: A role of the second HTO”, RSC Advances, 8, 3878-3888,(2018), DOI: 10.1039/C7RA13110K; T. Kawatsu, *M. Tachikawa, “The Quantum Fluctuations of the Fullerene Cage Modulate the Internal Magnetic Environment”, Phys. Chem. Chem. Phys., 20, 1673-1684,(2018), DOI: 10.1039/C7CP06401B; K. Suzuki, *T. Takayanagi, Y. Kita, M. Tachikawa, T. Oyamada, “Quantum Dynamics Calculations for e+ + LiH -> Li+ + [H; e+] Dissociative Positron Attachment Using a Pseudopotential Model”, Comput. Theo. Chem., 1123, 135-141, (2018), DOI: 10.1016/j.comptc.2017.11.023; S. Kai, V. Marti-Centelles, Y. Sakuma, T. Mashiko, T. Kojima, U. Nagashima, M. Tachikawa, P. J. Lusby, and *S. Hiraoka, “Quantitative Analysis of Self-Assembly Process of a Pd2L4 Cage Consisting of Rigid Ditopic Ligands”, Chem. Eur. J., 24, 663-671, (2018), DOI: 10.1002/chem.201704285; S. Kai, Y. Sakuma, T. Mashiko, T. Kojima, M. Tachikawa, *S. Hiraoka, “The Effect of Solvent and Coordination Environment of Metal Source on the Self-Assembly Pathway of a Pd(II)-mediated Coordination Capsule”, Inorg. Chem., 56, 12652-12663, (2017), DOI: 10.1021/acs.inorgchem.7b02152; S. Kai, Y. Sakuma, T. Mashiko, T. Kojima, M. Tachikawa, and *S. Hiraoka, "The Effect of Solvent and Coordination Environment of Metal Source on the Self-Assembly Pathway of a Pd(II)-mediated Coordination Capsule", Inorg. Chem., in press (2017). DOI: 10.1039/C6CP07754D; *N. Kungwan, C. Ngaojampa, Y. Ogata, T. Kawatsu, Y. Oba, Y. Kawashima, and *M. Tachikawa, "Solvent Dependence of Double Proton Transfer in the Formic Acid Formamidine Complex: Path Integral Molecular Dynamics Investigation", J. Phys. Chem. A, in press (2017). DOI: 10.1021/acs.jpca.7b07010; *T. Takayanagi, K. Suzuki, T. Yoshida, Y. Kita, M. Tachikawa, “Quantum Dynamics Study on the Binding of a Positron to Vibrationally Excited States of Hydrogen Cyanide Molecule”, Chem. Phys. Lett., 675, 118-123 (2017.5), DOI: 10.1016/j.cplett.2017.03.025; K. Yamamoto, Y. Kanematsu, U. Nagashima, A. Ueda, H. Mori, *M. Tachikawa,“Multicomponent DFT Study of Geometrical H/D Isotope Effect on Hydrogen-bonded Organic Conductor, κ-H₃(Cat EDT-ST)₂”, Chem. Phys. Lett., 674, 168-172 (2017.4), DOI: 10.1016/j.cplett.2017.02.073; *C. Ngaojampa, T. Kawatsu, Y. Oba, N. Kungwan, *M. Tachikawa,“Asymmetric Hydrogen Bonding in Formic Acid-nitric Acid Dimer Observed by Quantum Molecular Dynamics Simulations”, Theor. Chem. Acc., in press, (2017), DOI: 10.1007/s00214-017-2057-3; *T. Udagawa, K. Sugiura, K. Suzuki, *M. Tachikawa, “Unusual H/D isotope effect in isomerization and keto-enol tautomerism reactions of pyruvic acid: Nuclear quantum effect restricts some rotational isomerization reactions”, RSC Advances, 7, 9328-9337, (2017), DOI: 10.1039/C6RA28271G; T. Mashiko, S. Hiraoka, U, Nagashima, *M. Tachikawa, “Theoretical Study on Substituent and Solvent Effects for Nanocube Formed with Gear-shaped Amphiphile Molecules”, Phys. Chem. Chem. Phys., 19, 1627-1631, (2017), DOI: 10.1039/C6CP07754D; Y. Kita, *M. Tachikawa, “Effects of Vibrational Anharmonicity and Inter-mode Couplings on the Binding Energy of a Positron to Molecules”, AIP Conf. Proc., in press, (2017), DOI: 10.1088/1742-6596/791/1/012015; *T. Udagawa, *M. Tachikawa, “Nuclear Quantum Effect and H/D Isotope Effect on F + (H₂O)_n → FH + (H₂O)_n-1OH (n = 1-3) Reactions”, J. Chem. Phys., 145, 164310 (10 pages), (2016), DOI: 10.1063/1.4966162; K. Yamamoto, Y. Kanematsu, U. Nagashima, A. Ueda, H. Mori, *M. Tachikawa,“Theoretical Study of H/D Isotope Effect on Phase Transition of Hydrogen-bonded Organic Conductor κ-H₃(Cat-EDT-TTF)₂”, Phys. Chem. Chem. Phys. (Communication), 18, 29673-29680, (2016), DOI: 10.1039/C6CP05414E; Y. Hamada, Y. Kanematsu, *M. Tachikawa, “QM/MM Study on Sialyltransferase Reaction Mechanism”, Biochemistry, 55, 5764-5771, (2016), DOI: 10.1021/acs.biochem.6b00267; M. Narukawa-Nara, A. Nakamura, K. Kikuzato, Y. Kakei, A. Sato, Y. Mitani, Y. Yamasaki-Kokudo, T. Ishii, KI. Hayashi, T. Asami, T. Ogura, S. Yoshida, S. Fujioka, T. Kamakura, T. Kawatsu, M. Tachikawa, K. Soeno, *Y. Shimada, “Aminooxy-naphthylpropionic Acid and its Derivatives are Inhibitors of Auxin Biosynthesis Targeting Trp Aminotransferase: Structure-Activity Relationships”, The Plant Journal, 87, 245-257, (2016), DOI: 10.1111/tpj.13197; Y. Oba, T. Kawatsu, *M. Tachikawa, “A Path Integral Molecular Dynamics Study of the Hyperfine Coupling Constants of the Muoniated and Hydrogenated Acetone Radicals”, J. Chem. Phys., 145, 064301 (15 pages), (2016), DOI: 10.1063/1.4960077; Y. Ogata, T. Kawatsu, *M. Tachikawa,“Can Low-barrier Hydrogen Bond Exist in Systems with Second Row Elements? An ab Initio Path Integral Molecular Dynamics Study for Deprotonated Hydrogen Sulfide Dimer”, Theor. Chem. Acc., 135, 200 (11 pages), (2016), DOI: 10.1007/s00214-016-1958-x; M. Nummela, *H. Raebiger, D. Yoshida, M. Tachikawa, “Positron Binding Properties of Glycine and Its Aqueous Complexes”, J. Phys. Chem. A, 120, 4037-4042, (2016), DOI: 10.1021/acs.jpca.6b01780; *Y. Kanematsu, Y. Takano, M. Tachikawa, “Inverse Ubbelohde Effect in the Short Hydrogen Bond of Photosystem II: Relation between H/D Isotope Effect and Symmetry in Potential Energy Profile”, J. Comput. Chem., 37, 2140-2145, (2016), DOI: 10.1002/jcc.24438 (Cover Imageに採用); Y. Takeda, *Y. Kita, *M. Tachikawa, “Theoretical Study of a Positron-attachment to Vibrational Excited States for Non-polar Carbon Disulfide Molecule”, Eur. Phys. J. D, 70, 132 (5 pages), (2016), DOI: 10.1140/epjd/e2016-70140-7; Y. Oba, T. Kawatsu, *M. Tachikawa, “Thermal Dependence on Structures of Muoniated and Hydrogenated Acetone Radicals”, AIP Conf. Proc., 1790, 020022 (4pages), (2016), DOI: 10.1063/1.4968648; M. Hashimoto, T. Ishimoto, *M. Tachikawa, *T. Udagawa, “Analysis of Exponent Values of Gaussian-type Functions on Quantum Protons and Deuterons in Charged or Polarized Systems”, Int. J. Quant. Chem., 116, 961-967, (2016), DOI: 10.1002/qua.25117 (Cover Imageに採用); Y. Kanematsu, H. Kamikubo, M. Kataoka, *M. Tachikawa, “Vibrational Analysis on the Revised Potential Energy Curve of the Low-barrier Hydrogen Bond in Photoactive Yellow Protein”, Comput. Struct. Biotechnol. J., 14, 16-19, (2016), DOI: 10.1016/j.csbj.2015.10.003; *M. Tachikawa,　“Positron-attachment to Small Molecules: Vibrational Enhancement of Positron Affinities with Configuration Interaction Level of Multi-component Molecular Orbital Approach”, AIP Conf. Proc., 1702, 090038 (4pages), (2015), DOI: 10.1063/1.4938847; Y. Kanematsu, H. Kamikubo, M. Kataoka, *M. Tachikawa, “Vibrational Analysis on the Revised Potential Energy Curve of the Low-barrier Hydrogen Bond in Photoactive Yellow Protein”, Comput. Struct. Biotechnol. J. 14, 16-19, (2015), DOI: 10.1016/j.csbj.2015.10.003; Y. Kanematsu, Y. Kamiya, K. Matsuo, K. Gekko, *K. Kato, *M. Tachikawa, “Isotope Effect on the Circular Dichroism Spectrum of Methyl α-D-glucopyranoside in Aqueous Solution”, Sci. Rep., 5, 17900 (5pages) (2015), DOI: 10.1038/srep17900; Y. Ogata, Y. Kawashima, *K. Takahashi, *M. Tachikawa, “Theoretical Vibrational Spectra of OH^-(H₂O)₂: Effect of Quantum Distribution and Vibrational Coupling”, Phys. Chem. Chem. Phys., 17, 25505-25515, (2015), DOI: 10.1039/C5CP03632A; *T. Udagawa, K. Suzuki, *M. Tachikawa, “Multicomponent Molecular Orbital-climbing Image-nudged Elastic Band Method to Analyze Chemical Reactions Including Nuclear Quantum Effect: Application to Hydrogen Yransfer Reaction”, ChemPhysChem, 16, 3156-3160, (2015), DOI: 10.1002/cphc.201500498; S. Watanabe, Y. Ogata, T. Kawatsu, Y. Kawashima, *M. Tachikawa, “Effects of Monohydration on an Adenine-thymine Base Pair”, Theor. Chem. Acc., 134, 84 (12 pages),(2015),; *T. Udagawa,*M. Tachikawa, “H/D Isotope Effect on Charge-inverted Hydrogen-bonded Systems: Systematic Classification of Three Different Types in H₃XH...YH₃ (X = C, Si, or Ge, and Y = B, Al, or Ga) with Multicomponent Calculation”, J. Comput. Chem., 36, 1647-1654, (2015), DOI: 10.1002/jcc.23978; Y. Kanematsu and *M. Tachikawa,“Performance Test of Multicomponent Quantum Mechanical Calculation with Polarizable Continuum Model for Proton Chemical Shift”, J. Phys. Chem. A, 119, 4933-4938, (2015), DOI: 10.1021/jp512877a; *T. Udagawa and *M. Tachikawa,“Why does deuterium substitution lead to the contraction of X...Pi distance? Origin of the reverse Ubbelohde effect in XH...Pi interaction”, Theor. Chem. Acc., 134, 24 (5 pages), (2015), DOI: 10.1007/s00214-015-1633-7; *K. Egashira, Y. Yamada, Y. Kita, and M. Tachikawa,“Ferromagnetic spin coupling in the chromium dimer cation: Measurements by photodissociation spectroscopy combined with coupled-cluster calculations”, J. Chem. Phys., 142, 054309 (4pages) (2015), DOI: 10.1063/1.4907197; T. Mashiko, K. Yamada, S. Hiraoka, U. Nagashima, *M. Tachikawa, "Molecular Dynamics Simulations of Self-assembled Nanocubes in Methanol", Mol. Sim., 41, 845-849, (2014), DOI: 10.1080/08927022.2014.940523; K. Yamada, Y. Kawashima, *M. Tachikawa, "Quantum Simulation for Muoniated and Deuterated Methyl Radicals in Implicit Water Solvent: Combined Ab Initio Path Integral Molecular Dynamics and the Polarizable Continuum Model Simulation Study", Mol. Sim., 41, 832-839, (2014), DOI: 10.1080/08927022.2014.938070; Y. Ogata, Y. Kawashima, K. Takahashi, and *M. Tachikawa,“Is the structure of hydroxide dihydrate OH-(H₂O)₂? : An ab initio path integral molecular dynamics study”, Theor. Chem. Acc., 134, 1582-1587, (2014), DOI: 10.1007/s00214-014-1587-1; Y. Kanematsu and *M. Tachikawa,“Theoretical analysis of geometry and NMR isotope shift in hydrogen-bonding center of photoactive yellow protein by combination of multicomponent quantum mechanics and ONIOM scheme”, J. Chem. Phys., 141, 185101 (8pages), (2014), DOI: 10.1063/1.4900987; *N. Kungwana, Y. Ogata, S. Hannongbua, *M. Tachikawa, "Nuclear Quantum Effect and Temperature Dependency on the Hydrogen-bonded Structure of 7-azaindole Dimer", Theor. Chem. Acc., 133, 1553-1562, (2014), DOI: 10.1007/s00214-014-1553-y; *T. Udagawa, T. Ishimoto, *M. Tachikawa, "H/D Isotope Effect on Structures, Binding Energies, and Basis Set Superposition Errors in F-(H₂O)_n (n = 1-3) Clusters", Chem. Phys., 441,101-108 (2014), DOI: 10.1016/j.chemphys.2014.07.014; *T. Oyamad, *M. Tachikawa, "Multi-component Molecular Orbital Sudy on Positron Attachment to Alkali-metal Hydride Molecules: Nature of Chemical Bonding and Dissociation Limits in [LiH; e⁺]", Eur. Phys. J. D, 68, 231-239 (2014), DOI: 10.1140/epjd/e2014-40708-4; *M. Tachikawa, "Positron-attachment to Acetonitrile, Acetaldehyde, and Acetone Molecules: Vibrational Enhancement of Positron Affinities with Configuration Interaction Level of Multi-component Molecular Orbital Approach", J.Phys.Conf.Ser., 488, 012053 (7pages) (2014), DOI: 10.1088/1742-6596/488/1/012053; Y. Yamada, *Y. Kita, M. Tachikawa, "Theoretical Prediction of the Binding of a Positron to a Formaldehyde Molecule Using a First-principles Calculation", Phys. Rev. A, 89, 062711 (5pages), (2014), DOI: 10.1103/PhysRevA.89.062711; T. Udagawa, T. Tsuneda, *M. Tachikawa, "Electron-nucleus Correlation Functional for Multicomponent Density-functional Theory", Phys. Rev. A, 89, 052519 (5pages), (2014), DOI: 10.1103/PhysRevA.89.052519; Y. Kanematsu, *M. Tachikawa, "Development of Multicomponent Hybrid Density Functional Theory with Polarizable Continuum Model for the Analysis of Nuclear Quantum Effect and Solvent Effect on NMR Chemical Shift", J. Chem. Phys., 140, 164111 (7pages), (2014), DOI: 10.1063/1.4872006; K. Yamada, Y. Kawashima, *M. Tachikawa, "Accurate Prediction of Hyperfine Coupling Constants in Muoniated and Hydrogenated Ethyl Radicals: Ab Initio Path Integral Simulation Study with Density Functional Theory Method", J. Chem. Theor. Comput., 10(5), 2005-2015, (2014), DOI: 10.1021/ct500027z （表紙に採択）; *Y. Kita, M. Tachikawa, "Theoretical Investigation of the Binding of a Positron to Vibrational Excited States of Hydrogen Cyanide Molecule", Eur. Phys. J. D, 68, 116-122, (2014), DOI: 10.1140/epjd/e2014-40799-9; Y. Yamada, *Y. Kita, M. Tachikawa, M. Towler, R. J. Needs, "Quantum Monte Carlo and High-level Ab Initio Molecular Orbital Investigation of Dissociation Channels of the Positronic Alkali-metal Hydrides, [XH;e⁺] (X = Li, Na, and K)", Eur.Phys.J.D, 68, 63-68, (2014), DOI: 10.1140/epjd/e2014-40734-2; Oba, *M. Tachikawa, "Theoretical Investigation of a Positron Binding to an Aspartame Molecule Using the ab Initio Multicomponent Molecular Orbital Approach", Int. J. Quant. Chem., 114(17), 1146-1149 (2014), DOI: 10.1002/qua.24641 （表紙に採択）; *Y. Kawashima, *M. Tachikawa, "An Ab Initio Path Integral Molecular Dynamics Study of the Nuclear Quantum Effect on Out-of-plane Ring Deformation of Hydrogen Maleate Anion", J. Chem. Theor. Comput., 10(1), 153-163, (2014), DOI: 10.1021/ct4007986; *T. Udagawa, *M. Tachikawa, "Why is N...Be Distance of NH₃H⁺...DBeH Shorter than that of NH₃D⁺...HBeH? Paradoxical Geometrical Isotope Effects for Partially Isotope-substituted Dihydrogen-bonded Isotopomers", J. Comput. Chem. (Communication), 35(4), 271-274, (2014), DOI: 10.1002/jcc.23505 （表紙に採択）; K.Yamada, Y. Kawashima, *M. Tachikawa, "Muon-Electron Hyperfine Coupling Constants of Muoniated Ethyl Radical: a Path Integral Simulation Study with Semiempirical Molecular Orbital Method", Chin. J. Phys., 52, 126-137 (2014). DOI: 10.6122/CJP.52.126; 【図書】; 飯沼裕美, 大場優生，河村成肇，高妻孝光，菅原洋子，高柳敏幸, 立川仁典, 「新しい量子ビーム・ミュオン分光と理論的アプローチ」 J. Comput. Chem. Jpn., vol. 16 , A12-A17 (2017). (in Japanese); 川島雪生, 澤田啓介, 中嶋隆人, 立川仁典, 「酢酸－リン酸アニオンクラスターの分子間水素結合における核の量子揺らぎの効果に関する理論的研究」 J. Comput. Chem. Jpn.「量子水素の科学」特集号, vol. 15 , 203-209 (2016). (in Japanese); 木下郁雄, 北幸海, 立川仁典, 橘勝, 「カーボンナノウォールの電子状態と水素吸着」 J. Comput. Chem. Jpn.「量子水素の科学」特集号, vol. 15 , 177-183 (2016). (in Japanese); 宇田川太郎, 常田貴夫, 立川仁典, 「多成分密度汎関数のための電子-核相関汎関数の開発」 J. Comput. Chem. Jpn.「量子水素の科学」特集号, vol. 15 , 143-147 (2016). (in Japanese); 立川仁典, 「特集「量子水素の科学」に寄せて」 J. Comput. Chem. Jpn.「量子水素の科学」特集号, vol. 15 , A51 (2016). (in Japanese); 立川仁典, 北幸海, 小山田隆行, 「原子・分子の陽電子束縛機構と対消滅機構解明のための高精度第一原理計算 (Accurate ab initio calculation for the elucidation of the mechanism of positron binding and pair-annihilation in atoms and molecules)」陽電子科学, vol. 7 , 1-11 (2016). (in Japanese)
田中良和 ▲班員一覧に戻る▲: 【雑誌論文】; Z. Peng, M. Takeshita, N. Shibata, H. Tada, Y. Tanaka, *J. Kaneko, “Rim Domain Loops of Staphylococcal β-pore Forming Bi-component Toxin S-components 3 Recognize Target Human Erythrocytes in a Coordinated Manner,” J. Biochem., Accepted (2018), DOI: 10.1093/jb/mvy030.; *T. Uchida, T. Funamizu, M. Chen, Y. Tanaka, K. Ishimori, “Heme Binding to Porphobilinogen Deaminase from Vibrio cholerae Decelerates the Formation of 1-Hydroxymethylbilane,” ACS Chem. Biol., 13, 750-760, (2018), DOI: 10.1021/acschembio.7b00934; *S. Kato, T. Matsui, C. Gatsogiannis, *Y. Tanaka, “Molluscan Hemocyanin: Structure, Evolution, and Physiology”, Biophys. Rev., 10, 191-202 (2018), DOI: 10.1007/s12551-017-0349-4; M. Chen, S. Asai, S. Narai, S. Nambu, N. Omura, Y. Sakaguchi, T. Suzuki, M. Ikeda-Saito, K. Watanabe, M. Yao, *N. Shigi, Y. Tanaka, “Biochemical and Structural Characterization of Oxygen-sensitive 2-thiouridine Synthesis Catalyzed by the Iron-sulfur Protein TtuA”, Proc. Natl. Acad. Sci. USA, in press, (2017), DOI: 10.1073/pnas.1615585114; Y, Miyabe, T. Furuta, T. Takeda, G. Kanno, T. Shimizu, Y. Tanaka, Z. Gai, H. Yasui, *H. Kishimura, “Structural Properties of Phycoerythrin from Dulse Palmaria Palmate”, J. Food Biochem., 41, e12301, (2017), DOI: 10.1111/jfbc.12301; M. Chen, M. Kubo, K. Kato, Y. Tanaka, Y. Liu, F. Long, W. Whitman, P. Lill, C. Gatsogiannis, S. Raunser, N. Shimizu, A. Shinoda, A. Nakamura, I. Tanaka, *M. Yao, “Structural basis for tRNA-dependent cysteine biosynthesis”, Nature Commun., 8, 1512, (2017), DOI: 10.1038/s41467-017-01543-y.; T. Kunthic, H. Watanabe, R. Kawano, Y. Tanaka, B. Promdonkoy, M. Yao, *Boonserm, P., “pH Regulates Pore Formation of a Protease Activated Vip3Aa from Bacillus thuringiensis”, BBA Biomembranes, 1859, 2234-2241, (2017), DOI: 10.1016/j.bbamem.2017.08.018.; M. Chen, S. Narai, N. Omura, N. Shigi, S. Chimnaronk, *Y. Tanaka, M. Yao, “Crystallographic Study of Two-Thiouridine Synthetic Complex TtuA-TtuB from Thermus thermophiles”, Acta Crystallogr. F., 72, 777-781, (2016), DOI: 10.1107/S2053230X16014242; K. Oshima, Y, Kakiuchi, Y. Tanaka, T. Ueda, T. Nakashima, *M. Kimura, M. Yao, “Structural Basis for Recognition of a Kink-turn Motif by an Archaeal Homologue of Human RNase P Protein Rpp38”. Biochem. Biophys. Res. Commun., 474, 541-546, (2016), DOI: 10.1016/j.bbrc.2016.04.118; Y. Sekine, T. Tanzawa, Y. Tanaka, K. Ishimori, *T. Uchida, “Cytoplasmic Heme-binding Protein (HutX) from Vibrio cholerae is an Intracellular Heme Transport Protein for the Heme-degrading Enzyme, HutZ”, Biochemistry, 55, 884-893, (2016), DOI: 10.1021/acs.biochem.5b01273; Z.Gai, A. Matsuno, K. Kato, S. Kato, R.I.Khan, T. Shimizu, T. Yoshioka, Y. Kato, H. Kishimura, G. Kanno, Y, Miyabe, T. Terada, *Y. Tanaka, Y. Min, “Crystal Structure of the 3.8 MDa Respiratory Supermolecule Hemocyanin at 3.0 Angstrom Resolution”, Structure, 23, 2204-2212, (2015), DOI: 10.1016/j.str.2015.09.008; T. Sugawara, D. Yamashita,, K. Kato, Z. Peng, J. Ueda, J. Kaneko, Y, Kamio, Y. Tanaka, Min Yao, “Structural basis for pore-forming mechanism 1 of staphylococcal α-hemolysin”, Toxicon, 108, 226-231, (2015), DOI: 10.1016/j.toxicon.2015.09.033; T. Uchida, M. Sasaki, Y. Tanaka, K. Ishimori, “A dye-decolorizing peroxidase from Vibrio cholera”, Biochemistry, 54, 6610-6621, (2015), DOI: 10.1021/acs.biochem.5b00952; R.Sasaki, S.Kitazawa, R.Kitahara, H.Nakazawa, Y.Tanaka, I.Kumagai, M.Umetsu, *K.Makabe, “Zinc ion-binding activity of an anti-ZnO VHH antibody, 4F2”, Chem. Lett., 44, 1309-1311, (2015), DOI: 10.1246/cl.150537; 田中良和, “黄色ブドウ球菌の2成分性膜孔形成毒素γヘモリジンの膜孔形成メカニズム失敗から明らかになった毒素の戦略”, 化学と生物, 53, 136-137, (2015); 田中良和, “黄色ブドウ球菌が産生する膜孔形成毒素の作用機構”, Isotope News, 736, 7-11, (2015); A.Matsuno, Z.Gai, M. Taaka, K.Kato, S. Kato, T. Katoh, T. Shimizu, T.Yoshioka, H. Kishimura, Y.Tanaka, M. Yao, “Crystallization and Preliminary X-ray Crystallographic Study of a 3.8-MDa Respiratory Supermolecule Hemocyanin”, J. Struct. Biol., 190, 379-382, (2015), DOI: 10.1016/j.jsb.2015.04.015; S.Ito, S.Horikawa, T.Suzuki, H.Kawauchi, Y. Tanaka, T.Suzuki, T.Suzuki, “Human NAT10 is an ATP-dependent RNA Acetyltransferase Responsible for N4-acetylcytidine Formation in 18S rRNA.” J. Biol. Chem., 289, 35724-35730, (2014), DOI: 10.1074/jbc.C114.602698; T. Hayashi, *Y. Tanaka, N. Sakai, U. Okada, M. Yao, N. Watanabe, T. Tamura, I. Tanaka, “Structural and Genomic DNA Analysis of the Putative TetR Transcriptional Repressor SCO7518 from Streptomyces Coelicolor A3(2)”, FEBS Letters, 588, 4311-4318 (2014), DOI: 10.1016/j.febslet.2014.09.037; Y. Ushijima, R. Ohniwa, A. Maruyama, S. Saito, Y. Tanaka, K. Morikawa, “Nucleoid Compaction by MrgAAsp56Ala/Glu60Ala does not Contribute to Staphylococcal Cell Survival against Oxidative Stress and Phagocytic Killing by Macrophage”, FEMS Microbiol. Letters, 360, 144-151 (2014), DOI: 10.1111/1574-6968.12598; A. Shinoda, Y. Tanaka, M. Yao, I. Tanaka, “Anchoring Protein Crystals to Mounting Loops with Hydrogel Using Inkjet Technology”, Acta Cryst., D, 70, 2794-2799 (2014), DOI: 10.1107/S139900471401476X; D. Yamashita, T. Sugawara, M. Takeshita, J. Kaneko, Y. Kamio, I. Tanaka, *Y. Tanaka, M. Yao, “Molecular Basis of Transmembrane Beta-barrel Formation of Staphylococcal Pore-forming Toxins”, Nature Commun., 5, 4897 (2014), DOI: 10.1038/ncomms5897; T. Suzuki, K. Yamashita, Y. Tanaka, I. Tanaka, M. Yao, “Crystallization and Preliminary X-ray Crystallographic Analysis of a Bacterial Asn-transamidosome”, Acta Cryst. F, 70, 790-793 (2014), DOI: 10.1107/S2053230X14007274; 【図書】; 田中良和　Essential タンパク質科学第2章　タンパク質のドメイン，p59-94　南江堂（2016年）; Yamashita, D., Sugawara, T., Tanaka, I., Tanaka, Y., and Yao, M., Pore formation mechanism of staphylococcal pore forming toxin, PF activity report part A, 2014 Highlight, 46-47 (2015); 田中良和，陳明皓，姚閔，tRNAジヒドロウリジン合成酵素の分子機構生化学　86（3），395-399（2014）; 田中良和　環境と微生物の事典第6章　p135　人体環境での鉄の獲得　朝倉書店（2014）
寺嶋正秀 ▲班員一覧に戻る▲: 【雑誌論文】; Y. Nakasone, M. Ohshima, K. Okajima, S. Tokutomi, *M. Terazima, “Photoreaction Dynamics of LOV1 and LOV2 of Phototropin from Chlamydomonas Reinhardtii”, J.Phys.Chem.B, 122, 1801-1815, (2018), DOI: 10.1021/acs.jpcb.7b10266; A. Takakado, Y.Nakasone, *M. Terazima, “Sequential DNA Binding and Dimerization Processes of the Photosensory Protein EL222”, Biochemistry, 57,1603-1610, (2018), DOI: 10.1021/acs.biochem.7b01206; K. Shibata, Y. Nakasone, *M. Terazima, “Photoreaction of BlrP1: a Role of Nonlinear Photo-intensity Sensor”, Phys.Chem.Chem.Phys., 20, 8133-8142, (2018), DOI: 10.1039/c7cp08436f; *K. Iwata; *M. Terazima; *H. Masuhara , “Novel Physical Chemistry Approaches in Biophysical Researches with Advanced Application of Lasers: Detection and Manipulation”, Biochim.Biophys.Acta,(BBA), Gen. Subj., 1862, 335-357, (2018), DOI: 10.1016/j.bbagen.2017.11.003; S. Nozue, M. Katayama, M. Terazima, *S. Kumazaki, “Light-Induced Conformational Changes of the LOV2-Kinase and the Linker Region in Arabidopsis Phototropin2”, J. Phys. Chem. B, 121, 4414-4421, (2017), DOI: 10.1021/acs.jpcb.7b01552; S. Nozue, M. Katayama, M. Terazima, *S. Kumazaki, “Comparative study of thylakoid membranes in terminal heterocysts and vegetative cells from two cyanobacteria, Rivularia M-261 and Anabaena variabilis, by fluorescence and absorption spectral microscopy”, Biochim. Biophys. Acta, 1858, 742-749, (2017), DOI: 10.1016/j.bbabio.2017.05.007; A. Takakado, Y. Nakasone, *M. Terazima, “Photoinduced dimerization of a photosensory DNA-binding protein EL222 and its LOV domain”, Phys. Chem. Chem. Phys., 19, 24855-24865, (2017), DOI: 10.1039/c7cp03686h; M.Kondoh, *M. Terazima, “Conformational and Intermolecular Interaction Dynamics of Photolyase/Cryptochrome Proteins Monitored by the Time-resolved Diffusion Technique”, Photochem. Photobiol., 93, 15–25, (2017), DOI: 10.1111/php.12681; S. Nozue, A. Mukuno, Y. Tsuda, T. Shiina, M. Terazima, *S. Kumazaki,“Characterization of Thylakoid Membrane in Filamentous Cyanobacteria and Green Alga with Dual-detector Fluorescence Lifetime Imaging Microscopy with a Systematic Change of Incident Laser Power”, Biochim. Biophys. Acta., 1857, 46-59, (2016), DOI: 10.1016/j.bbabio.2015.10.003; K. Kuroi, F. Sato, Y. Nakasone, K. Zikihara, S. Tokutomi, *M. Terazima,“Time-Resolved Fluctuation during the Photochemical Reaction of a Photoreceptor Protein: Phototropin1LOV2-Linker”, Phys. Chem. Chem. Phys., 18, 6228-6238, (2016), DOI: 10.1039/c5cp07472j; T. Yoshitake, T. Toyooka, Y. Nakasone, K. Zikihara, S. Tokutomi, *M. Terazima, “Macromolecular Crowding Effect for Photoreactions of LOV2 Domains of Arabidopsis Thaliana Phototropin 1”, J. Mol.Liq., 217,43-50, (2016), DOI: 10.1016/j.molliq.2015.08.030; S. Choi,, Y. Nakasone, K. J Hellingwerf, *M. Terazima, “Photochemical Reactions of the LOV and the LOV-linker Domains of the Blue Light Sensor Protein YtvA”, Biochemistry, 55, 3107-3115, (2016), DOI: 10.1021/acs.biochem.6b00263; T. Nakajima, K.Kuroi, Y. Nakasone, K. Okajima, M. Ikeuchi, S. Tokutomi, *M. Terazima, “Anomalous Pressure Effects on the Photoreaction of a Light-sensor Protein from Synechocystis, PixD (Slr1694), and the Compressibility Change of its Intermediates”Phys. Chem. Chem. Phys., 18, 25915-25925, (2016), DOI: 10.1039/C6CP05091C; Y. Nakasone, H. Ooi, Y. Kamiya, H. Asanuma, *M. Terazima, “Dynamics of Inter-DNA Chain Interaction of Photoresponsive DNA”, J.Am.Chem.Soc.(Communication), 138, 9001-9004, (2016), DOI: 10.1021/jacs.6b02525; Y. Akiyama, Y. Nakasone, Y. Nakatani, O. Hisatomi, *M. Terazima, “Time-resolved Detection of Light-induced Dimerization of Monomeric Aureochrome-1 and Change in Affinity for DNA”, J. Phys. Chem.B, 120, 7360-7370, (2016), DOI: 10.1021/acs.jpcb.6b05760; S. Nozue, A. Mukuno, Y. Tsuda, T. Shiina, M. Terazima, *S. Kumazaki, “Characterization of Thylakoid Membrane in Filamentous Cyanobacteria and Green Alga with Dual-detector Fluorescence Lifetime Imaging Microscopy with a Systematic Change of Incident Laser Power”, Biochim.Biophys.Acta.,1857,46-59, (2016), DOI: 10.1016/j.bbabio.2015.10.003; K.Kuroi, F. Sato, Y. Nakasone, K. Zikihara, S. Tokutomi, * M. Terazima, ,“Time-Resolved Fluctuation during the Photochemical Reaction of a Photoreceptor Protein: Phototropin1LOV2-Linker”, Phys.Chem.Chem.Phys., 18, 6228-38, (2016), DOI: 10.1039/c5cp07472j.; K. Kuroi, K. Okajima, M. Ikeuchi, S. Tokutomi, T. Kamiyama, *M. Terazima, “Pressure-sensitive Reaction Yield of the TePixD Blue-light Sensor Protein”, J.Phys.Chem.B, 119, 2897-2907(2015), DOI: 10.1021/jp511946u; T. Miyamori, Y. Nakasone, K. Hitomi, J.M. Christie, E. D. Getzoff, M.Terazima, “Reaction dynamics of the UV-B photosensor UVR8”,　Photochem.Photobiol.Sci.,14, 995 – 1004, (2015), DOI: 10.1039/c5pp00012b; M. Terazima, “Photo-induced inter-protein interaction changes in the time domain; a blue　light sensor protein PixD”, Rapid Comm. Photosci., 4, 1-8 (2015), ISSN 2288-4564; *M.Nishiyama, Y.Shimoda, Y.Kimura, M. Terazima, M. Homma, S.Kojima, “Pressure-Speed Relationship of the Sodium-Driven Flagellar Motor of Vibrio Alginolyticus”, Biophys.J.,106, 578A-578A, (2014), DOI: 10.1016/j.bpj.2013.11.3206; Y. Nakasone, Y. Kawaguchi, S-G. Kong, M. Wada, *M. Terazima, "Photo-Induced Oligomerization of Arabidopsis Thaliana Phototropin 2 LOV1”, J.Phys.Chem.B,118, 14314-14325, （2014）, DOI: 10.1021/jp509448b; K. Kuroi, K. Okajima, M.Ikeuchi, S. Tokutomi, *M. Terazima, "TransientConformational Fluctuation of TePixD During a Reaction", Proc.Natl. Acad.Sci. USA,111, 14764-14769, （2014）, DOI: 10.1073/pnas.1413222111; K. Kuroi, K. Tanaka, K. Okajima, M. Ikeuchi, S. Tokutomi, *M. Terazima, “Anomalous Diffusion of TePixD and Identification of the Photoreaction Product”, Photochem. Photobiol. Sci., 12, 1180-1186, (2013), DOI: 10.1039/C3PP25434H; Y. Nakasone, K. Zikihara, S. Tokutomi, *M. Terazima, “Photochemistry of Arabidopsis Phototropin 1 LOV1: Transient Tetramerization”, Photochem. Photobiol. Sci., 12(7), 1171-1179, (2013), DOI: 10.1039/c3pp50047k; *M. Nishiyama, Y. Sowa, Y. Kimura, M. Homma, A. Ishijima, M. Terazima, “High Hydrostatic Pressure Induces Counterclockwise to Clockwise Reversals of the Escherichia coli Flagellar Motor”, J. Bacteriol. 195(8), 1809-1814, (2013), DOI: 10.1128/JB.02139-12; K. Suda, M. Terazima, *Y. Kimura, “Anomalous Ground-state Proton Transfer of 4'-N,N-diethylamino-3-hydroxyflavone in Ionic Liquids of Imidazolium-based Cations with Tetrafluoroborate”, Chem. Commun., 49(38), 3976-3978, (2013), DOI: 10.1039/c3cc40943k; K. Suda, M. Terazima, H. Sato, *Y. Kimura, “Excitation Wavelength Dependence of Excited State Intramolecular Proton Transfer Reaction of 4′-N,N-Diethylamino-3-hydroxyflavone in Room Temperature Ionic Liquids Studied by Optical Kerr Gate Fluorescence Measurement”, J. Phys. Chem. B, 117(41), 12567-12582, (2013), DOI: 10.1021/jp405537c; K. Takeda, Y. Nakasone, K. Zikihara, S. Tokutomi, *M. Terazima, “Dynamics of the Amino-Terminal and Carboxyl-Terminal Helices of Arabidopsis Phototropin 1 LOV2 Studied by the Transient Grating”, J. Phys. Chem. B, 117(49), 15606-15613, (2013), DOI: 10.1021/jp406109j; 【図書】; 黒井邦巧、寺嶋正秀「圧力印加過渡回折格子法による反応中のタンパク質圧縮率の時間分解計測」熱測定, 43, 66-71(2016); 寺嶋正秀「分子基盤に基づく生体機能ネットワークとダイナミクス」国際高等研究所アニュアルレポート2015, (2016); 中曽根祐介，寺嶋正秀「青色光センサータンパク質フォトトロピンの光制御機構」物性科学センター誌, 29,3-11(2016); 寺嶋正秀　(分担執筆)「過渡回折格子法」光と生命の事典、356-357, 2016, 朝倉書店 ISBN978-4-254-17161-7; M. Terazima, Time-Resolved Detection of Protein Fluctuations During Reactions, Molecular Science of Fluctuations Toward Biological Functions, Eds., M. Terazima, M. Kataoka, R. Ueoka, 1-28, Springer, ISBN 978-4-431-55840-8 (2016); 寺嶋正秀「時間分解熱力学量で見るタンパク質揺らぎと反応」パリティ, vol.30,No.08, 52-55(2015); 黒井邦巧、寺嶋正秀「タンパク質反応と揺らぎ」生物物理学会誌、55, 235-241(2015).; 寺嶋正秀「タンパク質の揺らぎが生体反応を決める」現代化学,534, 42-46(2015); 寺嶋正秀、馬場正昭、松本吉泰　共著「現代物理化学」2015年　化学同人　ISBN978-4-7598-1809-3; 寺嶋正秀　(分担執筆), “蛍光蛋白質”, 光化学の事典, 光化学協会光化学の事典編集委員会編, 朝倉書店, 2014; 寺嶋正秀, “揺らぎから観た生体分子科学”, Molecular Science, 7, (2013); 寺嶋正秀, “揺らぎ・ダイナミクスと生体機能: 物理化学的視点から見た生体分子” (DOJIN BIOSCIENCE SERIES) 第1章「揺らぎと生体反応概論」,(2013), 寺嶋正秀編,（化学同人,京都）ISBN:9784759815108; 寺嶋正秀, “揺らぎ・ダイナミクスと生体機能: 物理化学的視点から見た生体分子” (DOJIN BIOSCIENCE SERIES) 第2章「分光法」,(2013), 寺嶋正秀編,（化学同人,京都）ISBN:9784759815108; 寺嶋正秀, “揺らぎ・ダイナミクスと生体機能: 物理化学的視点から見た生体分子” (DOJIN BIOSCIENCE SERIES)第10章「新しい時間分解測定：拡散係数と熱力学量」, (2013), 寺嶋正秀編,（化学同人,京都）ISBN:9784759815108
内藤晶 ▲班員一覧に戻る▲: 【雑誌論文】; A. Naito, K. Okushita, K. Nishimura, G. B. Boutis, A. Aoki, *T. Asakura, “Quantitative Analysis of Solid-state Homonuclear Correlation Spectra of Antiparallel b-sheet Alanine Tetramers,” J. Phys. Chem. Chem. B, in press, DOI: 10.1021/acs.jpcb/b11126; B. Mijiddorj, S. Kaneda, H. Sato, Y. Kitahashi, N. Javkhlantugs, A. Naito, K. Ueda, *I. Kawamura“The role of D-allo-isoleucine in the deposition of the anti-Leishmania peptide bombinin H4 as revealed by 31P solid-state NMR, VCD spectroscopy, and MD simulation,” BBA-Proteins and Proteomics, in press, 10.1016/j.bbapap.2018.01.005; *A. Naito, N. Matsumori, A. Ramamoorthy, “Dynamic Membrane Interactions of Antibacterial and Antifungal Biomolecules, and Amyloid Peptides, Revealed by Solid-state NMR Spectroscopy”. Biochim. Biophys. Acta, (BBA), 1862, 307-323, (2018), DOI: 10.1016/j.bbagen.2017.06.004; 上田和義, *内藤晶, 川村出, “生体幕内でのペプチドの挙動の分子動力学シミュレーション,” 酵素工学ニュース, 79, 27-30, (2018); *内藤晶“固体高分解能NMRスペクトルに現れる異方性相互作用 –Narrrow is beautifull-,” 分光研究 67, 13-15, (2018); *T. Asakura, A. Nishimura, S. Kametani, S. Kawanishi, A. Aoki, F. Suzuki, H. Kaji, A. Naito. “Refined crystal structure of Samia Cynthia Silk Fibroin revealed by solid-state NMR investigations”. Biomacromolecules 18, 1965-1974 (2017). DOI: 10.1021/acs.biomac.7b00441; A. Naito, Y. Tasei, A. Nishimura, *T. Asakura. “Packing Arrangements and Intershet Interaction of Alanine Oligopeptides as Revealed by Relaxation Parameters Obtained from High-resolution ¹³C solid-state NMR”. J. Phys. Chem. B, 121(38), 8946-8955, (2017), DOI: 10.1021/acs.jpcb.7b07068; K. Kamgar-Parsi, L. Hong, A. Naito, C.L. Brooks III, *A. Ramamoorthy. “Growth-incompetent monomers of human calcitonin lead to a noncanonical direct relationship between peptide concentration and aggregation lag time”. J. Biol. Chem. 292, 14963-14976 (2017). DOI: 10.1074/jbc.M117.791236; K. Norisada, N. Javkhlantugs, D. Mishima, I. Kawamura, H. saito, K. Ueda, *A. Naito, “Dynamic Structure and Orientation of Melittin Bound to Acidic Lipid Bilayers, as Revealed by Solid-state NMR and Molecular Dynamic Simulation”, J. Phys. Chem. B. 121, 1802-1811, (2017), DOI: 10.1021/acs.jpcb.6b11207; *T. Asakura, K. Miyazawa, Y. Tasei, S. Kametani, Y. Nakazawa, A. Aoki, A. Naito, “Packing Arrangement of ¹³C selectively Labeled Sequence Model Peptides of Samia Cynthia Ricini Silk Fibroin Fiber Studied by Solid-state NMR,” Phys. Chem. Chem. Phys., 19, 13379-13386 (2017), DOI: 10.1039/C7CP01199G; T. Asakura, K. Horiguchi, A. Aoki, Y. Tasei, A. Naito, “Parallel β-sheet Structure of Alanine Tetrapeptide in the Solid State as Studied by Solid-state NMR Spectroscopy”, J. Phys. Chem B., 120, 8912-8941, (2016), DOI: 10.1021/acs.jpcb.6b06292; K. Kamgar-Parsi, J. Tolchard, B. Habenstein, A. Loquest, A. Naito, *A. Ramamoorthy, “Structural Biology of Calcitonin: from Aqueous Therapeutic Properties to Amyloid Aggregation,” Isr. J. Chem., 57, 634-650 (2016), DOI: 10.1002/ijch.201600096; *H. Yoshitake, T. Kodate, T.Takagi, I. Kawamura, A. Naito“Polysilsesquioxanes with Mixed Self-assembled Organic Tethers: Alkyl Chains and Alkanoate-aminopropyl Pairs.” React.Funct.Plym., 99, 9-16 (2016). DOI: 10.1016/j.reactfunctpolym.2015.12.002; T. Nagao, D. Mishima, N. Javkahlantugs, J. Wang, D. Ishioka, K. Yokota, K. Norisada, I. Kawamura, K. Ueda, *A. Naito, “Structure and Orientation of Antibiotic Peptide Alamethicin in Phospholipid Bilayers as Revealed by Chemical Shift Oscillation Analysis of Solid State Nuclear Magnetic Resonance and Molecular Dynamics Simulation”, Biochim. Biophys. Acta, 1848, 2789-2798, (2015), DOI: 10.1016/j.bbamem.2015.07.019; K. Oshima, A. Shigeta, Y. Makino, *I. Kawamura, T. Okitsu, A. Wada, S. Tuzi, T. Iwasa, *A. Naito, “Characterization of Photo-intermediates in the Photo-reaction Pathways of a Bacteriorhodopsin Y185F Mutant Using in Situ Photo-irradiation Solid-state NMR Spectroscopy”, Photoche. Photobiol. Sci. 14, 1694-1702, (2015), DOI: 10.1039/c5pp00154d; Y. Tasei, T. Yamakami, I. Kawamura, T. Fujito, K. Ushida, M. Sato, *A. Naito, “Mechanism for Microwave Heating of 1-(4’-cyanophenyl)-4-propylcyclohexane Characterized by in Situ Microwave Irradiation NMR Spectroscopy”, J. Magn. Reson., 254, 27-34, (2015), DOI: 10.1016/j.jmr.2015.02.002; Y. Tasei, F. Tanigawa, I. Kawamura, T. Fujito, M. Sato, *A. Naito, “The Microwave Heating Mechanism of N-(4-methoxybenzyliden)-4-butylaniline in Liquid Crystalline and Isotropic Phases as Determined Using in Situ Microwave Irradiation NMR Spectroscopy”, Phys. Chem. Chem. Phys. 17, 9082-9089 (2015), DOI: 10.1039/c5cp00476d; H. Yomoda, Y. Makino, Y. Tomonaga, T. Hidaka, *I. Kawamura, T. Okitsu, A. Wada, *Y. Sudo, *A. Naito, “Color-Discriminating Retinal Configurations of Sensory Rhodopsin I by Photo-Irradiation Solid-State NMR Spectroscopy”, Angew. Chem. Int. Ed. 53, 6960-6964 (2014), DOI: 10.1002/anie.201309258; A. Kira, N. Javkhlantugs, T. Miyamori, Y. Sasaki, M. Eguchi, I. Kawamura, K. Ueda, *A. Naito, “Interaction of Extracellular Loop II of k-Opioid Receptor (196-228) with Opioid Peptide Dynorphin in Membrane Environments as Revealed by Solid State Nuclear Magnetic Resonance, Quartz Crystal Microbalance and Molecular Dynamics Simulation”, J. Phys. Chem. B, 118, 9604-9612, (2014), DOI: 10.1021/jp505412j; 【図書】; *I. Kawamura, K. Norisada, A. Naito. "Structure determination of membrane peptides and proteins by solid-state NMR. Expefrimental approaches of NMR spectroscopy. Methodology and application of life science and materials science." The NMR Society of Japan. Ed. Springer in press (2017). DOI: 10.1007/978-981-10-5966-7_9; *A. Naito, Y. Makino, I. Kawamura, “In-situ Photo Irradiation Solid-state NMR Spectroscopy Applied to Retinal-binding Membrane Protein,” Mod. Magn. Reson. Webb ed. Springer (2017) in press, DOI: 10.1007/978-3-319-28275-6_51-1; *A. Naito, Y. Makino, Y. Tasei, I. Kawamura, “Photoirradiation and Microwave Irradiation NMR Spectroscopy,” Experimental Approaches of NMR Spectroscopy –Methodology and Application of Life Science and Material Science-. The NMR Society of Japan ed. Springer (2017) in press. DOI: 10.1007/978-981-10-5966-7_5; *内藤　晶, 固体高分解能NMR(Narrow is beautiful)の構造生命化学研究への展開　NMR (Bulletin of the nuclear magnetic society of japan) 日本核磁気共鳴学会　Vol. 7, pp 8-10, 2016年11月; 内藤　晶、“光と生命の事典”第５章「光による生命現象の計測」、第１７６節「ＮＭＲ分光法」、（２０１６）、日本光生物学協会　編　（朝倉書店）. ISBN: 978-4-254-17161-7 c3545; A.Naito, I. Kawamura, N. Javkhlantugs, “Recent solid-atate NMR studies of membrane-bound peptides and proteins.” Annu. Rep. NMR Spectrosc., Graham A. Webb, ed. Academic Press Vol 86, pp 333-411, 2015. DOI: 10.1016/bs.arnmr.2015.06.001; 内藤　晶, ”最新マイクロ波エネルギーと応用技術” 第1章「マイクロ波の基礎」, 第3節「電磁場相互作用のNMRによる研究」,（2014), 吉川　昇　編（産業技術サービスセンター）, ISBN:978-4-915957-94-9 C3053; A. Naito, I. Kawamura, “Photoactivated Structural Changes in Photoreceptor Membrane Proteins as Revealed by in situ Photoirradiation Solid-State NMR Spectroscopy,” Chapter 20 in “Advances in Biological Solid-State NMR”, (2014), Eds. F. Separovic, A. Naito, (Royal Society of Chemistry, UK), ISBN: 978-1-84973-910-8.
東雅大 ▲班員一覧に戻る▲: 【雑誌論文】; *N. Yoshida, *M. Higashi, H. Motoki, S. Hirota, “Theoretical Analysis of the Domain-swapped Dimerization of Cytochrome c: An MD and 3D-RISM Approach,” J. Chem. Phys., 148, 025102,(7 pages) (2018), DOI: 10.1063/1.5009785; 根木秀佳, 吉田紀生, 廣田俊, 東雅大, “シトクロムcの多量体形成に関する理論的研究,”, J. Comput. Chem. Jpn., 17, 8-13, (2018), DOI: 10.2477/jccj.2018-0006; H. Tsukamoto, M. Higashi, H. Motoki, H. Watanabe, C. Ganser, K. Nakajo, Y. Kubo, T. Uchihashi, *Y. Furutani, “Structural Properties Determining Low K⁺ affinity of the Selectivity Filter in the TWIK1 K⁺ Channel,” J. Biol. Chem., in press, DOI: 10.1074/jbc.RA118.001817; *H. Okumura, M. Higashi, Y. Yoshida, H. Sato, R. Akiyama, "Theoretical Approaches for Dynamical Ordering of Biomolecular Systems" Biochim. Biophys. Acta, (BBA), 1862, 212-228, (2018), DOI: 10.1016/j.bbagen.2017.10.001; *S. Arimitsu, T. Yonamine, *M. Higashi, "Cinchona-Based Primary Amine Catalyzed a Proximal Functionalization of Dienamines: Asymmetric α_Fluorination of α_Branched Enals," ACS Catal. 7, 4736 (2017) DOI: 10.1021/acscatal.7b01178; P. Ahmadi, M. Higashi, N. J. de Voogd, *Junichi Tanaka, "Two Furanosesterterpenoids from the Sponge Luffariella variabilis," Mar. Drugs. 15, 249 (2017) DOI: 10.3390/md15080249; I. Hermawan, A. Furuta, M. Higashi, Y. Fujita, N. Akimitsu, A. Yamashita, K. Moriishi, S. Tsuneda, H. Tani, M. Nakakoshi, M. Tsubuki, Y. Sekiguchi, *N. Noda, *J. Tanaka, “Four Aromatic Sulfates with an Inhibitory Effect against HCV NS3 Helicase from the Crinoid Alloeocomatella polycladia,” Mar. Drugs 15, 117, (2017), DOI: 10.3390/md15040117; A. Agena, S. Iuchi, M. Higashi, “Theoretical Study on Photoexcitation Dynamics of a Bis-diimine Cu(I) Complex in Solutions,” Chem. Phys. Lett., 679, 60-65, DOI: 10.1016/j.cplett.2017.04.082 (cover illustration); S. Tanimoto, *M. Higashi, *N. Yoshida, H. Nakano, “The Ion-dependence of Carbohydrate Binding of CBM36: MD and 3D-RISM Study,” J. Phys., Condens. Matter, 28, 344005, (2016), DOI: 10.1088/0953-8984/28/34/344005; K. Watanabe, *N. Nakatani, A. Nakayama, M. Higashi, *J. Hasegawa, “Spin-blocking Effect in CO and H2 Binding Reactions to Molybdenocene and Tungstenocene: A theoretical Study on the Reaction Mechanism via Minimum Energy Intersystem-crossing Point,” Inorg. Chem. 55, 8082-8090, (2016), DOI: 10.1021/acs.inorgchem.6b01187; *M. Higashi, *S. Saito, “Quantitative Evaluation of Site Energies and their Fluctuations of Pigments in the Fenna–Matthews–Olson Complex with an Efficient Method for Generating a Potential Energy Surface,” J. Chem. Theory Comput. 12, 4128-4137, (2016), DOI: 10.1021/acs.jctc.6b00516; Y. Toma, M. Kunigami, K. Watanabe, *M. Higashi, *S. Arimitsu, “One-pot Synthesis and Theoretical Calculation for Trifluoromethylated Pyrrolizidines by 1,3-dipolar Cycloaddition with Azomethine Ylides and β-trifluoromethyl Acrylamides,” J. Fluor. Chem. 22, 189, (2016), DOI: 10.1016/j.jfluchem.2016.07.013
松村浩由 ▲班員一覧に戻る▲: 【雑誌論文】; K. Nii, *M. Maruyama, S. Okada, H. Adachi, K. Takano, S. Murakami, H. Y. Yoshikawa, H. Matsumura, T. Inoue, M. Imanishi, K. Tsukamoto, M. Yoshimura, Y. Mori, “Improvement of Metastable Crystal of Acetaminophen via Control of Crystal Growth Rate,” Appl. Phys. Express., 11, 035501, (2018) DOI: 10.7567/APEX.11.035501; D. Murata, H. Okano, C. Angkawidjaja, M. Akutsu, S-i. Tanaka, K. Kitahara, T. Yoshizawa, H. Matsumura, Y. Kado, E. Mizohata, T. Inoue, S. Sano, Y. Koga, S. Kanaya, K. Takano “Structural basis for the Serratia marcescens lipase secretion system: Crystal structures of the membrane fusion protein and nucleotide-binding domain”, Biochemistry, 56, 6281-6291 (2017) DOI: 10.1021/acs.biochem.7b00985; J. Fujita, Y. Maeda, E. Mizohata, T. Inoue, M. Kaul, A. K. Parhi, E. J. LaVoie, D. S. Pilch*, H. Matsumura* “Structural flexibility of an inhibitor overcomes drug resistance mutations in Staphylococcus aureus FtsZ”, ACS Chem. Biol., 12(7), 1947-1955 (2017) DOI: 10.1021/acschembio.7b00323; H. Kajiura, N. Suzuki, Y. Tokumoto, T. Yoshizawa, S. Takeno, K. Fujiyama, Y. Kaneko, H. Matsumura, Y. Nakazawa “Two Eucommia farnesyl diphosphate synthases exhibit distinct enzymatic properties leading to end product preferences”, Biochimie, 139, 95-106 (2017) DOI: 10.1016/j.biochi.2017.05.001; J. Fujita, *R. Harada, Y. Maeda, Y. Saito, E. Mizohata, T. Inoue, Y. Shigeta, *H. Matsumura, “Identification of the Key Interactions in Structural Transition Pathway of FtsZ from Staphylococcus aureus”, J. Struct. Biol., 198, 65-73 (2017) DOI: 10.1016/j.jsb.2017.04.008; T. Kono, S. Mehrotra, C. Endo, N. Kizu, M. Matsuda, H. Kimura, E. Mizohata, T. Inoue, T. Hasunuma, A. Yokota, *H. Matsumura, *H. Ashida, “A RuBisCO-mediated Carbon Metabolic Pathway in Methanogenic Archaea”, Nature Commun., 8(14007), 1-12 (2017), DOI: 10.1038/ncomms14007; *T. Sato, T. Kawasaki, S. Mine, H. Matsumura, “Functional role of the C-terminal Amphipathic Helix 8 of Olfactory Receptors and Other G Protein-coupled Receptors”, Int. J. Mol. Sci., 17(11), 1930, (2016), DOI: 10.3390/ijms17111930; Y. Tominaga, M. Maruyama, M. Yoshimura, H. Koizumi, M. Tachibana, S. Sugiyama, H. Adachi, K. Tsukamoto, H. Matsumura, K. Takano, S. Murakami, T. Inoue, *H. Y. Yoshikawa, Y. Mori“Promotion of Protein Crystal Growth by Actively Switching Crystal Growth Mode via Femtosecond Laser Ablation”, Nature Photonics, 10, 723-726, (2016), DOI: 10.1038/nphoton.2016.202; *M. Maruyama, Y. Hayashi, H. Y. Yoshikawa, S. Okada, H. Koizumi, M. Tachibana, S. Sugiyama, H. Adachi, H. Matsumura, T. Inoue, K. Takano, S. Murakami, M. Yoshimura, Y. Mori,“A Crystallization Technique for Obtaining Large Protein Crystals with Increased Mechanical Stability Using Agarose Gel Combined with a Stirring Technique”, J. Crystal Growth, 452, 172-178, (2016), DOI: 10.1016/j.jcrysgro.2015.11.008; S. Sugiyama, S. Ishikawa, H. Tomitori, M. Niiyama, M. Hirose, Y. Miyazaki, K. Higashi, M. Murata, H. Adachi, K. Takano, S. Murakami, T. Inoue, Y. Mori, K. Kashiwagi, K. Igarashi, *H. Matsumura, “　 Molecular Mechanism Underlying Promiscuous Polyamine Recognition by Spermidine Acetyltransferase”, Int. J. Biochem. Cell Biol., 76, 87-97, (2016), DOI: 10.1016/j.biocel.2016.05.003; *T. Sato, R. Kobayakawa, K. Kobayakawa, M. Emura, S. Itohara, T. Kawasaki, A. Tsuboi, H. Matsumura, ”Supersensitive Odor Discrimination is Controlled in Part by Initial Transient Interactions between the Most Sensitive Dorsal Olfactory Receptors and G-proteins” Receptors Clin. Invest., 3, e1117, (2016), DOI: 10.14800/rci.1117; M. Matsuoka, K. Kakinouchi, H. Adachi, M. Maruyama, S. Sugiyama, I. Nakabayashi, H. Tsuchikura, A. Kuwahara, S. Sano, H. Y. Yoshikawa, Y. Takahashi, M. Yoshimura, H. Matsumura, S. Murakami, T. Inoue, Y. Mori, *K Takano ”Growth of High-strength Protein Crystals with Nanofibers” Appl. Phys. Express, 9, 035503, (2016), DOI: 10.7567/APEX.9.035503; Y. Kado, E. Mizohata, S. Nagatoishi, M. Iijima, K. Shinoda, T. Miyafusa, T. Nakayama, T. Yoshizumi, A. Sugiyama, T. Kawamura, Y-H Lee, H. Matsumura, H. Doi, H. Fujitani, T. Kodama, Y. Shibasaki, K. Tsumoto, *T. Inoue, “Epiregulin Recognition Mechanisms by Anti-epiregulin Antibody 9E5: Structural, Functional and Molecular Dynamics Simulation Analyses” J. Biol. Chem., 291, 2319-2330, (2016), DOI: 10.1074/jbc.M115.656009; Y. Fukuda , K. M. Tse , M. Suzuki, K. Diederichs, K. Hirata, T. Nakane, M. Sugahara, E. Nango, K. Tono, Y. Joti, T. Kameshima, C. Song, T. Hatsui, M. Yabashi, O. Nureki, H. Matsumura, T. Inoue, S. Iwata, *E. Mizohata, “Redox-coupled Structural Changes in Nitrite Reductase Revealed by Serial Femtosecond and Microfocus Crystallography” J. Biochem., in press, (2016), DOI: 10.1093/jb/mvv133; Y. Fukuda, K. M. Tse, Y. Kado, E. Mizohata, H. Matsumura, *T. Inoue “Insights into Unknown Foreign Ligand in Copper Nitrite Reductase” Biochem. Biophys. Res. Commun., 464, 622, (2015), DOI: 10.1016/j.bbrc.2015.07.025; A. Fujii, Y. Sekiguchi, *H. Matsumura, T. Inoue, *W-S. Chung, S. Hirota, *T. Matsuo “ Excimer Emission Properties on Pyrene-labeled Protein Surface: Correlation between Emission Spectra, Ring Stacking Modes, and Flexibilities of Pyrene Probes”, Bioconjugate Chem., 26, 537, (2015), DOI: 10.1021/acs.bioconjchem.5b00026; T. Kawasaki, T. Saka, S. Mine, E. Mizohata, T. Inoue, *H. Matsumura, T. Sato “The N-terminal Acidic Residue of the Cytosolic Helix 8 of an Odorant Receptor is Responsible for Different Response Dynamics via G-protein”, FEBS Lett., 589, 1136, (2015), DOI: 10.1016/j.febslet.2015.03.025; R.N. Abd Rahman, M.S. Ali, S. Sugiyama, A.T. Leow, T. Inoue, M. Basri, A.B. Salleh, *H. Matsumura, “A Comparative Analysis of Microgravity and Earth Grown Thermostable T1 Lipase Crystals using HDPCG Apparatus”, Protein Pept. Lett., 22, 173, (2015), DOI: 10.2174/0929866521666141019193604; *N. Maruyama, T. Goshi, S. Sugiyama, M. Niiyama, H. Adachi, K. Takano, S. Murakami, T. Inoue, Y. Mori, H. Matsumura, B. Mikami “ Preliminary X-ray Analysis of the Binding Domain of the Soybean Vacuolar Sorting Receptor Complexed with a Sorting Determinant of a Seed Storage Protein”, Acta Cryst., F71, 132, (2015), DOI: 10.1107/S2053230X14027484; K. Ishibashi, Y. Kezuka, C. Kobayashi, M. Kato, T. Inoue, T. Nonaka, M. Ishikawa, *H. Matsumura, *Etsuko Katoh , “ Structural Basis for the Recognition-evasion Arms Race between Tomato Mosaic Virus and the Resistance Gene Tm-1”, Proc. Natl. Acad. Sci. USA, 111, E3486, (2014), DOI: 10.1073/pnas.1407888111; J. Fujita, Y. Maeda, C. Nagao, Y. Tsuchiya, Y. Miyazaki, M. Hirose, E. Mizohata, Y. Matsumoto, T. Inoue, K. Mizuguchi, *H. Matsumura, ”Crystal Structure of FtsA from Staphylococcus Aureus” FEBS Lett., 588(10), 1879-1885, (2014), DOI: 10.1016/j.febslet.2014.04.008
松森信明 ▲班員一覧に戻る▲: 【雑誌論文】; Y. Wakamiya, M. Ebine, M. Murayama, H. Omizu, N. Matsumori, M. Murata, *T. Oishi, “Synthesis and Stereochemical Revision of the C31-C67 Section of Amphidinol 3” Angew. Chem. Int. Ed. Engl., (2018), in press, DOI: 10.1002/anie.201712167; T. Watanabe, H. Shibata, M. Ebine, H. Tsuchikawa, N. Matsumori, M. Murata, M. Yoshida, M. Morisawa, S. Lin, K. Yamauchi, K. Sakai, *T. Oishi, “Synthesis and Complete Structure Determination of a Sperm-Activating and -Attracting Factor Isolated from the Ascidian Ascidia sydneiensis.” J. Nat. Prod., (2018), in press, DOI: 10.1021/acs.jnatprod.7b01052; T. Matsufuji, M. Kinoshita, A. Möuts, J. P. Slotte, *N. Matsumori, “Preparation and Membrane Properties of Oxidized Ceramide Derivatives”, Langmuir, 34, 465-471, (2018), DOI: 10.1021/acs.langmuir.7b02654; *A. Naito, N. Matsumori, A. Ramamoorthy, “Dynamic Membrane Interactions of Antibacterial and Antifungal Biomolecules, and Amyloid Peptides, Revealed by Solid-state NMR Spectroscopy.” Biochim. Biophys. Acta., 1862, 307-323, (2018), DOI: 10.1016/j.bbagen.2017.06.004; Y. Umegawa, N. Matsumori, *M Murata, “Recent Solid-State NMR Studies of Hydrated Lipid Membranes”, Annual Reports on NMR Spectroscopy, 94, 41-72, (2018), DOI: 10.1016/bs.arnmr.2017.12.003; M. Kinoshita, H. Ano, M. Murata, K. Shigetomi, J. Ikenouchi, *N. Matsumori, “Emphatic Visualization of Sphingomyelin-rich Domains by Inter-lipid FRET Imaging Using Fluorescent Sphingomyelins.” Sci. Rep., 7, 16801, (2017), DOI: 10.1038/s41598-017-16361-x; *R. Ohtani, T. Tokita, T. Takaya, *K. Iwata, M. Kinoshita, N. Matsumori, M. Nakamura, L. F. Lindoy, *S. Hayami, “The Impact of Metal Complex Lipids on Viscosity and Curvature of Hybrid Liposomes.” Chem. Commun., 53, 13249-13252, (2017), DOI: 10.1039/c7cc07944c; M. Iwamoto, A. Sumino, E. Shimada, M. Kinoshita, N. Matsumori, *S. Oiki, “Channel Formation and Membrane Deformation via Sterol-Aided Polymorphism of Amphidinol 3” Sci. Rep., 7, 10782, (2017), DOI: 10.1038/s41598-017-11135-x.; *M. Satake, K. Cornelio, S. Hanashima, R. Malabed, M. Murata, N. Matsumori, H. Zhang, F. Hayashi, S. Mori, J.S. Kim, C.H. Kim, J.S. Lee, “Structures of the Largest Amphidinol Homologues from the Dinoflagellate Amphidinium carterae and Structure-Activity Relationships.” J. Nat. Prod., 80, 2883-2888, (2017), DOI: 10.1021/acs.jnatprod.7b00345. Epub 2017 Nov 9; 松森信明「脂質ラフトのNMR解析」, 日本核磁気共鳴学会機関紙 8, 9-16 (2017); M. Kinoshita, K.G.N. Suzuki, *N. Matsumori, M. Takada, H. Ano, K. Morigaki, M. Abe, A. Makino, T. Kobayashi, K.M. Hirosawa, T. K Fujiwara, *A. Kusumi, M. Murata, “Raft-based Sphingomyelin Interactions Revealed by New Fluorescent Sphingomyelin Analogs” J Cell Biol., 216, 1183, (2017), DOI: 10.1083/jcb.201607086; T. Nakane, S. Hanashima, M. Suzuki, H. Saiki, T. Hayashi, K. Kakinouchi, S. Sugiyama, S. Kawatake, S. Matsuoka, N. Matsumori, E. Nango, J. Kobayashi, T. Shimamura, K. Kimura, C. Mori, N.Kunishima, M. Sugahara, Y. Takakyu, S. Inoue, T. Masuda, T. Hosaka, K. Tono, Y. Joti, T. Kameshima, T. Hatsui, M. Yabashi, T. Inoue, O. Nureki, S. Iwata, *M. Murata, *E. Mizohata, “Membrane Protein Structure Determination by SAD, SIR, or SIRAS Phasing in Serial Femtosecond Crystallography Using an Iododetergent” Proc. Natl. Acad. Sci. USA, 113, 13039, (2016), DOI: 10.1073/pnas.1602531113; K. Cornelio, R.A. Espiritu, Y. Todokoro, S. Hanashima, M. Kinoshita, N. Matsumori, *M. Murata, S. Nishimura, H. Kakeya, M. Yoshida, S. Matsunaga, “Sterol-dependent Membrane Association of the Marine Sponge-derived Bicyclic Peptide Theonellamide A as Examined by 1H NMR” Bioorg. Med. Chem., 24, 5235, (2016), DOI: 10.1016/j.bmc.2016.08.043; R.A. Espiritu, K. Cornelio, M. Kinoshita, *N. Matsumori, M. Murata, S. Nishimura, H. Kakeya, M. Yoshida, S. Matsunaga,“Marine Sponge Cyclic Peptide Theonellamide A Disrupts Lipid Bilayer Integrity without Forming Distinct Membrane Pores” Biochim Biophys Acta Biomembranes, 1858, 1373, (2016), DOI: 10.1016/j.bbamem.2016.03.019; Y. Nakagawa, Y. Umegawa, N. Matsushita, T. Yamamoto, H. Tsuchikawa, S. Hanashima, T. Oishi, *N. Matsumori, *M. Murata, “The Structure of the Bimolecular Complex between Amphotericin B and Ergosterol in Membranes is Stabilized by Face-to-face Van Der Waals Interaction with their Rigid Cyclic Cores” Biochemistry 55, 3392, (2016), DOI: 10.1021/acs.biochem.6b00193; O. Engberg, T. Yasuda, V. Hautala, N. Matsumori, T.K.M. Nyholm, *M. Murata, *J. P. Slotte,“Lipid interactions and organization in complex bilayer Membranes” Biophys J, 110, 1563, (2016), DOI: 10.1016/j.bpj.2015.12.043; Y. Umegawa, Y. Tanaka, N. Matsumori, *M. Murata, “¹³C-TmDOTA as Versatile Thermometer Compound for Solid-state NMR of Hydrated Lipid Bilayer Membranes”, Magn Reson Chem., 54, 227, (2016), DOI: 10.1002/mrc.4371; J. Cui, S. Kawatake, Y. Umegawa, S. Lethu, M. Yamagami, S. Matsuoka, F. Sato, N. Matsumori, *M. Murata, “Stereoselective Synthesis of the Head Group of Archaeal Phospholipid PGP-Me to Investigate Bacteriorhodopsin-lipid Interactions,” Org. Biomol. Chem., 13, 10279 (2015), DOI: 10.1039/c5ob01252j; T, Yasuda, N. Matsumori, H. Tsuchikawa, M. Lonnfors, T. K. M. Nyholm, J. P. Slotte, *M. Murata, “Formation of Gel-like Nanodomains in Cholesterol-Containing Sphingomyelin or Phosphatidylcholine Binary Membrane As Examined by Fluorescence Lifetimes and H-2 NMR Spectra,” Langmuir, 31, 13783, (2015), DOI: 10.1021/acs.langmuir.5b03566; T. Yamamoto, Y. Umegawa, H. Tsuchikawa, N. Matsumori, S. Hanashima, *M. Murata, R. Haser, B.J. Rawlings, P. Caffrey P., “Role of Polyol Moiety of Amphotericin B in Ion Channel Formation and Sterol Selectivity in Bilayer Membrane”, Bioorg. Med. Chem. 23, 5782-5788, (2015), DOI: 10.1016/j.bmc.2015.07.00; *M. Murata, S. Sugiyama, S. Matsuoka, N. Matsumori, “Bioactive Structure of Membrane Lipids and Natural Products Elucidated by a Chemistry-Based Approach”, Chem. Rec. 15, 675-690, (2015), DOI: 10.1016/10.1002/tcr.201402097; *N. Matsumori, T. Yamaguchi, Y. Maeta, M. Murata, “Orientation and Order of the Amide Group of Sphingomyelin in Bilayers Determined by Solid-State NMR”, Biophys. J. 108, 2816-2824, (2015), DOI: 10.1016/j.bpj.2015.05.011; J. Cui, S. Matsuoka, M. Kinoshita, N. Matsumori, F. Sato, *M. Murata, J. Ando, H. Yamakoshi, K. Dodo, M. Sodeoka, “Novel Raman-tagged sphingomyelin that closely mimics original raft-forming behavior”, Bioorg. Med. Chem. 23, 2989-2994, (2015), DOI: 10.1016/j.bmc.2015.05.014; H. Shibata, H. Tsuchikawa, T. Hayashi, N. Matsumori, *M. Murata, T. Usui, “Modification of bafilomycin structure to efficiently synthesize solid-state NMR probes that selectively bind to vacuolar-type ATPase”, Chem. Asian J. 10, 915-924, (2015), DOI: 10.1002/asia.201403299; T. Yasuda, H. Tsuchikawa, M. Murata, *N. Matsumori, “Deuterium NMR of Raft Model Membranes Reveals Domain-specific Order Profiles and Compositional Distribution”, Biophysical J. 108, 2502-2506, (2015), DOI: 10.1016/j.bpj.2015.04.008; J. Cui, S. Lethu, T. Yasuda, S. Matsuoka, N. Matsumori, F. Sato, *M. Murata, “Phosphatidylcholine Bearing 6,6-dideuterated Oleic Acid: a Useful Solid-state (2)HNMR Probe for Investigating Membrane Properties”, Bioorg. Med. Chem. Lett. 25, 203, (2015), DOI: 10.1016/j.bmcl.2014.11.072; Y. Nakagawa, Y. Umegawa, K. Nonomura, N. Matsushita, T. Takano, H. Tsuchikawa, S. Hanashima, T. Oishi, *N. Matsumori, *M. Murata,“Axial Hydrogen at C7 Position and Bumpy Tetracyclic Core Markedly Reduce Sterol's Affinity to Amphotericin B in Membrane”, Biochemistry 54, 303, (2015), DOI: 10.1021/bi5012942; R. A. Espiritu, *N. Matsumori, M. Tsuda, M. Murata, "Direct and Stereospecific Interaction of Amphidinol 3 with Sterol in Lipid Bilayers" Biochemistry, 53(20), 3287-3293, (2014), DOI: 10.1021/bi5002932; Y. Nakagawa, Y. Umegawa, T. Takano, H. Tsuchikawa, *N. Matsumori, M. Murata, "Effect of Sterol Side Chain on Ion Channel Formation by Amphotericin B in Lipid Bilayers", Biochemistry, 53(19), 3088-3094, (2014), DOI: 10.1021/bi500122c; M. Kinoshita, N. Matsumori, *M. Murata. "Coexistence of Two Liquid Crystalline Phases in Dihydrosphingomyelin and Dioleoylphosphatidylcholine Binary Mixtures" Biochim. Biophys. Acta Biomembranes, 1838, 1372-1381, (2014), DOI: 10.1016/j.bbamem.2014.01.017; R. Sugiyama, S. Nishimura, N. Matsumori, Y. Tsunematsu, A. Hattori, *H. Kakeya, "Structure and Biological Activity of 8-deoxyheronamide C from a Marine-derived Streptomyces sp.: Heronamides Target Saturated Hydrocarbon Chains in Lipid Membranes" J. Am. Chem. Soc., 136(14), 5209-5212, (2014), DOI: 10.1021/ja500128u; H. Shibata, H. Tsuchikawa, N. Matsumori, *M. Murata, T. Usui, "Design and Synthesis of 24-Fluorinated Bafilomycin Analogue as an NMR Probe with Potent Inhibitory Activity to Vacuolar-type ATPase", Chem. Lett., 43(4), 474-476, (2014), DOI: 10.1246/cl.131099; *松森信明, "脂質膜における構造および相互作用解析:バイセルを用いた検討" 有機合成化学協会誌72(5), 529-537, (2014)
養王田正文 ▲班員一覧に戻る▲: 【雑誌論文】; N. Ogawa, Y. Y.Yamamoto, K. Abe, H. Sekiguchi, Y. C. Sasaki, A. Ishikawa, J. Frydman, *M. Yohda“Time-Resolved Measurement of the ATP-Dependent Motion of the Group II Chaperonin by Diffracted Electron Tracking,” Int. J. Mol. Sci., 19, E950, (2018), DOI: 10.3390/ijms19040950; M. Sahlan, T. Zako, *M. Yohda, “Prefoldin, a jellyfish-like Molecular Chaperone: Functional Cooperation with a Group II Chaperonin and Beyond,” Biophys. Rev., 10, 339, (2018), DOI: 10.1007/s12551-018-0400-0; M. Asakawa, Y. Fukutani, A. Savangsuksa, K. Noguchi, H. Matsunami, and *M. Yohda“Modification of the response of olfactory receptors to acetophenone by CYP1a2,” Sci. Rep. 7, 10167 (2017). DOI: 10.1038/s41598-017-10862-5; *M. Yohda, K. Ikegami, Y. Aita, M. Kitajima, A. Takechi, M. Iwamoto, T. Fukuda, N. Tamura, J. Shibasaki, S. Koike, D. Komatsu, S. Miyagi, M. Nishimura, Y. Uchino, A. Shiroma, M. Shimoji, H. Tamotsu, N. Ashimine, M. Shinzato, S. Ohki, K. Nakano, K. Teruya, K. Satou, T. Hirano, O. Yagi “Isolation and genomic characterization of a Dehalococcoides strain suggests genomic rearrangement during culture,” Sci. Rep. 7, 2230 (2017). DOI: 10.1038/s41598-017-02381-0; Y. Y. Yamamoto, Y. Uno, E. Sha, K. Ikegami, N. Ishii, N. Dohmae, H. Sekiguchi, Y. C. Sasaki, and *M. Yohda “Asymmetry in the function and dynamics of the cytosolic group II chaperonin CCT/TRiC,” PLoS One 12, e0176054 (2017). DOI: 10.1371/journal.pone.0176054; S. Sonotaki, T. Takami, K. Noguchi, M. Odaka, M. Yohda, and *Y. Murakami “Successful PEGylation of hollow encapsulin nanoparticles from Rhodococcus erythropolis N771 without affecting their disassembly and reassembly properties,” Biomater. Sci. 5, 1082-1089 (2017). DOI: 10.1039/c7bm00207f; K. Hasegawa, R. Negishi, M. Matsumoto, M. Yohda, *K. Hosokawa, and M. Maeda “Specificity of MicroRNA Detection on a Power-free Microfluidic Chip with Laminar Flow-assisted Dendritic Amplification,” Anal. Sci. 33,171-177 (2017). DOI: 10.2116/analsci.33.171; M. M. Islam, M. Yohda, S. I. Kidokoro, *Y. Kuroda, “Crystal Structures of Highly Simplified BPTIs Provide Insights into Hydration-driven Increase of Unfolding Enthalpy,” Sci. Rep., 7, 41205, (2017). DOI: 10.1038/srep41205; R. Sharma, Y. Ishimaru, I. Davison, K. Ikegami, M. S. Chien, H. You, Q. Chi, M. Kubota, M. Yohda, M. Ehlers, *H. Matsunami, “Olfactory Receptor Accessory Proteins Play Crucial Roles in Receptor Function and Gene Choice”, Elife 6, e21895 (2017), DOI: 10.7554/eLife.21895; Y. Fukutani, J. Ishii, A. Kondo, T. Ozawa, H. Matsunami, *M. Yohda, “Split Luciferase Complementation Assay for the Analysis of G Protein-coupled Receptor Ligand Response in Saccharomyces cerevisiae,” Biotechnol. Bioeng. 114(6), 1354-1361 (2017), DOI: 10.1002/bit.26255; C. Sugimoto, K. Takeda, Y. Kariya, H. Matsumura, M. Yohda, H. Ohno, *N. Nakamura, “A method of Expression for an Oxygen-tolerant Group III Alcohol Dehydrogenase from Pyrococcus horikoshii OT3,” J. Biol. Inorg. Chem., 22, 527-534, (2017), DOI: 10.1007/s00775-017-1439-2; K. Hakamada, H. Watanabe, R. Kawano, K. Noguchi, *M. Yohda, “Expression and Characterization of the Plasmodium Translocon of the Exported Proteins Component EXP2,” Biochem. Biophys. Res. Commun., 482, 700-705 (2017), DOI: 10.1016/j.bbrc.2016.11.097; Y. Y. Yamamoto, K. Tsuchida, K. Noguchi, N. Ogawa, H. Sekiguchi, Y. C. Sasaki, *M. Yohda, “Characterization of Group II Chaperonins from an Acidothermophilic Archaeon Picrophilus torridus,” FEBS Open Bio., 6, 751-764, (2016), DOI: 10.1002/2211-5463.12090; F. Watanabe, F. Yu, A. Ohtaki, Y. Yamanaka, K. Noguchi, M. Odaka, *M. Yohda, “Improvement of Enantioselectivity of the B-type Halohydrin Hydrogen-halide-lyase from Corynebacterium sp. N-1074,” J. Biosci. Bioeng., 122, 270-275, (2016), DOI: 10.1016/j.jbiosc.2016.02.003; T. Aihara, T. Ito, Y. Yamanaka, K. Noguchi, M. Odaka, M. Sekine, H. Homma, *M. Yohda, “Structural and Functional Characterization of Aspartate Racemase from the Acidothermophilic Archaeon Picrophilus torridus,” Extremophiles 20, 385-393, (2016), DOI: 10.1007/s00792-016-0829-7; T. Zako, M. Sahlan, S. Fujii, Y. Y. Yamamoto, P. T. Tai, K. Sakai, M. Maeda M, *M. Yohda, “Contribution of the C-Terminal Region of a Group II Chaperonin to its Interaction with Prefoldin and Substrate Transfer,” J. Mol. Biol., 428, 2405-2417, (2016), DOI: 10.1016/j.jmb.2016.04.006; M. Kayanuma, M. Shoji, M. Yohda, M. Odaka, *Y. Shigeta, “Catalytic Mechanism of Nitrile Hydratase Subsequent to Cyclic Intermediate Formation: A QM/MM Study,” J. Phys. Chem. B., 120, 3259-3266, (2016), DOI: 10.1021/acs.jpcb.5b11363; Y.Y. Yamamoto, M. Yohda.”Thermosome: A Group II Chaperonin of Archaea”,eLS. 1, (2016), DOI: 10.1002/9780470015902.a0026332; M. M. Islam, S. Nakamura, K. Noguchi, M. Yohda, S. Kidokoro, *Y. Kuroda, “Analysis and Control of Protein Crystallization Using Short Peptide Tags That Change Solubility without Affecting Structure, Thermal Stability, and Function”, Cryst Growth Des., 15, 2703, (2015), DOI: 10.1021/acs.cgd.5b00010; Y. Yamanaka, Y. Kato, K. Hashimoto, K. Iida, K. Nagasawa, H. Nakayama, M. Yohda, *M. Odaka, “Time-Resolved Crystallography of the Reaction Intermediate of Nitrile Hydratase: Revealing a Role for the Cysteinesulfenic Acid Ligand as a Catalytic Nucleophile”, Angew. Chem., 54, 10763, (2015), DOI: 10.1002/anie.201502731; F. Watanabe, F. Yu, A. Ohtaki, Y. Yamanaka, K. Noguchi, *M. Yohda, M. Odaka, “Crystal Structures of Halohydrin Hydrogen-halide-lyases from Corynebacterium sp. N-1074”, Proteins. 83, 2230-2239, (2015), DOI: 10.1002/prot.24938; T. Arai, S. Kimata, D. Mochizuki, K. Hara, T. Zako, M. Odaka, M. Yohda, F. Arisaka, S. Kanamaru, T. Matsumoto, S. Yajima, J. Sato, S. Kawasaki, *Y. Niimura, “NADH Oxidase and Alkyl Hydroperoxide Reductase Subunit C (peroxiredoxin) from Amphibacillus Xylanus Form an Oligomeric Assembly” FEBS Open Bio. 5, 124, (2015), DOI: 10.1016/j.fob.2015.01.005; Y. Fukutani, A. Hori, S. Tsukada, R. Sato, J. Ishii, A. Kondo, H. Matsunami, *M. Yohda“Improving the Odorant Sensitivity of Olfactory Receptor-expressing Yeast with Accessory Proteins”, Anal. Biochem. 471, 1, (2015), DOI: 10.1016/j.ab.2014.10.012; Y. Yokoyama, A. Ohtaki, I. Jantan, M. Yohda, *H. Nakamoto “Goniothalamin Enhances”the ATPase Activity of the Molecular Chaperone Hsp90 but Inhibits its Chaperone Activity,” J. Biochem. 157, 161, (2015), DOI: 10.1093/jb/mvu061; A. Tamura, Y. Fukutani, T. Takami, M. Fujii, Y. Nakaguchi, Y. Murakami, K. Noguchi, M. Yohda, *M. Odaka, “Packaging Guest Proteins into the Encapsulin Nanocompartment from Rhodococcus erythropolis N771”, Biotechnol. Bioeng., 112, 13-20 (2014), DOI: 10.1002/bit.25322; Y. Yamamoto, Y. Abe, K. Moriya, M. Arita, K. Noguchi, N. Ishii, H. Sekiguchi, Y. C. Sasaki, *M. Yohda, “Inter-ring Communication is Dispensable in the Reaction Cycle of Group II Chaperonins” J. Mol. Biol. 426(14), 2667-2678, (2014), DOI: 10.1016/j.jmb.2014.05.013; 【図書】; M. Yohda, “Aspartate Racemase: Function, Structure, and Reaction Mechanism”, D-Amino Acids :Physiology, Metabolism, and Application, T. Yoshimura, T. Nishikawa and H. Homma ed. Springer (Japan), pp 323-337, 2016, DOI: 10.1007/978-4-431-56077-7_21

公募班A02：動的秩序の創生

新井亮一 ▲班員一覧に戻る▲: 【雑誌論文】; N. Kobayashi, K. Inano, K. Sasahara, T. Sato, K. Miyazawa, T. Fukuma, M. H. Hecht, C. Song, K. Murata, *R. Arai, “Self-Assembling Supramolecular Nanostructures Constructed from de Novo Extender Protein Nanobuilding Blocks” ACS Synth. Biol.. in press (2018), DOI: 10.1021/acssynbio.8b00007; *R. Arai, “Hierarchical Design of Artificial Proteins and Complexes toward Synthetic Structural Biology” Biophys. Rev., 10, 391-410 (2018), DOI: 10.1007/s12551-017-0376-1; N. Kobayashi, *R. Arai, “Design and Construction of Self-assembling Supramolecular Protein Complexes Using Atificial and Fusion Proteins as Nanoscale Building Blocks.” Curr. Opin. Biotech., 46, 57-65, (2017), DOI: 10.1016/j.copbio.2017.01.001; 小林直也，*新井亮一，“人工蛋白質で「かたち」をつくろう—ブロック遊びしようよ！—”,　生物工学会誌, 　94, 270 (2016),（査読無し）; 小林直也，木村尚弥，*新井亮一，“バイナリーパターン配列デザインによるデノボ蛋白質の創出と蛋白質ナノブロックによる超分子複合体の創生”,　生物工学会誌, 94, 485-488, (2016)（査読無し）
飯野亮太 ▲班員一覧に戻る▲: 【雑誌論文】; A. Nakamura, T. Tasaki, Y. Okuni, C. Song, K. Murata, T. Kozai, M. Hara, H. Sugimoto, K. Suzuki, T. Watanabe, T. Uchihashi, H. Noji, R. Iino, “Rate constants, processivity, and productive binding ratio of chitinase A revealed by single-molecule analysis”, Phys. Chem. Chem. Phys., 20, 3010-3018, (2018), DOI: 10.1039/C7CP04606E(裏表紙に採用); *R. Iino, T. Iida, A. Nakamura, E. Saita, *H. You H, *Y. Sako, “Single-molecule imaging and manipulation of biomolecular machines and systems”, Biochim. Biophys. Acta, (BBA), Gen. Subj., 1862, 241-252, (2017), DOI: 10.1016/j.bbagen.2017.08.008; #M. Baba, #K. Iwamoto, R. Iino, H. Ueno, M. Hara, A. Nakanishia, J. Kishikawa, *H. Noji, *K. Yokoyama (#Equal contribution), “Rotation of Artificial Rotor Axles in Rotary Molecular Motors”, Proc Natl Acad Sci USA 113, 11214-11219, (2016), DOI: 10.1073/pnas.1605640113; A. Nakamura, T. Tasaki, D. Ishiwata, M. Yamamoto, Y. Okuni, A. Visootsat, M. Maximilien, H. Noji, T. Uchiyama, M. Samejima, K. Igarashi, *R. Iino, “Single-molecule Imaging Analysis of Binding, Processive Movement, and Dissociation of Cellobiohydrolase Trichoderma reesei Cel6A and its Domains on Crystalline Cellulose”, J. Biol. Chem., 291, 22404-22413, (2016), DOI: 10.1074/jbc.M116.752048(表紙に採用); #H. Isojima, #R. Iino, Y. Niitani, H. Noji, *M. Tomishige (#Equal contribution)“Direct Observation of Intermediate States During the Stepping Motion of Kinesin-1”Nat Chem Biol., 12, 290-297, (2016), DOI: 10.1038/nchembio.2028（News and Viewsで紹介）; *Y. Matsumoto, S. Sakakihara, A. Grushnikov, K. Kikuchi, H. Noji, A. Yamaguchi, R. Iino, Y. Yagi, K. Nishino, “A Microfluidic Channel Method for Rapid Drug-susceptibility Testing of Pseudomonas Aeruginosa”, PLOS ONE, 11, e0148797, (2016), DOI: 10.1371/journal.pone.0148797; Y. Obayashi, R. Iino, *H. Noji, “A single-molecule Digital Enzyme Assay Using Alkaline Phosphatase with a Cumarin-based Fluorogenic Substrate”, Analyst, 140, 5065-5073, (2015), DOI: 10.1039/c5an00714c.; A. Yukawa, R. Iino, R. Watanabe, S. Hayashi, *H. Noji“Key Chemical Factors of Arginine Finger Catalysis of F1-ATPase Clarified by an Unnatural Amino Acid Mutation“, Biochemistry, 54, 472–480, (2015), DOI: 10.1021/bi501138b; *R. Iino, H. Ueno, Y. Minagawa, K. Suzuki, *T. Murata“Rotational Mechanism of Enterococcus Hirae V1-ATPase by Crystal-structure and Single-molecule Analyses”, Curr. Opin. Struct. Biol., 31, 49-56, (2015), DOI: 10.1016/j.sbi.2015.02.013; S. Enoki, R. Iino, Y. Niitani, Y. Minagawa, M. Tomishige, *H. Noji, “High-speed Angle-resolved Imaging of Single Gold Nanorod with Microsecond Temporal Resolution and One-degree Angle Precision” Anal. Chem., 87, 2079-2086, (2015), DOI: 10.1021/ac502408c; H. Ueno, Y. Minagawa, M. Hara, S. Rahman, I. Yamato, E. Muneyuki, H. Noji, *T. Murata, *R. Iino, “Torque Generation of Enterococcus hirae V-ATPase” J. Biol. Chem., 289, 31212-31223, (2014), DOI: 10.1074/jbc.M114.598177; *R. Iino, Y. Minagawa, H. Ueno, M. Hara, K. Murata, “Molecular Structure and Rotary Dynamics of Enterococcus hirae V₁-ATPase” IUBMB Life, 66(9), 624-630, (2014), DOI: 10.1002/iub.1311; Y. Shibafuji, A. Nakamura, T. Uchihashi, N. Sugimoto, S. Fukuda, H. Watanabe, M. Samejima, T.Ando, H. Noji, A. Koivula, K. Igarashi, *R. Iino, “Single-molecule Imaging Analysis of Elementary Reaction Steps of Trichoderma reesei Cellobiohydrolase I (Cel7A) Hydrolyzing Crystalline Cellulose I_α and III_I”, J. Biol. Chem., 289, 14056-14065, (2014), DOI: 10.1074/jbc.M113.546085; T. Ikeda, R. Iino, *H. Noji, “Real-time Fuorescence Visualization of Slow Tautomerization of Single Free-base Phthalocyanines under Ambient Conditions”, Chem. Commun., 50, 9443-9446, (2014), DOI: 10.1039/C4CC02574A; T. Ikeda, T. Tsukahara, R. Iino, M. Takeuchi, *H. Noji, “Motion Capture and Manipulation of Single Synthetic Molecular Rotors by Optical Microscopy”, Angew. Chem. Int. Ed., 53, 10082–10085, (2014), DOI: 10.1002/anie.201403091; 【図書】; *R. Iino, S. Sakakihara, Y. Matsumoto, K. Nishino“Large Scale Femtoliter Droplet Array for Single Cell Efflux Assay of Bacteria”, Methods in Molecular Biology, 1700, 331-341 (2018), DOI: 10.1007/978-1-4939-7454-2_18; *R. Iino, S. Sakakihara, Y. Matsumoto, K. Nishino“Single-cell Detection and Collection of Persister Bacteria in a Directly Accessible Femtoliter Droplet Array”, Methods in Molecular Biology, 1333, 101-109 (2015) DOI: 10.1007/978-1-4939-2854-5_9; *飯野亮太“生体分子機械の作動原理”自己組織化マテリアルのフロンティア, p67-74, フロンティア出版 (2015); 飯野亮太,“薬剤排出トランスポーター活性のマイクロデバイスによる計測”化学療法の領域, 31, 440-448 (2015); R. Iino, S. Sakakihara, Y. Matsumoto, K. Nishino, “Single-cell detection and collection of persister bacteria in a directly accessible femtoliter droplet array”, Methods in Molecular Biology, in press (2015); 飯野亮太, 中村彰彦, 五十嵐圭日子, 鮫島正浩 “１分子計測からわかるエクソ型セルラーゼの分子機構”生物物理．54, 318-320 (2014); 飯野亮太“化学フロンティア23　1分子ナノバイオ計測：分子から生命システムを探る革新的技術” III部 Topics 5 “デジタルPCRとデジタルELISA”, (2014), 野地博行編,（化学同人,京都）; 内橋貴之, 飯野亮太, 安藤敏夫, 野地博行高速AFMによるF1-ATPase分子回転の直接可視化生化学．86, 127-136 (2014)
井上将彦 ▲班員一覧に戻る▲: 【雑誌論文】; Y. Oda, *J. Chiba, *M. Inouye, “Synthesis of Alkynyl C-Nucleotide Triphosphates Toward Enzymatic Elongation of Artificial DNA,” Heterocycles, published online, DOI: 10.3987/COM-18-S(T)48; *H. Abe, C. Sato, Y. Ohishi, *M. Inouye, “Metathesis-Based Stapling of a Pyridine-Acetylene-Phenol Oligomers Having Alkenyl Side Chains after Intermolecular Templation by Native Saccharides ,” Eur. J. Org. Chem. published online, DOI: 10.1002/ejoc.201800531; I.Sakaguchi, T. Fukasawa, K. Fujimoto, *M. Inouye, “Immobilization of Crosslinked Peptides that Possess High helical Contents and their Binding to Target DNAs on Au Surfaces,” Chem. Lett., 83, 3132, (2018), DOI: 10.1246/cl.171153; A.Yoshizawa, *M. Inouye, “A Bis(phenylethynyl)pyrene-Based [3]Rotaxane as an Extremely Photostable Fluorescence Probe Suitable for Hard-edged Irradiation Experiments,” ChemPhotoChem., 2, 353, (2018), DOI: 10.1002/cptc.201700223; *H. Abe, S. Takashima, *M. Inouye, “Kinetic Switching of Achirality/Chirality memorization of meta-Ethynylpyridine polymer by Coordination of Cu(II) Outside the Polymer” Heterocycles, 95, 730, (2017), DOI: 10.1002/ejoc.201700807; S. Hirokane, S. Takashima, *H. Abe, *M. Inouye, “Helix-Rotaxane hybrid Systems: Rotaxane-Stabilized, Saccharide-induced Chiral Ethynylpyridine Helices by Thermodynamic Process”, Eur. J. Org. Chem., 762 (2017), DOI: 10.1002/ejoc.201601323; Y. Ohishi, *H. Abe, *M. Inouye, "Saccharide Recognition and Helix Formation in Water with an Amphiphilic Pyridine–Phenol Alternating Oligomer", Eur. J. Org. Chem., 6975, (2017), DOI: 10.1002/ejoc.201701522; K. Hayashi, *M. Inouye, "Reliable and Reproducible Separation of 3,9- and 3,10-Dibromoperylenes and the Photophysical Properties of their Alkynyl Derivatives", Eur. J. Org. Chem., 4334 (2017), DOI: 10.1002/ejoc.201700807; D. Suzuki, *H. Abe, T. Minami, S. Matsumoto, *M. Inouye, "Preparation and Higher-Order Structures of 2,6-Pyridylene and 2,6-Pyrazylene Alternating Macrocycle with the Inner Nitrogen Atoms in All the Aromatic Rings", Chem. Lett., 46, 1740 (2017), DOI: 10.1246/cl.170815; K. Nogami, H. Tokumaru, G. Isokawa, T. Oyoshi, K. Fujimoto, *M. Inouye, "Bcl-XL-Binding Helical Peptides Possessing D-Ala Residues at their C-Termini with the Advantage of Long-Lasting Intracellular Stabilities", Chem. Commun., 53, 12104 (2017), DOI: 10.1039/c7cc06904a; *H. Abe, S. Takashima, *M. Inouye, “Kinetic Switching of Achirality/Chirality Memorization of meta-Ethynylpyridine Polymer by Coordination of Cu(II) Outside the Polymer”, Heterocycles, 95, 730 (2017), DOI: 10.3987/COM-16-S(S)64; S. Hirokane, S. Takashima, *H. Abe, *M. Inouye, “Helix-Rotaxane Hybrid Systems: Rotaxane-Stabilized, Saccharide-Induced Chiral Ethynylpyridine Helices by a Thermodynamic Process”, Eur. J. Org. Chem., 726−733, (2017), DOI: 10.1002/ejoc.201601323; *H. Abe, R. Yumoto, *M. Inouye, “A D_3h-Symmetric Macrocycle Alternatingly Composed of Pyridine and Benzyl Alcohol Units Linked with Acetylene Bonds”, Heterocycles, 93, 580−592, (2016),; *H. Abe T. Yoneda, Y. Ohishi, *M. Inouye, “D_3h-Symmetrical Shape-Persistent Macrocycles Consisting of Pyridine-Acetylene-Phenol Conjugates as a Highly Efficient Host Architecture for Saccharide Recognition”, Chem.−Eur. J., 22, 18944−18952, (2016), DOI: 10.1002/chem.201603987; *M. Inouye, A. Yoshizawa, M. Shibata, Y. Yonenaga, K. Fujimoto, T. Sakata, S. Matsumoto, M. Shiro, “Cyclodextrin-Isolated Alkynylpyrenes as UV-Stable and Blue-Light-Emitting Molecules Even in Condensed States”, Org. Lett., 18, 1960−1963 (2016), DOI: 10.1021/acs.orglett.6b00420
上野隆史 ▲班員一覧に戻る▲: 【雑誌論文】; H. Negishi, *S. Abe, K. Yamashita, K. Hirata, K. Niwase, M. Boudes, F. Coulibaly, H. Mori,*T. Ueno,“Supramolecular Protein Cages Constructed from a Crystalline Protein Matrix”, Chem. Commun., 54, 1988-1991, (2018), DOI: 10.1039/C7CC08689J; H. Tabe, H. Takahashi, T. Shimoi, S. Abe, *T. Ueno, *Y. Yamada, “Photocatalytic Hydrogen Evolution Systems Constructed in Cross-linked Porous Protein Crystals”, Appl. Catal., B, in press, (2018), DOI: 10.1016/j.apcatb.2018.01.046; S. Ryu, Y. Matsumoto, T. Matsumoto, T. Ueno, Y. R. Silberberg, *C. Nakamura, “Improved Efficiency of Nanoneedle Insertion by Modification with a Cell-puncturing Protein”, Jpn. J. Appl. Phys., 57, 03EB02 (2018), DOI: 10.7567/JJAP.57.03EB02; T. K. Nguyen and *T. Ueno, “Engineering of Protein Assemblies within Cells”, Curr. Opin. Struct. Biol., 51, 1-8, (2018), DOI: 10.1016/j.sbi.2017.12.005; S. Abe, B. Maity, T. Ueno, “Functionalization of Protein Crystals with Metal Ions, Complexes and Nanoparticles”, Curr. Opin. Chem. Biol., 43, 68-76, (2017), DOI: 10.1016/j.cbpa.2017.11.015; H. Inaba, T. Ueno, “Artificial bio-nanomachines based on protein needles derived from bacteriophage T4”, Biophys. Rev., in press, DOI: 10.1007/s12551-017-0336-9; S. Abe, K. Atsumi, K. Yamashita, K. Hirata, H. Mori, T. Ueno, “Structure of in Cell Protein Crystals Containing Organometallic Complexes”, Phys. Chem. Chem. Phys., 20, 2986-2989, (2017), DOI: 10.1039/C7CP06651A; B. Maity, S. Abe, and T. Ueno, “Observation of Gold Sub-nanocluster Nucleation Within a Crystalline Protein Cage”, Nat. Commun., 8, 14820, (2017), DOI: 10.1038/ncomms14820; S. Abe, H. Tabe, H. Ijiri, K. Yamashita, K. Hirata, K. Atsumi, T. Shimoi, M. Akai, H. Mori, S. Kitagawa and T. Ueno*, “Crystal Engineering of Self-Assembled Porous Protein Materials in Living Cells”, ACS Nano, 11, 2410-2419, (2017), DOI: 10.1021/acsnano.6b06099; B. Maity, and T. Ueno, “Design of Bioinorganic Materials At the Interface of Coordination and Biosupramolecular Chemistry”, Chem. Rec., 17, 383-398, (2017), DOI: 10.1002/tcr.201600122（Front Coverに採用）; 安部　聡、上野隆史, 金属錯体による細胞機能制御フロンティア生物無機化学（錯体化学会フロンティア選書、三共出版）, 476-496, (2016), （査読無し）; B. Maity, K. Fukumori, S. Abe, T. Ueno, “Immobilization of Two Organometallic Complexes into a Single Cage to Construct Protein-based Microcompartments”, Chem. Commun., 52, 5463-5466, (2016), DOI: 10.1039/C6CC00679E; H. Tabe, T. Shimoi, M. Boudes, S. Abe, F. Coulibaly, S. Kitagawa, H. Mori, *T. Ueno, “Photoactivatable CO Release from Engineered Protein Crystals to Modulate NF-κB Activation," Chem. Commun., 52, 4545-4548, DOI: 10.1039/C5CC10440H; K. Fujita, Y. Tanaka, S. Abe, *T. Ueno, “A Photoactive CO Releasing Protein Cage for Dose-Regulated Delivery in Living Cells”, Angew. Chem. Int. Ed., 55, 1056-1060, (2016). (selected as a Hot Paper), DOI: 10.1002/anie.201506738, It was featured on Kagaku Kogyo Nippo (Sep. 11, 2015), PHYS.ORG, and Wn.com.; S. Abe, H. Ijiri, H. Negishi, H. Yamanaka, K. Sasaki, K. Hirata, H. Mori, *T. Ueno, “Design of Enzyme-Encapsulated Protein Containers by in Vivo Crystal Engineering”, Adv. Mater., 27, 7951-7956, (2015), DOI: 10.1002/adma.201503827, It was featured on Kagaku Kogyo Nippo (Oct. 26, 2015), Nikkan Kogyo shinbun (Oct. 27, 2015), and Kyoto Shinbun (Nov. 03, 2015); *H. Nakajima, M. Kondo, T. Nakane, S. Abe, T. Nakao, Y. Watanabe, *T. Ueno, “Construction of an Enterobactin Analogue with Symmetrically Arranged　Monomer Subunits of Ferritin”, Chem. Commun., 51, 16609-16612, (2015), DOI: 10.1039/C5CC06904A; H. Inaba, N.J.M. Sanghamitra, K. Fujita, T. Sho, T. Kuchimaru, S. Kitagawa, S. Kizaka-Kondohc, *T. Ueno, “ A Metal Carbonyl-protein Needle Composite Designed for Intracellular CO Delivery to Modulate NF-κB activity”, Mol. BioSyst., 11, 3111-3118, (2015), DOI: 10.1039/C5MB00327J; H. Inaba, K. Fujita, *T. Ueno, “Design of Biomaterials for intracellular delivery of carbon monoxide”, Biomaterials Science, 3, 1423-1438, (2015), DOI: 10.1039/C5BM00210A; H. Tabe, T. Shimoi, K. Fujita, S. Abe, H. Ijiri, M. Tsujimoto, T. Kuchimaru, S. Kizaka-Kondo, H. Mori, S. Kitagawa, *T. Ueno, “Design of a CO-releasing Extracellular Scaffold using in-vivo Protein Crystals”, Chem. Lett., 44, 342-344, (2015), DOI: 10.1246/cl.141035; B. Maity, K. Fujita and *T. Ueno, “Use of the Confined Spaces of Apo-Ferritin and Virus Capsids as Nanoreactors for Catalytic Reactions”, Curr. Opin. Chem. Biol., 25, 88-97, (2015) DOI: 10.1016/j.cbpa.2014.12.026; S. Abe and *T. Ueno, “Design of Protein Crystals in the Development of Solid Biomaterials”, RSC Advances, 5, 21366-21375, (2015) DOI: 10.1039/C4RA16748A; H. Tabe, K. Fujita, S. Abe, M. Tsujimoto, T. Kuchimaru, S. Kizaka-Kondoh, M. Takano, S. Kitagawa, *T. Ueno, “Preparation of a Cross-linked Porous Protein Crystal containing Ru carbonyl complexes as a CO-releasing Extracellular Scaffold”, Inorg. Chem., 54, 215-220, (2015), DOI: 10.1021/ic502159x; S. Abe, Y. Tokura, R. Pal, N. Komura, A. Imamura, K. Matsumoto, H. Ijiri, N. J. M. Sanghamitra, H. Tabe, H. Ando, M. Kiso, H. Mori, S. Kitagawa, *T. Ueno, “Surface Functionalization of Protein Crystals with Carbohydrate Using Site-selective Bioconjugation” , Chem. Lett., 44, 29-31, (2015), DOI: 10.1246/cl.140865; H. Inaba, S. Kitagawa, *T. Ueno, “Protein Needles as Molecular Templates for Artificial Metalloenzymes” Isr. J. Chem., 55, 40-50, (2015), DOI: 10.1002/ijch.201400097; K. Fujita, Y. Tanaka, T. Sho, S. Ozeki, S.Abe, T. Hikage, T. Kuchimaru, S. Kizaka-Kondoh, *T. Ueno, "Intracellular CO Release from Composite of Ferritin and RutheniumCarbonyl Complexes", J. Am. Chem. Soc., 136(48), 16902-16908, (2014), DOI: 10.1021/ja508938f; H. Tabe, S. Abe, T. Hikage, S. Kitagawa, *T. Ueno, “Porous Protein Crystals as Catalytic Vessels for Organometallic Complexes” Chem. Asian J.,9, 1373-1378, (2014), (Selected as a Cover Picture) DOI: 10.1002/asia.201301347; H. Inaba, N. J. M. Sanghamitra, T. Fukai, T. Matsumoto, K. Nishijo, S. Kanamaru, F. Arisaka, S. Kitagawa, *T. Ueno, “Intracellular Protein Delivery System with Protein Needle-GFP Construct” Chem. Lett.,43, 1505-1507 (2014), DOI: 10.1246/cl.140481; N. J. M. Sanghamitra, H. Inaba, F. Arisaka, D. -O. Wang, S. Kanamaru, S. Kitagawa, *T. Ueno,“Plasma Membrane Translocation of a Protein Needle Based on a Triple-stranded β-helix Motif”Mol. BioSyst.,10, 2677-2683 (2014), DOI: 10.1039/C4MB00293H; 【図書】; 安部　聡、上野隆史「超分子タンパク質の分子設計によるバイオハイブリッド材料の開発」有機合成化学協会誌, (印刷中); 安部　聡、上野隆史「超分子タンパク質の分子設計によるバイオハイブリッド材料の開発」有機合成化学協会誌, (印刷中); 稲葉央、安部聡、*上野隆史「超分子タンパク質を用いて金属の反応を操る」化学, 70, 41-46, (2015).; T. Ueno (Guest Editor), Special Issue: Artificial Metalloenzymes, Isr. J. Chem., 55. (2015). DOI: 10.1002/ijch.201410018; 藤田健太、上野隆史「細胞への一酸化炭素ガス分子放出を指向した蛋白質集合体の機能化」酵素工学ニュース, 73, 14-16 (2015).; 稲葉央、上野隆史「タンパク質分子針の動的機能と細胞制御」生物物理, 55, 89-91 (2015).; 安部聡、上野隆史「タンパク質結晶の分子設計によるバイオ固体材料の開発」化学工業, 66, 264-272 (2015).; 藤田健太、上野隆史, 展望「X線結晶構造解析が解き明かすーカゴタンパク質のガス放出」日本アイソトープ協会"ISOTOPE NEWS", 64, 2-6 (2015)
大谷亮 ▲班員一覧に戻る▲: 【雑誌論文】; *R. Ohtani, T. Tokita, T. Takaya, *K. Iwata, M. Kinoshita, N. Matsumori, M. Nakamura, L. F. Lindoy, *S. Hayami, “The Impact of Metal Complex Lipids on Viscosity and Curvature of Hybrid Liposomes”, Chem. Commun., 53, 13249-13252, (2017), DOI: 10.1039/C7CC07944C; Y. Sekimoto, R. Ohtani, M. Nakamura, L. F. Lindoy, *S. Hayami, “Tuneable pressure effects in graphene oxide layers”, Sci. Rep., 7, 12159, (2017), DOI: 10.1038/s41598-017-12444-x; F. Kobayashi, R. Ohtani, S. Teraoka, W. Kosaka, H. Miyasaka, Y. Zhang, L. F. Lindoy, *S. Hayami, *M. Nakamura, “Syntheses, Structures and Magnetic Properties of Tetranuclear Cubane-type and Heptanuclear Wheel-type Nickel(II) Complexes with 3-Methoxysalicylic Acid Derivatives”, Dalton Trans., 46, 8555-8561, (2017), DOI: 10.1039/C7DT01757J; *R. Ohtani, A. Grosjean, R. Ishikawa, R. Yamamoto, M. Nakamura, J. K. Clegg, *S. Hayami, “Zero in-plane thermal expansion in guest-tunable 2D coordination polymers”, Inorg. Chem., 56, 6225-6233, (2017), DOI: 10.1021/acs.inorgchem.7b00282; R. Akiyoshi, K. Kuroiwa, S. A. Amolegbe, M. Nakaya, R. Ohtani, M. Nakamura, L. F. Lindoy, *S. Hayami, “Supramolecular architectures self-assembled using long chain alkylated spin crossover cobalt(II) compounds”, Chem. Commun., 53, 4685-4687, (2017), DOI: 10.1039/C7CC01501A; R. Akiyoshi, K. Kuroiwa, S. A. Amolegbe, M. Nakaya, R. Ohtani, M. Nakamura, L. F. Lindoy, *S. Hayami, “Supramolecular Architectures Self-assembled Using Long Chain Alkylated Spin Crossover Cobalt(II) Compounds”, Chem. Commun., in press, (2017), DOI: 10.1039/C7CC01501A; M. Nakaya, R. Ohtani, K. Sugimoto, M. Nakamura, L. F. Lindoy, *S. Hayami, “Molecular Assemblies of Metal Complexes via Base Pairing of Nucleic Acids in the Crystalline State”, Chem. Eur. J., 23, 7232-7237, (2017), DOI: 10.1002/chem.201700593; *R. Ohtani, Y. Kitamura, Y. Hijikata, M. Nakamura, L. F. Lindoy, *S. Hayami, “Modulation of Redox Potentials Utilizing the Flexible Coordination Sphere of a Penta-coordinate Complex in the Solid States”, Dalton Trans., 46, 3749-3754, (2017), DOI: 10.1039/c7dt00233e; *R. Ohtani, *S. Hayami, “Guest-dependent Spin-transition Behavior of Porous Coordination Polymers”, Chem. Eur. J. 23, 2236-2248, (2017), DOI: 10.1002/chem.201601880; Y. Sekimoto, M. R. Karim, N. Saigo, R. Ohtani, M. Nakamura, *S. Hayami, “Crystal Structures and Spin-Crossover Behavior of Iron(II) Complexes with Chiral and Racemic Ligands”, Eur. J. Inorg. Chem., 2017, 1049-1053, (2017), DOI: 10.1002/ejic.201601232（Front Coverに採用）; K. Wakata, M. R. Karim, M. S. Islam, R. Ohtani, M. Nakamura, M. Koinuma, *S. Hayami, “Superionic Conductivity in Hybrid of 3-hydroxypropanesulfonic Acid and Graphene Oxide”, Chem. Asian J., 12, 194-197, (2017), DOI: 10.1002/asia.201601488; H. Ohmagari, R. Ohtani, M. Nakaya, M. Ohba, M. Nakamura, L. F. Lindoy, *S. Hayami, “Water-Dependent Charge-transfer-induced Spin Transition of a Prussian Blue Analog”, Dalton Trans., 45, 16784-16788, (2016), DOI: 10.1039/C6DT03474H
片山勉 ▲班員一覧に戻る▲: 【雑誌論文】; Y. Sakiyama, K. Kasho, Y. Noguchi, H. Kawakami, *T. Katayama “Regulatory Dynamics in the Ternary DnaA Complex for Initiation of Chromosomal Replication in Escherichia coli”, Nucleic Acids Res., 45, 12354-12373, (2017), DOI: 10.1093/nar/gkx914; *T. Katayama, K. Kasho, H. Kawakami, “The DnaA cycle in Escherichia coli: Activation, Function and Inactivation of the Initiator Protein”, Front. Microbiol., 8, 2496, (2017), DOI: 10.3389/fmicb.2017.02496; K. Kasho, H. Tanaka, R. Sakai, *T. Katayama, “Cooperative DnaA Binding to the Negatively Supercoiled datA Locus Stimulates DnaA-ATP Hydrolysis”, J. Biol. Chem., 292, 1251-1266, (2017), DOI: 10.1074/jbc.M116.762815; M. Shimizu, Y. Noguchi, Y. Sakiyama, H. Kawakami, *T. Katayama, *S. Takada, “Near-atomic Structural model for Bacterial DNA Replication Initiation Complex and its Functional Insights”, Proc. Natl. Acad. Sci. USA, 113, E8021-E8030, (2016), DOI: 10.1073/pnas.1609649113; Y. Inoue, H. Tanaka, K. Kasho, K. Fujimitsu, T. Oshima, *T. Katayama, “Chromosomal Location of the DnaA-reactivating Sequence DARS2 is Important to Regulate Timely Initiation of DNA Replication in Escherichia Coli”, Genes Cells., 21, 1015-1023, (2016), DOI: 10.1111/gtc.12395; 【図書】; *T. Katayama, “Initiation of DNA replication at the chromosomal origin of E. coli, oriC”, DNA Replication: From Old Principles to New Discovery, H. Masai and M. Foiani ed. SpringerNature, in press, (2018); 神崎秀嗣, 片山勉, 児玉　悟, 新蔵礼子, 矢島孝浩“「微生物と人類の共存」をゲノムの視点から ---「日本遺伝学会第88会大会」の１ワークショップ報告”, 生物の科学遺伝, Vol. 71, No. 1, pp77-85 (2017)
神谷由紀子 ▲班員一覧に戻る▲: 【雑誌論文】; *Y. Kamiya, Y. Arimura, H. Ooi, K. Kato, X.G. Liang, *H. Asanuma, “Development of visible light-responsive RNA scissors based on the 10-23 DNAzyme”, ChemBioChem, (2018), accepted; *Y. Kamiya, Y. Yamada, T. Muro, K. Matsuura, *H. Asanuma "DNA Microcapsule for Photo-triggered Drug Release System" ChemMedChem, 12, 2016-2021, (2017), DOI: 10.1002/cmdc.201700512 フロントカバーイラストレーションに採用; *Y. Kamiya, Y. Donoshita, H. Kamimoto, K. Murayama, J. Ariyoshi, *H. Asanuma"Introduction of 2,6-diaminopurines into serinol nucleic acid (SNA) improves anti-miRNA performance" ChemBioChem, 18, 1917-1922 (2017). DOI: 10.1002/cbic.201700272; Y. Nakasone, H. Ooi, Y. Kamiya, H. Asanuma, *M. Terazima “Dynamics of Inter-DNA Chain Interaction of Photoresponsive DNA”, J. Am. Chem. Soc., 138, 9001, (2016), DOI: 10.1021/jacs.6b02525; *H. Asanuma, R. Niwa, M. Akahane, K. Murayama, H. Kashida, Y. Kamiya, “Strand-invading Linear Probe Combined with Unmodified PNA”, Bioorg. Med. Chem., 24, 4129, (2016), DOI: 10.1016/j.bmc.2016.06.055; *H. Kashida, T. Osawa, K. Morimoto, Y. Kamiya, *H. Asanuma, “Molecular Design of Cy3 Derivative for Highly Sensitive in-stem Molecular Beacon and its Application to the Wash-free FISH”, Bioorg. Med. Chem., 23, 1758-1762, (2015), DOI: 10.1016/j.bmc.2015.02.030; K. Murayama, Y. Kamiya, *H. Kashida, *H. Asanuma, “Ultra-Sensitive Molecular Beacon Designed with Totally Serinol Nucleic Acid (SNA) for Monitoring mRNA in Cell”, ChemBioChem, 16, 1298-1301, (2015), DOI: 10.1002/cbic.201500167; Y. Kamiya, K. Iishiba, T. Doi. K. Tsuda, H. Kashida, *H. Asanuma, “Terminus-free siRNA Prepared by Photo-crosslinking Activated via Slicing by Ago2”, Biomater. Sci., 3, 1534-1538, (2015), DOI: 10.1039/C5BM00231A; Y. Kanematsu, Y. Kamiya, K. Matsuo, K. Gekko, *K. Kato, *M. Tachikawa“Isotope Effect on the Circular Dichroism Spectrum of Methyl α-D-glucopyranoside in Aqueous Solution”, Sci. Rep., 5, 17900, (2015), DOI: 10.1038/srep17900; S. Ninagawa, T. Okada, Y. Sumitomo, S. Horimoto, T. Sugimoto, T. Ishikawa, S. Takeda, T Yamamoto, T. Suzuki, Y. Kamiya, *K. Kato, *K. Mori, “Forcible Destruction of Severely Misfolded Mammalian Glycoproteins by the Non-glycoprotein ERAD Pathway”", J. Cell Biol., 211, 775-784, (2015), DOI: 10.1083/jcb.201504109; K. Inagaki, T. Satoh, M. Yagi-Utsumi, A.C. Gulluche, T. Anzai, Y. Uekusa, Y. Kamiya, *K. Kato, “Redox-coupled Structural Changes of the Catalytic a' domain of Protein Disulfide Isomerase”, FEBS Lett., 589, 2690-2694, (2015), DOI: 10.1016/j.febslet.2015.07.041; Y. Kamiya, T. Takagi, H. Ooi, H. Ito, X.G. Liang, *H. Asanuma, “Synthetic Gene Iinvolving Azobenzene-tethered T7 Promoter for the Photocontrol of Gene Expression by Visible Light”, ACS Synth. Biol., 4 (4), 365–370, (2015), DOI: 10.1021/sb5001092; *H. Asanuma, M. Akahane, R. Niwa, H. Kashida, Y. Kamiya, "Highly Sensitive and Robust Linear Probe for Detection of mRNA in Cells" Angew. Chem. Int. Ed., 15, 54, 4315-4319, (2015), DOI: 10.1002/anie.201411000; *H. Asanuma, H. Kashida, Y. Kamiya, "De Novo Design of Functional Oligonucleotides with Acyclic Scaffolds" Chem. Rec., 14(6), 1055-1069, (2014), DOI: 10.1002/tcr.201402040; Y. Kamiya, *H. Asanuma, "Light-driven DNA Nanomachine with a Photoresponsive Molecular Engine." Acc. Chem. Res., 47(6), 1663-1672, (2014) , DOI: 10.1021/ar400308f; Y. Kamiya, J. Takai, H. Ito, K. Murayama, H. Kashida, *H. Asanuma, “Enhancement of Stability and Activity of siRNA by Terminal Substitution with Serinol Nucleic Acid (SNA)”, ChemBioChem, 15(17), 2549-2555, (2014), DOI: 10.1002/cbic.201402369; S. Ninagawa, T. Okada, Y. Sumitomo, Y. Kamiya, K. Kato, S. Horimoto, T. Ishikawa, S. Takeda, T. Sakuma, T. Yamamoto, *K. Mori, “EDEM2 initiates mammalian glycoprotein ERAD by catalyzing the first mannose trimming step”, J. Cell Biol., 206(3), 347-356, (2014) DOI: 10.1083/jcb.201404075; 【図書】; 神谷由紀子、村山恵司、樫田啓、浅沼浩之, “非環状骨格型人工核酸：aTNA, SNA”, “核酸医薬の創製と応用展開”、監修：和田猛、p79-86、シーエムシー出版(2016); Y. Zhang, T. Yamaguchi, M. Yagi-Utsumi, Y. Kamiya, Y. Sakae, Y. Okamoto, *K. Kato “Conformational Dynamics of Oligosaccharides Characterized by Paramagnetism-assisted NMR Spectroscopy in Conjunction with Molecular Dynamics Simulation”, Advances in Experimental Medicine and Biology, A.Chakrabarti and A.Surolia ed., Springer (Switzerland), Vol. 842, pp 389-401, 2015、 DOI: 10.1007/978-3-319-11280-0_14
佐田和己 ▲班員一覧に戻る▲: 【雑誌論文】; M. Naya, Y. Hamano, K. Kokado, *K. Sada, “Organic Reaction as a Stimulus for Polymer Phase Separation.” ACS Macro Lett. 2017, 6, 898-902. DOI: 10.1021/acsmacrolett.7b00315; *K.Hirai, S.Isobe, *K. Sada, “Gas-generated Thermal Oxidation of a Coordination Cluster for an Anion-doped Mesoporous Metal Oxide”, Sci. Rep. 5, 18468, (2015), DOI: 10.1038/srep18468; D.H.Gharib, S.Amemori, M.Naya, *K.Kokado *K. Sada, “Gel Thermoresponsiveness Driven by Switching of the Charge-transfer Interaction”, RSC Advances, 5, 89319, (2015), DOI: 10.1039/C5RA18388J; *K.Kokado, R.Taniguchi, * K. Sada, “Rigidity- induced Emission Enhancement of Network Polymers Crosslinked by Tetraphenylethene Derivatives”, J. Mater. Chem. C, 3, 8504, (2015), DOI: 10.1039/C5TC01597A; K.Nishi, S.Tochioka, T.Hiroi, T.Yamada, K.Kokado, T.-H.Kim, E.P.Gilbert, K. Sada, *M.Shibayama, “Structural Analysis of Lipophilic Polyelectrolyte Solutions and Gels in Low- Polar Solvents”, Macromolecules 48, 3613, (2015), DOI: 10.1021/acs.macromol.5b00753; S.Nagata, *K.Kokado, * K. Sada, “Metal-organic Framework Tethering PNIPAM for ON- OFF Controlled Release in Solution”, Chem. Commun. 51, 8614, (2015), DOI: 10.1039/C5CC02339D; R. Taniguchi, T. Yamada, K. Sada, *K. Kokado, “Stimuli-responsive Fluorescence of AIE Elastomer Based on PDMS and Tetraphenylethene”, Macromolecules, 47(18), 6382-6388, (2014), DOI: 10.1021/ma501198d; T. Yamada, K. Kokado, Y. Higaki, A. Takahara, *K. Sada, “Preparation and Morphology Variation of Lipophilic Polyelectrolyte Brush Functioning in Non-Polar Solvents”, Chem. Lett., 43(8), 1300-1302, (2014),DOI: 10.1246/cl.140341; S. Sudo, S. Nagata, K. Kokado, *K. Sada, “Direct Synthesis of Liquid Metal Colloids and Their Transmetalation into Noble Metal Nanoparticles”, Chem. Lett., 43(8), 1207-1209, (2014),DOI: 10.1246/cl.140359; A. Md. R. Kabir, D. Inoue, Y. Hamano, H. Mayama, K. Sada, *A. Kakugo, “Biomolecular Motor Modulates Mechanical Property of Microtubule”, Biomacromol., 15(5), 1797-1805, (2014),DOI: 10.1021/bm5001789; M. Ito, A. Md. R. Kabir, D. Inoue, T. Torisawa, Y. Toyoshima, K. Sada, *A. Kakugo, “Formation of Ring-shaped Microtubule Assemblies Through Active Self-organization on Dynein”, Polym. J., 46(4), 220-225, (2014),DOI: 10.1038/pj.2013.89; 佐田和己, 小門憲太, ”MOFを用いた新しい結晶重合”, 高分子, 63(4), 225-226, (2014); 小門憲太, 佐田和己, ”結晶のようなゲルをつくる”, 現代化学, (524), 42-46, (2014).; 佐田和己, 小門憲太, ”超分子相互作用を駆使した新しい温度応答性高分子の開発”, 高分子, 63(12), in press, (2014); 【図書】; S. Amemori, K. Kokado, K. Sada“Chemo-sensitive Soft Matters Based on Thermo-sensitive Polymers”, Synergy in Supramolecular Chemistry, T. Nabeshima, ed. Taylor & Francis (USA) Chapter 5, pp. 75-90, 2014.; Kazuki Sada, Yuki Furukawa, Kenta Kokado “Encyclopedia of Polymeric Nanomaterials” “Polyacrylonitrile”, (2014), in press; Kazuki Sada, Takumi Ishiwata, Kenta Kokado “Advances in Organic Crystal Chemistry: Comprehensive Reviews 2015” “Topochemical Polymerizations & Crystal Cross-linking of Metal Organic Frameworks”, (2014), in press, Rui Tamura, Mikiji Miyata, eds. (Springer, Germany); Shogo Amemori, Kenta Kokado, Kazuki Sada“Synergy in Supramolecular Chemistry”Chapter 5, “Chemo-sensitive Soft Matters Based on Thermo-sensitive Polymers”, (2014), in press, p.75-T. Nabeshima, ed. (Taylor & Francis, USA); 小門憲太、佐田和己“クリックケミストリー　—基礎から実用まで—” 第１７章「多孔性配位高分子のクリックケミストリー」, pp.161-173,（2014)高田十志和、小山靖人、深瀬浩一編,（シーエムシー出版, 東京、日本）; 小門憲太、佐田和己“ゲルテクノロジーハンドブック　—機能設計・評価。シミュレーションから製造プロセスまで—” 1-3-5「有機溶媒高吸収性親油性高分子電解質ゲル」, pp.97-103, (2014)中野義夫他編,（エヌ・ティー・エス出版, 東京,日本）; 上西恭平、井上大介、佐田和己、角五彰 “ゲルテクノロジーハンドブック　—機能設計・評価。シミュレーションから製造プロセスまで—” 1-5-2「ATP 駆動型運動素子」, pp.167-172, (2014), 中野義夫他編,（エヌ・ティー・エス出版, 東京,日本）
佐藤宗太 ▲班員一覧に戻る▲: 【雑誌論文】; T. Matsuno, Y. Nakai, S. Sato, Y. Maniwa, *H. Isobe, “Ratchet-Free Solid-State Inertial Rotation of a Guest Ball in a Tight Tubular Host” Nature Commun., 9, 026103, (2018), DOI: 10.1063/1.5021711, accepted.; *Y. Nagata, T. Nishikawa, M. *Suginome, S. Sato, *M. Sugiyama, L. Porcar, A. Martel, R. Inoue, N. Sato “Elucidating the Solvent Effect on the Switch of the Helicity of Poly(quinoxaline-2,3-diyl)s: A Conformational Analysis by Small-Angle Neutron Scattering”, J. Am. Chem. Soc., 140, 2722–2726, (2018). DOI: 10.1021/jacs.7b11626; S.-T. Pham, K. Ikemoto, K. Z. Suzuki, T. Izumi, H. Taka, H. Kita, S. Sato, H. Isobe, *S. Mizukami “Magneto-Electroluminescence Effects in the Single-Layer Organic Light-Emitting Devices with Macrocyclic Aromatic HydrocarbonsQ”, APL Materials, 6, 026103, (2018), DOI: 10.1063/1.5021711 (Editor's Pickに選出される); N. Miyamoto, Y. Nakazawa, T. Nakamura, K. Okano, S. Sato, Z. Sun, H. Isobe, *H. Tokuyama “Synthesis of 9,10-Diarylanthracenes via Mg(TMP)₂·2LiCl-Mediated Benzyne Generation/[4+2] Cycloaddition and Deoxygenation of 9,10-Epoxyanthracene Intermediates” ,Synlett, 29, 513-518, (2017), DOI: 10.1055/s-0036-1591510; T. Matsuno, K. Kogashi, S. Sato, *H. Isobe “Enhanced yet Inverted Effects of π-Extension in Self-Assembly of Curved π-Systems with HelicityA”, Org. Lett., 19, 6456-6459 (2017), DOI: 10.1021/acs.orglett.7b03534; K. Kurihara, M. Matsuo, *T. Yamaguchi, *S. Sato“Synthetic Approach to Biomolecular Science by Cyborg Supramolecular Chemistry”Biochim. Biophys. Acta, (BBA) General Subjects, 1862, 358-364, (2017), DOI: 10.1016/j.bbagen.2017.11.002; J. Uchida, *M. Yoshio, *S. Sato, H. Yokoyama, *M. Fujita, *T. Kato "Self-Assembly of Giant Spherical Liquid-Crystalline Complexes and Formation of Nanostructured Dynamic Gels Exhibiting Self-Healing Properties" Angew. Chem. Int. Ed., 56, 14085-14089, (2017), DOI: 10.1002/anie.201707740; *S. Sato, A. Yoshii, S. Takahashi, S. Furumi, M. Takeuchi, *H. Isobe "Chiral intertwined spirals and magnetic transition dipole moments dictated by cylinder helicity" Proc. Natl. Acad. Sci. U.S.A., 114, 13097-13101, (2017), DOI: 10.1073/pnas.1717524114; T. Matsuno, S. Kamata, S. Sato, A. Yokoyama, P. Sarkar, *H. Isobe "Assembly, Thermodynamics, and Structure of a Two-Wheeled Composite of a Dumbbell-Shaped Molecule and Cylindrical Molecules with Different Edges" Angew. Chem. Int. Ed., 56, 15020-150247, DOI: 10.1002/anie.201709442; S. Hitosugi, S. Sato, T. Matsuno, T. Koretsune, R. Arita, *H. Isobe "Pentagon-Embedded Cycloarylene Molecules with Cylindrical Shapes" Angew. Chem. Int. Ed., 56, 9106-9110 (2017). DOI: 10.1002/anie.201704676; Y. Tian, K. Ikemoto, *S. Sato, *H. Isobe "[n]Cyclo-3,6-Phenanthrenylenes: Synthesis, Structure and Fluorescence" Chem. Asian J., 12, 2093-2097 (2017). DOI: 10.1002/asia.201700563; K. Ikemoto, R. Kobayashi, S. Sato, *H. Isobe, “Entropy-Driven Ball-in-Bowl Assembly of Fullerene and Geodesic Phenylene Bowl”, Org.Lett., 19 (9), 2362–2365, (2017), DOI: 10.1021/acs.orglett.7b00899; G. Yan, T. Yamaguchi, T. Suzuki, S. Yanaka, S. Sato, M. Fujita, *K. Kato, “Hyper-assembly of Self-assembled Glycoclusters Mediated by Specific Carbohydrate-carbohydrate Interactions”, Chem. Asian J., 12(9):968-972, (2017), DOI: 10.1002/asia.201700202; K. Ikemoto, R. Kobayashi, S. Sato, *H. Isobe, “Synthesis and Bowl-in-bowl Assembly of a Geodesic Phenylene Bowl”, Angew. Chem. Int. Ed., 56, 6511-6514, (2017), DOI: 10.1002/anie.201702063(Very Important Pater(VIP)に採用)(Inside Back Cover Pictureに採用); *K. Z. Suzuki, T. Izumi, X. Zhang, A. Sugihara, S.-T. Pham, H. Taka, S. Sato, H. Isobe, S. Mizukami, “Room Temperature Magnetoresistance in an Organic Spin Valve with an Aromatic Hydrocarbon macrocycle”, APL Mater., 5, 046101, (2017), DOI: 10.1063/1.4979548; Y. Suzuki, S. Ishida, S. Sato, H. Isobe, *T. Iwamoto, “An Isolable Potassium Salt of a Borasilene–Chloride Adduct”, Angew. Chem. Int. Ed., 56, 4593-4597, (2017), DOI: 10.1002/anie.201612545; T. Izumi, Y. Tian, K. Ikemoto, A. Yoshii, T. Koretsune, R. Arita, H. Kita, H. Taka, *S. Sato, *H. Isobe, “Efficient Blue Electroluminescence from a Single-Layer Organic Device Composed Solely of Hydrocarbons”, Chem. Asian J., 12, 730-733, (2017), DOI: 10.1002/asia.201700198; A. Yoshii, K. Ikemoto, T. Izumi, H. Kita, H. Taka, T. Koretsune, R. Arita, *S. Sato, *H. Isobe, “Structural Modulation of Macrocyclic Materials for Charge Carrier Transport Layers in Organic Light-Emitting Devices”, ECS J. Solid State Sci. Technol., 6, M3065-M3067, (2017), DOI: 10.1149/2.0111706jss; S. Kamata, S. Sato, *J. Wu, *H. Isobe, “Crystal Structure of 7,15-Bis(4-tert-butylphenyl)-1,9-dimethylheptazethrene”, Acta Cryst, E73, 99-102, (2017), DOI: 10.1107/S2056989016020247; Z. Sun, N. Miyamoto, S. Sato, *H. Tokuyama, *H. Isobe, “An Obtuse-Angled Corner Unit for Fluctuating Carbon Nanohoops”, Chem. Asian J., 12, 271-275, (2017), DOI: 10.1002/asia.201601614; *D. Fujita, Y. Ueda, S. Sato, N. Mizuno, T. Kumasaka, *M. Fujita, “Self-assembly of Tetravalent Goldberg Polyhedra from 144 Small Components”, Nature, 540, 563-566, (2016), DOI: 10.1038/nature20771(News & Views欄でハイライトされる); D. Fujita, Y. Ueda, S. Sato, H. Yokoyama, N. Mizuno, T. Kumasaka, *M. Fujita, “Self-Assembly of M₃₀L₆₀ Icosidodecahedron”, Chem, 1, 91-101, (2016), DOI: 10.1016/j.chempr.2016.06.007(Cover Pictureに採用)(Preview欄でハイライトされる); M. Sato, H. Azuma, A. Daigaku, S. Sato, K. Takasu, K. Okano, *H. Tokuyama, “Total Synthesis of (-)-Histrionicotoxin through a Stereoselective Radical Translocation-Cyclization Reaction”, Angew. Chem. Int. Ed., 56, 1087-1091, (2016), DOI: 10.1002/anie.201609941; T. Matsuno, S. Sato, A. Yokoyama, S. Kamata, *H. Isobe, “Self-Sorting of Two Hydrocarbon Receptors with One Carbonaceous Ligand”, Angew. Chem. Int. Ed., 55, 15339-15343, (2016), DOI: 10.1002/anie.201609444; P. Sarkar, Z. Sun, T. Tokuhira, M. Kotani, S. Sato, *H. Isobe, “Stereoisomerism in Nanohoops with Heterogeneous Biaryl Linkages of E/Z- and R/S-Geometries”, ACS Cent. Sci., 2, 740-747, (2016), DOI: 10.1021/acscentsci.6b00240; M. Kanto, S. Sato, N. Tsuda, *M. Sasaki, “Stereodivergent Synthesis and Configurational Assignment of the C1–C15 Segment of Amphirionin-5”, J. Org. Chem., 81, 9105-9121, (2016), DOI: 10.1021/acs.joc.6b01700; Z. Sun, T. Suenaga, P. Sarkar, S. Sato, M. Kotani, *H. Isobe, “Stereoisomerism, Crystal Structures, and Dynamics of Belt-shaped Cyclonaphthylenes”, Proc. Natl. Acad. Sci. U.S.A., 113, 8109-8114, (2016), DOI: 10.1073/pnas.1606530113(AIMResearchにハイライトされる)(2016年6月28日 KEK物構研トピックスにハイライトされる); *S. Sato, A. Unemoto, T. Ikeda, *S. Orimo, *H. Isobe, “Carbon-rich Active Materials with Macrocyclic Nanochannels for High-Capacity Negative Electrodes in All-Solid-State Lithium Rechargeable Battery”, Small, 12, 3381-3387, (2016), DOI: 10.1002/smll.201600916(Back Cover Pictureに採択)（2016年9月26日 AIMResearchにハイライトされる）; K. Ikemoto, M. Fujita, P. Too, Y. Tnay, S. Sato, S. Sato, *H. Isobe, “Synthesis and Structures of π-Extended [n]Cyclo-para-phenylenes (n = 12, 16, 20) Containing n/2 Nitrogen Atoms”, Chem. Lett., 45, 658-660 (2016), DOI: 10.1246/cl.160258; J. Xue, K. Ikemoto, S. Sato, *H. Isobe, “Introduction of Nitrogen Atoms in [n]Cyclo-meta-phenylenes via Cross Coupling Macrocyclization”, Chem. Lett., 45, 676-678 (2016), DOI: 10.1246/cl.160218; *H. Isobe, K. Nakamura, S. Hitosugi, S. Sato, H. Tokoyama, H. Yamakado, K.Ohno, *H Kono, 　　“Reply to the ‘Comment on “Theoretical studies on a carbonaceous molecular bearing: association thermodynamics and dual-mode rolling dynamics”’ by E. M. Cabaleiro-Lago, J. Rodriguez-Otero and A. Gil, Chem. Sci., 2016, 7, DOI: 10.1039/C5SC04676A”, Chem. Sci., 7, 2929-2932 (2016), DOI: 10.1039/C6SC00550K; K. Ikemoto, S. Sato, *H. Isobe, “One-pot Synthesis of [n]Cyclo-1,3-pyrenylenes via Ni-mediated Macrocyclization”, Chem. Lett., 45, 217-219, (2016), DOI: 10.1246/cl.151112; K. Ikemoto, A. Yoshii, T. Izumi, H. Taka, H. Kita, J. Y. Xue, R. Kobayashi, *S. Sato, *H. Isobe, “Modular Synthesis of Aromatic Hydrocarbon Macrocycles for Simplified, Single-Layer Organic Light-Emitting Devices”, J. Org. Chem., 81, 662-666, (2016), DOI: 10.1021/acs.joc.5b02620; J. Y. Xue, T. Izumi, A. Yoshii, K. Ikemoto, T. Koretsune, R. Akashi, R. Arita, H. Taka, H. Kita, *S. Sato, *H. Isobe, “Aromatic Hydrocarbon Macrocycles for Highly Efficient Organic Light-emitting Devices with Single-layer Architectures”, Chem. Sci., 7, 896-904, (2016), DOI: 10.1039/C5SC03807C; P. Sarkar, S. Sato, S. Kamata, T. Matsuno, *H. Isobe, “Synthesis and Dynamic Structures of a Hybrid Nanohoop Molecule Composed of Anthanthrenylene and Phenylene Panels”, Chem. Lett., 44, 1581-1583, (2015), DOI: 10.1246/cl.150801; Z. Sun, P. Sarkar, T. Suenaga, S. Sato, *H. Isobe, “Belt-shaped Cyclonaphthylenes”, Angew. Chem. Int. Ed., 54, 12800-12804, (2015), DOI: 10.1002/anie.201506424; E. Takahashi, K. Kamata, Y. Kikukawa, S. Sato, K. Suzuki, K. Yamaguchi, *N. Mizuno, “Synthesis and Oxidation Catalysis of a Ti-Substituted Phosphotungstate, and Identification of the Active Oxygen Species”, Catal. Sci. Technol., 5, 4778-4789, (2015), DOI: 10.1039/C5CY01031D; *S. Sato, M. Ikemi, T. Kikuchi, S. Matsumura, *K. Shiba, *M. Fujita, “Bridging Adhesion of a Protein onto an Inorganic Surface Using Self-Assembled Dual Functionalized Spheres”, J. Am. Chem. Soc., 137, 12890-12896, (2015), DOI: 10.1021/jacs.5b06184; H. Yokoyama, Y. Ueda, D. Fujita, S. Sato, *M. Fujita, “Finely Resolved Threshold for the Sharp M₁₂L₂₄/M₂₄L₄₈ Structural Switch in Multi-Component MnL2n Polyhedral Assemblies: X-ray, MS, NMR, and Ultracentrifugation Analyses”, Chem. Asian J., 10, 2292-2295, (2015), DOI: 10.1002/asia.201500519; P. Bonakdarzadeh, F. Topić, E. Kalenius, S. Bhowmik, S. Sato, M. Groessl, R. Knochenmuss, *K. Rissanen, “DOSY NMR, X-ray Structural and Ion-Mobility Mass Spectrometric Studies on Electron-Deficient and Electron-Rich M6L4 Coordination Cages”, Inorg. Chem., 54, 6055-6061, (2015), DOI: 10.1021/acs.inorgchem.5b01082; *M. Kobayashi, T. Okuhara, H. Kato, S. Sato, M. Kakihana, “Novel Titanium Complexes with a Reversible Structure Change on Solvent Adsorption and Desorption”, Chem. Lett., 44, 1050-1052, (2015), DOI: 10.1246/cl.150393; S. Hitosugi, K. Ohkubo, Y. Kawashima, T. Matsuno, S. Kamata, K. Nakamura, H. Kono, S. Sato, S. *Fukuzumi, *H. Isobe, “Modulation of Energy Conversion Processes in Carbonaceous Molecular Bearings”, Chem. Asian J., 10, 2404-2410, (2015), DOI: 10.1002/asia.201500673; *S. Sato, Y. Yoshimasa, D. Fujita, M. Yagi-Utsumi, T. Yamaguchi, *K. Kato, *M. Fujita, “A Self-Assembled Spherical Complex Displaying a Gangliosidic Glycan Cluster Capable of Interacting with Amyloidogenic Proteins”, Angew. Chem. Int. Ed., 54, 8435-8439, (2015), DOI: 10.1002/anie.201501981; *H. Isobe, K. Nakamura, S. Hitosugi, S. Sato, H.,Tokoyama, H. Yamakado, K. Ohno, *H. Kono, “Theoretical Studies on a Carbonaceous Molecular Bearing: Association Thermodynamics and Dual-mode Rolling Dynamics”, Chem. Sci., 6, 2746-2753, (2015), DOI: 10.1039/C5SC00335K; *S. Sato, R. Takeuchi, M. Yagi-Utsumi, T. Yamaguchi, Y. Yamaguchi, K. Kato, *M. Fujita, “Self-Assembled, π-Stacked Complex as a Finely-Tunable Magnetic Aligner for Biomolecular NMR Applications”, Chem. Comm., 51, 2540-2543 (2015), DOI: 10.1039/C4CC09354B; D. Fujita, H. Yokoyama, Y. Ueda, S. Sato, *M. Fujita, “Geometrically Restricted Intermediates in the Self-Assembly of an M12L24 Cuboctahedral Complex”, Angew. Chem. Int. Ed., 54, 155-158 (2015), DOI: 10.1002/anie.201409216; C. J. Bruns, D. Fujita, M. Hoshino, S. Sato, *J. F. Stoddart, *M. Fujita, “Emergent Ion-Gated Binding of Cationic Host–Guest Complexes within Cationic M₁₂L₂₄ Molecular Flasks”, J. Am. Chem. Soc., 136, 12027-12034, (2014), DOI: 10.1021/ja505296e; J. Y. Xue, K. Ikemoto, N. Takahashi, T. Izumi, H. Taka, H. Kita, *S. Sato, *H. Isobe, “Cyclo-meta-phenylenes Revisited: Nickel-mediated Synthesis, Mstructures and Device Applications”, J. Org. Chem., 79, 9735-9739, (2014), DOI: 10.1021/jo501903n; Q.-F. Sun, S. Sato, *M. Fujita, “An M₁₂(L¹)₁₂(L²)₁₂ Cantellated Tetrahedron: A Case Study for Mixed-Ligand Self-Assembly”, Angew. Chem. Int. Ed., 53, 13510-13513 (2014), DOI: 10.1002/anie.201408652; T. Matsuno, S. Sato, R. Iizuka, *H. Isobe, “Molecular recognition in curved π-systems: Effects of π-lengthening of tubular molecules on structures and thermodynamics”, Chem. Sci., 6, 909-916 (2014), DOI: 10.1039/C4SC02812K; S. Hitosugi, K. Ohkubo, R. Iizuka, Y. Kawashima, K. Nakamura, S. Sato, H. Kono, S. Fukuzumi, *H. Isobe. “Photoinduced Electron Transfer in a Dynamic Supramolecular System with Curved π-Structures”, Org. Lett., 16(12), 3352-3355, (2014), DOI: 10.1021/ol501381x; T. Kikuchi, S. Sato, D. Fujita, *M. Fujita, “Stepwise DNA Condensation by a Histone-mimic Peptide-coated M₁₂L₂₄ Spherical Complex”, Chem. Sci., 5, 3257-3260, (2014), DOI: 10.1039/C4SC00656A; T. Matuno, H. Naito, S. Hitosugi, S. Sato, M. Kotani, *H. Isobe, ”Geometric Measures of Finite Carbon Nanotube Molecules: a Proposal for Length Index and Filling Indexes”, Pure Appl. Chem., 86(4), 489-495, (2014), DOI: 10.1515/pac-2014-5006; S. Sato, T. Yamasaki, *H. Isobe, “Solid-state Structures of Peapod Bearings Composed of Finite Single-wall Carbon Nanotube and Fullerene Molecules”, Proc. Natl. Acad. Sci. USA, 111(23), 8374-8379, (2014), DOI: 10.1073/pnas.1406518111; *M. Yoneya, S. Tsuzuki, T. Yamaguchi, S. Sato, M. Fujita, “Coordination-Directed Self-Assembly of M₁₂L₂₄ Nanocage: Effects of Kinetic Trapping on the Assembly Process”, ACS Nano, 8(2), 1290-1296, (2014), DOI: 10.1021/nn404595j; 【図書】; T. Matsuno, S. Sato, H. Isobe, "Curved π-Receptors" Comprehensive Supramolecular Chemistry II, 2017, vol. 3, p. 311-328, Elsevier.; 池本晃喜，佐藤宗太，磯部寛之，"芳香環で「笊」を編む　−ナノメートルサイズのボウル分子のボトムアップ合成−" 化学, 2017, vol. 72, No. 7, p. 31-35. (Cover Picture); 磯部寛之，佐藤宗太，”炭素と水素の構造化学：ありふれた元素・分子からつくる機能性材料”，パリティ（クローズアップ）， 2017, vol. 32, No. 3, p. 39-42.; 磯部寛之，佐藤宗太，”「防虫剤」からリチウムイオン2次電池負電極”，パリティ（特集物理科学，この１年）, 2017, vol. 32, No. 1, p. 35-36.; 佐藤宗太，”サイボーグ超分子により解き明かされる生命現象〜生体分子クラスターを人工巨大分子に移植した一義構造の巨大分子”，分子研レターズ73，2016年3月; 佐藤宗太，加藤晃一，藤田誠, “生命現象の解明に挑むサイボーグ超分子　− 機能を維持したまま生体分子クラスターを人工分子に移植 −”, 月刊化学, 2015, vol. 70, No. 11, p. 31-36.; 佐藤宗太, “巨大な中空球状錯体を骨格として構築した生体分子インターフェースの開発”, Bull. Jpn. Soc. Coord. Chem., 65, 30-37 (2015), (Award Accounts).; 藤田大士，佐藤宗太，藤田　誠, “長期利用課題報告　放射光X線を用いた多成分からなる自己集合性錯体の単結晶構造解析”, SPring-8/SACLA 利用者情報 「最近の研究から」欄, 20, 130-133 (2015).; 佐藤宗太，磯部寛之, “カーボンナノチューブの筒内平滑曲面：炭素性分子ベアリングの構造化学”, 日本結晶学会誌 「最近の研究から」欄, 56, 405-410 (2015).
杉安和憲 ▲班員一覧に戻る▲: 【雑誌論文】; T. Fukui, *M. Takeuchi, *K. Sugiyasu, “Impact of a Subtle Structural Difference on the Kinetic Behavior of Metastable Supramolecular Assemblies” Polymer, 128, 311-316 (2017), DOI: 10.1016/j.polymer.2016.12.027; T. Fukui, *M. Takeuchi, *K. Sugiyasu, “Autocatalytic Time-Dependent Evolution of Metastable Two-Component Supramolecular Assemblies to Self-Sorted or Coassembled State” Sci. Rep., 7, 2425 (2017), DOI: 10.1038/s41598-017-02524-3; T. Fukui, S. Kawai, S. Fujinuma, Y. Matsushita, T. Yasuda, T. Sakurai, S. Seki, M. *Takeuchi, *K. Sugiyasu, “Control over Differentiation of a Metastable Supramolecular Assembly in One and Two Dimensions” Nature Chem., 9, 493-499, (2017), DOI: 10.1038/NCHEM.2684; M. Endo, T. Fukui, S. H. Jung, S. Yagai, M. Takeuchi, *K. Sugiyasu, “Photoregulated Living Supramolecular Polymerization of Established by Combining Energy Landscapes of Photoisomerization and Nucleation-elongation Processes”, J. Am. Chem. Soc., 138, 14347, (2016), DOI: 10.1021/jacs.6b08145; 福井智也, 大城宗一郎, 竹内正之, *杉安和憲“アミロイド繊維のように成長する超分子集合体：メカニズムの解明と時間発展プログラム”,生物物理, 2015, 55, 154-156, DOI: 10.2142/biophys.55.154; *杉安和憲,“超分子ポリマーの長さをそろえる”,現代化学, 2015, 9月号, 32-36,; C. Pan, C. Zhao, M. Takeuchi, K. Sugiyasu* “Conjugated Oligomers and Polymers Sheathed with Designer Side Chains”, Chem. Asian J.,( 2015), 10, 1820-1835, DOI: 10.1002/asia.201500452; S. Ogi, V. Stepanenko, K. Sugiyasu, M. Takeuchi, *F. Würthner “Mechanism of Self-Assembly Process and Seeded Supramolecular Polymerization of Perylene Bisimide Organogelator”, J. Am. Chem. Soc., 137, 3300-3307, (2015), DOI: 10.1021/ja511952c; S. Ogi, T. Fukui, M. Jue, *M. Takeuchi, *K. Sugiyasu “Kinetic Control over Pathway Complexity in Supramolecular Polymerization through Modulating the Energy Landscape by Rational Molecular Design”, Angew. Chem. Int. Ed., 53, 14363-14367 (2014), DOI: 10.1002/anie.201407302; *杉安和憲, 大城宗一郎, 竹内正之, “リビング超分子重合の実現” 高分子, 63, 851-854, (2014); *K. Sugiyasu, S. Ogi, M. Takeuchi, “Strapped Porphyrin-Based Polymeric Systems”, Polymer J., 46, 674-681, (2014), DOI: 10.1038/pj.2014.58; C. Pan, *K. Sugiyasu, J. Aimi, A. Sato, M. Takeuchi “Picket-Fence Polythiophene and its Diblock Copolymers that Afford Microphase Separation Comprising a Stacked and an Isolated Polythiophene Ensemble” Angew. Chem. Int. Ed., 53, 8870-8875, (2014), DOI: 10.1002/anie.201402813; D. Sahoo, K. Sugiyasu, Y. Tian, M. Takeuchi, *I. G. Schblykin “Effect of Conjugated Backbone Protection on Intrinsic and Light-Induced Fluorescence Quenching in Polythiophene” Chem. Mater., 26, 4867-4875, (2014), DOI: 10.1021/cm5021959; C. Pan, *K. Sugiyasu, *M. Takeuchi “Blending Conjugated Polymers without Phase Separation for Fluorescent Colour Tuning of Polymeric Materials through FRET” Chem. Commun., 50, 11814-11817, (2014), DOI: 10.1039/c4cc03594a
鈴木大介 ▲班員一覧に戻る▲: 【雑誌論文】; H. Minato, M. Murai, T. Watanabe, S. Matsui, M. Takizawa, *T. Kureha, *D. Suzuki, “The Deformation of Hydrogel Microspheres at the Air/Water Interface”, Chem. Commun., 54, 932-935, (2018), DOI: 10.1039/C7CC09603H; S. Minami, T. Watanabe, *D. Suzuki, *K. Urayama, “Viscoelasticity of Dense Suspensions of Thermosensitive Microgel Mixtures Undergoing Colloidal Gelation”, Soft Matter, 14, 1596-1607, (2018), DOI: 10.1039/C7SM02411H; M. Takizawa, Y. Sazuka, K. Horigome, Y. Sakurai, S. Matsui, H. Minato, T. Kureha, *D. Suzuki, “Self-organization of Soft Hydrogel Microspheres during the Evaporation of Aqueous Droplets”, Langmuir, accepted (2018), DOI: 10.1021/acs.langmuir.8b00230; T. Kureha, *D. Suzuki “Nanocomposite Microgels for the Selective Separation of Halogen Compounds from Aqueous Solution”, Langmuir, 34, 837-846, (2018), DOI: 10.1021/acs.langmuir.7b01485 (Invited article for special issue “Early Career Authors in Fundamental Colloid and Interface Science."); *Daisuke Suzuki　“Control of Spatio-temporal Structures for Polymeric Hydrogel Microspheres”, 高分子, 66, 6 (2017); *Daisuke Suzuki, Koji Horigome, Takuma Kureha, Shusuke Matsui, Takumi Watanabe “Polymeric Hydrogel Microspheres; Design Synthesis, Characterization, Assembly and Applications”, Polym. J., 49, 695-702 (2017) (Focus Review); 渡邊拓巳、*鈴木大介 “シード乳化重合による新奇複合ゲル微粒子の合成とその構造制御”, Colloid & Interface Communication, 42, 2 (2017); Seina Hiroshige, Takuma Kureha, Daichi Aoki, Jun Sawada, Daisuke Aoki, *Toshikazu Takata, and *Daisuke Suzuki “Formation of Tough Films via the Evaporation of Water from Dispersions of Elastomer Microspheres Crosslinked with Rotaxane Supramolecules”, Chem. Eur. J., 23, 8405-8408 (2017), DOI: 10.1002/chem.201702077; Shusuke Matsui, Takuma Kureha, Seina Hiroshige, Mikihiro Shibata, *Takayuki Uchihashi and *Daisuke Suzuki “Fast Adsorption of Soft Hydrogel Microspheres on Solid Surfaces in Aqueous Solution”, Angew. Chem. Intl. Ed., 56, 12146 -12149 (2017), DOI: 10.1002/anie.201705808; 10. T. Kureha, D. Aoki, S. Hiroshige, K. Iijima, D. Aoki, *T. Takata, *D. Suzuki “Decoupled Thermo- and pH-responsive Hydrogel Microspheres Cross-linked by Rotaxane Networks”, Angew. Chem. Intl. Ed., 56, 15393-15396, (2017), DOI: 10.1002/ange.201709633 (VIP (Very Important Paper)); Takuma Kureha, Yuichiro Nishizawa, *Daisuke Suzuki “Controlled Separation and Release of Organoiodine Compounds using Poly(2-methoxyethyl acrylate)-analogue Microspheres”, ACS Omega, 2, 7686-7694 (2017), DOI: 10.1021/acsomega.7b01556; T. Kureha, S. Hiroshige, S. Matsui, *D. Suzuki, “Water-immiscible Bioinert Coatings and Film Formation from Aqueous Dispersions of poly(2-methoxyethyl acrylate)Microspheres”, Colloids Surf. B, 155, 166-172, (2017), DOI: 10.1016/j.colsurfb.2017.04.001; K. Horigome, T. Ueki, *D. Suzuki, “Direct Visualization of Swollen Microgels via Scanning Electron Microscopy Using Ionic Liquids”, Polym. J., 48, 273–279, (2016), DOI: 10.1038/pj.2015.103; C. Kobayashi, T. Watanabe, K. Murata, T. Kureha, *D. Suzuki, “Localization of Polystyrene Particles on the Surface of Poly(N-isopropylacrylamide-co-methacrylic acid) Microgels Prepared by Seeded Emulsion Polymerization of Styrene”, Langmuir, 32(6):, 1429-1439, (2016), DOI: 10.1021/acs.langmuir.5b03698; S. Minami, T. Watanabe , *D. Suzuki, *K. Urayama, “Rheological Properties of Suspensions of Thermo-responsive Poly(N-isopropylacrylamide) Microgels Undergoing Volume Phase Transition”, Polym. J., 48, 1079-1086, (2016), DOI: 10.1038/pj.2016.79; T. Watanabe, C. Kobayashi, C. Song, K. Murata, T. Kureha, *D. Suzuki, “Impact of Spatial Distribution of Charged Groups in Core Poly(N-isopropyl acrylamide)-Based Microgels on the Resultant Composite Structures Prepared by Seeded Emulsion Polymerization of Styrene”, Langmuir, 32, 12760-12773, (2016), DOI: 10.1021/acs.langmuir.6b03172; T. Kureha, T. Shibamoto, S. Matsui, T. Sato, *D. Suzuki“Investigation of Changes in the Microscopic Structure of Anionic Poly(N-isopropylacrylamide-co-Acrylic acid) Microgels in the Presence of Cationic Organic Dyes toward Precisely Controlled Uptake/Release of Low-molecular-weight Chemical Compound”, Langmuir, 32, 4575-4585 (2016), DOI: 10.1021/acs.langmuir.6b00760; *鈴木大介, 呉羽拓真, “ソフトヒドロゲル微粒子の表面・内部構造と機能” 高分子1月号Vol.64「高分子科学最近の進歩」, (2016), 高分子学会; S. Matsui, T. Kureha, Y. Nagase, K. Okeyoshi, R. Yoshida, T. Sato, *D. Suzuki, “Small-angle X-ray Scattering Study on Internal Microscopic Structures of Poly(N-isopropylacrylamide-co-tris(2,2’- bipyridyl))ruthenium(II) Complex Microgels”, Langmuir, 31, 7228-7237, (2015), DOI: 10.1021/acs.langmuir.5b01164; S. Matsui, T. Kureha, K. Okeyoshi, R. Yoshida, T. Sato, *D. Suzuki “Small-angle X-ray Scattering Study on Internal Microscopic Structures of Poly(N-isopropylacrylamide-co-tris(2,2′-bipyridyl))ruthenium(II) Complex Microgels”, Langmuir, 31, 7228-7237, (2015), DOI: 10.1021/acs.langmuir.5b01164; D. Suzuki, K. Shibata, A. Tsuchida, *T. Okubo, “Thermo-sensitive Colloidal Crystals Composed of Monodisperse Colloidal Silica- and Poly (N-isopropyl acrylamide) Gel-Spheres”, Colloid Polym Sci., 293, 2763-2769, (2015), DOI: 10.1007/s00396-015-3661-1; 鈴木大介, “刺激応答性ヒドロゲル微粒子の創製と構造評価-アクリルアミド誘導体から出発する単分散ゲル微粒子の展開-” 化学と工業, 68, (2015); *K. Urayama, S. Cong, T. Saeki, S. Uratani, T. Takigawa, M. Murai, *D. Suzuki, “A Simple Feature of Yielding Behavior of Highly Dense Suspensions of Soft Micro-hydrogel Particles” Soft Matter, 10, 9486-9495 (2014), DOI: 10.1039/c4sm01841a; *D. Suzuki and C. Kobayashi “Raspberry-shaped Composite Microgel Synthesis by Seeded Emulsion Polymerization with Hydrogel Particles”Langmuir, 30(24), 7085-7092 (2014), DOI: 10.1021/la5017752; T. Kureha, T. Sato, *D. Suzuki “Relationship between Temperature-Induced Changes in Internal Microscopic Structures of Poly(N-isopropylacrylamide) Microgels and Organic Dye Uptake Behavior” Langmuir, 30(29), 8717-8725 (2014), DOI: 10.1021/la501838c; 【図書】; Daisuke Suzuki*,Takuma Kureha and Koji Horigome:“Hydrogel Microspheres”, Encyclopedia of Biocolloid and Biointerface Sciences (H. Ohshima Ed.) Wiley InterScience, (2015), ISBN:9781118485590; 鈴木大介「ゲル微粒子の自己組織化」　新版ゲルテクノロジーハンドブック, エヌ・ティー・エス、pp186-193 (2014)
平岡秀一 ▲班員一覧に戻る▲: 【雑誌論文】; *S. Hiraoka, "Unresolved Issues that Remain in Molecular Self-Assembly," Bull. Chem. Soc. Jpn., in press. (Vol. 90 Commemorative Accounts: Self-Organization), DOI: 10.1246/bcsj.20180008; S. Kai, T. Kojima, F. L. Thorp-Greenwood, M. J. Hardie, *S. Hiraoka, "How Does Chiral Self-sorting Take Place in the Formation of Homochiral Pd₆L₈ Capsules Consisting of Cyclotriveratrylene-based Chiral Tritopic Ligands?," Chem. Sci., in press, DOI: 10.1039/C8SC01062E; Y.-Y. Zhan, N. Tanaka, Y. Ozawa, T. Kojima, T. Mashiko, U. Nagashima, M. Tachikawa, *S. Hiraoka, "Importance of Molecular Meshing for the Stabilization of Solvophobic Assemblies," J. Org. Chem., in press, DOI: 10.1021/acs.joc.8b00495; Y.-Y. Zhan, T. Kojima, T. Koide, M. Tachikawa, *S. Hiraoka, "A Balance Between van der Waals and Cation-_ Interactions That Stabilizes Hydrophobic Assemblies," Chem. Eur. J., in press, DOI: 10.1002/chem.201801376; M. Nakagawa, S. Kai, T. Kojima, and *S. Hiraoka, "Energy-Landscape-Independent Kinetic Trap of Incomplete Cage in the Self-assembly of a Pd₂L₄ Cage," Chem. Eur. J., in press, (selected as Hot Paper); S. Kai, M. Nakagawa, T. Kojima, X. Li, M. Yamashina, M. Yoshizawa, *S. Hiraoka, "Steric Interaction between Neighboring Components Favors the Formation of Large Intermediates in the Self-Assembly Process of a Pd₂L₄ Capsule," Chem. Eur. J. 24, 3965-3969, (2018). (selected as Hot Paper and Cover Feature), DOI: 10.1002/chem.201705253; T. Tateishi, W. Zhu, L. H. Foianesi-Takeshige, T. Kojima, K. Ogata, *S. Hiraoka, "Self-assembly of a Pd₄L₈ Double-walled Square Partly Takes Place through the Formation of Kinetically Trapped Species," Eur. J. Inorg. Chem., 2018, 1192-1197 (2018), DOI: 10.1002/ejic.201800037; Y. Matsumura, S. Iuchi, S. Hiraoka, *H. Sato, "Chiral Effects on the Final Step of an Octahedron-Shaped Coordination Capsule Self-Assembly," Phys. Chem. Chem. Phys. 20, 7383-7386, (2018) (selected as Hot Paper and Back Cover) DOI: 10.1039/C7CP08237A; T. Tateishi, T. Kojima, *S. Hiraoka, "Multiple Pathways in the Self-assembly Process of a Pd₄L₈ Coordination Tetrahedron," Inorg. Chem., 57, 2686-2694, (2018), DOI: 10.1021/acs.inorgchem.7b03085; Y.-Y. Zhan, K. Ogata, T. Kojima, T. Koide, K. Ishii, T. Mashiko, M. Tachikawa, S. Uchiyama, *S. Hiraoka, "Hyperthermostable Cube-shaped Assembly in Water," Comms. Chem., 1, 14 (2018). DOI: DOI: 10.1038/s42004-018-0014-2; S. Kai, S. P. Maddala, T. Kojima, S. Akagi, K. Harano, E. Nakamura, *S. Hiraoka, "Flexibility of Components Alters the Self-assembly Pathway of Pd₂L₄ Coordination Cages," Dalton Trans. 47, 3258-3263 (2018) (selected as Outside Front Cover), DOI: 10.1039/C8DT00112J; N. Tanaka, Y.-Y. Zhan, Y. Ozawa, T. Kojima, T. Koide, T. Mashiko, U. Nagashima, M. Tachikawa, *S. Hiraoka, "Semi-quantitative Evaluation of Molecular Meshing by Surface Analysis with Varying Probe Radii," Chem. Commun., 54, 3335-3338, (2018), (selected as Back Cover), DOI: 10.1039/c8cc00695d; *R. Harada, T. Mashiko, M. Tachikawa, S. Hiraoka, *Y. Shigeta, "Programed Dynamical Ordering in the Self-organization Processes of a Nanocube: A Molecular Dynamics Study," Phys. Chem. Chem. Phys., 20, 9115-9122, (2018), DOI: 10.1039/C8CP00284C; T. Tateishi, T. Kojima, *S. Hiraoka, " Chiral Self-sorting Process in the Self-assembly of Homochiral Coordination Cages from Axially Chiral Ligands," Comms Chem., 1, 20, (2018), DOI: 10.1038/s42004-018-0020-4; 増子貴子，平岡秀一，長嶋雲兵，*立川仁典, "歯車状両親媒性分子からなるナノキューブの置換基効果と溶媒効果の理論的研究," J. Comp. Chem. Jpn., 17, 31-37, (2018), DOI: 10.2477/jccj.2018-0010; A. Baba, T. Kojima, *S. Hiraoka, “Quantitative Analysis of Self-Assembly Process of Hexagonal Pt(II) Macrocyclic Complexes: Effect of Solvent and Components”, Chem. Eur. J., 24, 838–847, (2018), DOI: 10.1002/chem.201702955(Hot Paper and Front Coverに選出); S. Kai, V. Marti-Centelles, Y. Sakuma, T. Mashiko, T. Kojima, U. Nagashima, M. Tachikawa, P. J. Lusby, *S. Hiraoka, “Quantitative Analysis of Self-Assembly Process of a Pd₂L₄ Cage Consisting of Rigid Ditopic Ligands”, Chem. Eur. J., 24, 663–671, (2018), DOI: 10.1002/chem.201704285; S. Kai, T. Shigeta, T. Kojima, *S. Hiraoka, “Quantitative Analysis of Self-assembly Process of a Pd₁₂L₂₄ Coordination Sphere”, Chem. Asian J., 12, 3203–3207, (2017), DOI: 10.1002/asia.201701351; S. Kai, Y. Sakuma, T. Mashiko, T. Kojima, M. Tachikawa, *S. Hiraoka, “The Effect of Solvent and Coordination Environment of Metal Source on the Self-Assembly Pathway of a Pd(II)-mediated Coordination Capsule”, Inorg. Chem., 56, 12652-12663, (2017), DOI: 10.1021/acs.inorgchem.7b02152; Y. Matsumura, S. Hiraoka, *H. Sato, “A Reaction Model on the Self-assembly Process of Octahedron-shaped Coordination Capsules”, Phys. Chem. Chem. Phys., 19, 20338–20342, (2017), DOI: 10.1039/c7cp03493h; T. Mashiko, S. Hiraoka, U. Nagashima, *M. Tachikawa, “Theoretical Study on Substituent and Solvent Effects for Nanocubes Formed with Gear-shaped Amphiphile Molecules”, Phys. Chem. Chem. Phys., 19, 1627-1631, (2017), DOI: 10.1039/C6CP07754D; V. E. Pritchard, D. R. Martir, S. Oldknow, S. Kai, S. Hiraoka, N. J. Cookson,*E. Zysman-Colman, *M. J. Hardie, “Homochiral Self-sorted and Emissive Ir^III metallo-cryptophanes”, Chem. Eur. J. 23, (2017.4), 23, 6290–6294, DOI: 10.1002/chem.201701348; *S. Hiraoka, "What Do We Learn from the Molecular Self-Assembly Process?”, Chem. Rec. 15, 1144-1147 (2015), DOI: 10.1002/tcr.201510005; A. Baba, T. Kojiam, *S. Hiraoka, "Self-Assembly Process of Dodecanuclear Pt(II)-Linked Cyclic Hexagon”, J. Am. Chem. Soc. 137, 7664-7667, (2015), DOI: 10.1021/jacs.5b04852; T. Mashiko, K. Yamada, S. Hiraoka, U. Nagashima, *M. Tachikawa, “Molecular Dynamics Simulation of Self-assembled Nanocubes in Methanol”, Mol. Simulation, 41, 845-849, (2014), DOI: 10.1080/08927022.2014.940523; Y. Tsujimoto, T. Kojima, *S. Hiraoka, “Rate-determining Step in the Self-assembly Process of Supramolecular Coordination Capsules”, Chem. Sci., 5, 4167-4172, (2014), DOI: 10.1039/C4SC01652A (Back Coverに採択); T. Mashiko, K. Yamada, T. Kojima, S. Hiraoka, U. Nagashima, *M. Tachikawa, “Molecular Dynamics and Principal Component Analysis for a Self-assembled Nanocube in Aqueous Solution” Chem. Lett., 43(3), 366-368, (2014), DOI: 10.1246/cl.130928; *T. Kojima, *S. Hiraoka, “Mesityllithium and p-(dimethylamino)Phenyllithium for the Selective Alternate Trilithiation of the Hexaphenylbenzene Framework”, Chem. Commun., 50, 10420-10423, (2014), DOI: 10.1039/C4CC04520C; *T. Kojima, *S. Hiraoka, “Selective Alternate Derivatization of the Hexaphenylbenzene Framework through a Thermodynamically Controlled Halogen Dance”, Org. Lett., 16(3), 1024-1027, (2014), DOI: 10.1021/ol500041j; J. Koseki, Y. Kita, S. Hiraoka, U. Nagashima, *M. Tachikawa, “Temperature Dependence of Self-assembled Molecular Capsules Consisting of Gear-shaped Amphiphile Molecules with Molecular Dynamics Simulations”, Int. J. Quan. Chem., 113(4), 397-400, (2013), DOI: 10.1002/qua.24108; 【図書】; 平岡秀一, “水の不思議と自己組織化”, 現代化学，6, 34–36, (2017); 平岡秀一, “溶液における分子認識と自己集合の原理：分子間相互作用”, サイエンス社 (2017) ISBN 978-4-7819-1403-9; 平岡秀一, “自己組織化の過程を調べる”, 現代化学，3, 30–35, (2015); 平岡秀一, “なぜヤモリは壁に貼りついて歩けるのか？”, じっきょう理科資料，78, 14–18, (2015)
二井勇人 ▲班員一覧に戻る▲: 【雑誌論文】; *E. Futai, S. Osawa, T. Cai, T. Fujisawa, S. Ishiura, T. Tomita, “Suppressor Mutations for Presenilin 1 Familial Alzheimer Disease Mutants Modulate γ-secretase Activities,” J. Biol. Chem., 291, 435-446, (2016), DOI: 10.1074/jbc.M114.629287; T. Onodera, E. Futai, E. Kan, N. Abe, T. Uchida, Y. Kamio, *J. Kaneko, “Phosphatidylethanolamine Plasmalogen Enhances the Inhibiting Effect of Phosphatidylethanolamine on γ-secretase activity” J. Biochem., 157, 30-309 (2015), DOI: 10.1093/jb/mvu074; 二井勇人. “膜内切断プロテアーゼによるタンパク質分解の制御機構” 日本応用酵素協会誌, 49, 17-28, (2015.03)
二木史朗 ▲班員一覧に戻る▲: 【雑誌論文】; K. Shinoda, S. Tsuji, S. Futaki, *M. Imanishi, “Nested PUF Proteins: Extending Target RNA Elements for Gene Regulation”, ChemBioChem., 19, 171, (2018), DOI: 10.1002/cbic.201700458; K. Sakagami, T. Masuda, K. Kawano, *S. Futaki, “Importance of Net Hydrophobicity in the Cellular Uptake of All-hydrocarbon Stapled Peptides,” Mol. Pharm., 15, 1332, (2018), DOI: 10.1021/acs.molpharmaceut.7b01130; *M. Imanishi, S. Tsuji, A. Suda, S. Futaki, “Detection of N⁶-methyladenosine Based on the Methyl-sensitivity of MazF RNA Endonuclease,”Chem. Commun., 53, 12930, (2017), DOI: 10.1039/c7cc07699a; A. Oku, M. Imanishi, D. Noshiro, T. Murayama, T. Takeuchi, I. Nakase, *S. Futaki, “Use of Calmodulin EF-hand Peptides as Ca²⁺-switchable Recognition Tags”, Biopolymers, Pept. Sci., 108, (2017), DOI: 10.1002/bip.22937; *I. Nakase, K. Noguchi, I. Fujii, S. Futaki “Vectorization of Biomacromolecules into Cells Using Extracellular Vesicles with Enhanced Internalization Induced by Macropinocytosis" Sci. Rep. 6, 34937 (2016) DOI: 10.1038/srep34937; *I. Nakase, K. Noguchi, A. Aoki, T. Takatani-Nakase, I. Fujii, S. Futaki “Arginine-rich Cell-penetrating Peptide-modified Extracellular Vesicles for Active Macropinocytosis Induction” Sci. Rep., 7, 1991 (2017) DOI: 10.1038/s41598-017-02014-6; M. Akishiba, T. Takeuchi, Y. Kawaguchi, K. Sakamoto, H. Yu, I. Nakase, T. Takatani-Nakase, F. Madani, A. Gräslund, *S. Futaki “Cytosolic Antibody Delivery by Lipid-sensitive Endosomolytic Peptide” Nat. Chem. 9, 751 (2017) DOI: 10.1038/NCHEM.2779; T. Murayama, T. Masuda, S. Afonin, K. Kawano, T. Takatani-Nakase, H. Ida, Y. Takahashi, T. Fukuma, A. S. Ulrich, *S. Futaki, Angew. Chem. Int. Ed., 129, 7752 (2017) DOI: 10.1002/anie.201703578 (German version: DOI: 10.1002/ange.201703578); *二木史朗 “アルギニンに富む膜透過ペプチドの細胞内移行” 生化学, 89(1), 8–14 (2017) DOI: 10.14952/SEIKAGAKU.2017.890008; *S. Futaki, I. Nakase “Cell-Surface Interactions on Arginine-Rich Cell-Penetrating Peptides Allow for Multiplex Modes of Internalization” Acc. Chem. Res., 50, 2449 (2017) DOI: 10.1021/acs.accounts.7b00221; K. Motoyama, R. Nishiyama, Y. Maeda, T. Higashi, Y. Kawaguchi, S. Futaki, Yoichi Ishitsuka, Y. Kondo, T. Irie, T. Era, *H. Arima “Cholesterol-lowering Effect of Octaarginine-appended β-Cyclodextrin in Npc1-trap-CHO Cells” Biol. Pharm. Bull. 39, 1823 (2016) DOI: 10.1248/bpb.b16-00369; *I. Nakase, N. Ueno, M. Katayama, K. Noguchi, T. Takatani-Nakase, N. B. Kobayashi, T. Yoshida, I. Fujii, S. Futaki “Receptor Clustering and Activation by Multivalent Interaction through Recognition Peptides Presented on Exosomes” Chem. Commun., 53, 317 (2016) DOI: 10.1039/C6CC06719K; C. M. Backlund, F. Sgolastra, R. Otter, L. Minter, T. Takeuchi, S. Futaki, *G. N. Tew “Increased Hydrophobic Block Length of PTDMs Promotes Protein Internalization” Polym. Chem., 7, 7514 (2016) DOI: 10.1039/C6PY01615D; Y. Kawaguchi, T. Takeuchi, K. Kuwata, J. Chiba, Y. Hatanaka, I. Nakase, *S. Futaki. “Syndecan-4 Is a Receptor for Clathrin-Mediated Endocytosis of Arginine-Rich Cell-Penetrating Peptides,” Bioconjug. Chem.. 27, 1119 (2016) DOI: 10.1021/acs.bioconjchem.6b00082; C. M, Backlund, T. Takeuchi, S. Futaki, *G. N. Tew. “Relating structure and internalization for ROMP-based protein mimics,” Biochim. Biophys. Acta, 1858, 1443-1450. DOI: 10.1016/j.bbamem.2016.03.024; R. Miyajima, Y. Tsuda, T. Inokuma, A. Shigenaga, M. Imanishi, S. Futaki, *A. Otaka, “Preparation of Peptide Thioesters from Naturally Occurring Sequences Using Reaction Sequence Consisting of Regioselective S-cyanylation and Hydrazinolysis,” Biopolymers, 106(4), 531-46, (2015), DOI: 10.1002/bip.22757; T. Murayama, S. Pujals, H. Hirose, I. Nakase, *S. Futaki “Effect of Amino Acid Substitution in the Hydrophobic Face of Amphiphilic Peptides on Membrane Curvature and Perturbation: N-Terminal Helix Derived From Adenovirus Internal Protein VI As a Model,” Biopolymers, 106 ,430-439, (2015), DOI: 10.1002/bip.22797; *二木史朗, “細胞内・遺伝子デリバリー,” 日本防菌防黴学会誌, 43, 259 (2015); Nakase, Y. Kawaguchi, M. Nomizu, *S. Futaki “Cellular Uptake of Arginine-Rich Cell-Penetrating Peptides and the Contribution of Membrane-Associated Proteoglycans,” Trends Glycosci. Glycotech., 27, 81 (2015), DOI: 10.4052/tigg.1420.1; I. Nakase, T. Takeuchi, *S. Futaki, “Cell Penetrating Peptides for Chemical Biological Studies”, Methods Mol. Biol., 1324, 387-396, (2015), DOI: 10.1007/978-1-4939-2806-4_26; Y. Kuroda, N. *Kato-Kogoe, E. Tasaki, M. Yuasa-Sunagawa, K. Yamanegi, K. Nakasyo, I. Nakase, S. Futaki, Y. Tohyama, M. Hirose, “Suppressive Effect of Membrane-permeable Peptides Derived from Autophosphorylation Sites of the IGF-1 Receptor on Breast Cancer Cells”, Eur. J. Pharmacol., 765, EJP41801, (2015), DOI: 10.1016/j.ejphar.2015.08.004; T. Takeuchi, M. Suzuki, N. Fujikake, H. A. Popiel, H. Kikuchi, S. Futaki, K. Wada, *Y. Nagai, “Intercellular Chaperone Transmission via Exosomes Contributes to Maintenance of Protein Homeostasis at the Organismal Level”, Proc. Natl. Acad. Sci. U.S.A., 112, E2497-2506, (2015), DOI: 10.1073/pnas.1412651112; *I. Nakase, S. Futaki“Combined Treatment with a pH-sensitive Fusogenic Peptide and Cationic Lipids Achieves Enhanced Cytosolic Delivery of Exosomes,” Sci. Rep., 5,10112, (2015), DOI: 10.1038/srep10112; *S. Futaki, T. Murayama, S. Pujals, S. Katayama, H. Hirose, H. Miyamae, I. Nakase, “Membrane Translocation of Arginine-rich Peptides and the Effect of Membrane Curvature”, Peptide Science 2014 (Ed., A. Otaka), The Japanese Peptide Society, pp 67-68 , 2015, ISBN 978-4-931541-15-3; T. Murayama, S. Pujals, *S. Futaki,“Curvature Sensitive Membrane Disruption by Amphypathic Peptides Derived from Adenovirus Protein VI”, Peptide Science 2014 (Ed., A. Otaka), The Japanese Peptide Society, pp 151-152 , 2015, ISBN 978-4-931541-15-3; Y. Azuma, T. Kükenshöner, G. Ma, J. Yasunaga, M. Imanishi, G. Tanaka, I. Nakase, T. Maruno, Y. Kobayashi, *K. M. Arndt, *M. Matsuoka, *S. Futaki. “Controlling Leucine-zipper Partner Recognition in Cells Through Modification of a-g Interactions”, Chem. Commun., 50, 6364-6867, (2014), DOI: 10.1039/c4cc00555d; *I. Nakase, K. Osaki, G. Tanaka, A. Utani, *S. Futaki. “Molecular Interplays Involved in the Cellular Uptake of Octaarginine on Cell Surfaces and the Importance of Syndecan-4 Cytoplasmic V Domain for the Activation of Protein Kinase Cα”. Biochem. Biophys. Res. Commun., 446, 857-862, (2014), DOI: 10.1016/j.bbrc.2014.03.018; *T. Takeuchi, H. A. Popiel, S. Futaki, K. Wada, *Y. Nagai. “Peptide-based Therapeutic Approaches for Treatment of the Polyglutamine Diseases”, Curr. Med. Chem., 21, 2575-2582, (2014), DOI: 10.2174/0929867321666140217124038; *佐々木茂貴, 二木史朗. “薬学における生命指向型化学 (生命の謎を探る化学の力)” 薬学雑誌, 134, 499-500, (2014), DOI: 10.1248/yakushi.13-00251-F; 【図書】; I. Nakase, T. Takeuchi, S. Futaki, “Cell Penetrating Peptides for Chemical Biological Studies”, In Cell-penetrating Peptides: Methods and Protocols, Ülo Langel Eds. Humana Press, Springer, New York, pp 387-396, (2015); 二木史朗 “膜透過ペプチドを利用する細胞内デリバリー”,　遺伝子医学MOOK別冊次世代ペプチド医薬創製, 赤路健一編, メディカルドゥ, 大阪, pp68-72, (2014)
芳坂貴弘 ▲班員一覧に戻る▲: 【雑誌論文】; Y. Mori, *H. Okumura, T. Watanabe, T. Hohsaka, “Antigen-dependent Fluorescence Response of Anti-c-Myc Quenchbody Studied by Molecular Dynamics Simulations”, Chem. Phys. Lett., 698, 223-226,(2018), DOI: 10.1016/j.cplett.2018.03.011; M.Yamaguchi, E. Ohta, T. Muto, T. Watanabe, *T. Hohsaka, Y. Yamazaki, H. Kamikubo, *M. Kataoka, “Statistical description of the denatured structure of a single protein, staphylococcal nuclease, by FRET analysis”, Biophys. Rev., 10, 145-152,(2018),, DOI: 10.1007/s12551-017-0334-y; S. Ahmed, T. Nakaji-Hirabayashi, T. Watanabe, T. Hohsaka, *K. Matsumura, “Freezing Assisted Gene Delivery Combined with Polyampholyte Nanocarriers”, ACS Biomater. Sci. Eng., 3, 1677-1689, (2017) DOI: 10.1021/acsbiomaterials.7b00176; K. P. Huynh Nhat, T. Watanabe, K. Yoshikoshi, *T. Hohsaka, “Antibody-based Fluorescent and Fluorescent Ratiometric Indicators for Detection of Phosphotyrosine”, J. Biosci. Bioeng., 122, 146-154, (2016), DOI: 10.1016/j.jbiosc.2016.01.010; K. Yoshikoshi, T. Watanabe, *T. Hohsaka, “Double-fluorescent-labeled Single-chain Antibodies Showing Antigen-dependent Fluorescence Ratio Change”, Bull. Chem. Soc. Jpn., 89, 573-580, (2016), DOI: 10.1246/bcsj.20150384; A. Yamaguchi, T. Matsuda, K. Ohtake T. Yanagisawa, S. Yokoyama, Y. Fujiwara, T. Watanabe, *T. Hohsaka, *K. Sakamoto, “Incorporation of a Doubly Functionalized Synthetic Amino Acid into Proteins for Creating Chemical and Light-Induced Conjugates”, Bioconjugate Chem., 27, 198–206, (2016), DOI: 10.1021/acs.bioconjchem.5b00602; A. Uyeda, T. Watanabe, Y. Kato, H. Watanabe, T. Yomo, *T. Hohsaka, *T. Matsuura“Liposome-Based in Vitro Evolution of Aminoacyl-tRNA Synthetase for Enhanced Pyrrolysine Derivative Incorporation”, ChemBioChem. ,16, 1797-1802, (2015), DOI: 10.1002/cbic.201500174; T. Ezure, K. Nanatani, Y. Sato, S. Suzuki, K. Aizawa, S. Souma, M. Ito, T. Hohsaka, G. von Heijine, T. Utsumi, K. Abe, E. Ando, N. Uozumi*, “A Cell-free Translocation System Using Extracts of Cultured Insect Cells to Yield Functional Membrane Proteins”, PLoS One., 9, e112874 , (2014), DOI: 10.1371/journal.pone.0112874; Y. Ito, *T. Hohsaka, “Incorporation of Fluorescent Nonnatural Amino Acid into Sialic Acid-Binding Lectin for Fluorescence Detection of Ligand-Binding”, Bull. Chem. Soc. Jpn., 86(6), 729-735, (2013), DOI: 10.1246/bcsj.20120345; T. Matsubara, K. Iijima, T. Watanabe, T. Hohsaka, *T. Sato, “Incorporation of Glycosylated Amino Acid into Protein by an in Vitro Translation System”, Bioorg. Med. Chem. Lett., 23(20), 5634-5636, (2013), DOI: 10.1016/j.bmcl.2013.08.035; 【図書】; “非天然アミノ酸の導入”, 人工細胞の創製とその応用（植田充美監修）1-5章, 2017, ISBN 978-4-7813-1233-0; “揺らぎ・ダイナミクスと生体機能: 物理化学的視点から見た生体分子” (DOJIN BIOSCIENCE SERIES)第6章「変異導入法」, (2013), 寺嶋正秀編、（化学同人,京都）ISBN:9784759815108
松浦友亮 ▲班員一覧に戻る▲: 【雑誌論文】; M. Iwamoto, M.A. Elfaramawy, M. Yamatake, T. Matsuura, S. Oiki,“Concurrent In Vitro Synthesis and Functional Detection of Nascent Activity of the KcsA Channel under a Membrane Potential”, ACS Synth Biol, 7, 1004-1011, (2018), DOI: 10.1021/acssynbio.7b00454; *T. Matsuura, N. Tanimura, K. Hosoda, Y. Yomo, Y. *Shimizu, “Reaction Dynamics Analysis of a Reconstituted Escherichia coli Protein Translation System by Computational Modeling”, Proc. Natl. Acad. Sci. U S A, 114, E1336-E1344, (2017), DOI: 10.1073/pnas.1615351114; A. Uyeda, S. Nakayama, Y. Kato, H. Watanabe, T. Matsuura, (2016), “Construction of an in vitro Gene Screening System of the E. coli EmrE Transporter Using Liposome Display”, Anal. Chem., 88, 12028-12035, DOI: 10.1021/acs.analchem.6b02308; N. Ohta, Y. Kato, H. Watanabe, H. Mori, *T. *Matsuura, (2016), “In vitro Membrane Protein Synthesis Inside Sec Translocon-reconstituted Cell-sized Liposomes”, Sci, Rep., 6, 36466, DOI: 10.1038/srep36466; A. Uyeda, T. Watanabe, Y. Kato, H. Watanabe, T. Yomo, T. Hohsaka, *T. Matsuura, “Liposome-based in vitro Evolution of Aminoacyl-tRNA Synthetase for Enhanced Pyrrolysine Derivative Incorporation”, Chembiochem. 16, 1797-802, (2015), DOI: 10.1002/cbic.201500174; S. Fujii, T. Matsuura, *T. Yomo, “Membrane Curvature Affects the Formation of alpha-Hemolysin Nanopores”, ACS Chem Biol, 10, 1694-1701, (2015), DOI: 10.1021/acschembio.5b00107; A.Uyeda, T. Watanabe, Y. Kato, H. Watanabe, T. Yomo, *T. Hohsaka, *T. Matsuura, “Liposome-Based in Vitro Evolution of Aminoacyl-tRNA Synthetase for Enhanced Pyrrolysine Derivative Incorporation”, Chembiochem, 16, 1797-1802, (2015), DOI: 110.1002/cbic.201500174; S. Fujii, T. Matsuura, *T.Yomo, “In Vitro Directed Evolution of Alpha-hemolysin by Liposome Display”, Biophysics 11, 67-72, (2015), DOI: 10.2142/biophysics.11.67; K.Usui, N.Ichihashi, Y. Kazuta, T. Matsuura, *T.Yomo, “Effects of Ribosomes on the Kinetics of Qbeta Replication”, FEBS Lett., 588, 117-123, (2014), DOI: 10.1016/j.febslet.2013.11.018; K.Uno, T.Sunami, N.Ichihashi, Y.Kazuta, T.Matsuura, *T.Yomo, “The Evolutionary Enhancement of Genotype-phenotype Linkages in the Presence of Multiple Copies of Genetic Material”, Chembiochem, 15, 2281-2288, (2014), DOI: 10.1002/cbic.201402299; Y. Kazuta, T. Matsuura, N. Ichihashi, *T. Yomo, “Synthesis of Milligram Quantities of Proteins Using a Reconstituted in Vitro Protein Synthesis System”, J. Biosci. Bioeng., 118, 554-557 (2014), DOI: 10.1016/j.jbiosc.2014.04.019; H. Soga, S. Fujii, T. Yomo, Y. Kato, H. Watanabe, *T. Matsuura, “In Vitro Membrane Protein Synthesis Inside Cell-sized Vesicles Reveals the Dependence of Membrane Protein Integration on Vesicle Volume”, ACS Synth. Biol., 3, 372-379 (2014), DOI: 10.1021/sb400094c; T. Okano, T. Matsuura, H. Suzuki, *T. Yomo, “Cell-free Protein Synthesis in a Microchamber Revealed the Presence of an Optimum Compartment Volume for High-order Reactions”, ACS Synth. Biol.,3, 347-352 (2014), DOI: 10.1021/sb400087e; K. Nishimura, T. Matsuura, T. Sunami, S. Fujii, K. Nishimura, H. Suzuki, *T. Yomo, “Identification of Giant Unilamellar Vesicles with Permeability to Small Charged Molecules”, RSC. Advances, 4, 35224, (2014), DOI: 10.1039/c4ra05332j; S. Fujii, T. Matsuura, T. Sunami, T. Nishikawa, Y. Kazuta, *T. Yomo, “Liposome Display for in Vitro Selection and Evolution of Membrane Proteins”, Nature protocols, 9, 1578-1591 (2014), DOI: 10.1038/nprot.2014.107; 【図書】; 松浦友亮 (2017) セルフリータンパク質合成系を用いた進化分子工学技術の開発, 日本生物工学会誌, 95, 121-126; 松浦友亮 (2016) ネオバイオ分子創生を目指した配列空間探索, 日本生物工学会誌, 94, 471-472
三宅弘之 ▲班員一覧に戻る▲: 【雑誌論文】; T. Sagami, Y. O. Tahara, M. Miyata, H. Miyake, *S. Shinoda, “Luminescence Sensing of Weakly-Hydrated Anions in Aqueous Solution by Self-assembled Europium(III) Complexes”, Chem. Commun., 53, 3967-3970, (2017), DOI: 10.1039/C7CC00477J; T. Sagami, S. Umemoto, Y. O Tahara, M. Miyata, Y. Yonamine, D. Ishikawa, T. Mori, K. Ariga, H. Miyake, *S. Shinoda, “pH-Responsive Cotton Effects in the d-d Transition Band of Self-Assembling Copper(II) Complexes with a Cholesteryl-armed Ligand”, Bull. Chem. Soc. Jpn., 90, 739-745 (2017), DOI: 10.1246/bcsj.20170054; J. Gregoliński, M. Hikita, T. Sakamoto, H. Sugimoto, H. Tsukube, *H. Miyake, “Redox-Triggered Helicity Inversion in Chiral Cobalt Complexes in Combination with H⁺ and NO₃^– Stimuli”, Inorg. Chem., 55, 633-643, (2016), DOI: 10.1021/acs.inorgchem.5b01902; 相模拓哉、篠田哲史、*三宅弘之, “希土類錯体の形態制御と発光特性”, 化学工業－特集／希土類の機能発現と応用, 66, 696-702, (2015); *K. Singh, P. Kaur, *H. Miyake, H. Tsukube, “Supramolecular Chemistry Strategies for Naked-eye Detection and Sensing”, In Synergy in Supramolecular Chemistry, 301–320, (2014), T. Nabeshima, ed., CRC Press. ISBN 9781466595026; *H. Miyake, “Supramolecular Chirality in Dynamic Coordination Chemistry”, Symmetry, 6, 880-895, (2014), DOI: 10.3390/sym6040880; 【図書】; *K. Singh, P. Kaur, *H. Miyake, H. Tsukube, “Supramolecular chemistry strategies for naked-eye detection and sensing”, Synergy in Supramolecular Chemistry, (ed) T. Nabeshima, CRC Press. ISBN 9781466595026

公募班A03：動的秩序の展開

稲垣直之 ▲班員一覧に戻る▲: 【雑誌論文】; K. Abe, H. Katsuno, M. Toriyama, K. Baba, T. Mori, T. Hakoshima Y. Kanemura, R. Watanabe, *N. Inagaki, “Grip and slip of L1-CAM on Adhesive Substrates Direct Growth Cone Haptotaxis”, Proc. Natl. Acad. Sci. USA, 115, 2764-2769, (2018), DOI: 10.1073/pnas.1711667115; *N. Inagaki, H. Katsuno, “Actin Waves: Origin of Cell Polarization and Migration?” Trends Cell Biol., 27, 515-526, (2017), DOI: 10.1016/j.tcb.2017.02.003; Y. Higashiguchi, K. Katsuta, T. Minegishi, S. Yonemura, A. Urasaki, *N. Inagaki, “Identification of a Shootin1 Isoform Expressed in Peripheral Tissues”, Cell Tissue Res., 366, 75-87, (2016), DOI: 10.1007/s00441-016-2415-9; K. Tahara, M. Tsukui,T. Maeno, N. Inagaki, *J. Kikuchi, “Efficient Solid-Phase Gene Delivery Mediated by Cerasome: Effect of Reverse Procedure on Transfection Performances in Comparison with Solution-Based Method”, Chem. Lett., 44(12), 1643-1645, (2015), DOI: 10.1246/cl.150777; Y. Kubo, K. Baba, M. Toriyama, Y. Minegishi, T. Sugiura, S. Kozawa, K. Ikeda, *N. Inagaki, “Shootin1-cortactin interaction mediates signal-force transduction for axon outgrowth”, J. Cell Biol. 210, 663-676, (2015),DOI: 10.1083/jcb.201505011; H. Katsuno, M. Toriyama, Y. Hosokawa, K. Mizuno, K. Ikeda, Y. Sakumura, *N. Inagaki, “Actin migration driven by directional assembly and disassembly of membrane anchored actin filaments”, Cell Reports, 12, 648-660, (2015), DOI: 10.1016/j.celrep.2015.06.048; *加藤晃一, *稲垣直之, “離合集散が織りなす生命分子機能の研究フロンティア”, 実験医学, 33, 1316-1320 (2015); 馬場健太郎, 浦崎明宏, 稲垣直之,　ラージゲルプロテオミクスを基盤とした神経細胞の軸索形成とガイダンスの解析,　電気泳動　58, 49-52 (2014); S. Kozawa, Y. Sakumura, M. Toriyama, N. Inagaki, *K. Ikeda, “Bayesian Cell Force Estimation Considering Force Directions”, Neural Process Lett., 41, 191-200, (2013), DOI: 10.1007/s11063-013-9320-y; K. Tahara, T. Moriuchi, M. Tsukui, A. Hirota, T. Maeno, M. Toriyama, N. Inagaki, *J. Kikuchi. “Ceramic Coating of Liposomal Gene Carrier for Minimizing Toxicity to Primary Hippocampal Neurons”, Chem. Lett., 42(10), 1265-1267, (2013), DOI: 10.1246/cl.130541
内山進 ▲班員一覧に戻る▲: 【雑誌論文】; Y. Zhan, K. Ogata, T. Kojima, T. Koide, K. Ishii, T. Mashiko, M. Tachikawa, S. Uchiyama, *S. Hiraoka, "Hyperthermostable Cube-shaped Assembly in Water", Commun. Chem., 1, 1-14, (2018), DOI: 10.1038/s42004-018-0014-2; R. Kim, S. Kanamaru, T. Mikawa, C. Pr思ost, K. Ishii, K. Ito, S. Uchiyama, M. Oda, H. Iwasaki, S. K Kim, *M. Takahashi、"RecA Requires Two Molecules of Mg2+ ions for its Optimal Strand Exchange Activity in Vitro", Nucleic Acids Res., 46: 2548-2559, (2018), DOI: 10.1093/nar/gky048; T. Maruno, H. Watanabe, S. Yoneda, T. Uchihashi, S. Adachi K. Arai, T. Sawaguchi, * S. Uchiyama, "Sweeping of Adsorbed Therapeutic Protein on Prefillable Syringes Promotes Micron Aggregate Generation", J. Pharm. Sci., in press, (2018), DOI: 10.1016/j.xphs.2018.01.021; 石井健太郎、*内山　進, "タンパク質のネイティブ質量分析—動的なタンパク質複合体形成機構の解明にむけて—,", ぶんせき, 10, 472-475, (2017); S. Yanaka, T. Yamazaki, R. Yogo, M. Noda, S. Uchiyama, H. Yagi, *K. Kato, “NMR Detection of Semi-Specific Antibody Interactions in Serum Environments”, Molecules, 22, 275-286, (2018),DOI: 10.3390/molecules22101619; K. Ishii, M. Zhou, *S. Uchiyama, “Native mass spectrometry for understanding dynamic protein complex”, Biochim Biophys Acta General Subjects, 1862, 275-286, (2018),DOI: 10.1016/j.bbagen.2017.09.019; Q. Wang, R. Marchetti, S. Prisic, K. Ishii, Y. Arai, I. Ohta, S. Inuki, S. Uchiyama, A. Silipo, A. Molinaro, R. N. Husson, K. Fukase, *Y. Fujimoto, “A Comprehensive Study of the Interaction between Peptidoglycan Fragments and the Extracellular Domain of Mycobacterium tuberculosis Ser/Thr Kinase PknB”, ChemBioChem, 18, 2094-2098, (2017),DOI: 10.1002/cbic.201700385; *A. Ishii-Watabe, H. Shibata, A. Harazono, M. Hyuga, M. Kiyoshi, S. Saitoh, T. Iwura, T. Torisu, Y. Goda, S. Uchiyama, “Recent Topics of Research in the Characterization and Quality Control of Biopharmaceuticals in Japan”, J. Pharm. Sci., 106, 3431-3437, (2017),DOI: 10.1016/j.xphs.2017.07.024; R. Phengchat, H. Takata, *S. Uchiyama, K. Fukui, “Calcium depletion destabilises kinetochore fibres by the removal of CENP-F from the kinetochore”, Sci. Rep., 7, 7335, (2017),DOI: 10.1038/s41598-017-07777-6; R. Poonperm, H. Takata, S. Uchiyama, *K. Fukui, “Interdependency and phosphorylation of KIF4 and condensin I are essential for organization of chromosome scaffold”, PloS One., 12, e0183298, (2017),DOI: 10.1371/journal.pone.0183298; N. Shinozaki, R. Hashimoto, K. Fukui, *S. Uchiyama, “Efficient generation of single domain antibodies with high affinities and enhanced thermal stabilities”, Sci. Rep., 7, 5794, (2017),DOI: 10.1038/s41598-017-06277-x; T. Torisu, T. Maruno, Y. Hamaji, T. Ohkubo, *S. Uchiyama, “Synergistic Effect of Cavitation and Agitation on Protein Aggregation”, J. Pharm. Sci., 106, 521-529, (2017),DOI: 10.1016/j.xphs.2016.10.015; T. Torisu, T. Maruno, S. Yoneda, Y. Hamaji, S. Honda, *T. Ohkubo, *S. Uchiyama, “Friability Testing as a New Stress-Stability Assay for Biopharmaceuticals”, J. Pharm. Sci., 106, 2966-2978, (2017),DOI: 10.1016/j.xphs.2017.05.035; E. Krayukhina, M. Noda, K. Ishii, T. Maruno, H. Wakabayashi, M. Tada, T. Suzuki, A. Ishii-Watabe, M. Kato, *S. Uchiyama, “Analytical Ultracentrifugation with Fluorescence Detection System Reveals Differences in Complex Formation between Recombinant Human TNF and Different Biological TNF Antagonists in Various Environments,”, MAbs., 9, 664-679, (2017),DOI: 10.1080/19420862.2017.1297909; Z. Zhang, U. Ohto, T. Shibata, E. Krayukhina, M. Taoka, Y. Yamauchi, H. Tanji, T. Isobe, S. Uchiyama, K. Miyake, *T. Shimizu, “Structural Analysis Reveals that Toll-like Receptor 7 Is a Dual Receptor for Guanosine and Single-Stranded RNA,” Immunity. 45, 737-748, (2016), DOI: 10.1016/j.immuni.2016.09.011; S. Toma-Fukai, J. D. Kim, K. E. Park, N. Kuwabara, N. Shimizu, E. Krayukhina, S. Uchiyama, A. Fukamizu, *T. Shimizu, “Novel Helical Assembly in Arginine Methyltransferase 8,” J. Mol.Biol., 428, 1197-1208, (2016), DOI: 10.1016/j.jmb.2016.02.007; *M. Sugiyama, H. Yagi, K. Ishii, L. Porcar, A. Martel, K. Oyama, M. Noda, Y. Yunoki, R. Murakami, R. Inoue, N. Sato, Y. Oba, K. Terauchi, S. Uchiyama, *K. Kato, “Structural Characterization of the Circadian Clock Protein Complex Composed of KaiB and KaiC by Inverse Contrast-matching Small-angle Neutron Scattering,” Sci Rep., 6, 35567, (2016), DOI: 10.1038/srep35567; S. Seetaha, M. Yagi-Utsumi, T. Yamaguchi, K. Ishii, S. Hannongbua, *K. Choowongkomon, *K. Kato, “Application of Site-Specific Spin Labeling for NMR Detecting Inhibitor-Induced Conformational Change of HIV-1 Reverse Transcriptase,” ChemMedChem. 11, 363-366, (2016), DOI: 10.1002/cmdc.201500554; *T. Satoh, T. Toshimori, M. Noda, S. Uchiyama, *K. Kato, “Interaction Mode between Catalytic and Regulatory Subunits in Glucosidase II Involved in ER Glycoprotein Quality Control,” Protein Sci., 25, 2095-2101, (2016), DOI: 10.1002/pro.3031; R. Phengchat, *H. Takata, K. Morii, N. Inada, H. Murakoshi, S. Uchiyama, *K. Fukui,“Calcium Ions Function as a Booster of Chromosome Condensation,” Sci. Rep., 6, 38281, (2016), DOI: 10.1038/srep38281; *U. Ohto, H. Ishida, E. Krayukhina, S. Uchiyama, N. Inoue, *T. Shimizu, “Structure of IZUMO1-JUNO Reveals Sperm-oocyte Recognition During Mammalian Fertilization”, Nature, 534, 566-569, (2016), DOI: 10.1038/nature18596; *M. Oda, Y. Tanabe, M. Noda, S. Inaba, E. Krayukhina, H. Fukada, S. Uchiyama, “Structural and Binding Properties of Laminarin Revealed by Analytical Ultracentrifugation and Calorimetric Analyses”, Carbohydr Res., 431, 33-38, (2016), DOI: 10.1016/j.carres.2016.05.008; E. Nango, S. Akiyama, S. Maki-Yonekura, Y. Ashikawa, Y. Kusakabe, E. Krayukhina, T. Maruno, S. Uchiyama, N. Nuemket, K. Yonekura, M. Shimizu, N. Atsumi, N. Yasui, T. Hikima, M. Yamamoto, Y. Kobayashi, *A. Yamashita, “Taste Substance Binding Elicits Conformational Change of Taste Receptor T1r Heterodimer Extracellular Domains,” Sci Rep., 6, 25745, (2016), DOI: 10.1038/srep25745; A.Masato, F. Kiichi, *S. Uchiyama, “Suppression of Methionine Oxidation of a Pharmaceutical Antibody Stored in a Polymer-Based Syringe,” J Pharm. Sci., 105, 623-629, (2016), DOI: 10.1002/jps.24675; *Y. Kabe, T. Nakane, I. Koike, T. Yamamoto, Y. Sugiura, E. Harada, K. Sugase, T. Shimamura, M. Ohmura, K. Muraoka, A. Yamamoto, T. Uchida, S. Iwata, Y. Yamaguchi, E. Krayukhina, M. Noda, H. Handa, K. Ishimori, S. Uchiyama, *T. Kobayashi, *M. Suematsu, “Haem-dependent Dimerization of PGRMC1/Sigma-2 Receptor Facilitates Cancer Proliferation and Chemoresistance,” Nat. Commun., 7, 11030, (2016), DOI: 10.1038/ncomms11030; *R. Inoue, T. Takata, N. Fujii, K. Ishii, S. Uchiyama, N. Sato, Y. Oba, K. Wood, K. Kato, N. Fujii, *M. Sugiyama, “New Insight into the Dynamical System of AlphaB-crystallin Oligomers,” Sci Rep., 6, 29208, (2016), DOI: 10.1038/srep29208; S. Uchiyama, “Biophysical Characterization of Biopharmaceuticals, Including Antibody Drugs”, Yakugaku Zasshi, 136, 443-448, (2016), DOI: 10.1248/yakushi.15-00236-2; R. Thammaporn, K. Ishii, M. Yagi-Utsumi, S. Uchiyama, *S. Hannongbua, *K. Kato, “Mass Spectrometric Characterization of HIV-1 Reverse Transcriptase Interactions with Non-nucleoside Reverse Transcriptase Inhibitors”, Biol Pharm Bull.,39(3), 450-4, (2016), DOI: 10.1248/bpb.b15-00880; K. Ishii, M. Noda, S. Uchiyama, “Mass Spectrometric Analysis of Protein-ligand Interaction”Biophys. Physicobiology, 13, 87-95 (2016), DOI: 10.2142/biophysico.13.0_87; A. Fujikawa, A.Nagahira, H. Sugawara, K. Ishii, S. Imajo, M. Matsumoto, K. Kuboyama, R. Suzuki, N. Tanga, M. Noda, S. Uchiyama, T. Tomoo, A. Ogata, M. Masumura, *M. Noda, “Small-molecule Inhibition of PTPRZ Reduces Tumor Growth in a Rat Model of Glioblastoma”, Sci Rep., 6, 20473, (2015), DOI: 10.1038/srep20473; K. Ishii, M. Noda, H. Yagi, R. Thammaporn, S. Seetaha, T. Satoh, *K. Kato, *S. Uchiyama, “Disassembly of the Self-assembled, Double-ring Structure of Proteasome α7 Homo-tetradecamer by α6”, Sci Rep.,5, 18167, (2015), DOI: 10.1038/srep18167; S. Uchiyama, K. Kawahara, Y. Hosokawa, S. Fukakusa, H. Oki, S. Nakamura, Y. Kojima, M. Noda R. Takino, Y. Miyahara, T. Maruno, Y. Kobayashi, T. Ohkubo, K. Fukui, “Structural Basis for Dimer Formation of Human Condensin Structural Maintenance of Chromosome Proteins and Its Implications for Single-stranded DNA Recognition”,J Biol Chem., 290(49), 29461-77, (2015), DOI: 10.1074/jbc.M115.670794; H. Zhao, S. Uchiyama, *P. Schuck, “Multilaboratory Comparison of Calibration Accuracy and the Performance of External References in Analytical Ultracentrifugation”, PLoS ONE, 10, e0126420, (2015), DOI: 10.1371/journal.pone.0126420.; R. Poonperm, H. Takata, T. Hamano, A. Matsuda, S. Uchiyama, Y. Hiraoka, *K.Fukui, “Chromosome Scaffold is a Double-Stranded Assembly of Scaffold Proteins”, Sci. Rep., 5, 11916, (2015), DOI: 10.1038/srep11916.; *S. Kita, *H. Matsubara, Y. Kasai, T. Tamaoki, Y. Okabe, H. Fukuhara, J. Kamishikiryo, E. Krayukhina, S. Uchiyama, T. Ose, K. Kuroki, K. Maenaka, “Crystal Structure of Extracellular Domain of Human Lectin-like Transcript 1 (LLT1), the Ligand for Natural Killer Receptor-P1A”, Eur. J. Immunol., 45(6), 1605-13, (2015), DOI: 10.1002/eji.201545509.; S. Harada, Y. Hiromori, S. Nakamura, K.. Kawahara, S.. Fukakusa, T. Maruno, M. Noda, S. Uchiyama, K.Fukui, J. Nishikawa, H. Nagase, Y. Kobayashi, *T. Yoshida, T. Ohkubo, *T. Nakanishi, “Structural Basis for PPARgamma Transactivation by Endocrine Disrupting Organotin Compounds.”, Sci. Rep. 5, 8520, (2015), DOI: 10.1038/srep08520.; U. Ohto, T. Shibata, H. Tanji, E. Krayukhina, S. Uchiyama, K. Miyake, *T. Shimizu, “Structural Basis of CpG and Inhibitory DNA Recognition by Toll-like receptor 9.” Nature 520, 702-705, (2015), DOI: 10.1038/nature14138; W. Han, M. Yamauchi, U. Hasegawa, M. Noda, K. Fukui, A.J. van der Vlies, S. Uchiyama, *H. Uyama, “Pepsin Iimmobilization on an Aldehyde-modified Polymethacrylate Monolith and Its Application for Protein Analysis,” J. Biosci. Bioeng. 119, 505-510 (2015), DOI: 10.1016/j.jbiosc.2014.10.018; D. Volkin, S. Hershenson, R. Ho, S. Uchiyama, G. Winter, *J. Carpenter, “Two Decades of Publishing Excellence in Pharmaceutical Biotechnology,” J. Pharm. Sci., 104, 290-300, (2014), DOI: 10.1002/jps.24285; S. Totoki, G. Yamamoto, K. Tsumoto, S. Uchiyama, *K. Fukui, “Quantitative Laser Diffraction Method for the Assessment of Protein Subvisible Particles,” J. Pharm. Sci., 104, 618-626, (2014), DOI: 10.1002/jps.24288; E. Krayukhina, K. Tsumoto, *S. Uchiyama, K. Fukui, “Effects of Syringe Material and Silicone Oil Lubrication on the Stability of Pharmaceutical Proteins.” J. Pharm. Sci. 104, 527-535, (2014), DOI: 10.1002/jps.24184; *S. Uchiyama, “Liquid Formulation for Antibody Drugs.” BBA - Proteins and Proteomics. 1844, 2041-2052, (2014), DOI: 10.1016/j.bbapap.2014.07.016; T. Hamano, A. Dwiranti, K. Kaneyoshi, S. Fukuda, R. Kometani, M. Nakao, H. Takata, S. Uchiyama, N. Ohmido, *K. Fukui. “Chromosome Interior Observation by Focused Ion Beam/Scanning Electron Microscopy (FIB/SEM) Using Ionic Liquid Technique” Microsc. Microanal. 20, 1340-1347, (2014), DOI: 10.1017/S143192761401280X; M. Amano, N. Kobayashi, M. Yabuta, S. Uchiyama, *K. Fukui, “Detection of Histidine Oxidation in a Monoclonal Immunoglobulin Gamma (IgG) 1 Antibody.” Anal. Chem. 86, 7536-7543, (2014), DOI: 10.1021/ac501300m; 【図書】; E. Krayukhina, S. Uchiyama, “Analytical Ultracentrifugation”, Advanced Methods in Structural Biology, T. Senda and K. Maenaka ed. Springer (Japan), 165-183, 2016, DOI: 10.1007/978-4-431-56030-2; M. Noda, K. Fukui, S. Uchiyama“Mass Spectrometry”, Advanced Methods in Structural Biology, T. Senda, K. Maenaka, ed. Springer (Japan), 185-198, 2016, DOI: 10.1007/978-4-431-56030-2; S. Uchiyama, F. Arisaka, “Important and Essential Theoretical Aspects of AUC”, Analytical Ultracentrifugation, S. Uchiyama, F. Arisaka, W. F. Stafford, T. Laue ed. Springer (Japan), 3-14, 2016, DOI: 10.1007/978-4-431-55985-6_1; F. Arisaka, S. Uchiyama, “Experimental Design and Practical Aspect”, Analytical Ultracentrifugation, S. Uchiyama, F. Arisaka, W. F. Stafford, T. Laue ed. Springer (Japan), 15-21, 2016, DOI: 10.1007/978-4-431-55985-6_2; S. Saito, S. Uchiyama, “Biopharmaceutical Evaluation of Intermolecular Interactions by AUC-SE”, Analytical Ultracentrifugation, S. Uchiyama, F. Arisaka, W. F. Stafford, T. Laue ed. Springer (Japan), 419-440, 2016, DOI: 10.1007/978-4-431-55985-6_21
老木成稔 ▲班員一覧に戻る▲: 【雑誌論文】; M. Iwamoto, M.A. Elfaramawy, M. Yamatake, T. Matsuura, S. Oiki, “Concurrent in vitro Synthesis and Functional Detection of Nascent Activity of the KcsA Channel under the Membrane Potential”, ACS Synth. Biol., 7 (4), 1004-1011, (2018), DOI: 10.1021/acssynbio.7b00454; S. Kojima, M. Iwamoto, S. Oiki, S. Tochigi, H. Takahashi, “Thylakoid membranes contain a non-selective channel permeable to small organic molecules”, J. Biol. Chem., in press, (2018), DOI: 10.1074/jbc.RA118.002367; S. Oiki, M. Iwamoto, “Channel-Membrane Interplay in Lipid Bilayer Membranes Manipulated through Monolayer Technologies”,Biological & Pharmaceutical Bulletin, 41, 303-311, (2018), DOI: 10.1248/bpb.b17-00708; 炭竈享司、老木成稔：“チャネルの入口がイオンの透過速度を決める”, 生物物理　58,(1), 012-016, (2018), DOI: 10.2142/biophys.58.012; S. Oiki, M. Iwamoto, “Channel-Membrane Interplay in Lipid Bilayer Membranes Manipulated through Monolayer Technologies”, Biol. Pharm. Bull., in press; N. Kalathingal, T. Sumikama, T. Mori, S. Oiki, S. Saito, “Structure and dynamics of solvent molecules inside Polytheonamide B channel in different environments: A molecular dynamics study”, Phys. Chem. Chem. Phys., 20, 3334-3348, (2017), DOI: 10.1039/c7cp06299k; M. Iwamoto, A. Sumino, E. Shimada, M. Kinoshita, N. Matsumori, S. Oiki, “Oriented Reconstitution of the Full-length KcsA Potassium Channel in a Lipid Bilayer for AFM Imaging”, Sci. Rep., 7, 10782, (2017), DOI: 10.1038/s41598-017-11135-x; M. Iwamoto, A. Sumino, E. Shimada, M. Kinoshita, N. Matsumori, S. Oiki, “Membrane Perfusion of Hydrophobic Substances Around Channels Embedded in the Contact Bubble bilayer”, Sci. Rep., 7, 6857, (2017), DOI: 10.1038/s41598-017-07048-4; M. Iwamoto, S. Oiki, “Oriented Reconstitution of the Full-length KcsA Potassium Channel in a Lipid Bilayer for AFM Imaging”, J. Phys. Chem. Lett., 8, 785-793, (2017), DOI: 10.1021/acs.jpclett.6b03058; Y. Matsuki, M. Iwamoto, K. Mita, K. Shigemi, S. Matsunaga, *S. Oiki, “Rectified Proton Grotthuss Conduction Across a Long Water-Wire in the Test Nanotube of the Polytheonamide B Channel”, J. Am. Chem. Soc., 138, (12), 4168-4177, (2016), DOI: 10.1021/jacs.5b13377 (ACS Select: Nanoreactorsに選出); T. Sumikama, *S. Oiki, “Digitalized K⁺ Occupancy in the Nanocavity Holds and Releases Queues of K⁺ in a Channel”, J. Am. Chem. Soc., 138, 10284-10292, (2016), DOI: 10.1021/jacs.6b05270; 老木成稔：イオンチャネルの分子構造「特集　電解質の新しい見方・考え方」【水電解質と機能蛋白調節（基礎）】腎と透析, 2016; 岩本真幸、老木成稔：“脂質平面膜とパッチクランプのハイブリッドとしてのCBB（接触液胞2重膜）法”, 生物物理, 57(6), 313-317 (2015), DOI: 10.2142/biophys.57.313; H.-K, Chang, M. Iwamoto, *S. Oiki, *R.-C Shieh, “Mechanism for Attenuated Outward Conductance Induced by Mutations in the Cytoplasmic Pore of Kir2.1 Channels”, Sci. Rep.,5, 18404 (1-14), (2015), DOI: 10.1038/srep18404; *Y. Furutani, H. Shimizu, Y. Asai, S. Oiki, H. Kandori, “Specific Interactions between Alkali Metal Cations and the KcsA Channel Studied Using ATR-FTIR Spectroscopy”, Biophys. Physicobiology,12, 37-45, (2015), DOI: 10.2142/biophysico.12.0_37; A. Yamakata, H. Shimizu, *S. Oiki, “Surface-Enhanced IR Absorption Spectroscopy of the KcsA Potassium Channel upon Application of an Electric Field”, Phys. Chem. Chem. Phys. 17, 21104-21111, (2015), DOI: 10.y1039/C5CP02681D; *S. Oiki, “Channel Function Reconstitution and Re-animation: A Single-channel Strategy in the Post-crystal Age”, J. Physiol. 593, 2553-2573, (2015), DOI: 10.1113/JP270025; M. Iwamoto, and *S. Oiki, “Contact Bubble Bilayers with Flush Drainage”, Sci. Rep. 5, 9110 (2015), DOI: 10.1038/srep09110; H. Nakao, K. Ikeda, M. Iwamoto, H. Shimizu, S. Oiki, Y. Ishihara, M. Nakano, “pH-Dependent Promotion of Phospholipid Flip-Flop by the KcsA Potassium Channel”, BBA Biomemb., 1848(1),Part.A, 145-150, (2015), DOI: 10.1016/j.bbamem.2014.10.001; *老木成稔, "膜内KcsAカリウムチャネルの原子間力顕微鏡による構造・動態解析”, 生物物理, 55(1), 005-010, (2015), DOI: 10.2142/biophys.55.005; S. Phongphanphanee, N. Yoshida, *S. Oiki, F. Hirata, “Distinct Configurations of Cations and Water in the Selectivity Filter of the KcsA Potassium Channel Proved by 3D-RISM Theory”, J. Mol. Liq. 200,Part.A, 52-58 (2014), DOI: 10.1016/j.molliq.2014.03.050; S. Phongphanphanee, N. Yoshida, *S. Oiki,　F. Hirata, “The “Ambivalent” Snug-Fit Sites in the KcsA Potassium Channel Probed by “3D-RISM Microscopy”, Pure and Applied Chemistry., 86, 97-104, (2014), DOI: 10.1515/pac-2014-5018; M. Iwamoto, S. Matsunaga, *S. Oiki, “Paradoxical One-ion Pore Behavior of a Long β-helical Peptide of Marine Cytotoxic Polytheonamide B”, Sci. Rep., 4, 3636, (2014), DOI: 10.1038/srep03636; A. Sumino, D. Yamamoto, M. Iwamoto, T. Dewa, *S. Oiki, “Gating-Associated Clustering-Dispersion Dynamics of the KcsA Potassium Channel in a Lipid Membrane”, J. Phys. Chem. Lett., 5, 578-584, (2014), DOI: 10.1021/jz402491t (ACS Live Slides); 老木成稔, "KcsAカリウムチャネルでみるチャネル－膜相互作用"　膜 39, 309-315, (2014).; 【図書】; *Oiki, S.: Gating Dynamics of the Potassium Channel Pore. Reference Module in Life Sciences, 2016, Protein Biophysics, Ion Channels and Transporter Proteins, http://www.sciencedirect.com/science/article/pii/B9780128096338080924; 化学フロンティア２３“１分子ナノバイオ計測〜分子から生命システムを探る革新的技術” 第5章「イオン透過装置：イオンチャネル」, 69-80 , (2014)、野地博行編、(化学同人、京都、日本)
岡本祐幸 ▲班員一覧に戻る▲: 【雑誌論文】; S. Kawano, Y. Tamura, R. Kojima, S. Bala, E. Asai, A.H. Michel, B. Kornmann, I. Riezman, H. Riezman, Y. Sakae, Y. Okamoto, *T. Endo, “Structure-function Insights into Phospholipid Transfer by Mmm1-Mdm12 of ERMES between Membranes”, J. Cell Biol. , 217, 959-974 (2018), DOI: 10.1083/jcb.201704119; S. Tsukamoto, Y. Sakae, Y. Itoh, T. Suzuki, and *Y. Okamoto, “Computational Analysis for Selectivity of Histone Deacetylase Inhibitor by Replicaexchange Umbrella Sampling Molecular Dynamics Simulations”, J. Chem. Phys., 148, 125102 , (6 pages), (2018), DOI: 10.1063/1.5019209; S. Ito, D.G. Fedorov, *Y. Okamoto, and *S. Irle, “Implementation of Replica-exchange Umbrella Sampling in GAMESS”, Comput. Phys. Commun., 228, 152-162, (2018), DOI: 10.1016/j.cpc.2018.01.014; S. Ito, S. Irle, Y. Okamoto, “Implementation of Replica-exchange Umbrella Sampling in the DFTB+ Semiempirical Quantum Chemistry Package,” Comput. Phys. Commun., 204, 1-10, (2016), DOI: 10.1016/j.cpc.2016.02.010; G. La Penna, Y. Mori, R. Kitahara, K. Akasaka, Y. Okamoto,“Modeling ¹⁵N NMR Chemical Shift Changes in Protein Backbone with Pressure,” J. Chem. Phys.,145, 085104 (12 pages), (2016), DOI: 10.1063/1.4961507; 榮慶丈，西川直宏，塚本修一朗，鈴木孝禎，岡本祐幸, “分子動力学シミュレーションによる医学・創薬に向けたタンパク質の構造解析”, YAKUGAKU ZASSHI 136, 113-120, (2016), DOI: 10.1248/yakushi.15-00230-4; 岡本祐幸, 巻頭言：計算生物物理学の将来, 生物物理 (日本生物物理学会誌) , 56巻, 75, (2016), DOI: 10.2142/biophys.56.075; X. Lu, D. Fang, S. Ito, Y. Okamoto, V. Ovchinnikov, Q. Cui, “QM/MM Free Energy Simulations: Recent Progress and Challenges,” Molecular Simulation, 42, 1056-1078, (2016), DOI: 10.1080/08927022.2015.1132317; R. Urano, Y. Okamoto, “New Implementations of Replica-exchange Method for Simulations of Complex Systems: Dsigned-walk and Deterministic Replica-exchange Methods”, Phys. Procedia., 68, 100-104, (2015), DOI: 10.1016/j.phpro.2015.07.116; R. Urano, *H. Kokubo, Y. Okamoto, “Predictions of Tertiary Structures of a-helical Membrane Proteins by Replica-exchange Method with Consideration of Helix Deformations”, J. Phys. Soc. Jpn.,84, 084802 (12 pages), (2015), DOI: 10.7566/JPSJ.84.084802; *R. Urano,Y. Okamoto, “Designed-walk Replica-exchange Method for Simulations of Complex Systems”, Comput. Phys. Commun., 380-383, (2015), DOI: 10.1016/j.cpc.2015.07.007; *R. Urano, Y. Okamoto, “Deterministic Replica-exchange Method without Pseudo Random Numbers for Simulations of Complex Systems”, Comput. Phys. Commun., 197, 128-135, (2015), DOI: 10.1016/j.cpc.2015.08.020; R. Urano, *Y. Okamoto “Observation of Helix Associations for Insertion of a Retinal Molecule and Distortions of Helix Structures in Bacteriorhodopsin”, J. Chem. Phys.,143, 235101 (10 pages), (2015), DOI: 10.1063/1.4935964; Y. Okamoto, “Editorial: ICMS2013”, in Special Issue: ICMS2013 Molecular Simulation 41, 779 (2015), DOI: 10.1080/08927022.2015.1048075; S. Somani, Y. Okamoto, A.J. Ballard, and *D.J. Wales, “Equilibrium molecular thermodynamics from Kirkwood sampling”, Journal of Physical Chemistry B, 119, 6155-6169, (2015), DOI: 10.1021/acs.jpcb.5b01800; Y. Sakae, T. Hiroyasu, M. Miki, K. Ishii, and *Y. Okamoto, “Conformational search simulations of Trp-cage using genetic crossover”, Molecular Simulation 41, 1045-1049, (2015), DOI: 1080/08927022.2015.1016937; *N. Nishikawa, P.H. Nguyen, P. Derreumaux, and Y. Okamoto, “Replica-exchange molecular dynamics simulation for understanding the initial process of amyloid peptide aggregation”, Molecular Simulation 41, 1041-1044, (2015), DOI: 10.1080/08927022.2014.938445; *N. Nishikawa, Y. Sakae, and Y. Okamoto, “Molecular dynamics simulations to clarify the concentration dependency of protein aggregation”, JPS Conference Proceedings 5, 011020 (7 pages) (2015), DOI: 10.7566/JPSCP.5.011020; Y. Sakae, T. Hiroyasu, M. Miki, K. Ishii, and *Y. Okamoto, “A conformational search method for protein systems using genetic crossover and Metropolis criterion”, Journal of Physics: Conference Series 487, 012003 (5 pages) (2014), DOI: 10.1088/1742-6596/487/1/012003; *T. Yoda, Y. Sugita, Y. Okamoto, “Salt Effects on Hydrophobic-core Formation in Folding of a Helical Miniprotein Studied by Molecular Dynamics Simulations”, PROTEINS: Structure, Function, and Bioinformatics 82, 933-943, (2014), DOI: 10.1002/prot.24467; *Y. Okamoto, H. Kokubo, T. Tanaka, “Prediction of Ligand Binding Affinity by the Combination of Replica-exchange Method and Double-decoupling Method”, Journal of Chemical Theory and Computation 10, 3563-3569, (2014), DOI: 10.1021/ct500539u; T. Yamaguchi, Y. Sakae, Y. Zhang, S. Yamamoto, Y. Okamoto, *K. Kato, “Exploration of Conformational Spaces of High-mannose-type Oligosaccharides by an NMR-validated Simulation”, Angewandte Chemie International Edition 53, 10941-10944, (2014), DOI: 10.1002/anie.201406145; *H. Kokubo, T. Tanaka, Y. Okamoto, “Prediction of Protein-ligand Binding Structures by Replica-exchange Umbrella Sampling Simulations: Application to Kinase Systems”, Journal of Chemical Theory and Computation 9, 4660-4671,(2013), DOI: 10.1021/ct4004383; *H. Kokubo, T. Tanaka, Y. Okamoto, “Two-dimensional Replica-exchange Method for Predicting Protein-ligand Binding Structures”, Journal of Computational Chemistry 34, 2601-2614, (2013), DOI: 10.1002/jcc.23427; 【図書】; M. Terazima, M. Kataoka, R. Ueoka, Y. Okamoto (eds.)“Molecular Science of Fluctuations toward Biological Functions”(Springer, Tokyo, 2016) 270 pages. 全体を編集すると共に，以下の第9章（pp. 183-204）を著す．Structural fluctuations of proteins in folding and ligand docking studied by generalized-ensemble Simulations, (Y. Okamoto), DOI: 10.1007/978-4-431-55840-8; Y. Zhang, T. Yamaguchi, T. Satoh, M. Yagi-Utsumi, Y. Kamiya, Y. Sakae, Y. Okamoto, K. Kato, “Conformational dynamics of oligosaccharides characterized by paramagnetism-assisted NMR spectroscopy in conjunction with molecular dynamics simulation”, in Advances in Experimental Medicine and Biology 842: Biochemical Roles of Eukaryotic Cell Surface Macromolecules, A. Chakrabarti and A. Surolia.(ed.) (Springer, Heidelberg, 2015) pp. 217-230, DOI: 10.1007/978-3-319-11280-0_14; Y. Sakae and Y. Okamoto,“Optimizations of Protein Force Fields”, in Computational Methods to Study the Structure and Dynamics of Biomolecules and Biomolecular Processes – from Bioinformatics to Molecular Quantum Mechanics, A.Liwo (ed.) (Springer-Verlag, 2014) pp. 195-247, DOI: 10.1007/978-3-642-28554-7_7; T. Yoda, Y. Sugita, and Y. Okamoto“Protein Folding Simulations by Generalized-ensemble Algorithms”, in Protein Conformational Dynamics, Advances in Experimental Medicine and Biology, Vol. 805, K.-L. Han, Xin Zhang, and M.-J. Yang (eds.) (Springer, 2014) pp. 1-27; H. Kokubo, T. Tanaka, and Y. Okamoto“Ligand Docking Simulations by Generalized-ensemble Algorithms”, in Advances in Protein Chemistry and Structural Biology, Vol. 92, T. Karabencheva-Christova (ed.) (Academic Press, 2013) pp. 63-91, DOI: 10.1016/B978-0-12-411636-8.00002-X
奥村久士 ▲班員一覧に戻る▲: 【雑誌論文】; Y. Mori, *H. Okumura, T. Watanabe, and T. Hohsaka, “Antigen-dependent Fluorescence Response of Anti-c-Myc Quenchbody Studied by Molecular Dynamics Simulations”, Chem. Phys. Lett., 698, 223, (2018), DOI: 10.1016/j.cplett.2018.03.011; H. Nishizawa, *H. Okumura, “Classical Molecular Dynamics Simulation to Understand Uole of a Zinc Ion for Aggregation of Amyloid-β Peptides”, J. Comput. Chem. Jpn., 17, 76, (2018), DOI: 10.2477/jccj.2018-0005; *H. Okumura, M. Higashi, Y. Yoshida, H. Sato, R. Akiyama, “Theoretical approaches for dynamical ordering of biomolecular systems”, BBA - General Subjects, 1862, 212-228, (2018), DOI: 10.1016/j.bbagen.2017.10.001; *M. Yamauchi, *H. Okumura, “Development of isothermal-isobaric replica-permutation method for molecular dynamics and Monte Carlo simulations and its application to reveal temperature and pressure dependence of folded, misfolded, and unfolded states of chignolin”, J. Chem. Phys., 147, 184107 (15 pages), (2017), DOI: 10.1063/1.4996431; *H. Okumura, S. G. Itoh, “Structural and Fluctuational Difference between Two Eds of Aβ Amyloid Fibril: MD Simulation Predicts Only One End has Open Conformations”, Sci. Rep., 6, 38422, (2016), DOI: 10.1038/srep38422; R. Gupta, *S. Saito, Y. Mori, S. G. Itoh, H. Okumura, *M. Tominaga, “Structural Basis of TRPA1 Inhibition by HC-030031 Utilizing Species-specific Differences”, Sci. Rep., 6, 37460, (2016), DOI: 10.1038/srep37460; H. Nishizawa, *H. Okumura, “Rapid QM/MM Approach for Biomolecular Systems Under Periodic Boundary Conditions: Combination of the Density-functional Tight-binding Theory and Particle Mesh Ewald Method”, J. Comput. Chem., 37, 2701-2711, (2016), DOI: 10.1002/jcc.24497（カバーイラストレーションに採用）; S. G. Itoh, *H. Okumura, “Oligomer Formation of Amyloid-β(29-42) from its Monomers Using the Hamiltonian Replica-permutation Molecular Dynamics Simulation”, J. Phys. Chem. B, 120, 6555-6561, (2016), DOI: 10.1021/acs.jpcb.6b03828; *伊藤暁，*奥村久士：「レア・イベントを捕えるための新たな分子シミュレーション手法－アミロイド線維形成の理解に向けた取り組み－」日本物理学会誌 71(7), 463-468, (2016), DOI: 10.11316/butsuri.71.7_463; W. Khuntawee, T. Rungrotmongkol, P. Wolschann, P Pongsawasdi, N. Kungwan, *H. Okumura, *S. Hannongbua, “Conformation Study of ε-cyclodextrin: Replica-exchange Molecular Dynamics Simulations”, Carbohydr. Polym., 141, 99-105, (2016), DOI: 10.1016/j.carbpol.2015.10.018; Y. Mori, *H. Okumura: “Simulated Tempering Based on Global Balance or Detailed Balance Conditions: Suwa-Todo, Heat bath, and Metropolis algorithms”, J. Comput. Chem.,36, (2015), 2344-2349.; Y. Mori, H. Okumura, “Molecular Dynamics Simulation Study on the High-pressure Behaviour of an AK16 Peptide”, Mol. Sim. 41, 1035-1040, (2015), DOI: 10.1080/08927022.2014.938071; S. G. Itoh, H. Okumura, “Replica-permutation Method to Enhance Sampling Efficiency”, Mol. Sim. 41, 1021-1026, (2015), DOI: 10.1080/08927022.2014.923576; H. Nishizawa, *H. Okumura, “Comparison of Replica-permutation Molecular Dynamics Simulations with and without Detailed Balance Condition”, J. Phys. Soc. Jpn. 84, 074801 (6 pages), (2015), DOI: 10.7566/JPSJ.84.074801; K. Inagaki, T. Satoh, S. G. Itoh, H. Okumura, *K. Kato, “Redox-dependent Conformational Transition of Catalytic Domain of Protein Disulfide Isomerase Indicated by Crystal Structure-based Molecular Dynamics Simulation”, Chem. Phys. Lett., 618, 203-207, (2015), DOI: 10.1016/j.cplett.2014.11.017; 奥村久士, “タンパク質の折りたたみ、変性、凝集、アミロイド線維：生体分子動力学シミュレーションの最前線”, 分子研レターズ, 70, 4-7, (2014); H.-L. Chiang, C.-J. Chen, H. Okumura, *C.-K. Hu, “Transformation between α-helix and β-sheet Structures of One and Two Polyglutamine Peptides in Explicit Water Molecules by Replica-exchange Molecular Dynamics Simulations”, J. Comput. Chem. 35, 1430-1437, (2014), DOI: 10.1002/jcc.23633; Y. Mori, *H. Okumura, “Molecular Dynamics Study on the Structural Changes of Helical Peptides Induced by Pressure”, Proteins, 82, 2970-2981, (2014), DOI: 10.1002/prot.24654; S. G. Itoh, *H. Okumura, “Dimerization Process of Amyloid-β(29-42) Studied by the Hamiltonian Replica-permutation Molecular Dynamics Simulations”, J. Phys. Chem. B, 118, 11428-11436, (2014), DOI: 10.1021/jp505984e; *H. Okumura, S. G. Itoh, “Amyloid Fibril Disruption by Ultrasonic Cavitation: Nonequilibrium Molecular Dynamics Simulations”, J. Am. Chem. Soc. 136(30), 10549-10552, (2014), DOI: 10.1021/ja502749f
加藤晃一 ▲班員一覧に戻る▲: 【雑誌論文】; H. Yagi, G. Yan, T. Suzuki, S. Tsuge, T. Yamaguchi, *K. Kato, “Lewis X-carrying Neoglycolipids Evoke Selective Apoptosis in Neural Stem Cells”, Neurochem. Res., 43, 212-218, (2018), DOI: 10.1007/s11064-017-2415-5; M. Yagi-Utsumi, A. Sikdar, T. Kozai, R. Inoue, M. Sugiyama, T. Uchihashi, H. Yagi, T. Satoh, d *K. Kato, “Conversion of Functionally Undefined Homopentameric Protein PbaA into a Proteasome Activator by Mutational Modification of its C-terminal Segment Conformation”, Protein Eng. Des. Sel., 31, 29-36,(2018),DOI: 10.1093/protein/gzx066; J. Kicuntod, K. Sangpheak, M. Mueller, P. Wolschann, H. Viernstein, S. Yanaka, *K. Kato, W. Chavasiri, P. Pongsawasdi, N. Kungwan, T. Rungrotmongkol, “Theoretical and Experimental Studies on Inclusion Complexes of Pinostrobin and β-Cyclodextrins”, Sci. Pharm., 86, 5, (2018),DOI: 10.3390/scipharm86010005; H. Yagi, D. Takakura, L. T. Roumenina, W. H. Fridman, C. Sautès-Fridman, N. Kawasaki, *K. Kato, “Site-specific N-glycosylation Analysis of Soluble Fcγ Receptor IIIb in Human Serum, Sci. Rep., 8, Article number: 2719, (2018),DOI: 10.1038/s41598-018-21145-y; K. Kato, T. Furuhashi, K. Kato, A. Oda, *E. Kurimoto, “The Assembly Mechanism of Coiled-coil Domains of the Yeast Cargo Receptors Emp46p/47p and the Mutational Alteration of pH-dependency of Complex Formation”, J Biochem., in press, (2018), DOI: 10.1093/jb/mvy011; R.Yogo, S. Yanaka, *K. Kato, “Backbone 1H, 13C, and 15N Assignments of the Extracellular Region of Human Fcγ Receptor IIIb”, Biomol. NMR Assign., in press, (2018), DOI: 10.1007/s12104-018-9809-4; K. Mukaigasa, T. Tsujita, V. Thanh Nguyen, L. Li , H. Yagi, Y. Fuse, Y. Nakajima-Takagi, K. Kato, M.Yamamoto, *M. Kobayashi, “Nrf2 Activation Attenuates Genetic Endoplasmic Reticulum Stress Induced by a Mutation in the Phosphomannomutase 2 Gene in Zebrafish”, Proc. Natl. Acad. Sci. USA, 115，2758-2763, (2018), DOI: 10.1073/pnas.1714056115; S. Yanaka, H. Yagi, R. Yogo, M. Yagi-Utsumi, *K. Kato, “Stable Isotope Labeling Approaches for NMR Characterization of Glycoproteins Using Eukaryotic Expression Systems”, J. Biomol. NMR, in press, (2018), DOI: 10.1007/s10858-018-0169-2; T. Ikeya, D. Ban, D. Lee, Y. Ito, K. Kato, *Christian Griesinger, “Solution NMR Views of Dynamical Ordering of Biomacromolecules”, Biochim. Biophys. Acta –General Subjects, 1862, 287-306 (2018). DOI: 10.1016/j.bbagen.2017.08.020; K. Kurihara, M. Matsuo, *T. Yamaguchi, *S. Sato, “Synthetic Approach to biomolecular science by cyborg supramolecular chemistry,” Biochimica et Biophysica Acta (BBA) - General Subjects, 1862, 358, (2018), DOI: 10.1016/j.bbagen.2017.11.002; K. Matsuzaki, K. Kato, *K. Yanagisawa, “Ganglioside-mediated Assembly of Amyloid β-protein: Roles in Alzheimer's Disease”, Prog. Mol. Biol. Transl. Sci., in press, (2018); *K. Kato, S. Yanaka, H. Yagi, “Technical basis for nuclear magnetic resonance approach for glycoproteins”, Experimental Approaches of NMR Spectroscopy (The Nuclear Magnetic Resonance Society of Japan ed.), Springer International Publishing, in press, (2018); H.Yagi and K.Kato, “Functional roles of glycoconjugates in the maintenance of stemness and differentiation process of neural stem cells,” Glycoconjugate J., in press, (2017).; M. Nagae, S. K. M., M. Neyazaki, R. Oi, A. Ikeda, N. Matsugaki, S. Akashi, H. Manya, M. Mizuno, H. Yagi, K. Kato, T. Senda, T. Endo, T. Nogi, *Y. Yamaguchi, “3D structural Analysis of Protein O-mannosyl Kinase, POMK, a Causative Gene Product of Dystroglycanopathy”, Genes Cells, 22, 348-359, (2017), DOI: 10.1111/gtc.12480; S. Sawaguchi, S. Varshney, M. Ogawa, Y. Sakaidani, H. Yagi, K. Takeshita, T. Murohara, K. Kato, S. Sundaram, P. Stanley, *T. Okajima, “GlcNAc on NOTCH1 EGF Repeats Regulates Ligand-induced Notch Signaling and Vascular Development in Mammals”, eLife, 6, e24419, (2017), DOI: 10.7554/eLife.24419; E. Kurimoto, T. Satoh, Y. Ito, E. Ishihara, K. Okamoto, M. Yagi-Utsumi, K. Tanaka, *K. Kato,“Crystal Structure of Human Proteasome Assembly Chaperone PAC4 Involved in Proteasome Formation”, Protein Sci., 26, 1080-1085, (2017), DOI: 10.1002/pro.3153; T. Kato, N. Kako, K. Kikuta, T. Miyazaki, S. Kondo, H. Yagi, K. Kato, *E. Y. Park, “N-Glycan Modification of a Recombinant Protein via Coexpression of Human Glycosyltransferases in Silkworm Pupae”, Sci. Rep., 7, Article number: 1409, (2017),DOI: 10.1038/s41598-017-01630-6; G. Yan, T. Yamaguchi, T. Suzuki, S. Yanaka, S. Sato, M. Fujita, *K. Kato, “Hyper-assembly of Self-Assembled Glycoclusters Mediated by Specific Carbohydrate–carbohydrate Interactions”, Chem. Asian J.,12, 968-972, (2017), DOI: 10.1002/asia.201700202; T. Kato, K. Kikuta, A. Kanematsu, S. Kondo, H. Yagi, K. Kato, *E. Y. Park, “Alteration of a Recombinant Protein N-glycan Structure in Silkworms by Partial Suppression of N-acetylglucosaminidase Gene Expression”, Biotechnol. Lett., 39, 1299-1308, (2017), DOI: 10.1007/s10529-017-2361-y; H. Yagi, H. Tateno, K. ayashi, T. Hayashi, K. Takahashi, J. Hirabayashi, K. Kato, *M. Tsuboi, “Lectin Microarray Analysis of Isolated Polysaccharides from Sasa Veitchii”, Biosci. Biotechnol. Biochem., 81, 1687-1689, (2017), DOI: 10.1080/09168451.2017.1340089; R. Yogo, S. Yanaka, H. Yagi, A. Martel, L. Porcar, Y. Ueki, R. Inoue, N. Sato, M. Sugiyama, *K. Kato,　“Characterization of Conformational Deformation-coupled Interaction between Immunoglobulin G1 Fc Glycoprotein and a Low-affinity Fcγ Receptor by Deuteration-assisted Small-angle Neutron Scattering”, Biochem. Biophys. Rep., 12, 1-4, (2017), DOI: 10.1016/j.bbrep.2017.08.004; T. Satoh, C. Song, T. Zhu, T. Toshimori, K. Murata, Y. Hayashi, H. Kamikubo, T. Uchihashi, *K. Kato,“Visualisation of a flexible modular structure of the ER folding-sensor enzyme UGGT”, Sci. Rep., 7, Article number: 12142, (2017),DOI: 10.1038/s41598-017-12283-w; S. Kitazawa , M. Yagi-Utsumi, K. Kato, *R. Kitahara, “Interactions Controlling the Slow Dynamic Conformational Motions of Ubiquitin”, Molecules, 22, 1414, (2017), DOI: 10.3390/molecules22091414; S. Yanaka, T. Yamazaki , R. Yogo , M. Noda , S. Uchiyama, H. Yagi, *K. Kato, “NMR Detection of Semi-specific Antibody Interactions in Serum Environments”, Molecules, 22, 1619, (2017), DOI: 10.3390/molecules22101619; Y. Sakae, T. Satoh, H. Yagi, S. Yanaka, T. Yamaguchi, Y. Isoda, S. Iida, Y. Okamoto, *K. Kato,“Conformational Effects of N-glycan Core fucosylation of Immunoglobulin G Fc Region on its Interaction with Fcγ Receptor IIIa”, Sci. Rep., 7, Article number: 13780, (2017),DOI: 10.1038/s41598-017-13845-8; T. Takenaka, T. Nakamura, S. Yanaka, M. Yagi-Utsumi, M. S. Chandak, K. Takahashi, S. Paul, K. Makabe, M. Arai, K. Kato, *K. Kuwajima, “Formation of the Chaperonin Complex Studied by 2D NMR Spectroscopy”, PLOS ONE, 12, e0187022, (2017), DOI: 10.1371/journal.pone.0187022; T. Kozai, T. Sekiguchi, T. Satoh, H. Yagi, K. Kato, *T. Uchihashi, “Two-step Process for Disassembly Mechanism of Proteasome α7 Homo-tetradecamer by α6 Revealed by High-speed Atomic Force Microscopy”, Sci. Rep., 7, Article number: 15373, (2017),DOI: 10.1038/s41598-017-15708-8; 矢木宏和，*加藤晃一, "NMRを利用して糖タンパク質糖鎖の構造動態と相互作用を観る"医学のあゆみ，262, 467-473, (2017); T.Suzuki, M.Kajino, S.Yanaka, T.Zhu, H.Yagi, T.Satoh, T.Yamaguchi, and *K. Kato, “Conformational analysis of a high-mannose-type oligosaccharide displaying glucosyl determinant recognised by molecular chaperones using NMR-validated molecular dynamics simulation,” ChemBioChem 18, 396-410 (2017). DOI: 10.1002/cbic.201600595; T.Yoshimura, A.Hayashi, M.Handa-Narumi, H.Yagi, N.Ohno, T.Koike, Y.Yamaguchi, K.Uchimura, K.Kadomatsu, J.Sedzik, K.Kitamura, K. Kato, B.D.Trapp, H.Baba, and *K.Ikenaka, “GlcNAc6ST-1 regulates sulfation of N-glycans and myelination in the peripheral nervous system,” Sci. Rep. 7, Article number: 42257 (2017). DOI: 10.1038/srep42257; M.Nagae, S.K.Mishra, M.Neyazaki, R.Oi, A.Ikeda, N.Matsugaki, S.Akashi, H.Manya, M.Mizuno, H.Yagi, K. Kato, T.Senda, T.Endo, T.Nogi, and *Y.Yamaguchi, “3D structural analysis of protein O-mannosyl kinase, POMK, a causative gene product of dystroglycanopathy,” Genes Cells 22, 348-359 (2017). DOI: 10.1111/gtc.12480; S.Sawaguchi, S.Varshney, M.Ogawa, Y.Sakaidani, H.Yagi, K.Takeshita, T.Murohara, K. Kato, S.Sundaram, P.Stanley, and *T.Okajima, “O-GlcNAc on NOTCH1 EGF repeats regulates ligand-induced Notch signaling and vascular development in mammals,” eLife 6, Article number: e24419 (2017).; E. Kurimoro, T.Satoh, Y.Ito, E.Ishihara, K.Okamoto, M.Yagi-Utsumi, K.Tanaka, and *K. Kato, “Crystal structure of human proteasome assembly chaperone PAC4 involved in proteasome formation,” Protein Sci. 26, 1080-1085 (2017). DOI: 10.1002/pro.3153; T.Kato, N.Kako, K.Kikuta, T.Miyazaki, S.Kondo, H.Yagi, K. Kato, and E.Y.Park, ”N-Glycan modification of a recombinant protein via coexpression of human glycosyltransferases in silkworm pupae,“ Sci. Rep. 7, Article number: 1409 (2017).; G.Yan, T.Yamaguchi, T.Suzuki, S.Yanaka, S.Sato, M.Fujita, and *K. Kato, “Hyper-assembly of self-assembled glycoclusters mediated by specific carbohydrate–carbohydrate interactions,” Chem. Asian J. 12, 968-972 (2017). DOI: 10.1002/asia.201700202; T.Kato, K.Kikuta, A.Kanematsu, S.Kondo, H.Yagi, K. Kato, and E.Y.Park, “Alteration of a recombinant protein N-glycan structure in silkworms by partial suppression of N-acetylglucosaminidase gene expression,” Biotechnol. Lett 39, 1299-1308 (2017). DOI: 10.1007/s10529-017-2361-y; H.Yagi, H.Tateno, K.Hayashi, T.Hayashi, K.Takahashi, J.Hirabayashi, K.Kato, and M.TsuboiK.Kato, “Lectin microarray analysis of isolated polysaccharides from Sasa veitchii,” Biosci. Biotechnol. Biochem. 81, 1687-1689 (2017). DOI: 10.1007/s10529-017-2361-y; R.Yogo, S.Yanaka, H.Yagi, A.Martel, L.Porcar, Y.Ueki, R.Inoue, N.Sato, M.Sugiyama, and K.Kato, “Characterization of conformational deformation-coupled interaction between immunoglobulin G1 Fc glycoprotein and a low-affinity Fcγ receptor by deuteration-assisted small-angle neutron scattering,” Biochem. Biophys. Rep. 12, 1-4 (2017). DOI: 10.1016/j.bbrep.2017.08.004; T.Satoh, C.Song, T.Zhu, T.Toshimori, K.Murata, Y.Hayashi, H.Kamikubo, T.Uchihashi, and K.Kato, “Visualisation of a flexible modular structure of the ER folding-sensor enzyme UGGT,” Sci. Rep 7, Article number: 12142 (2017). DOI: 10.1038/s41598-017-12283-w; S.Kitazawa, M.Yagi-Utsumi, K.Kato, and R.Kitahara, “Interactions controlling the slow dynamic conformational motions of ubiquitin,” Molecules 22, Article number: 1414 (2017). DOI: 10.3390/molecules22091414; S.Yanaka, T.Yamazaki, R.Yogo, M.Noda, S.Uchiyama, H.Yagi, and K.Kato, “NMR detection of semi-specific antibody interactions in serum environments,” Molecules 22, Article number: 1619 (2017). DOI: 10.3390/molecules22101619; Y.Sakae, T.Satoh, H.Yagi, S.Yanaka, T.Yamaguchi, Y.Isoda, S.Iida, Y.Okamoto, and K.Kato, “Conformational effects of N-glycan core fucosylation of immunoglobulin G Fc region on its interaction with Fcγ receptor IIIa,” Sci. Rep. 7, Article number: 13780 (2017). DOI: 10.1038/s41598-017-13845-8; T.Takenaka, T.Nakamura, S.Yanaka, M.Yagi-Utsumi, M.S. Chandak, K.Takahashi, S.Paul, K.Makabe, M.Arai, K.Kato, and K.Kuwajima, “Formation of the chaperonin complex studied by 2D NMR spectroscopy,” PLoS ONE 12, Article number: e0187022 (2017). DOI: 10.1371/journal.pone.0187022; T.Kozai, T.Sekiguchi, T.Satoh, H. Yagi, K.Kato, and T.Uchihashi, “Two-step process for disassembly mechanism of proteasome α7 homo-tetradecamer by α6 revealed by high-speed atomic force microscopy,” Sci. Rep 7, Article number: 15373 (2017). DOI: 10.1038/s41598-017-15708-8; M. Yagi-Utsumi, K. Kato, *K. Nishimura, “Membrane-induced dichotomous conformation of amyloid β with the disordered N-terminal segment followed by the stable C-terminal β structure”, PLoS ONE, 11, e0146405 (2016), DOI: 10.1371/journal.pone.0146405; S. Seetaha, M. Yagi-Utsumi, T. Yamaguchi, K. Ishii, S. Hannongbua, *K. Choowongkomon, *K. Kato, “Application of site-specific spin labeling for NMR detecting inhibitor-induced conformational change of HIV-1 reverse transcriptase”, Chem.Med.Chem., 11, 363-366, (2016), DOI: 10.1002/cmdc.201500554; *T. Satoh, T. Toshimori, G. Yan, T. Yamaguchi, *K. Kato, “Structural basis for two-step glucose trimming by glucosidase II involved in ER glycoprotein quality control”, Sci. Rep., 6, Article number: 20575, (2016), DOI: 10.1038/srep20575; R. Thammaporn, K. Ishii, M. Yagi-Utsumi, S. Uchiyama, *S. Hannongbua, *K. Kato, “Mass spectrometric characterization of HIV-1 reverse transcriptase interactions with non-nucleoside reverse transcriptase inhibitors”, Biol. Pharm. Bull., 39, 450-454, (2016), DOI: 10.1248/bpb.b15-00880; R.Inoue, T.Takata, N.Fujii, K.Ishii, S.Uchiyama, N.Sato, Y.Oba, K.Wood, K. Kato, N.Fujii, and *M.Sugiyama, “New insight into the dynamical system of αB-crystallin oligomers,” Sci. Rep. 6, Article number: 29208 (2016). DOI: 10.1038/srep29208; H.Ito, H.Kaji, A.Togayachi, P.Azadi, M.Ishihara, R.Geyer, C.Galuska, H.Geyer, K.Kakehi, M.Kinoshita, N.G.Karlsson, C.Jin, K. Kato, H.Yagi, S.Kondo, N.Kawasaki, N.Hashii, D.Kolarich, K.Stavenhagen, N.H.Packer, M.Nakano, N.Taniguchi, A.Kurimoto, Y.Wada, M.Tajiri, P.Yang, W.Cao, H.Li, P.M.Rudd, and *H.Narimatsu, “Comparison of analytical methods for profiling N- and O-linked glycans from cultured cell lines: HUPO Human Disease Glycomics/Proteome Initiative multi-institutional study,” Glycoconjugate J. 33, 405-415 (2016). DOI: 10.1007/s10719-015-9625-3; M.Sugiyama, H.Yagi, K.Ishii, L.Porcare, A.Martele, K.Oyama, M.Noda, Y.Yunoki, R.Murakami, R.Inoue, N.Sato, Y.Oba, K.Terauchi, S.Uchiyama, and *K. Kato, “Structural characterization of the circadian clock protein complex composed of KaiB and KaiC by inverse contrast-matching small-angle neutron scattering,” Sci. Rep. 6, Article number: 35567 (2016). DOI: 10.1038/srep35567; T.Satoh, T.Toshimori, M.Noda, S.Uchiyama, and *K. Kato, “Interaction mode between catalytic and regulatory subunits in glucosidase II involved in ER glycoprotein quality control,” Protein Sci. 25, 2095-2101 (2016). DOI: 10.1002/pro.3031; H.Yagi, C.-W.Kuo, T.Obayashi, S.Ninagawa, K.-H.Khoo, and *K. Kato, “Direct mapping of additional modifications on phosphorylated O-glycans of α-dystroglycan by mass spectrometry analysis in conjunction with knocking out of causative genes for dystroglycanopathy,” Mol. Cell Proteomics 15, 3424-3434 (2016). DOI: 10.1074/mcp.M116.062729; M. Yagi-Utsumi, T. Satoh, *K. Kato, “Structural Basis of Redox-dependent Substrate Binding of Protein Disulfide Isomerase”, Sci. Rep. 5, 13909, (2015), DOI: 10.1038/srep13909; K. Inagaki, T. Satoh, M. Yagi-Utsumi, A.-C. Le Gulluche, T. Anzai, Y. Uekusa, Y. Kamiya, *K. Kato, “Redox-coupled Structural Changes of the Catalytic a′ Domain of Protein Disulfide Isomerase”, FEBS Lett., 589, 2690-2694, (2015), DOI: 10.1016/j.febslet.2015.07.041; Y. Isoda, H. Yagi, T. Satoh, M. Shibata-Koyama, K. Masuda, M. Satoh, K. Kato, *S. Iida, “Importance of the Side Chain at Position 296 of Antibody Fc in Interactions with Fcγ RIIIa and Other Fcγ Receptors”, PLoS ONE, 10, e0140120, (2015), DOI: 10.1371/journal.pone.0140120; K. Ishii, H. Enda, M. Noda, M. Kajino, A. Kim, E. Kurimoto, K. Sato, A. Nakano, Y. Kobayashi, H. Yagi, S. Uchiyama, *K. Kato, “pH-dependent Assembly and Segregation of the Coiled-coil Segments of Yeast Putative Cargo Receptors Emp46p and Emp47p”, PLoS ONE, 10, e0140287, (2015), DOI: 10.1371/journal.pone.0140287; R. Thammaporn, M. Yagi-Utsumi, T. Yamaguchi, P. Boonsri, P. Saparpakorn, K. Choowongkomon, S. Techasakul, *K. Kato, *S. Hannongbua, “NMR Characterization of HIV-1 Reverse Transcriptase Binding to Various Non-nucleoside Reverse Transcriptase Inhibitors with Different Activities”, Sci. Rep., 5, 15806, (2015), DOI: 10.1038/srep15806; T. Zhu, T. Yamaguchi, T. Satoh, *K. Kato, “A Hybrid Strategy for the Preparation of 13C-labeled High-Mannose-type Oligosaccharides with Terminal Glucosylation for NMR Study”, Chem. Lett., 44, 1744-1746, (2015), DOI: 10.1246/cl.150898; *S. Sato, Y. Yoshimasa, D. Fujita, M. Yagi-Utsumi, T. Yamaguchi, *K. Kato, *M. Fujita, “Self-Assembled Spherical Complex Displaying a Gangliosidic Glycan Cluster Capable of Interacting with Amyloidogenic Proteins”, Angew. Chem. Int. Ed., 54, in press, (2015), DOI: 10.1002/anie.201501981R1; T. Yamaguchi and *K. Kato, “Paramagnetic NMR probes for characterization of the dynamic conformations and interactions of oligosaccharides”, Glycoconjugate J., 32, 505–513, (2015) DOI: 10.1007/s10719-015-9599-1; H. Yagi, Y. Zhang, M. Yagi-Utsumi, T. Yamaguchi, S. Iida, Y. Yamaguchi, and *K. Kato, “Backbone ¹H, ¹³C, and ¹⁵N Resonance Assignments of the Fc Fragment of Human Immunoglobulin G Glycoprotein”, Biomol. NMR Assign., in press, (2015), DOI: 10.1007/s12104-014-9586-7; 蜷川暁, 加藤晃一, *森和俊, “糖鎖依存的構造異常タンパク質分解に必須な糖鎖刈り込み機構を解明〜革新的ゲノム編集技術によって従来のモデルを一新〜”, 化学と生物, 53, 571-573 (2015); N. Nakagawaa, H. Yagi, K. Kato, H.Takematsu, and *S.Oka, “Ectopic clustering of Cajal-Retzius and subplate cells is an initial pathological feature in Pomgnt2-knockout mice, a model of dystroglycanopathy”, Sci. Rep. 5, 11163 (2015), DOI: 10.1038/srep11163; S. H. Kang, H. S. Jung, S. J. Lee, C. I. Park, S. M. Lim, H. Park, B. S. Kim, K. H. Na, G. J. Han, J. W. Bae, H. J. Park, K .C. Bang, B. T. Park, H. S. Hwang, I.-Soo .Jung, J. I. Kim, D. B. Oh, D. I. Kim, H. Yagi, K. Kato, D. K. Kim, and *H. H. Kim, “Glycan structure and serum half-life of recombinant CTLA4Ig, an immunosuppressive agent, expressed in suspension-cultured　rice cells with coexpression of human β1,4-galactosyltransferase and human CTLA4Ig”, Glycoconjugate J. 32, 161-72 (2015), DOI: 10.1007/s10719-015-9590-x; *加藤晃一, *佐藤匡史, “生命分子の自己組織化のダイナミクス”, 化学工業, 66, 32-37 (2015); H. Yagi, N. Fukuzawa, Y. Tasaka, K. Matsuo, Y. Zhang, T. Yamaguchi, S. Kondo, S. Nakazawa, N. Hashii, N. Kawasaki, T. Matsumura, and *K. Kato, “NMR-based Structural Validation of Therapeutic Antibody Produced in Nicotiana benthamiana”, Plant Cell Rep., 34, 959-968, (2015), DOI: 10.1007/s00299-015-1757-1; H. Yagi, M. Nakamura, J. Yokoyama, Y. Zhang, T. Yamaguchi, S. Kondo, J. Kobayashi, T. Kato, E. Y. Park, S. Nakazawa, N. Hashii, N. Kawasaki, and *K. Kato, “Stable Isotope Labeling of Glycoprotein Expressed in Silkworms Using Immunoglobulin G as a Test Molecule”, J. Biomol. NMR, 62, 157-167, (2015), DOI: 10.1007/s10858-015-9930-y; *加藤晃一, *稲垣直之, “離合集散が織りなす生命分子機能の研究フロンティア”, 実験医学, 33, 1316-1320 (2015); M. Yagi-Utsumi and *K. Kato, “Structural and Dynamic Views of GM1 Ganglioside”, Glycoconjugate J., 32, 105-112 (2015), DOI: 10.1007/s10719-015-9587-5; Y. Kitago, M. Nagae, Z. Nakata, M. Yagi-Utsumi, S. Takagi-Niidome, E. Mihara, T. Nogi, K. Kato, *J. Takagi, “Structural basis for amyloidogenic peptide recognition by sorLA”, Nature Struct. Mol. Biol. 22, 199-206 (2015), DOI: 10.1038/nsmb.2954; *加藤晃一, “糖鎖構造学研究の新展開”, BIOTOVO, 23, 2-3, (2015); 山口拓実, *加藤晃一, “糖鎖の立体構造を描き出す”, 生物物理, 55, 81-83 (2015), DOI: 10.2142/biophys.55.081; *T. Satoh, T. Yamaguchi, *K. Kato, “Emerging structural insights into glycoprotein quality control coupled with N-glycan processing in the endoplasmic reticulum”, Molecules, 20, 2475-2491 (2015),DOI: 10.3390/molecules20022475; *S. Sato, R. Takeuchi, M. Yagi-Utsumi, T. Yamaguchi, Y. Yamaguchi, K. Kato, *M. Fujita, “Self-Assembled, π-Stacked Complex as a Finely-Tunable Magnetic Aligner for Biomolecular NMR Applications”, Chem. Comm., 51, 2540-2543 (2015), DOI: 10.1039/c4sc02812k; M. Ogawa, S. Sawaguchi, T. Kawai, D. Nadano, T. Matsuda, H. Yagi, K. Kato, K. Furukawa, *T. Okajima, “Impaired O-linked N-acetylglucosaminylation in the endoplasmic reticulum by mutated EGF domain-specific O-linked N-acetylglucosamine transferase found in Adams-Oliver syndrome”, J. Biol. Chem. 290, 2137-2149, (2015), DOI: 10.1074/jbc; K. Inagaki, T. Satoh, S. G. Itoh, H. Okumura, *K. Kato, “Redox-dependent Conformational Transition of Catalytic Domain of Protein Disulfide Isomerase Indicated by Crystal Structure-based Molecular Dynamics Simulation”, Chem. Phys. Lett., 618, 203-207 (2015), DOI: 10.1016/j.cplett.2014.11.017; M. Tagawa, K. Shirane, L. Yu, T. Sato, S. Furukawa, H. Mizuguchi, R. Kuji, K. Kawamura, N. Takahashi, K. Kato, S. Hayakawa, S. Sawada, and *K. Furukawa, “Enhanced Expression of the β4-galactosyltransferase 2 Gene Impairs Mammalian Tumor Growth”, Cancer Gene Therapy 21, 219-227 (2014), DOI: 10.1038/cgt.2014.21; N. Kawasaki, T. Okumoto, Y. Yamaguchi, N. Takahashi, W. H. Fridman, C. Sautès-Fridman, H. Yagi, and *K. Kato, “Site-specific Classification of N-linked Oligosaccharides of the Extracellular Regions of Fcγ Receptor IIIb Expressed in Baby Hamster Kidney Cells”, J. Glycomics Lipidomics 4, 116, (2014), DOI: 10.4172/2153-0637.1000116; A. Sikdar, T. Satoh, M. Kawasaki, *K. Kato, “Crystal structure of archaeal homolog of proteasome-assembly chaperone PbaA”, Biochem. Biophys. Res. Commun. 453, 493-497 (2014), DOI: 10.1016/j.bbrc; T. Zhu, T. Satoh, *K.Kato, “Structural insight into substrate recognition by the endoplasmic reticulum folding-sensor enzyme: crystal structure of third thioredoxin-like domain of UDP-glucose:glycoprotein glucosyltransferase,” Sci. Rep. 4, 7322, (2014), DOI: 10.1038/srep07322; T. Satoh, A. Sumiyoshi, M. Yagi-Utsumi, E. Sakata, H. Sasakawa, E. Kurimoto, Y. Yamaguchi, W. Li, C.A.P. Joazeiro, T. Hirokawa, *K.Kato, “Mode of substrate recognition by the Josephin domain of ataxin-3, which has an endo-type deubiquitinase activity,” FEBS Lett. 588, 4422-4430, (2014), DOI: 10.1016/j.febslet.2014.10.013; T. Yamaguchi, Y. Sakae, Y. Zhang, S. Yamamoto, Y. Okamoto, *K. Kato, “Exploration of Conformational Spaces of High-Mannose-Type Oligosaccharides by an NMR-Validated Simulation,” Angew. Chem. Int. Ed. 53, 10941-10944, (2014).DOI: 10.1002/anie.201406145; Y. Uekusa, K. Okawa, M. Yagi-Utsumi, O. Serve, Y. Nakagawa, T. Mizushima, H. Yagi, Y. Saeki, K. Tanaka, *K. Kato, “Backbone ¹H, ¹³C, and ¹⁵N Assignments of Yeast Ump1, an Intrinsically Disordered Protein that Functions as a Proteasome Assembly Chaperone”, Biomol. NMR Assign, 8, 383-386, (2014), DOI: 10.1007/s12104-013-9523-1; S. Ninagawa, T. Okada, Y. Sumitomo, Y. Kamiya, K. Kato, S. Horimoto, T. Ishikawa, S. Takeda, T. Sakuma, T. Yamamoto, *K. Mori, “EDEM2 initiates mammalian glycoprotein ERAD by catalyzing the first mannose trimming step,” J. Cell Biol. 206, 347-356, (2014), DOI: 10.1083/jcb.201404075; K. Takagi, Y. Saeki, H. Yashiroda, H. Yagi, A. Kaiho, S. Murata, T. Yamane, K. Tanaka, T. Mizushima, *K. Kato, “Pba3-Pba4 Heterodimer Acts as a Molecular Matchmaker in Proteasome α-ring Formation”, Biochem. Biophys. Res. Commun., 450(2), 1110-1114, (2014), DOI: 10.1016/j.bbrc.2014.06.119; T. Satoh, Y. Saeki, T. Hiromoto, Y. H. Wang, Y. Uekusa, H. Yagi, H. Yoshihara, M. Yagi-Utsumi, T. Mizushima, K. Tanaka, *K. Kato, “Structural Basis for Proteasome Formation Controlled by an Assembly Chaperone Nas2”, Structure, 22(5), 731-743, (2014), DOI: 10.1016/j.str.2014.02.014; *T. Doi, M. Yoshida, K. Ohsawa, K. Shin-ya, M. Takagi, Y. Uekusa, T. Yamaguchi, K. Kato, T.Hirokawa, T. Natsume, “Total Synthesis and Characterization of Thielocin B1 as a Protein-protein Interaction Inhibitor of PAC3 Homodimer”, Chem. Sci., 5, 1860-1868, (2014), DOI: 10.1039/C3SC53237B; T. Satoh, K. Suzuki, T. Yamaguchi, *K. Kato, “Structural Basis for Disparate Sugar-binding Specificities in the Homologous Cargo Receptors ERGIC-53 and VIP36”, PLoS One, 9(2), e87963, (2014), DOI: 10.1371/journal.pone.0087963; M. Sugiyama, H. Yagi, T. Yamaguchi, K. Kumoi, M. Hirai, Y. Oba, N. Sato, L. Porcar, A. Martel, *K. Kato, “Conformational Characterization of a Protein Complex Involving Intrinsically Disordered Protein by Small-angle Neutron Scattering Using the Inverse Contrast Matching Method: a Case Study of Interaction between α-synuclein and PbaB Tetramer as a Model Chaperone”, J. Appl. Cryst., 47(1), 430-435, (2014), DOI: 10.1107/S1600576713033475; S. Kitazawa, T. Kameda, A. Kumo, M. Yagi-Utsumi, N. J. Baxter, K. Kato, M. P. Williamson, *R. Kitahara, “Close Identity between Alternatively Folded State N2 of Ubiquitin and the Conformation of the Protein Bound to the Ubiquitin-activating Enzyme”, Biochemistry, 53(3), 447-449, (2014), DOI: 10.1021/bi401617n; 矢木宏和，矢木-内海真穂，*加藤晃一, “糖鎖構造生物学の最前線”ファルマシア, 50, 746-750（2014）; Y. Kamiya, T. Satoh, *K. Kato, “Recent Advances in Glycoprotein Production for Structural Biology: Toward Tailored Design of Glycoforms”, Curr. Opin. Struct. Biol., 26, 44-53, (2014), DOI: 10.1016/j.sbi.2014.03.008; H. Yagi, N. Nakagawa, T. Saito, H. Kiyonari, T. Abe, T. Toda, S-W. Wu, K-H. Khoo, *S. Oka, *K. Kato, “AGO61-dependent GlcNAc Modification Primes the Formation of Functional Glycans on α-dystroglycan”, Sci. Rep., 3, 3288, (2013), DOI: 10.1038/srep03288; S. Horimoto, S. Ninagawa, T. Okada, H. Koba, T. Sugimoto, Y. Kamiya, K. Kato, S. Takeda, *K. Mori, “The Unfolded Protein Response Transducer ATF6 Represents a Novel Transmembrane-type Endoplasmic Reticulum-associated Degradation Substrate Requiring Both Mannose Trimming and SEL1L Protein”, J. Biol. Chem., 288, 31517-31527, (2013), DOI: 10.1074/jbc.M113.476010; K. Araki, S. Iemura, Y. Kamiya, D. Ron, K. Kato, T. Natsume, *K. Nagata, “Ero1-α and PDIs Constitute a Hhierarchical Electron Transfer Network of Endoplasmic Reticulum Oxidoreductases” J. Cell Biol., 202(6), 861-874, (2013), DOI: 10.1083/jcb.201303027; Y. Zhang, T. Yamaguchi, *K. Kato, “New NMR Tools for Characterizing the Dynamic Conformations and Interactions of Oligosaccharides”, Chem. Lett., 42(12), 1455-1462, (2013), DOI: 10.1246/cl.130789; 【図書】; K. Kato, H. Yagi, *Y. Yamaguchi, “NMR Characterization of the Dynamic Conformations of Oligosaccharides”, Modern Magnetic Resonance, 2nd Edition, (G.A.Webb ed.), Springer International Publishing, in press, (2018), DOI: 10.1007/978-3-319-28275-6_35-1; Y. Yamaguchi, H. Yagi, *K. Kato, “Stable Isotope Labeling of Glycoproteins for NMR Study”, NMR in Glycoscience and Glycotechnology, (K.Kato and T.Peters ed.), RSC Publishing (Cambridge), pp.194-207, (2017), 10.1039/9781782623946-00194; M. Yagi-Utsumi, T. Yamaguchi, Y. Uekusa, *K. Kato, “NMR Characterization of the Conformations, Dynamics, and Interactions of Glycosphingolipids”, NMR in Glycoscience and Glycotechnology, (Kato,K. and Peters ed,T.), RSC Publishing (Cambridge), pp.161-178, (2017), DOI: 10.1039/9781782623946-00161; K.Kato, S.Yanaka and H.Yagi, “Technical basis for nuclear magnetic resonance approach for glycoproteins,” Experimental Approaches of NMR Spectroscopy (2017).; T.Ikeya, D.Ban, D.Lee, Y.Ito, K.Kato, and C.Griesinger, “Solution NMR views of dynamical ordering of biomacromolecules,” Biochim. Biophys. Acta –General Subjects (2017).; K.Matsuzaki, K.Kato, and K.Yanagisawa, “Ganglioside-mediated assembly of amyloid β-protein: Roles in Alzheimer's disease,” Prog. Mol. Biol. Transl. Sci. (2017).; 加藤晃一, 谷中冴子, 矢木-内海真穂 “NMR構造生物学がもたらす新たな創薬研究のツール”MEDCHEM NEWS, 26, 195-200, (2016); G. Mandal, H. Yagi, K. Kato, and B. P. Chatterjee, “Structural heterogeneity of glycoform of alpha-1 acid glycoprotein in alcoholic cirrhosis patient”, Advances in Experimental Medicine and Biology (A.Chakrabarti and A.Surolia ed.), Springer (Switzerland), 842, 389-401, (2015); Y. Zhang, T. Yamaguchi, T. Satoh, M. Yagi-Utsumi, Y. Kamiya, Y. Sakae, Y. Okamoto, K. Kato, “Conformational dynamics of oligosaccharides characterized by paramagnetism-assisted NMR spectroscopy in conjunction with molecular dynamics simulation”, Advances in Experimental Medicine and Biology, Volume 842, pp 217-230 (2015). (A. Chakrabarti and A. Surolia ed. Springer) DOI: 10.1007/978-3-319-11280-0_14; T. Yamaguchi, K. Kato, “Paramagnetism-assisted nuclear magnetic resonance analysis of dynamic conformations and interactions of oligosaccharides,” Glycoscience: Biology and Medicine, Volume 1, pp 137-145 (2014). (N. Taniguchi, T. Endo, G.W. Hart, P. Seeberger, and C.-H. Wong ed. Springer Japan) DOI: 10.1007/978-4-431-54841-6_101; Y. Yamaguchi, T. Yamaguchi, K. Kato, “Structural analysis of oligosaccharides and glycoconjugates using NMR,” Glycobiology of the Nervous System, pp.165-183 (2014). (R. K. Yu and C.-L. Schengrund ed. Springer New York) DOI: 10.1007/978-1-4939-1154-7_8; 加藤晃一，山口拓実, “NMR 原理”, 揺らぎ・ダイナミクスと生体機能（寺嶋正秀編）, 化学同人, pp. 69-79, (2013); 矢木宏和，加藤晃一, “IgG-FcとFc受容体の複合体形成における糖鎖の役割”, 実験医学増刊, 31(10), 6月号, pp.1602-1606, (2013), (羊土社、東京), ISBN:9784758103312; 矢木宏和，加藤晃一, “神経幹細胞の幹細胞性維持における複合糖質の役割”, 生化学, 85(11), 11月号, pp.1012-1016, (2013), (日本生化学会,東京)
菊地和也 ▲班員一覧に戻る▲: 【雑誌論文】; Y. Hori, N. Otomura, A. Nishida, M. Nishiura, M. Umeno, I. Suetake, K. Kikuchi*, “Synthetic-Molecule/Protein Hybrid Probe with Fluorogenic Switch for Live-Cell Imaging of DNA Methylation”, J. Am. Chem. Soc. 2018, 140, 1686-1690, DOI: 10.1021/jacs.7b09713; R. Sato, J. Kozuka, *M. Ueda, R. Mishima, *Y. Kumagai, A. Yoshimura, M. Minoshima, S. Mizukami, *K. Kikuchi "Intracellular Protein Labeling Probes for Multicolor Single-molecule Imaging of Immune Receptor-adaptor Molecular Dynamics," J. Am. Chem. Soc., in press (2017), DOI: 10.1021/jacs.7b08262; Y. Matsui, *S. Mizukami, *K. Kikuchi ''Ratiometric Imaging of Intracellular Mg²⁺ Dynamics Using a Red Fluorescent Turn-off Probe and a Green Fluorescent Turn-on Probe'', Chem. Lett. in press (2017), DOI: 10.1246/cl.170918; Y. Hori, S. Hirayama, *K. Kikuchi ''Development of Cyanine Probes with Dinitrobenzene Quencher for Rapid Fluorogenic Protein Labeling'' Philos. Trans. R. Soc. A, 375, in press (2017), DOI: 10.1098/rsta.2017.0018; Y. Matsui, Y. Funato, H. Imamura, H. Miki, *S. Mizukami, *K. Kikuchi ''Visualization of Long-term Mg²⁺ Dynamics in Apoptotic Cells with a Novel Targetable Fluorescent Probe'', Chem. Sci., in press (2017), DOI: 10.1039/c7sc03954a; Y. Matsui, K. K. Sadhu, *S. Mizukami, *K. Kikuchi ''Highly Selective Tridentate Fluorescent Probes for Visualizing Intracellular Mg²⁺ Dynamics without Interference from Ca²⁺ Fluctuation'', Chem. Commun., 53, 10644-10647 (2017), DOI: 10.1039/c7cc06141b; S. Mizukami, M. Kashibe, K. Matsumoto, Y. Hori, *K. Kikuchi, “Enzyme-triggered Compound Release Using Functionalized Antimicrobial Peptide Derivatives”, Chem. Sci., 8, 3047-3052, (2017), DOI: 10.1039/C6SC04435B; M. Minoshima, and *K. Kikuchi, “Photostable and Photoswitching Fluorescent Dyes for Super-resolution Imaging”, J. Biol. Inorg. Chem., 22, 1_14 (2017), DOI: 10.1007/s00775-016-1435-y; S. Hirayama, Y. Hori, Z. Benedek, T. Suzuki, *K. Kikuchi, “Fluorogenic Probes Reveal a Role of GLUT4 N-glycosylation in Intracellular Trafficking”, Nat. Chem. Biol., 12, 853-859, (2016), DOI: 10.1038/nchembio.2156; H. Maeda, T. Kowada, J. Kikuta, M. Furuya, M. Shirazaki, S. Mizukami, M, Ishii, *K. Kikuchi, “Real-time Intravital Imaging of pH Variation Associated with Osteoclast Activity and Motility Using Designed Small Molecular Probe”, Nat. Chem. Biol., 12, 579-585, (2016), DOI: 10.1038/nchembio.2096; S. Sotoma, J. Iimura, R. Igarashi, K.M. Hirosawa, H. Ohnishi, S. Mizukami, K. Kikuchi, T.K. Fujiwara, *M. Shirakawa, *H. Tochio, “Selective Labeling of Proteins on Living Cell Membranes Using Fluorescent Nanodiamond Probes”, Nanomaterials, 6, 56, 9p (2016), DOI: 10.3390/nano6040056; T. Wasin, K. Enomoto, T. Sakurai, V. Padalkar, H. Cheng, M. Tang, A. Horio, D., Sakamaki, M. Omichi, A. Saeki, K. Kikuchi, Y. Hori, A. Chiba, Y. Saito, T. Kamiya, M. Sugimoto, *S. Seki, “Fabrication of ‘Clickable’ Polyfluorene Nanowires with High Aspect Ratio as Biological Sensing Platforms”, ACS Sensors, 6, 766-774, (2016), DOI: 10.1021/acssensors.6b00070; Y. Kamikawa, Y. Hori, K. Yamashita, L. Jin, S. Hirayama, D.M. Standley, *K. Kikuchi, “Design of a Protein tag and Fluorogenic Probe with Modular Structure for Live-Cell Imaging of Intracellular Proteins”, Chem. Sci., 7, 308-314, (2016), DOI: 10.1039/C5SC02351C; Y. Hori, S. Hirayama, M. Sato, *K. Kikuchi, “Redesign of Fluorogenic Labeling System to Improve Surface Charges, Brightness, and Binding Kinetics for Imaging Functional Localization of Bromodomains”, Angew. Chem. Int. Ed., 54, 14368-14371, (2015), DOI: 10.1002/anie.201506935; Z. Zhang, S. Mizukami, K. Fujita, *K. Kikuchi, “An Enzyme-Responsive Metal-Enhanced Near-Infrared Fluorescence Sensor Based on Functionalized Gold Nanoparticles”, Chem. Sci., 6, 4934-4939, (2015), DOI: 10.1039/C5SC01850A; K. Mochizuki, L. Shi, S. Mizukami, M. Yamanaka, M. Tanabe, W.T. Gong, A.F. Palonpon, S. Kawano, S. Kawata, K. Kikuchi, *K. Fujita, “Nonlinear Fluorescence Imaging by using Photoinduced Charge Separation”, Jpn. J. Appl. Phys., 54, 042403, (2015), DOI: 10.7567/JJAP.54.042403; *K. Kikuchi, “¹⁹F MRI Probes with Tunable Switches and Highly Sensitive ¹⁹F MRI Nano-probes”, Bull. Chem. Soc. Japan, 88, 518-522, (2015), DOI: 10.1246/bcsj.20140392; M. Minoshima, *K. Kikuchi, “Chemical Probes for Elucidating Histone Deacetylase Function”, Anal. Sci., 31, 287-292, (2015), DOI: 10.2116/analsci.31.287; T. Kowada, Y. Hori, *K. Kikuchi, “BODIPY-based Fluorescent Probes for Biological Applications”, Chem. Soc. Rev., 44, 4953-4972, (2015), DOI: 10.1039/c5cs00030k; T. Nakamaura, F. Sugihara, H. Matsushita, Y. Yoshioka, S. Mizukami, *K. Kikuchi“Mesoporous Silica Nanoparticles for 19F Magnetic Resonance Imaging, Fluorescence Imaging, and Drug Delivery”, Chem. Sci., 6, 1986-1990, (2015), DOI: 10.1039/C4SC03549F; R. Baba, Y. Hori, *K. Kikuchi, “Intramolecular Long-distance Nucleophilic Reactions as a Rapid Fluorogenic Switch Applicable to detection of Enzymatic Activity”, Chem. Eur. J. 21, 4695-4702, (2015), DOI: 10.1002/chem.201406093; T. Nakamura, H. Matsushita, F. Sugihara, Y. Yoshioka, S. Mizukami, *K. Kikuchi, “Activatable 19F MRI Nanoparticle Probes for the Detection of Reducing Environments”, Angew. Chem. Int. Ed., 54, 1007-1010, (2015), DOI: 10.1002/anie.201409365; M. Minoshima, T. Matsumoto, *K. Kikuchi, “Development of Fluorogenic Probe based on a DNA Staining Dye for Continuous Monitoring of the Histone Deacetylase Reaction”, Anal. Chem., 86(15), 7925-7930, (2014), DOI: 10.1021/ac501881s; S. Okada, S. Mizukami, T. Sakata, Y. Matsumura, Y. Yoshioka, *K. Kikuchi, “Ratiometric MRI Sensors Based on Core-Shell Nanoparticles for Quantitative pH Imaging”, Adv. Mater., 26(19), 2989-2992, (2014), DOI: 10.1002/adma.201305018; H. Matsushita, S. Mizukami, F. Sugihara, Y. Nakanishi, Y. Yoshioka, *K. Kikuchi, “Multifunctional Core-shell Silica Nanoparticles for Highly Sensitive ¹⁹F MRI”, Angew. Chem. Int. Ed., 53(4), 1008-1011, (2014), DOI: 10.1002/anie.201308500; A. Yoshimura, S. Mizukami, Y. Mori, Y. Yoshioka, *K. Kikuchi, “¹H MRI Detection of Gene Expression in Living Cells by Using Protein Tag and Biotinylation Probe”, Chem. Lett., 43, 219-221, (2014), DOI: 10.1246/cl.130942; S. Mizukami, Y. Hori, *K. Kikuchi, “Small-Molecule-Based Protein-Labeling Technology in Live Cell Studies: Probe-Design Concepts and Applications”, Acc. Chem. Res., 47(1), 247–256, (2014), DOI: 10.1021/ar400135f
佐甲靖志 ▲班員一覧に戻る▲: 【雑誌論文】; *Y. Shindo, Y. Kondo, *Y. Sako, “Inferring a Nonlinear Biochemical Network Model from a Heterogeneous Single-cell Time Course Data,” Sci. Rep., in press.; R. Maeda, M. Hiroshima, T. Yamashita, A. Wada, Y. Sako, Y. Shichida, *Y. Imamoto, “Shift in Conformational Equilibrium Induces Constitutive Activity of G-Protein Coupled Receptor, Rhodopsin,” J. Phys. Chem. B. in press, DOI: 10.1021/acs.jpcb.8b02819; K. Okamoto., M. Hiroshima, *Y. Sako “Single-molecule fluorescence based analysis of protein conformation, interaction, and oligomerization in cellular systems,” Biophys. Rev. in press.; S. Magi, K. Iwamoto, N. Yumono, M. Hiroshima, T. Nagashima, R. Ohki, A. Garcia-Munoz, N. Volinsky, A. Von Kriegsheim, Y. Sako, K. Takahashi, S. Kimura, B. N. Kholodenko, *M. Okada-Hatakeyama、“Transcriptionally Inducible Pleckstrin Homology-like Domain Family A Member 1 Attenuates ErbB Receptor Activity by Inhibiting Receptor Oligomerization,” J. Biol. Chem., 293, 2206, (2018), DOI: 10.1074/jbc.M117.778399; R. Maeda, T. Sato, K. Okamoto, M. Yanagawa, *Y. Sako, “Lipid-protein Interplay in Dimerization of the Juxtamembrane Domains of Epidermal Growth Factor Receptor,” Biophys. J., 114, 893, (2018), DOI: 10.1016/j.bpj.2017.12.029; M. Hiroshima, C.-g. Pack, K. Kaizu, K. Takahashi, M. Ueda, *Y. Sako, “Transient Acceleration of Epidermal Growth Factor Receptor Dynamics Produces Higherorder Signaling Clusters,” J. Mol. Biol., 430(9), 1386-1401, DOI: 10.1016/j.jmb.2018.02.018; Y, Nakamura, N. Umeki, M. Abe *Y. Sako “Mutation-specific mechanisms of hyperactivation of Noonan syndrome SOS molecules detected with single-molecule imaging in living cells,” Sci. Rep. 7, 14153 (2017) DOI: 10.1038/s41598-017-14190-6; *R. Iino, T. Iida, A. Nakamura, E. Saita, H. You, Y. Sako “Single-molecule imaging and manipulation of biomolecular machines and systems,” Biochem. Biophys. Acta. General Subjects, Available online (2017) DOI: 10.1016/j.bbagen.2017.08.008; R. Yoshizawa, *N. Umeki, M. Yanagawa, M. Murata, *Y. Sako “Single-molecule fluorescence imaging of RalGDS on cell surfaces during signal transduction to Ras to Ral,” Biophys. Physicobiol. 14, 75-84 (2017) DOI: 10.2142/biophysico.14.0_75; *K. Okamoto, Y. Sako, “Recent Advances in FRET for the Study of Protein Interactions and Dynamics,” Curr. Opin. Strct. Biol. 46, 16-23, (2017), DOI: 10.1016/j.sbi.2017.03.010; *Y. Arata, M. Hiroshima, C.-G. Pack, R. Ramanujam, F. Motegi, K. Nakazato, P. W. Wiseman, H. Sawa, T. J. Kobayashi, H. B. Brandão, T. Shibata, *Y. Sako, “Cortical Polarity of the RING Protein PAR-2 is Maintained by Exchange Rate Kinetics at the Cortical-cytoplasm Boundary,”, Cell Rep. 16, 2156-2168, (2016), DOI: 10.1016/j.celrep.2016.07.047; 新土優樹、小迫英尊、佐甲靖志、高橋恒一 “細胞内シグナルのアナログ・デジタル変換” 生物物理 56, 334, (2016), DOI: 10.2142/biophys.56.334; K. Okamoto, *Y. Sako, “State Transition Analysis of Spontaneous Branch Migration of the Holliday Junction by Photon-based Single-molecule Fluorescence Resonance Energy Transfer” Biophys. Chem., 209, 21-27, (2016), DOI: 10.1016/j.bpc.2015.11.004; Y. Nakamura, K. Hibino, T. Yanagida, *Y. Sako, “Switching of the Positive Feedback for RAS Activation by a Concerted Function of SOS Membrane Association Domains, ” Biophys. Physicobiol., 13, 1-11, (2016), DOI: 10.2142/biophysico.13.0_1; Y. Zhou, H. Mao, B. Joddar, N. Umeki, Y. Sako, C. Nishioka, E. Takahashi, K. Wada, Y. Wang, *Y. Ito, “The Significance of Membrane Fluidity of Feeder Cell-derived Substrates for Maintenance of iPS Cell Stemness”, Sci. Rep. 5, 11386, (2015), DOI: 10.1038/srep11386; M.Yanagawa, K. Kojima, T. Yamashita, Y. Imamoto, T. Matsuyama, K. Nakanishi, Y. Yamano, A. Wada, Y. Sako, *Y. Shichida, “Origin of the Low Thermal Isomerization Rate of Rhodopsin Chromophore”, Sci. Rep. 5, 11081, (2015), DOI: 10.1038/srep11081; S. Iwata, K. Masuhara, N. Umeki, Y. Sako, *S. Maruta, “Interaction of a Novel fluorescent GTP Analogue with the Small G-protein K-Ras”, J. Biochem. on line, (2015), DOI: 10.1093/jb/mvv071; H. Park, S.-S. Han, Y. Sako, *C.-G. Pack, “Dynamic and Unique Nucleolar Microenvironment Revealed by Fluorescence Correlation Spectroscopy”, FASEB J. 29, 837, (2015), DOI: 10.1096/fj.14-254110; H. Shinohara, M. Behar, K. Inoue, M. Hiroshima, T. Yasusda, T. Nagashima, S. Kimura, H. Sanjo, S. Maeda, N. Yumoto, S. Ki, S. Akira, Y. Sako, A. Hoffman, T. Kurosaki,* M. Okada-Hatakeyama, “Positive Feedback within a Kinase Signaling Complex Functions as a Switch Mechanism for NF-κΒ Activation”, Science, 344(6185), 760-764, (2014), DOI: 10.1126/science.1250020; 【図書】; 柳川正隆、佐甲靖志“細胞膜受容体の１分子イメージング”, 生体の科学 68, 386-387 (2017); 廣島通夫、佐甲靖志“蛍光１分子可視化技術と超局在化顕微鏡法”　実験医学別冊「初めてでもできる！超解像イメージング」岡田康志編、羊土社（日本）、pp. 213-218, 2016; Pack, C.-G., Jung, M.-K., Song, M.-R., Kim, J.-S., Han, S.-S., and Sako, Y.“Use of engineered nanoparticle-based fluorescence methods for live-cell phenomena”Fluorescence Microscopy: Super-Resolution and Other Novel Techniques, 　153-170,(2014),Cornea,A. and Conn, P. M. eds. (Elsevier, the Netherlands); 佐甲靖志、廣島通夫、日比野佳代 “細胞内情報処理反応の１分子計測：蛋白質ダイナミクスと分子認識”「１分子ナノバイオ計測、分子から生命システムを探る革新的技術」,pp.180-189, (2014), 野地博行編, (化学同人, 京都, 日本)
笹井理生 ▲班員一覧に戻る▲: 【雑誌論文】; T. Okuno, K. Kato, S. Minami, T. P. Terada, M. Sasai, *G. Chikenji, “Importance of Consensus Region of Multiple-ligand Templates in a Virtual Screening Method”, Biophys. Physicobiol., 13, 149-156 (2016)DOI: 10.2142/biophysico.13.0_149; *笹井理生，寺田智樹“真核細胞のルースな遺伝子制御とクロマチン動態, ” 生物物理 56, 106-108 (2016); *K. Maeshima, S. Ide, K. Hibino, M. Sasai, “Liquid-like Behavior of Chromatin”, Curr Opin Genet Dev., 37, 36-45, (2016), DOI: 10.1016/j.gde.2015.11.006; S. S. Ashwin, *M. Sasai, “Effects of Collective Histone State Dynamics on Epigenetic Landscape and Kinetics of Cell Reprogramming,” Sci. Rep., 5, 16746, (2015), DOI: 10.1038/srep16746; C. Chen, K. Zhang, H. Feng, M. Sasai, *J. Wang, “Multiple Coupled Landscapes and Non-diabatic Dynamics with Applications to Self Activating Genes,” Phys. Chem. Chem. Phys. 17, 29036-29044, (2015), DOI: 10.1039/C5CP04780C; T. Okuno, K. Kato, T. Terada, M. Sasai, *G. Chikenji, “VS-APPLE: A Virtual Screening Algorithm Using Promiscuous Protein-Ligand Complexes”, J. Chem. Inf. Model., 55, 1108–1119, (2015), DOI: 10.1021/acs.jcim.5b00134; S. S. Ashwin, M. Sasai, “Epigenetic Dynamics of Cell Reprogramming””, arXiv, 1410.2337, (2014), http://arxiv.org/abs/1410.2337; T. Inanami, T. P. Terada, *M. Sasai, “Coupling of Lever Arm Swing and Biased Brownian Motion in Actomyosin”, Proc. Natl. Acad. Sci., USA, 111, 15969–15974, (2014), DOI: 10.1371/journal.pcbi.1003552; 【図書】; Naoko Tokuda and Masaki Sasai, “Modeling of genomes”, Coarse-Grained Modeling of Biomolecules 第21章 in press Garegin A. Papoian編, (Taylor & Francis Books, UK)
佐藤健 ▲班員一覧に戻る▲: 【雑誌論文】; A. Sakaguchi, M. Sato, K. Sato, K. Gengyo-Ando, T. Yorimitsu, J. Nakai, T. Hara, K. Sato, *K. Sato, “REI-1 is a Guanine Nucleotide Exchange Factor Regulating RAB-11 Localization and Function in C. elegans embryos”, Dev. Cell., 35, 211-221, (2015), DOI: 10.1016/j.devcel.2015.09.013; K. Ishii, H. Enda, M. Noda, M. Kajino, A. Kim, E. Kurimoto, K. Sato, A. Nakano, Y. Kobayashi, H. Yagi, S. Uchiyama, *K. Kato, “pH-dependent Assembly and Segregation of the Coiled-coil Segments of Yeast Putative Cargo Receptors Emp46p and Emp47p”, PLoS ONE, 10, e140287, (2015), DOI: 10.1371/journal.pone.0140287; H. Iwasaki, T. Yorimitsu, *K. Sato“Distribution of Sec24 Isoforms to each ER Exit Site is Dynamically Regulated in Saccharomyces Cerevisiae”, FEBS Lett. 589, 1234-1239, (2015), DOI: 10.1016/j.febslet.2015.04.006; T. Yorimitsu, K. Sato, *M. Takeuchi, “Molecular Mechanisms of Sar/Arf GTPases in Vesicular Trafficking in Yeast and Plant.”, Front.Plant Sci. 5, 411, (2014), DOI: 10.3389/fpls.2014.00411; C. Kodera, T. Yorimitsu, *K. Sato, “Sec23 Homolog Nel1 is a Novel GTPase-activating Protein for Sar1 but Does Not Function as a Subunit of the COPII Coat.”, J. Biol. Chem. 289, 21423-21432, (2014), DOI: 10.1074/jbc.M114.553917; K. Ebine, T. Inoue, J. Ito, E. Ito, T. Uemura, T. Goh, H. Abe, K. Sato, A. Nakano, *T. Ueda, “Plant Vacuolar Trafficking Occurs through Distinctly Regulated Pathway.”, Curr. Biol. 24(12), 1375-1382, (2014), DOI: 10.1016/j.cub.2014.05.004
申惠媛 ▲班員一覧に戻る▲: 【雑誌論文】; N. Takada, T. Naito, T. Inoue, K. Nakaama, H. Takatsu, *H.-W. Shin, “Phospholipid-flipping Activity of P4-ATPase Drives Membrane Curvature,” EMBO J., in press, (2018), DOI: 10.15252/embj.201797705 プレスリリース：http://www.kyoto-u.ac.jp/ja/research/research_results/2017/180329_1.html, https://www.eurekalert.org/pub_releases/2018-03/ku-flf032818.php; H. Takatsu, M. Takayama, T. Naito, N. Takada, K. Tsumagari, Y. Ishihama, K. Nakayama, *H.-W. Shin “Phospholipid flippase ATP11C is endocytosed and downregulated following Ca2+-mediated protein kinase C activation,” Nat. Commun. 8, 1423 (2017) DOI: 10.1038/s41467-017-01338-1; K.H. Tomaszowski, N. Hellmann, V. Ponath, H. Takatsu, H.-W. Shin, *B. Kaina “Uptake of glucose-conjugated MGMT inhibitors in cancer cells: role of flippases and type IV P-type ATPases,” Sci. Rep. 7, 13925 (2017) DOI: 10.1038/s41598-017-14129-x; A. Hanai, M. Ohgi, C. Yagi, T. Ueda, H.-W. Shin, *K. Nakayama, “Class I Arfs (Arf1 and Arf3) and Arf6 are Localized to the Flemming Body and Play Important Roles in Cytokinesis’', J. Biochem., 159, 201 (2016) DOI: 10.1093/jb/mvv088 (2017年JB論文賞); Y. Tanaka, N. Ono, T. Shima, G. Tanaka, Y. Katoh, K. Nakayama, H. Takatsu, *H.-W. Shin, “The Phospholipid Flippase ATP9A is Required for Recycling Pathway from Endosomes to the Plasma Membrane”, Mol. Biol. Cell., 27, 3883, (2016), DOI: 10.1091/mbc.E16-08-0586 (Selected for highlights); R. Miyano, T. Matsumoto, H. Takatsu, K. Nakayama, *H.-W. Shin, “Alteration of Transbilayer Phospholipid Compositions is Involved in Cell Adhesion, Cell Spreading, and Focal Adhesion Formation”, FEBS Lett., 590, 2138, (2016), DOI: 10.1002/1873-3468.12247; A. Hanai, M. Ohgi, C. Yagi, T. Ueda, H.-W. Shin, *K. Nakayama, “Class I Arfs (Arf1 and Arf3) and Arf6 are Localized to the Flemming Body and Play Important Roles in Cytokinesis”, J. Biochem., 159, 201, (2016), DOI: 10.1093/jb/mvv088; 【図書】; *申　惠媛、中山和久, 8章Arfファミリーによるメンブレントラフィックの調節．Dojin BioScience Series 24 メンブレントラフィック　福田光則・吉森保編　化学同人　pp. 114-129, 2016
真行寺千佳子 ▲班員一覧に戻る▲: 【雑誌論文】; H. Yoke, *C. Shingyoji, “Effects of External Strain on the Regulation of Microtubule Sliding Induced by Outer arm Dynein of Sea Urchin Sperm Flagella,” J. Exp. Biology, 1122-1134, (2017), DOI: 10.1242/jeb.147942; *C. Shingyoji, I. Nakano, Y. Inoue, H. Higuchi, “Dynein arms are strain-dependent direction-switching force Generators,“ Cytoskeleton , 72, 388-401, (2015), DOI: 10.1002/cm.21232; 【図書】; C. Shingyoji, “Regulation of Dynein-driven Ciliary and Flagellar Movement,” In Dyneins - Structure, Biology and Disease (2nd ed.), S. M. King ed., Chapter11. pp. 337-367, (Academic Press, N.Y.), (2017), in press.; H. Higuchi and C. Shingyoji, “Measuring the Motile Properties of Single Dynein Molecules,” In Handbook of Dynein, K. Hirose ed.,_Chapter 5 (Pan Stanford Publishing Pte. Ltd.), (2017), in press; C. Shingyoji“Regulation of Dynein Activity in Oscillatory Movement of Sperm Flagella”, Muscle Contraction and Cell Motility, H. Sugi ed., Pan Stanford Publishing, Chap. 15, pp.371 -386, (2016)
杉山正明 ▲班員一覧に戻る▲: 【雑誌論文】; *Y. Nagata, T. Nishikawa, *M. Suginome, S. Sato, *M. Sugiyama, L. Porcar, A. Martel, R. Inoue, N. Sato, “Elucidating the Solvent Effect on the Switch of the Helicity of Poly(quinoxaline-2,3-diyl)s: A Conformational Analysis by Small-Angle Neutron Scattering”, J. Am. Chem. Soc., 140, 2722–2726, (2018), DOI: 10.1021/jacs.7b11626; M. Yagi-Utsumi, A. Sikdar, T. Kozai, R. Inoue, M. Sugiyama, T. Uchihashi, H. Yagi, T. Satoh, K. Kato, “Conversion of Functionally Undefined Homopentameric Protein PbaA into a Proteasome Activator by Mutational Modification of its C-terminal Segment Conformation”, Protein Eng. Des.Sel., 31, 29-36, (2018), DOI: 10.1093/protein/gzx066; P. Bernadó, N. Shimizu, G. Zaccai, H. Kamikubo, *M. Sugiyama, “Solution scattering approaches to dynamical ordering in biomolecular systems”, Biochimica et Biophysica Acta-General Subjects, 1862, 253-274, (2017), DOI: 10.1016/j.bbagen.2017.10.015; E. Hibino, R. Inoue, M. Sugiyama, J. Kuwahara, K. Matsuzaki, M. Hoshino, “Identification of heteromolecular binding sites in transcription factors Sp1 and TAF4 using high-resolution NMR spectroscopy”, Protein Sci., 26, 2280-2290, (2017), DOI: 10.1002/pro.3287; R. Yogo, S. Yanaka, H. Yagi, A. Martel, L. Porcar, Y. Ueki, R. Inoue, N. Sato, M. Sugiyama, K. Kato, “Characterization of conformational deformation-coupled interaction between immunoglobulin G1 Fc glycoprotein and a low-affinity Fcγ receptor by deuteration-assisted small-angle neutron scattering”, Biochem. Biophys. Rep., 12, 1-4, (2017), DOI: 10.1016/j.bbrep.2017.08.004; J. Trewhella, A. P. Duff, D. Durand, F. Gabel, J. M. Guss, W. A. Hendrickson, G. L. Hura, D. A. Jacques, N. M. Kriby, A. H. Kwan, J. Perez, L. Pollack, T. M. Ryan, A. Sali, D. Schneidman-Duhovny, T. Schwede, D. I. Svergun, M. Sugiyama, J. A. Tainer, P. Vachette, J. Westbrook, and A. E. Whitten, “2017 Publication guidelines for structural modelling of small-angle scattering data from biomolecules in solution: an update”, Acta Crystallographica, D73, 710-728, (2017), DOI: 10.1107/S2059798317011597; M. Sugiyama, H. Nakagawa, R. Inoue, Y. Kawakita, “Neutron Biology for Next Generation”, J-PARC-Review, 2017-024, 1-46, (2017)(Japanese); *M. Sugiyama, H. Yagi, K. Ishii, L. Porcar, A. Martel, K. Oyama, M. Noda, Y. Yunoki, R. Murakami, R. Inoue, N. Sato, Y. Oba, K. Terauchi, S. Uchiyama, *K. Kato, “Structural Characterization of the Circadian Clock Protein Complex Composed of KaiB and KaiC by Inverse Contrast-matching Small-angle Neutron Scattering”, Sci Rep., 6, 35567, (2016), DOI: 10.1038/srep35567; E. Hibino, R. Inoue, M. Sugiyama, J. Kuwahara, K. Matsuzaki, and *M. Hoshino, “Interaction between Intrinsically Disordered Regions in Transcription Factors Sp1 and TAF4”, Protein Sci., 25, 2006-2017, (2016), DOI: 10.1002/pro.3013; R. Inoue, T. Takata, N. Fujii, K. Ishii, S. Uchiyama, N. Sato, Y. Oba, K. Wood, K. Kato, N. Fujii, and *M. Sugiyama, “New Insight into the Dynamical System of αB-crystallin Oligomers”, Sci Rep., 6, 29208, (2016), DOI: 10.1038/srep29208; *杉山正明, “中性子小角散乱による溶液中のタンパク質の構造解析”, 展望(日本アイソトープ協会学会誌)、3月号2016年; Y. Takemoto, T. Yamamoto, N. Ikuma, Y. Uchida, K. Suzuki, S. Shimono, H. Takahashi, N. Sato, Y. Oba, R. Inoue, M. Sugiyama, H. Tsue, T. Kato, J. Yamauchi, R. Tamura, “Preparation, Characterization and Magnetic Behavior of a Spin-labelled Physical Hydrogel Containing a Chiral Cyclic Mitroxide Radical Unit Fixed Inside the Gelator Molecule”, Soft Matter, 11, 5563-5570, (2015), DOI: 10.1039/C5SM01216C; *E. Chatani, *R. Inoue, H. Imamura, M. Sugiyama, Mi. Kato, M. Yamamoto, K. Nishida, T. Kanaya, “Early Aggregation Preceding the Nucleation of Insulin Amyloid Fibrils as Monitored by Small Angle X-ray Scattering”, Sci. Rep., 5, 15485, (2015), DOI: 10.1038/srep15485; *N. Sato, A. Matsumiya, Y. Higashino, S. Funaki, Y. Kitao, Y. Oba, R Inoue, F. Arisaka, Fumio, *M. Sugiyama, *R. Urade, “Molecular Assembly of Wheat Gliadins into Nanostructures: A Small-Angle X-Ray Scattering Study of Gliadins in Distilled Water over a Wide Concentration Range”, J. Agric. Food Chem., 63, 8715–8721, (2015), DOI: 10.1021/acs.jafc.5b02902; *M. Sugiyama, N. Horikoshi, Y. Suzuki, H. Taguchib, T. Kujirai, R. Inoue, Y. Oba, N. Sato, A. Martel, L. Porcar, *H. Kurumizaka, “Solution Structure of Variant H2A.Z.1 Nucleosome Investigated by Small-angle X-ray and Neutron Scatterings”, Biochem. Biophys. Rep., 4, 28-32, (2015), DOI: 10.1016/j.bbrep.2015.08.019; *M. Sugiyama, Y. Arimura, K. Shirayama, R. Fujita, Y. Oba, N. Sato, R. Inoue, T. Oda, M. Sato, R. K. Heenan; H. Kurumizaka, “Distinct Features of the Histone Core Structure in Nucleosomes Containing the Histone H2A.B Variant”, Biophys. J., 106, 2206-2213, (2014), DOI: 10.1016/j.bpj.2014.04.007; *N. Rahman, N. Sato, M. Sugiyama, Y. Hidaka, H. Okabe, K. Hara, “The Effect of Hot DMSO Treatment on the γ-ray-induced Grafting of Acrylamide onto PET films”, Polym. J., 46, 412–421, (2014), DOI: 10.1038/pj.2014.12; N. Rahman, N. Sato, M. Sugiyama, Y. Hidaka, H. Okabe, K. Hara, “Selective Hg(II) Adsorption from Aqueous Solutions of Hg(II) and Pb(II) by Hydrolyzed Acrylamide-grafted PET films”, J. Environ. Sci. Health., Part A, 49, 798-806, (2014), DOI: 10.1080/10934529.2014.882209; *K. Mori, K. Iwase, Y. Oba, T. Fukunaga, M. Sugiyama, “Surface Observation of LaNi5 under Deuterium Atmosphere Using Small-Angle Neutron Scattering”, Mater. Trans., 55, 1643-1646, (2014), DOI: 10.2320/matertrans.M2014009; Y. Oba, S. Abe, M. Ohnuma, N. Sato, M. Sugiyama, “Temperature dependence of the nanostructure in a PbSe–ZnSe composite thin film”, J. Phys. D: Appl. Phys., 47, (2014), 435102/1-6.; *M. Sugiyama*, H. Yagi, T. Yamaguchi, K. Kumoi, M. Hirai, Y. Oba, N. Sato, L. Porcar, A. Martel, *K. Kato, “Conformational Characterization of a Protein Complex Involving Intrinsically Disordered Protein by Small-angle Neutron Scattering Using the Inverse Contrast Matching Method: a Case Study of Interaction between α-synuclein and PbaB Tetramer as a Model Chaperone”, J. Appl. Crystallogr., 47, 430–435, (2014), DOI: 10.1107/S1600576713033475
茶谷絵理 ▲班員一覧に戻る▲: 【雑誌論文】; N. Yamamoto, S. Ito, M. Nakanishi, E. Chatani, K. Inoue, H. Kandori, K. Tominaga, “Effect of Temperature and Hydration Level on Purple Membrane Dynamics Studied Using Broadband Dielectric Spectroscopy from sub-GHz to THz Regions” J. Phys. Chem. B, 122, 1367-1377, (2018), DOI: 10.1021/acs.jpcb.7b10077; N. Yamamoto, S. Tsuhara, A. Tamura, *E. Chatani, “A Specific Form of Prefibrillar Aggregates that Functions as a Precursor of Amyloid Nucleation” Sci. Rep. 8, 62, (2018), DOI: 10.1038/s41598-017-18390-y; *E. Chatani, N. Yamamoto, “Recent Progress on Understanding the Mechanisms of Amyloid Nucleation”, Biophys. Rev., 10, 527-534, (2018), DOI: 10.1007/s12551-017-0353-8; T.H. Liu, K.I. Yuyama, T. Hiramatsu, N. Yamamoto, *E. Chatani, *H. Miyasaka, T. Sugiyama, *H. Masuhara, “Femtosecond-Laser-Enhanced Amyloid Fibril Formation of Insulin”, Langmuir 33, 8311-8318, (2017), DOI: 10.1021/acs.langmuir.7b01822; A. Nitani, H. Muta, M. Adachi, M. So, K. Sasahara, K. Sakurai, E. Chatani, K. Naoe, H. Ogi, D. Hall, *Y. Goto, “Heparin-dependent aggregation of hen egg white lysozyme reveals two distinct mechanisms of amyloid fibrillation”, J. Biol. Chem. in press, (2017), DOI: 10.1074/jbc.M117.813097; *E. Chatani, *R. Inoue, H. Imamura, M. Sugiyama, M. Kato, M. Yamamoto, K. Nishida, T. Kanaya, “Early Aggregation Preceding the Nucleation of Insulin Amyloid Fibrils as Monitored by Small Angle X-ray Scattering”, Sci. Rep. 5, 15485, (2015), DOI: 10.1038/srep15485; *茶谷絵理, “プログラムされていないフォールディング－アミロイド線維の形成－”, 生化学, 87, 292-297, (2015); *井上倫太郎, 茶谷絵理, 金谷利治, “小角X線散乱によるアミロイド線維形成機構に関する研究”, SPring-8/SACLA利用研究成果集 3, 2011B1996/BL40B2,(2015); *E. Chatani, H. Imamura, N. Yamamoto, *M. Kato, "Stepwise Organization of the β-structure Identifies Key Regions Essential for the Propagation and Cytotoxicity of Insulin Amyloid Fibrils", J. Biol. Chem., 289, 10399-10410, (2014), DOI: 10.1074/jbc.M113.520874; *E. Chatani, Y. Tsuchisaka, Y. Masuda, *R. Tsenkova "Water Molecular System Dynamics Associated with Amyloidogenic Nucleation as Revealed by Real Time Near Infrared Spectroscopy and Aquaphotomics", PLos One 9, e101997, (2014), DOI: 10.1371/journal.pone.0101997
寺内一姫 ▲班員一覧に戻る▲: 【雑誌論文】; *T. Teramoto, C. Azai, K. Terauchi, M. Yoshimura, T. Ohta, “Soft X-ray Imaging of Cellular Carbon and Nitrogen Distributions in Heterocystous Cyanobacterium”, Plant Physiology, in press; K. Oyama, C. Azai, J. Matsuyama, * K. Terauchi, “Phosphorylation at Thr432 Induces Structural Destabilization of the CII Ring in the Circadian Oscillator KaiC”, EBS Lett, 592, 36–45, (2018), DOI: 10.1002/1873-3468.12945; C. Azai, M. Kobayashi, T. Mizoguchi, H. Tamiaki, K. Terauchi, *Y. Tsukatani, “Rapid C8-vinyl Reduction of Divinyl-chlorophyllide a by BciA from Rhodobacter capsulatus” J. Photochem. Photobiol. A: Chemistry, 353, 661-666, (2018), DOI: 10.1016/j.jphotochem.2017.09.010; *寺内一姫, 大山克明, 浅井智広, “ブルーネイティブ電気泳動による時計タンパク質KaiCの動的構造解析” 電気泳動, 61, 107-110, (2017); *T. Teramoto, M. Yoshimura, C. Azai, K. Terauchi, T. Ohota, “Determination of carbon-to-nitrogen ratio in the filamentous and heterocystous cyanobacterium Anabaena sp. PCC” J. Phys. :Conf. Ser., 849, 012005, (2017), DOI: 10.1088/1742-6596/849/1/012005; K. Terauchi, R. Sobue, Y. Furutani, R.Aoki, *Y.Fujita, “Isolation of Cyanobacterial Mutants Exhibiting Growth Defects under Microoxic Conditions by Transposon Tagging Mutagenesis of Synechocystis sp. PCC 6803.” J. Gen. Appl. Microbiol., 63, 131-138, (2017), DOI: 10.2323/jgam.2016.08.004; K. Oyama, C. Azai, K. Nakamura, S. Tanaka, *K. Terauchi, “Conversion between Two Conformational States of KaiC is Induced by ATP Hydrolysis as a Trigger for Cyanobacterial Circadian Oscillation” Sci. Rep. 6, 32443, (2016), DOI: 10.1038/srep32443; M. Sugiyama, H. Yagi, K. Ishii, L. Porcar, A. Martel, K. Oyama, M. Noda, Y. Yunoki, R. Murakami, R. Inoue, N. Sato, Y. Oba, K. Terauchi, S. Uchiyama, *K. Kato, “Structural Characterization of the Circadian Clock Protein Complex Composed of KaiB and KaiC by Inverse Contrast Matching Small-angle Neutron Scattering”, Sci. Rep., 6, 35567, (2016), DOI: 10.1038/srep35567; *T. Teramoto, M. Yoshimura, C. Azai, K. Terauchi, T. Ohota, “Nitrogen mapping of the filamentous and heterocystous cyanobacterium Anabaena sp. PCC 7120 cells by soft X-ray microscopy”, Mem. SR cent. Ritsumeikan Univ. 18, 125-126, (2016); J. Nomata, K. Terauchi, *Y. Fujita, “Stoichiometry of ATP Hydrolysis and Chlorophyllide Formation of Dark-operative Protochlorophyllide Oxidoreductase from Rhodobacter Capsulatus”, Biochem. Biophys. Res. Commun., 470, 704-709, (2016), DOI: 10.1016/j.bbrc.2016.01.070; 大山克明, 浅井智広, *寺内一姫 “3つの時計タンパク質によるシアノバクテリア生物時計再構成系の解析”, 光合成研究 25, 175-180,（2015); *T. Teramoto, M. Yoshimura, C. Azai, K. Terauchi, H. Namba, T. Ohta, “Direct Observation of Nitrogen Fixation in Filamentous Cyanobacteria by Using Soft X-ray Microscopy”, Memoirs of the SR center Ritsumeikan Univ. , 17, 147-148, (2015); Y. Hiraide, K. Oshima, T. Fujisawa, K. Uesaka, Y. Hirose, R. Tsujimoto, H. Yamamoto, S. Okamoto, Y. Nakamura, K. Terauchi, T. Omata, K. Ihara, M.Hattori, *Y. Fujita, “Loss of Cytochrome cM Stimulates Cyanobacterial Heterotrophic Growth in the Dark”, Plant Cell Physiol., 56, 334-345, (2015), DOI: 10.1093/pcp/pcu165
水野健作 ▲班員一覧に戻る▲: 【雑誌論文】; C. Wille, T. Eiseler, S. T. Langenberger, J. Richter, K. Mizuno, P. Radermacher, M. Huber-Lang, T. Seufferlein, S. Paschke, “PKD Regulates Actin Polymerization, Neutrophil Deformability and Transendothelial Migration in Response to fMLP and Trauma,” J. Leukocyte Biol., in press, (2018), DOI: 10.1002/JLB.4A0617-251RR; S. Fujiwara, T. Matsui, K. Ohashi, S. Deguchi, *K. Mizuno, “Solo, a RhoA-targeting Guanine Nucleotide Exchange Factor, is Critical for Hemidesmosome Formation and Acinar Development in Epithelial Cells,” PLoS One, 13, e0195124, (2018), DOI: 10.1371/journal.pone.0195124; R. Nishimura, K. Kato, S. Fujiwara, K. Ohashi, *K. Mizuno, “Solo and Keratin Filaments Regulate Epithelial Tubule Morphology,” Cell Struc. Funct., in press, (2018); K. Takahashi, T. Nagai, S. Chiba, K. Nakayama, *K. Mizuno “Glucose Deprivation Induces Primary Cilium Formation through mTORC1 Inactivation,” J. Cell Sci., 131, jcs208769, (2018), DOI: 10.1242/jcs.208769; T. Nagai, *K. Mizuno “Jasplakinolide induces primary cilium formation through cell rounding and YAP inactivation,” PLoS ONE 12, e0183030 (2017) DOI: 10.1371/journal.pone.0183030; K. Geng, S. Kumar, S. G. Kimani, V. Kholodovych, C. Kasikara, K. Mizuno, O. Sandiford, P. Rameshwar, S. V. Kotenko, R. B. Birge “Requirement of gamma-carboxyglutamic acid modification and phosphatidylserine binding for the activation of Tyro3, Axl, and Mertk receptors by growth arrest-specific 6,” Front. Immunol. 8, 1521 (2017) DOI: 10.3389/fimmu.2017.01521; K. Takahashi, H. Okabe, S. Kanno, T. Nagai, *K. Mizuno, “A Pleckstrin Homology-like Domain is Critical for F-actin Binding and Cofilin-phosphatase Activity of Slingshot-1”, Biochem. Biophys. Res. Commun., 482, 686-692, (2017), DOI: 10.1016/j.bbrc.2016.11.095; *K. Ohashi, S. Fujiwara, K. Mizuno, “Roles of the Cytoskeleton, Cell Adhesion and Rho Signaling in Mechanosensing and Mechanotransduction,” J. Biochem., 161, 245-254, (2017), DOI: 10.1093/jb/mvw082（表紙に採用）; R. Morita, M. Kihara, Y. Nakatsu, Y. Nomoto, M. Ogawa, K. Ohashi, K. Mizuno, T. Tachikawa, Y. Ishimoto, Y. Morishita, *T. Tsuji, “Coordination of Cellular Dynamics Contributes to Tooth Epithelium Deformations,” PLoS One, 11, e0161336, (2016), DOI: 10.1371/journal.pone.0161336; G. Konotop, E. Bausch, T. Nagai, A. Turchinovich, N. Becker, A. Benner, M. Boutros, K. Mizuno, *A. Krämer, M. S. Raab, “Pharmacological Inhibition of Centrosome Clustering by Slingshot-Mediated Cofilin Activation and Actin Cortex Destabilization,” Cancer Res., 76, 6690-6700, (2016), DOI: 10.1158/0008-5472.CAN-16-1144; 藤原佐知子,大橋一正,水野健作, “メカノセンシングにおける細胞骨格、細胞接着の機能,”生化学 88, 443-451, (2016); S. Fujiwara, *K. Ohashi, T. Mashiko, H. Kondo, *K. Mizuno, “Interplay between Solo and Keratin Filaments is Crucial for Force-induced Stress Fiber Reinforcement.”, Mol. Biol. Cell., 27(6), 954-66, (2016), DOI: 10.1091/mbc.E15-06-0417; H. Katsuno, M. Toriyama, Y. Hosokawa, K. Mizuno, K. Ikeda, Y. Sakumura, *N. Inagaki, “Actin migration driven by directional assembly and disassembly of membrane anchored actin filaments”, Cell Reports, 12, 648-660, (2015), DOI: 10.1016/j.celrep.2015.06.048; H. Abiko, S. Fujiwara, *K. Ohashi, R. Hiatari, T. Mashiko, N. Sakamoto, M. Sato, *K. Mizuno, “Rho Guanine Nucleotide Exchange Factors Involved in Cyclic-stretch-induced Reorientation of Vascular Endothelial Cells. ”J. Cell Sci. 128, 1683-1695, (2015), DOI: 10.1242/jcs.157503; Y. Amagai, T. Itoh, M. Fukuda, *K. Mizuno, “Rabin8 Suppresses Autophagosome Formation Independently of its Guanine Nucleotide Exchange Activity Toward Rab8. ” J. Biochem. 158, 139-153, (2015), DOI: 10.1093/jb/mvv032; K. Takahashi, S. Kanno, *K. Mizuno, “Activation of Cytosolic Slingshot-1 phosphatase by Gelsolin-generated Soluble Actin Filaments”, Biochem. Biophys. Res. Commun., 454, 471-477 (2014), DOI: 10.1016/j.bbrc.2014.10.108; T. Oda, S. Chiba, T. Nagai, *K. Mizuno, “Binding to Cep164, but not EB1, is Essential for Centriolar Localization of TTBK2 and its Function in Ciliogenesis”, Genes Cells, 19, 927-940 (2014).; K. Ohashi, K. Sampei,, M. Nakagawa, N. Uchiumi, T. Amanuma, S. Aiba, M. Oikawa, *K. Mizuno, “Damnacanthal, an Effective Inhibitor of LIM-kinase, Inhibits Cell Migration and Invasion”, Mol. Biol. Cell, 25, 828-840, (2014), DOI: 10.1091/mbc.E13-09-0540; T. Nagai, *K. Mizuno, "Multifaceted Roles of Furry Proteins in Invertebrates and Vertebrates", J. Biochem., 155, 137-146, (2014), DOI: 10.1093/jb/mvu001; Y. Homma, S. I. Kanno, K. Sasaki, M. Nishita, A. Yasui, T. Asano, K. Ohashi, *K. Mizuno, “Insulin Receptor Substrate-4 Binds to Slingshot-1 and Promotes Cofilin Dephosphorylation”, J. Biol. Chem., 289, 26302-26313, (2014), DOI: 10.1074/jbc.M114.565945; 【図書】; S. Fujiwara, *K. Mizuno “Role of intermediate filaments in cell locomotion,” In: eLS (Encyclopedia of Life Sciences), A26365, John Wiley & Sons, Ltd.: Chichester (2017.6). in press DOI: 10.1002/9780470015902.a0026365; 永井友朗, 水野健作, “哺乳類NDRキナーゼの細胞機能：もうひとつのHippo下流キナーゼ", 医学のあゆみ, 251 (5), pp. 365-370, (2014), （医歯薬出版，東京，日本）; K. Ohashi, K. Mizuno, "A novel pair of split venus fragments to detect protein-protein interactions by in vitro and in vivo bimolecular fluorescence complementation assays" in "Methods in Molecular Biology, Exocytosis and Endocytosis II", 1174, 247-262 (2014). (A. I. Ivanov Ed., Humana Press, New York) DOI: 10.1007/978-1-4939-0944-5_17
村田和義 ▲班員一覧に戻る▲: 【雑誌論文】; T. Uchihashi, Y. Watanabe, Y. Nakazaki, T. Yamasaki, H. Watanabe, T. Maruno, K. Ishii, S. Uchiyama, C. Song, K. Murata, R. Iino, T. Ando “Dynamic Structural States of ClpB Involved in Its Disaggregation Function”, Nature Commun., in press, (2018); *K. Murata, Y. Kaneko, “Visualization of DNA Compaction in Cyanobacteria by High-voltage Cryo-electron Tomography”, J. Visual. Exper., in press, (2018); N. Kobayashi, K. Inano, K. Sasahara, T. Sato, K. Miyazawa, T. Fukuma, M. Hecht, C. Song, K. Murata, R. Arai, “Self-Assembling Supramolecular Nanostructures Constructed from de Novo Extender Protein Nanobuilding Blocks”, ACS Synthetic Biology, in press, (2018); KK. Asare, M. Sakaguchi, AB. Lucky, M. Asada, S. Miyazaki, Y. Katakai, S. Kawai, S. Song, K. Murata , K. Yahata, O. Kaneko, “The Plasmodium Knowlesi MAHRP2 Ortholog Localizes to Structures Connecting Sinton Mulligan's Clefts in the Infected Erythrocyte”, Parasitology International, in press, (2018); *K. Okamoto, N. Miyazaki, HKN. Reddy, MF. Hantke, FRNC. Maia, DSD. Larsson, C. Abergel, JM. Claverie, J. Hajdu, *K. Murata, M. Svenda, “Cryo-EM Structure of a Marseilleviridae Virus Particle Reveals a Large Internal Microassembly”, Virology, 516, 239–245, (2018), DOI: 10.1016/j.virol.2018.01.021（ハイライトに採用）; 宋致宖，*村田和義「クライオ電子顕微鏡によるタンパク質の動的構造解析」,　J. Comput. Chem. Japan, 17(1) : 38-45, (2018), DOI: 10.2477/jccj.2018-0007; A. Nakao, N. Miyazaki, K. Ohira, H. Hagihara, T. Takagi, N. Usuda, S. Ishii, K. Murata, *T. Miyakawa, “Immature Morphological Properties in Subcellular-scale Structures in the Dentate Gyrus of Schnurri-2 Knockout Mice: a Model for Schizophrenia and Intellectual Disability”, Mol Brain, 10, 60, (2017), DOI: 10.1186/s13041-017-0339-2; Nakamura A, Tasaki T, Okuni Y, Song C, Murata K, Kozai T, Hara M, Sugimoto H, Suzuki K, Watanabe T, Uchihashi T, Noji H, Iino R*, “Rate constants, processivity, and productive binding ratio of chitinase A revealed by single-molecule analysis.”, Phys. Chem. Chem. Phys., (2017), DOI: 10.1039/C7CP04606E; Okamoto K*, Miyazaki N, Song C, Maia FRNC, Reddy HKN, Abergel C, Claverie J-M, Hajdu J, Svenda M, Murata K*, “Structural variability and complexity of the giant Pithovirus sibericum particle revealed by high-voltage electron cryo-tomography and energy-filtered electron cryo-microscopy.”, Sci. Rep. 7, 13291, (2017), DOI: 10.1038/s41598-017-13390-4; Satoh T*, Song C, Zhu T, Toshimori T, Murata K, Hayashi Y, Kamikubo H, Uchihashi T, Kato K* "Visualisation of a flexible modular structure of the ER folding-sensor enzyme UGGT”, Sci. Rep. 7, 12142, (2017), DOI: 10.1038/s41598-017-12283-w; Murata K*, Wolf M*, “Cryo-electron microscopy for structural analysis of dynamic biological macromolecules.”, Biochim Biophys Acta pii: S0304-4165(17)30237-4, (2017), DOI: 10.1016/j.bbagen.2017.07.020; Conley M, Emmott E, Orton R, Taylor D, Carneiro DG, Murata K, Goodfellow IG, Hansman GS, Bhella D*, “Vesivirus 2117 capsids more closely resemble sapovirus and lagovirus particles than other known vesivirus structures”, J. Gen. Virol., 98, 68–76, (2017), DOI: 10.1099/jgv.0.000658; Sai K, Wang S, Kaito A, Fujiwara T, Maruo T, Itoh Y, Miyata M, Sakakibara S, Miyazaki N, Murata K, Yamaguchi Y, Haruta T, Nishioka H, Motojima Y, Komura M, Kimura K, Mandai K, Takai Y*, Mizoguchi A*, “Multiple roles of afadin in the ultrastructural morphogenesis of mouse hippocampal mossy fiber synapses.”, J. Comp. Neurol., 525, 2719–2734, (2017), DOI: 10.1002/cne.24238; C. Song, K. Murata, T. Suzaki, “Intracellular Symbiosis of Algae with Possible Involvement of Mitochondrial Dynamics”, Sci. Rep., 7, 1221, (2017), DOI: 10.1038/s41598-017-01331-0; K. Murata, Q. Zhang, JG. Galaz-Montoya, C. Fu, ML. Coleman, MS. Osburne, MF. Schmid, MB. Sullivan, SW. Chisholm, W. Chiu, “Visualizing Adsorption of Cyanophage P-SSP7 onto Marine Prochlorococcus”, Sci. Rep., 7, 44176, (2017), DOI: 10.1038/srep44176; K. Ichimura, S. Kakuta, Y. Kawasaki, T. Miyaki, T. Nonami, N. Miyazaki, T. Nakao, S. Enomoto, S. Arai, M. Koike, K. Murata, T. Sakai, “Morphological Process of Podocyte Development Revealed by Block- face Scanning Electron Microscopy”, J. Cell Sci., 130, 132-142, (2016), DOI: 10.1242/jcs.187815; T. Watanabe, C. Kobayashi, C. Song, K. Murata, T. Kureha, D. Suzuki D, “Impact of Spatial Distribution of Charged Groups in Core Poly( N _ isopropylacrylamide)-Based Microgels on the Resultant Composite Structures Prepared by Seeded Emulsion Polymerization of Styrene”, Langmuir, 32, 12760-12773, (2016), DOI: 10.1021/acs.langmuir.6b03172; *K. Murata, S. Hagiwara, Y. Kimori, *Y. Kaneko, “Ultrastructure of Compacted DNA in Cyanobacteria by High-voltage Cryo-electron Tomography”, Sci. Rep., 6, 34934, (2016), DOI: 10.1038/srep34934; K. Haga, A. Fujimoto, R. Takai-Todaka, M. Miki, YH. Doan, K. Murakami, M. Yokoyama, K. Murata, A. Nakanishi, K. Katayama, “Functional Receptor Molecules CD300lf and CD300ld Within the CD300 Family Enable Murine Noroviruses to Infect Cells”, Proc. Natl. Acad. Sci. USA, 113(41), E6248-E6255, (2016), DOI: 10.1073/pnas.1605575113; *K. Okamoto, N. Miyazaki, DS. Larsson, D. Kobayashi, M. Svenda, K. Mühlig, FR. Maia, LH. Gunn, H. Isawa, M. Kobayashi, K. Sawabe, *K. Murata, J. Hajdu, “The Infectious Particle of Insectborne Totivirus-like Omono River Virus has Raised Ridges and Lacks Fibre Complexes”, Sci. Rep., 6, 33170, (2016), DOI: 10.1038/srep33170; T. Negishi, N. Miyazaki, K. Murata, H. Yasuo, N. Ueno, “Physical Association between a Novel Plasma-membrane Structure and Centrosome Orients Cell Division”, eLife, 5, e16550, (2016), DOI: 10.7554/eLife.16550; M. Yamaguchi, H. Yamada, K. Higuchi, Y. Yamamoto, S. Arai, K. Murata, Y. Mori, H. Furukawa, MS, Uddin, H. Chibana, “High-voltage Electron Microscopy Tomography and Structome Analysis of Unique Spiral Bacteria from the Deep Sea”, Microscopy, 65, 363-369, (2016), DOI: 10.1093/jmicro/dfw016; M. Takeuchi, I. Karahara, N. Kajimura, A. Takaoka, K. Murata, K. Misaki, S. Yonemura, LA, Staehelin, Y. Mineyuki, “Single Microfilaments Mediate the Early Steps of Microtubule Bundling during Preprophase Band Formation in Onion Cotyledon Epidermal Cells”, Mol. Biol. Cell., 27, 1809-1820, (2016), DOI: 10.1091/mbc.E15-12-0820; T. Kaji, K. Kakui, N. Miyazaki, K. Murata, AR Palmer, “Mesoscale Morphology at Nanoscale Resolution: Serial Block-face Scanning Electron Microscopy Reveals Fine 3D Detail of a Novel Silk Spinneret System in a Tube-building Tanaid Crustacean”, Front. Zool., 13, 14, (2016), DOI: 10.1186/s12983-016-0146-0; A. Oshima, T. Matsuzawa, K. Murata, K. Tani, Y Fujiyoshi, “Hexadecameric Structure of an Invertebrate Gap Junction Channel”, J. Mol. Biol., 428, 1227-36, (2016), DOI: 10.1016/j.jmb.2016.02.011; C. Kobayashi, T. Watanabe, K. Murata, T. Kureha, *D. Suzuki, “Localization of Polystyrene Particles on the Surface of Poly( N -isopropylacrylamide- co -methacrylic acid) Microgels Prepared by Seeded Emulsion Polymerization of Styrene” Langmuir 32, 1429–1439, (2016), DOI: 10.1021/acs.langmuir.5b03698; *M. Sakaguchi, N. Miyazaki, H. Fujioka, O. Kaneko, *K. Murata, “Three-dimensional Analysis of Morphological Changes in the Malaria Parasite Infected Red Blood Cell by Serial Block-face Scanning Electron Microscopy”, J. Struct. Biol., 193, 162–171, (2016), DOI: 10.1016/j.jsb.2016.01.003; N. Miyazaki, D.W. Taylor, *G.S. Hansman, *K. Murata, “Antigenic and Cryo-electron Microscopy Structure Analysis of a Chimeric Sapovirus Capsid”, J. Virol., 90, 2664–2675, (2015), DOI: 10.1128/JVI.02916-15; M. Watanabe, Y. Suzuki, K. Uchida, N. Miyazaki, K. Murata, S. Matsumoto, H. Kakizaki, *M, Tominaga, “Trpm7 Contributes to Intercellular Junction Formation in Mouse Urothelium” J. Biol. Chem., 290, 29882-92, (2015), DOI: 10.1074/jbc.M115.667899.; 宮崎直幸，*村田和義「Serial Block-Face SEM（SBF-SEM）による細胞小器官の3次元形態観察」　Plant Morphology 27: 9-13 (2015); K. Satoh, K. Takanami, K. Murata, M. Kawata, T. Sakamoto, H. Sakamoto, “Effective Synaptome Analysis of Itch-mediating Neurons in the Spinal Cord : A novel Immunohistochemical Methodology Using High-voltage Electron Microscopy“, Neurosci Let., 599, 86–91, (2015), DOI: 10.1016/j.neulet.2015.05.031; K. Satoh, K. Takanami, K. Murata, M. Kawata, T. Sakamoto, H. Sakamoto, “Three-dimensional Visualization of Multiple Synapses in Thick Sections Using High-voltage Electron Microscopy in the Rat Spinal Cord“, Data Br., 4, 566–570, (2015), DOI: 10.1016/j.dib.2015.07.005; *K. Ichimura, N. Miyazaki, S. Sadayama, K. Murata, M. Koike, K. Nakamura, K. Ohta, T. Sakai, “Three-dimensional Architecture of Podocytes Revealed by Block-face Scanning Electron Microscopy“, Sci. Rep., 5, 8993, (2015), DOI: 10.1038/srep08993; *K. Murata, M. Esaki, T. Ogura, S. Arai, Y. Yamamoto, N. Tanaka, “Whole-Cell Imaging of the Budding Yeast Saccharomyces cerevisiae by High-Voltage Scanning Transmission Electron Tomography”, Ultramicroscopy 146, 39-45, (2014), DOI: 10.1016/j.ultramic.2014.05.008; N. Miyazaki, M. Esaki, T. Ogura, *K. Murata, “Serial Block-face Scanning Electron 　Microscopy for Three-dimensional Analysis of Morphological Changes in Mitochondria Regulated by Cdc48p/p97 ATPase”, J. Struct. Biol, 187, 187-193, (2014), DOI: 10.1016/j.jsb.2014.05.010; M, Yoshioka-Nishimura, D, Nanba, T. Takaki, C. Ohba, N. Tsumura, N. Morita, H. Sakamoto, K. Murata, Y, Yamamoto, “Quality Control of Photosystem II: Direct Imaging of the Changes in the Thylakoid Structure and Distribution of FtsH Proteases in Spinach Chloroplasts under Light Stress”, Plant and Cell Physiology, 55(7) 1255-1265, (2014), DOI: 10.1093/pcp/pcu079; 【図書】; 村田和義「超高圧電子顕微鏡による分析」　マイクロビーム　アナリシス・ハンドブック 5.1.3, P.459-464, (2014),(オーム社,東京、日本); 村田和義「電子顕微鏡によるバイオイメージング」　画像ラボ Vol.25, No.4, P.6-13、（2014）、（日本工業出版, 東京、日本）
山本量一 ▲班員一覧に戻る▲: 【雑誌論文】; N. Oyama, J.J. Molina, *R. Yamamoto, “Simulations of model micro-swimmers with fully resolved hydrodynamics”, J. Phys. Soc. Japan, 86, 101008, (2017), DOI: 10.7566/JPSJ.86.101008; M. Tarama, *R. Yamamoto, “Mechanics of cell crawling by means of force-free cyclic motion”, J. Phys. Soc. Japan, 87, 044803, (2018), DOI: 10.7566/JPSJ.87.044803; *R. Yamamoto, J.J. Molina, S.K. Schnyder, 「基板上で遊走•増殖する細胞集団のモデリング」J. Comput. Chem. Japan 17, 14 (2018), DOI: 10.2477/jccj.2018-0003; N. Oyama, J. J. Molina, *R. Yamamoto, “Do hydrodynamically assisted binary collisions lead to orientational ordering of microswimmers?” Eur. Phys. J. E, 40, 95 (2017), DOI: 10.1140/epje/i2017-11586-4; S. K. Schnyder, Y. Tanaka, J. J. Molina, *R. Yamamoto, “Collective motion of cells crawling on a substrate: roles of cell shape and contact inhibition” Sci. Rep., 7, 5163 (2017), DOI: 10.1038/s41598-017-05321-0; N. Oyama, J. J. Molina, *R. Yamamoto, “Simulations of Model Micro-swimmers with Fully Resolved Hydrodynamics” J. Phys. Soc. Jpn., 86, 101008 (2017), DOI: 10.7566/JPSJ.86.101008; S. Mehdi, A. Hamid, A. Ullah, *R. Yamamoto, “Microstructure of Rod like Sedimenting Particles: Direct Numerical Simulations,” IBCAST, 622-626 (2017), DOI: 10.1109/IBCAST.2017.7868115; G. Lecrivain, R. Yamamoto, U. Hampel, *T. Taniguchi, “Direct Numerical Simulation of a Single Particle Attachment on a Stationary Immersed Bubble, ” Phys. Fluids, 28, 083301, (2016), DOI: 10.1063/1.4960627; 【図書】; 山本量一、大山倫弘、John J. Molina、Simon K. Schyder「ソフトマターのモデリング：非平衡系・生物系への挑戦」化学工学, 81, 282–285, (2017); John. J. Molina, Ryoichi Yamamoto, Chapter 8 of “Computer Simulation of Polymeric Materials: Applications of the OCTA System”, (Springer, ISBN:978-9811008146), pp 149-167, 2016. DOI: 10.1007/978-981-10-0815-3

班友

澤田知久 ▲班員一覧に戻る▲: 【雑誌論文】; *T. Sawada, Y. Inomata, M. Yamagami, *M. Fujita “Self-Assembly of a Peptide [2]Catenane through Ω-loop Folding,” Chem. Lett. 46, 1119–1121 (2017) DOI: 10.1246/cl.170438 (Editor's choice論文); *T. Sawada, M. Yamagami, S. Akinaga, T. Miyaji, *M. Fujita, “Porous Peptide Complexes by a Folding-and-Assembly Strategy”, Chem. Asian J., 12(14), 1715–1718 (2017.6) DOI: 10.1002/asia.201700458 (Very Important Paper); S. Wang, T. Sawada, *M. Fujita, “Capsule–bowl Conversion Triggered by a Guest Reaction”, Chem. Commun., 52, 11653, (2016), DOI: 10.1039/c6cc06551a; B. M. Schmidt, T. Osuga, T. Sawada, M. Hoshino, *M. Fujita, “Compressed Corannulene in a Molecular Cage”, Angew. Chem. Int. Ed., 55, 1561, (2016), DOI: 10.1002/anie.201509963; S. Wang, T. Sawada, K. Ohara, K. Yamaguchi, *M. Fujita, “Capsule–Capsule Conversion by Guest Encapsulation,” Angew. Chem. Int. Ed., 55, 2063, (2016), DOI: 10.1002/anie.201509278; *T. Sawada, M. Yamagami, K. Ohara, K. Yamaguchi, *M. Fujita, “Peptide [4]Catenane via Folding and Assembly,” Angew. Chem. Int. Ed.,55, 4519–4522, DOI: 10.1002/anie.201600480; *T. Sawada, A. Matsumoto, *M. Fujita, “Coordination-Driven Folding and Assembly of a Short Peptide into a Protein-like Two-Nanometer-Sized Channel” Angew. Chem. Int. Ed., 53 (28), 7228-7232, (2014), DOI: 10.1002/anie.201403506; T. Sawada, H. Hisada, *M. Fujita, “Mutual Induced Fit in a Synthetic Host–Guest System”, J. Am. Chem. Soc., 136 (12), 4449-4451, (2014), DOI: 10.1021/ja500376x
重田　育照 ▲班員一覧に戻る▲: 【雑誌論文】; *R. Harada, T. Mashiko, M. Tachikawa, S. Hiraoka, *Y. Shigeta, “Programmed Dynamical Ordering in Self-organization Processes of Nano-cube: A Molecular Dynamics Study”, Phys. Chem. Chem. Phys., 20, 9115-9122, (2018), DOI: 10.1039/C8CP00284C; R. Sato*, R. Harada, Y. Shigeta*, "The binding structure and affinity of photodamaged duplex DNA with members of the photolyase/cryptochrome family: A computational study", Biophysics and Physicobiology 15, 18-27 (2018). DOI: 10.2142/biophysico.15.0_18; R. Harada *, Y. Shigeta*, "Self-Avoiding Conformational Sampling (SACS) Based on Histories of Past Conformational Searches", J. Chem. Inf. Model., 57, 3070-3078, (2017), DOI: 10.1021/acs.jcim.7b00573; Y. Sasano, R. Sato, Y. Shigeta, N. Yasuda, H. Maeda*, "H-aggregated π-systems based on disulfide-linked dimers of dipyrrolyldiketone boron complexes", J. Org. Chem., 82, 11166–11172, (2017), DOI: 10.1021/acs.joc.7b02185; R. Harada*, Y. Shigeta, "An Assessment of Optimal Time Scale of Conformational Resampling in Parallel Cascade Molecular Dynamics", Molecular Simulation, accepted (2017). DOI: 10.1080/08927022.2017.1362696; R. Harada*, Y. Shigeta, "Dynamic Specification of Initial Structures in Parallel Cascade Selection Molecular Dynamics (PaCS-MD) Efficiently Promotes Biologically Relevant Rare Events", Bulletin of the Chemical Society of Japan, 90 1236-1243 (2017). DOI: 10.1246/bcsj.20170177; R. Harada*, Y. Shigeta, " Temperature-shuffled parallel cascade selection molecular dynamics accelerates the structural transitions of proteins", Journal of Computational Chemistry (Rapid Communication) 38, 2671–2674 (2017). DOI: 10.1002/jcc.25060; R. Harada*, Y. Shigeta, "Structural Dissimilarity Sampling with Dynamically Self-Guiding Selection", Journal of Computational Chemistry 38, 1921-1929(2017). DOI: 10.1002/jcc.24837; Y. Shigeta*, R. Harada, R. Sato, H. Kitoh-Nishioka, T. K. M. Bui, A. Sato, A. Kyan, Y. Ishii, M. Kimatsuka, S. Yamasaki, M. Kayanuma, M. Shoji, "Classical Cumulant Dynamics for Statistical Chemical Physics", Molecular Simulation 43 (13-16), 1260-1268(2017). DOI: 10.1080/08927022.2017.1315770; J. Fujita, R. Harada, Y. Maeda, Y. Saito, E. Mizohata, T. Inoue, Y. Shigeta*, H. Matsumura*, " Identification of the key interactions in structural transition pathway of FtsZ from Staphylococcus aureus", Journal of Structural Biology 198, 65-73 (2017). DOI: 10.1016/j.jsb.2017.04.008; R. Harada*, Y. Shigeta, "How does the number of initial structures affect the conformational sampling efficiency and quality in Parallel Cascade Selection Molecular Dynamics (PaCS-MD)?" , Chemistry Letters 46, 862-865 (2017). DOI: 10.1246/cl.170207; R. Harada*, Y. Shigeta, "Efficient conformational search based on Structural Dissimilarity Sampling: Applications to reproductions of structural transitions on Maltodextrin Binding Protein", Journal of Chemical Theory and Computation 13, 1411-1423(2017). DOI: 10.1021/acs.jctc.6b01112; R. Yamakado, Y. Ashida, R. Sato, Y. Shigeta, N. Yasuda, H. Maeda*, "Cooperatively Interlocked [2+1]-Type π-System-Anion Complexes", Chemistry A European Journal, 23, 4160–4168 (2017). DOI: 10.1002/chem.201605765; R. Harada*, Y. Takano, Y. Shigeta, “Common folding processes of mini proteins: Partial formations of secondary structures initiate the immediate protein folding", Journal of Computational Chemistry 38 (Front Cover), 790-797(2017). DOI: 10.1002/jcc.24748; *R. Sato, R. Harada, Y. Shigeta, “Theoretical Analyses on a Flipping Mechanism of UV-Induced DNA Damage”, Biophysics and Physicobiology, 13, 311-319, (2016), DOI: 10.2142/biophysico.13.0_311; W. Tanaka, *M Shoji, F. Tomoike, Y. Ujiie, K. Hanaoka, R. Harada, M. Kayanuma, K. Kamiya, T. Ishida, R. Masui, S. Kuramitsu, Y. Shigeta,, “Molecular Mechanisms of Substrate Specificities of Uridine-Cytidine Kinase”, Biophysics and Physicobiologoy, 13, 77-84, (2016), DOI: 10.2142/biophysico.13.0_77; *R. Harada, T. Nakamura, Y. Shigeta,, “A Fast Convergent Simulated Annealing Algorithm: Simulated Annealing Outlier FLOODing (SA-OFLOOD) Method”, Bull. Chem. Soc. Jap., 89, 1361-1367, (2016), DOI: 10.1246/bcsj.20160244; R. Yamakado, S. Sato, Y. Shigeta,, *H. Maeda, “Ion-Pairing Crystal Polymorphs of Interlocked [2+1]-type Receptor–Anion Complexes”, J. Org. Chem., 81, 8530–8536, (2016), DOI: 10.1021/acs.joc.6b01688; *S. Negoro, Y. Kawashima, N. Shibata, T. Kobayashi, T. Baba, Y.-H. Lee, K. Kamiya, Y. Shigeta,, K. Nagai, I. Takehara, D.-I. Kato, M. Takeo, Y. Higuchi, “Mutations Affecting the Internal Equilibrium of the 6-aminohexanoate-dimer Hydrolase Reaction”, FEBS Letter., 590, 3133-3143, (2016), DOI: 10.1002/1873-3468.12354; W. Naito, N. Yasuda, T. Morimoto, Y. Shigeta,, H. Takaya, I, Hisaki, *H. Maeda, “Doubly N-Methylated Porphyrinoids”, Org. Lett., 18, 3006-3009, (2016), DOI: 10.1021/acs.orglett.6b01377; *R. Harada, Y. Takano, Y. Shigeta,, “TaBoo SeArch (TBSA) Algorithm with a Modified Inverse Histogram for Reproducing Biologically Relevant Rare-events of Proteins”, J. Chem. Theory Comput., 12(5), 2436-2445,(2016), DOI: 10.1021/acs.jctc.6b00082; M. Kayanuma, M. Shoji, M. Yoda, M. Odaka, Y. Shigeta,, “Catalytic Mechanism of Nitrile Hydratase Subsequent to Cyclic Intermediate Formation: A QM/MM Study”, J. Phys. Chem. B, 120, (13), 3259–3266, (2016), DOI: 10.1021/acs.jpcb.5b11363; R. Harada, T. Nakamura, Y. Shigeta, “Sparsity-weighted Outlier FLOODing (OFLOOD) Method: Efficient Rare Event Sampling Method Using Sparsity of Distribution”, J. Comput. Chem., 37, 724–738,(2016), DOI: 10.1002/jcc.24255; R. Harada, Y. Inagaki, Y. Shigeta, “Protein Folding and Evolution” (invited review), Reference modules in Materials Science and Engineering 2016, Article ID: Protein Folding and Evolution Elsevier, DOI: 10.1016/B978-0-12-803581-8.09800-3; R. Harada, *T. Nakamura, *Y. Shigeta, “Automatic Detection of Hidden Dimension in Outlier FLOODing (OFLOOD) Method”, Chem. Phys. Lett., 639, 269-274,(2015), DOI: 10.1016/j.cplett.2015.09.031; *M. Shoji, M. Kayanuma, H. Umeda, Y. Shigeta, “Performance of the Divide-and-conquer Approach Used as an Initial Guess”, Chem. Phys. Lett., 634, 181–187, (2015), DOI: 10.1016/j.cplett.2015.06.011; *R. Harada, *Y. Takano, *Y. Shigeta, “Efficient Conformational Sampling of Proteins Based on a Multi-dimensional Inverse Histogram: An Application to Folding of Chignolin in Explicit Solvent”, Chem. Phys. Lett., 630, 68-75, DOI: 10.1016/j.cplett.2015.04.039; H. Harada, Y. Takano, T. Baba, Y. Shigeta, “Simple, Yet Powerful Methodologies for Conformational Sampling of Proteins”, Phys. Chem. Chem. Phys., 17, 6155-6173, (2015), DOI: 10.1039/C4CP05262E; Y. Shigeta, H. Harada, M. Kayanuma, M. Shoji, “Quantal Cumulant Dynamics for Real-time Simulations of Quantum Many-body Systems”, Int. J. Quant. Chem., 115, 300-308, (2015), DOI: 10.1002/qua.24820; S. Maekawa, T. Matsui, K. Hirao, *Y. Shigeta, “A Theoretical Study on Reaction Mechanisms of Nitrite Reduction in Copper Nitrite Complexes as Models for the Copper Nitrite Reductase”, J. Phys. Chem. B, 119, 5392–5403, (2015), DOI: 10.1021/acs.jpcb.5b01356; K. Okuno, Y. Shigeta, R. Kishi, *M. Nakano, “Theoretical Design of Solvatochromism Switching by Photochromic Reactions Using Donor-acceptor Disubstituted Diarylethene Derivatives with Oxidized Thiophene Rings”, Phys. Chem. Chem. Phys., 17, 6484-6494, (2015), DOI: 10.1039/C4CP05946H; R. Nakamura, *Y. Shigeta, K. Okuno, M. Fukushima, M. Hasegawa, S. Suzuki, M. Kozaki, K. Okada, M. Nakano, “Substitution Effects on Optical Properties of Iminonitroxide-substituted Iminonitroxide Diradical”, Mol. Phys., 113, 267-273, (2015), DOI: 10.1080/00268976.2014.937777; *R. Harada, *Y. Takano, *Y. Shigeta, “Enhanced Conformational Sampling Method for Proteins Based on the TaBoo SeArch (TBSA) Algorithm: Application to the Folding of a Mini-protein, Chignolin”, J. Comput. Chem. , 36, 763-772, (2015), DOI: 10.1002/jcc.23854; *T. Baba, M. Boero, K. Kamiya, H. Ando, S. Negoro, M. Nakano, *Y. Shigeta, “Unraveling the Degradation of Artificial Amide Bonds in Nylon Oligomer Hydrolase: from Induced-fit to Acylation Processes”, Phys. Chem. Chem. Phys., 17, 4492-4504, (2015), DOI: 10.1039/C4CP04419C; *T. Matsui, Y. Kitagawa, M. Okumura, *Y. Shigeta, “Accurate Standard Hydrogen Electrode Potential and Applications to the Redox Potentials of Vitamin C and NAD/NADH”, J. Phys. Chem. A, 119, 369-376, (2015), DOI: 10.1021/jp508308y; *R. Harada, T. Nakamura, Y. Takano, *Y. Shigeta, T. Baba, C. Watanabe, Y. Okiyama, Y. Mochizuki, M. Nakano, “Protein Folding Pathways Extracted by OFLOOD: Outlier FLOODing Method”, J. Comput. Chem., 36, 97-102, (2015), DOI: 10.1002/jcc.23773; T. Baba, T. Matsui, K. Kamiya, M. Nakano, *Y. Shigeta, “A Density Functional Study on pK_a of Small Polyprotic Molecules”, Int.J.Quant.Chem., 114, 1128–1134, (2014), DOI: 10.1002/qua.24631; *R. Harada, Y. Takano, *Y. Shigeta, “Fluctuation Flooding Method (FFM) for Accelerating Conformational Transitions of Proteins”, J. Chem. Phys., 140, 125103, (2014), DOI: 10.1063/1.4869594; *K. Kamiya, T. Baba, M. Boero, T. Matsui, S. Negoro, Y. Shigeta, “A Nylon-oligomer Hydrolase Promoting Cleavage Reactions in Unnatural Amide Compounds”, J. Phys. Chem. Lett., 5, 1210-1216, (2014), DOI: 10.1021/jz500323y; H. Ando, *Y. Shigeta, T. Baba, C. Watanabe, Y. Okiyama, Y. Mochizuki, M. Nakano, “Hydration Effects on Enzyme-Substrate Complex of Nylon Oligomer Hydrolase: Inter-Fragment Interaction Energy Study by the Fragment Molecular Orbital Method”, Molecular Physics, 113, 319-326, (2014), DOI: 10.1080/00268976.2014.941311; T. Baba, R. Harada, M. Nakano, *Y. Shigeta, "On the Induced-fitmechanism of Substrate-enzyme Binding Structures of Nylon-oligomer Hydrolase”, Journal of Computational Chemistry 35, 1240-1247, (2014), DOI: 10.1002/jcc.23614; 【図書】; Y. Shigeta, Y. Kitagawa Book Chapter (Chap. 4-1) of “Quantum and Computational Chemistry for Transition Metal Complexes”, Ed. K. Yamaguchi, S. Sakaki, A Series Books of Transition Metal Complexes 10, Sankyo Publishing (2014). ISBN-13: 978-4782707098
塚崎　智也 ▲班員一覧に戻る▲: 【雑誌論文】; A. Furukawa, S. Nakayama, K. Yoshikaie, Y. Tanaka, *T. Tsukazaki T. “Remote Coupled Drastic β-Barrel to β-Sheet Transition of the Protein Translocation Motor,” Structure 26, 485–489, (2018), DOI: 10.1016/j.str.2018.01.002; *T. Tsukazaki. “Structure-based Working Model of SecDF, a Proton-driven Bacterial Protein Translocation Factor,” in press.; Y. Daimon, C. Iwama-Masui, Y. Tanaka, T. Shiota, T. Suzuki, R. Miyazaki, H. Sakurada, T. Lithgow, N. Dohmae, H. Mori, *T. Tsukazaki, *S. Narita, *Y Akiyama. “The TPR Domain of BepA is Required for Productive Interaction with Substrate Proteins and the β-barrel Assembly Machinery Complex,” Mol. Microbiol., 106, 760-776, DOI: 10.1111/mmi.13844; Y. Sugano, A. Furukawa, O. Nureki, Y. Tanaka, *T. Tsukazaki. “SecY-SecA fusion protein retains the ability to mediate protein transport,” PLoS One 12, e0183434 (2017) DOI: 10.1371/journal.pone.0183434; Y. Tanaka, S. Iwaki, *T. Tsukazaki. “Crystal Structure of a Plant Multidrug and Toxic Compound Extrusion Family Protein,” Structure 25, 1455-1460 (2017) DOI: 10.1016/j.str.2017.07.009; Furukawa, K. Yoshikaie, T. Mori, H. Mori, V.Y. Morimoto, Y. Sugano, S. Iwaki, T. Minamino, Y. Sugita, Y. Tanaka, T. Tsukazaki, “Tunnel Formation Inferred from the I-Form Structures of the Proton-Driven Protein Secretion Motor SecDF.”, Cell Rep., 9(5), 895-901, (2017), DOI: 10.1016/j.celrep.2017.04.030; Y. Tanaka, Y. Sugano, M. Takemoto, T. Mori, A. Furukawa, T. Kusakizako, K. Kumazaki, A. Kashima, R. Ishitani, Y. Sugita, *O. Nureki, *T. Tsukazaki, “Crystal Structures of SecYEG in Lipidic Cubic Phase Elucidate a Precise Resting and a Peptide-Bound State ”, Cell Rep., 13, 1561-1568, (2015), DOI: 10.1016/j.celrep.2015.10.025; N. Shimokawa-Chiba, K. Kumazaki, T. Tsukazaki, O. Nureki, K. Ito, *S. Chiba,“Hydrophilic Microenvironment Required for the Channel-independent Insertase Function of YidC Protein”, Proc. Natl. Acad. Sci. USA, 112, 5063-5068, (2015), DOI: 10.1073/pnas.1423817112; K. Kumazaki, T. Kishimoto, A. Furukawa, H. Mori, Y. Tanaka, N. Dohmae, R. Ishitani, *T. Tsukazaki, O. Nureki, “Crystal structure of Escherichia coli YidC, a membrane protein chaperone and insertase”, Sci. Rep., 4, 7299 (2014), DOI: 10.1038/srep07299; K. Kumazaki, S. Chiba, M. Takemoto, A. Furukawa, K. Nishiyama, Y. Sugano, T. Mori, N. Dohmae, K. Hirata, Y. Nakada-Nakura, AD. Maturana, Y. Tanaka, H. Mori, Y. Sugita, F. Arisaka, K. Ito, R. Ishitani, *T. Tsukazaki, *O. Nureki, “Structural Basis of Sec-independent Membrane Protein Insertion by YidC.”, Nature, 509, 516-520 (2014), DOI: 10.1038/nature13167; K. Kumazaki, *T. Tsukazaki, T. Nishizawa, Y. Tanaka, HE. Kato, K. Hirata, Y. Nakada-Nakura, Y. Mori , H. Suga, N. Dohmae, R. Ishitani, *O. Nureki,. “Crystallization and Preliminary X-ray Diffraction Analysis of YidC, a Membrane Chaperone/insertase from Bacillus halodurans”, Acta Crystallogr. F, 70, 1056-1060 (2014), DOI: 10.1107/S2053230X14012540; 【図書】; 塚崎　智也“タンパク質を透過させる分子装置の活写”生化学 88,114-118, (2016) DOI: 10.14952/SEIKAGAKU.2016.880114; 塚崎智也“実験医学(増刊「構造生命科学で何がわかるのか，何ができるのか」）” 第２章，第６節「２つのSecモーター蛋白質による蛋白質膜透過のしくみ」 p113-117 (2014) 田中啓二，若槻壮市編,（羊土社,東京,日本）
長田裕也 ▲班員一覧に戻る▲: 【雑誌論文】; Y. Nagata,* T. Nishikawa, M. Suginome,* S. Sato, M. Sugiyama,* L. Porcar, A. Martel, R. Inoue, N. Sato, “Elucidating the Solvent Effect on the Switch of the Helicity of Poly(quinoxaline-2,3-diyl)s: A Conformational Analysis by Small-Angle Neutron Scattering”, J. Am. Chem. Soc. 140, 2722, (2018), DOI: 10.1021/jacs.7b11626.; *T. Miura, T. Nakamuro, S. G. Stewart, Y. Nagata, *M. Murakami "Synthesis of Enantiopure C3-Symmetric Triangular Molecules", Angew. Chem. Int. Ed., 3334 (2017) DOI: 10.1002/anie.201612585; F. K. C. Leung, F. Ishiwari, Y. Shoji, T. Nishikawa, R. Takeda, Y. Nagata, M. Suginome, Y. Uozumi, *Y. M. A. Yamada, *T. Fukushima "Synthesis and Catalytic Applications of a Triptycene-Based Monophosphine Ligand for Palladium-Mediated Organic Transformations", ACS Omega 2, 1930 (2017) DOI: 10.1021/acsomega.7b00200; H. Hasegawa, *Y. Nagata, *K. Terao, M. Suginome "Synthesis and Solution Properties of a Rigid Helical Star Polymer: Three-Arm Star Poly(quinoxaline-2,3-diyl)", Macromolecules 50, 7491 (2017) DOI: 10.1021/acs.macromol.7b01797; T. Nishikawa, Y. Nagata, M. Suginome, “Poly(quinoxaline-2,3-diyl) as a Multifunctional Chiral Scaffold for Circularly Polarized Luminescent Materials: Color Tuning, Energy Transfer, and Switching of the CPL Handedness”, ACS Macro Lett., 6, 431, (2017), DOI: 10.1021/acsmacrolett.7b00131; Y. Nagata, R. Takeda, and M. Suginome, “High-Pressure Circular Dichroism Spectroscopy up to 400 MPa Using Polycrystalline Yttrium Aluminum Garnet (YAG) as Pressure-Resistant Optical Windows”, RSC Adv., 6, 109726, (2016), DOI: 10.1039/C6RA23736C; Y. Nagata, M. Uno, and M. Suginome, “Three-Way-Switchable (Right/Left/OFF) Selective Reflection of Circularly Polarized Light on Solid Thin Films of Helical Polymer Blends”, Angew. Chem., Int. Ed., 55, 7126, (2016), DOI: 10.1002/anie.201602035; Y. Nagata, T. Nishikawa, and M. Suginome, “Solvent Effect on the Sergeants-and-Soldiers Effect Leading to Bidirectional Induction of Single-Handed Helical Sense of Poly(quinoxaline-2,3-diyl)s Copolymers in Aromatic Solvents”, ACS Macro Lett., 5, 519, (2016), DOI: 10.1021/acsmacrolett.6b00191
濵田大三 ▲班員一覧に戻る▲: 【雑誌論文】; Y. Matsushita, H. Sekiguchi, J.W. Chang, M. Nishijima, K. Ikezaki, D. Hamada, Y. Goto, *Y.C. Sasaki, “Nanoscale dynamics of protein assembly networks in supersaturated solutions”, Sci. Rep., 7, 13883, (2017), DOI: 10.1038/s41598-017-14022-7; M. Nawata, H. Tsutsumi, Y Kobayashi, S. Unzai, S. Mine, T. Nakamura, K. Uegaki, H. Kamikubo, M. Kataoka, *D. Hamada, “Heat-induced native dimerization prevents amyloid formation by variable domain from immunoglobulin light-chain REI”, FEBS J., 284, 3114-3127, (2017), DOI: 10.1111/febs.14181; K. Kuroki, K. Mio, A. Takahashi, H. Matsubara, Y. Kasai, S. Manaka, M. Kikkawa, D. Hamada, C. Sato, *K. Maenaka. “Cutting Edge: Class II-like Structural Features and Strong Receptor Binding of the Nonclassical HLA-G2 Isoform Homodimer”, J Immunol., 198, 3399-3403, (2017), DOI: 10.4049/jimmunol.1601296; B. Wang, M. Nishimura, H. Tang, A. Kawabata, N. F. Mahmoud, Z. Khanlari, D. Hamada, H. Tsuruta, *Y. Mori, “Crystal Structure of Human Herpesvirus 6B Tegument Protein U14”, PLoS Pathog., 12, e1005594, (2016), DOI: 10.1371/journal.ppat.1005594
原野幸治 ▲班員一覧に戻る▲: 【雑誌論文】; *Y. Zhen, K. Inoue, Z. Wang, T. Kusamoto, K. Nakabayashi, S. Ohkoshi, W. Hu, *Y. Guo, *K. Harano, *E. Nakamura, “Acid-Responsive Conductive Nanofiber of Tetrabenzoporphyrin Made by Solution Processing” J. Am. Chem. Soc. 140, 62-65, (2018), DOI: 10.1021/jacs.7b10575 (Cover pictureに採択); S. Kai, S. P. Maddala, T. Kojima, S. Akagi, K. Harano, E. Nakamura, *S. Hiraoka, “Flexibility of Components Alters the Self-assembly Pathway of Pd₂L₄ Coordination Cages” Dalton Trans., 47, 3258-3263, (2018) DOI: 10.1039/C8DT00112J; S. Okada, S. Kowashi, L. Schweighauser, K. Yamanouchi, *K. Harano, *E. Nakamura, “Direct Microscopic Analysis of Individual C₆₀ Dimerization Events: Kinetics and Mechanisms” J. Am. Chem. Soc. 139, 18281-18287 (2017), DOI: 10.1021/jacs.7b09776; R. Aoki, R. Toyoda, J. F. Kögel, *R. Sakamoto, J. Kumar, Y. Kitagawa, K. Harano, T. Kawai, *H. Nishihara, “Bis(dipyrrinato)zinc(II) Complex Chiroptical Wires: Exfoliation into Single Strands and Intensification of Circularly Polarized Luminescence,” J. Am. Chem. Soc., 139, 16024–16027, (2017), DOI: 10.1021/jacs.7b07077; *原野幸治，お茶のなかの分子世界，現代化学，556, 42–45 (2017).; L. Schweighauser, *K. Harano, *E. Nakamura, “Experimental Study on Interconversion between Cubic MOF-5 and Square MOF-2 Arrays,” Inorg. Chem. Commun., 84, 1–4 (2017). DOI: 10.1016/j.inoche.2017.07.009; H. Nitta, *K. Harano, M. Isomura, E. H. G. Backus, M. Bonn, *E. Nakamura, “Conical Ionic Amphiphiles Endowed with Micellization Ability but Lacking Air– and Oil–Water Interfacial Activity,” J. Am. Chem. Soc., 139, 7677–7680 (2017). DOI: 10.1021/jacs.7b01596; M. Yamada, N. Yoshinari, N. Kuwamura, T. Saito, S. Okada, S. P. Maddala, K. Harano, E. Nakamura, K. Yamagami, K. Yamanaka, A. Sekiyama, T. Suenobu, Y. Yamada, *T. Konno, “Heterogeneous Catalase-like Activity of Gold(I)-Cobalt(III) Metallosupramolecular Ionic Crystals,“ Chem. Sci., 8, 2671–2676 (2017). DOI: 10.1039/C6SC04993A; P. Bairi, *K. Minami, J. P. Hill, W. Nakanishi, *L. K. Shrestha, C. Liu, K. Harano, E. Nakamura, *K. Ariga, “Supramolecular Differentiation for Constructing Anisotropic Fullerene Nanostructures by Time-Programmed Control of Interfacial Growth,“ ACS Nano, 10, 8796–8802 (2016). DOI: 10.1021/acsnano.6b04535; R. M. Gorgoll, *K. Harano, *E. Nakamura, “Nanoscale Control of Polymer Assembly on a Synthetic Catalyst-Bilayer System,” J. Am. Chem. Soc., 138, 9675–9681 (2016). DOI: 10.1021/jacs.6b05414
前田　大光 ▲班員一覧に戻る▲: 【雑誌論文】; *H. Maeda, Y. Takeda, Y. Haketa, Y. Morimoto, N. Yasuda, "Ion-Pairing Assemblies of π-Electronic Anions Formed by Intramolecular Hydrogen Bonding," Chem. Eur. J. 24, in press, (2018) , DOI: 10.1002/chem.201801375; N. Oka, *F. Ito, Y. Haketa, *H. Maeda, T. Miyano, N. Tohnai, S. Ito, H. Miyasaka, S. Ozeki, "Dynamic Polymorph Formation During Evaporative Crystallization from Solution: The Key Role of Liquid-like Clusters as "Crucible" at Ambient Temperature," Chem. Eur. J. 24(17), 4343-4349, (2018), DOI: 10.1002/chem.201705356; Y. Haketa, *H. Maeda,"Dimension-Controlled π-Electronic Ion-Pairing Assemblies," Bull. Chem. Soc. Jpn. 91(3), 420-436, (2018), DOI: 10.1246/bcsj.20170434; R. Yamakado, M. Hara, S. Nagano, T. Seki, *H. Maeda,,"Complexation of Anion-Responsive π-Electronic System with Alkyl-Substituted Azobenzene Carboxylate Providing Ion-Pairing Assemblies," Chem. Lett. 47(4), 404-407, (2018), DOI: 10.1246/cl.171128; Y. Sasano, R. Sato, Y. Shigeta, N. Yasuda, *H. Maeda, “H-Aggregated π-Systems Based on Disulfide-Linked Dimers of Dipyrrolyldiketone Boron Complexes”, J. Org. Chem., 82, 11166-11172, (2017), DOI: 10.1021/acs.joc.7b02185; A. Kuno, N. Tohnai, N. Yasuda, *H. Maeda, “Conjunction of Pyrrole and Amide Moieties: Highly Anion-Responsive π-Electronic Molecules Forming Ion-Free and Ion-Pairing Assemblies”, Chem. Eur. J., 23, 11357-11365, (2017), DOI: 10.1002/chem.201701921; *T. Fujita, Y. Haketa, H. Maeda, DOI: 10.1016/j.orgel.2017.06.028; K. Nakamura, *H. Maeda, “Pyrrole-Based Hydrogen-Bonding Dimers Providing Discotic Columnar Structures”, Chem. Lett., 46, 1269-1271, (2017), DOI: 10.1246/cl.170487; R. Yamakado, M. Hara, S. Nagano, T. Seki, *H. Maeda, “Photo-Responsive Soft Ionic Crystals: Ion-Pairing Assemblies of Azobenzene Carboxylates”, Chem. Eur. J., 23, 1269-1271, (2017), DOI: 10.1002/chem.201701925; Y. Sasano, N. Yasuda, *H. Maeda, “Deprotonated meso-hydroxyporphyrin as a stable π-electronic anion: the building unit of ion-pairing assembly”, Dalton Trans., 46, 8924-8928, (2017), DOI: 10.1039/c7dt01635b(インサイドカバーに採択); V. Lakshmi, Y. Haketa, R. Yamakado, N. Yasuda, *H. Maeda, “Dimension-controlled Assemblies of Anion-responsive π-electronic Systems Bearing Aryl Substituents with Fan-Shaped Geometries”, Chem. Commun., 53(27), 3834–3837, (2017), DOI: 10.1039/c7cc01551h; R. Yamakado, Y. Ashida, R. Sato, Y. Shigeta, N. Yasuda, *H. Maeda, “Cooperatively Interlocked [2+1]-Type π-System-Anion Complexes”, Chem. Eur. J., 23(17), 4160–4168, (2017), DOI: 10.1002/chem.201605765; Y. Haketa, *H. Maeda, “Dimension-controlled Ion-pairing Assemblies Based on π-electronic Charged Species”, Chem. Commun., 53(20), 2894–2909, (2017), DOI: 10.1039/c6cc10255g; Y. Sasano, N. Yasuda, *H. Maeda, “Negatively Charged π-Electronic Systems by Deprotonation of Hydroxy-Substituted Dipyrrolyldiketone Boron Complexes”, Chem. Asian J., 11(23), 3423–3429, (2016), DOI: 10.1002/asia.201601205; R. Yamakado, R. Sato, Y. Shigeta, *H. Maeda, “Ion-Pairing Crystal Polymorphs of Interlocked [2+1]-Type Receptor-Anion Complexes”, J. Org. Chem., 81(18), 8530–8536, (2016), DOI: 10.1021/acs.joc.6b01688; Y. Haketa, Y. Tamura, N. Yasuda, *H. Maeda, “Dipyrrolylpyrimidines as Anion-responsive π-Electronic Systems”, Org. Biomol. Chem., 14(34), 8035–8038, (2016), DOI: 10.1039/c6ob01466f; Y. Haketa, D. Katayama, S. Fukunaga, Y. Bando, T. Sakurai, W. Matsuda, S. Seki, *H. Maeda, “Ion-Free and Ion-Pairing Assemblies of Anion-Responsive π-Electronic Systems Possessing Directly Linked Alkyl Chains”, Chem. Asian J., 11(14), 2025–2029, (2016), DOI: 10.1002/asia.201600712; W. Naito, N. Yasuda, T. Morimoto, Y. Shigeta, H. Takaya, I. Hisaki, *H. Maeda, “Doubly N-Methylated Porphyrinoids”, Org. Lett., 18(12), 3006–3009, (2016), DOI: 10.1021/acs.orglett.6b01377; Y. Haketa, R. Takasago, *H. Maeda, “β-Perfluoroalkyl-substituted Pyrrole as an Anion-Responsive π-electronic System Through a Single NH Moiety”, Chem. Commun., 52(46), 7364–7367, (2016), DOI: 10.1039/c6cc03619h; K. Nakamura, N. Yasuda, *H. Maeda, “Dimension-controlled Assemblies of Modified Bipyrroles Stabilized by Electron-withdrawing Moieties”, Chem. Commun., 52(44), 7157–7160, (2016), DOI: 10.1039/c6cc03423c; Y. Bando, Y. Haketa, T. Sakurai, W. Matsuda, S. Seki, H. Takaya, *H. Maeda "Ion-Pairing Assemblies Based on Pentacyano-Substituted Cyclopentadienide as a π-Electronic Anion" Chem. Eur. J. 22(23), 7843-7850 (2016) DOI: 10.1002/chem.201600686; R. Yamakado, T. Sakurai, W. Matsuda, S. Seki, N. Yasuda, S. Akine, *H. Maeda, "π-Electronic Systems That Form Planar and Interlocked Anion Complexes and Their Ion-Pairing Assemblies," Chem. Eur. J., 22, 626-638, (2016), DOI: 10.1002/chem.201503654; R. Yamakado, *H. Maeda, "Ion-pairing Assemblies of Photoresponsive Cations and an Interlocked [2+1]-type π-system-anion Complex" J. Photochem. Photobiol. A, 331, 215–223 (2016), DOI: 10.1016/j.jphotochem.2015.10.013; 羽毛田洋平・山門陵平・*前田大光「イオンペア集合体を形成するアニオン応答性π電子系の合成」有機合成化学協会誌 74 (3), 243-253, (2016); *H. Maeda, A. Fukui, R. Yamakado, N. Yasuda, "Dipyrrolyphenol as a Precursor of π-electronic Anion that Forms Ion Pairs with Cations" Chem. Commun., 51, 17572-17575, (2015), DOI: 10.1039/c5cc07493b; *H. Maeda“Dimension-Controlled Assemblies Comprising π-Electronic Systems” Chem. Rec. 15, 1151-1152 (2015) DOI: 10.1002/tcr.201510007; *H. Maeda, K. Chigusa, R. Yamakado, T. Sakurai, S. Seki“Carboxylate-Driven Supramolecular Assemblies of Protonated meso-Aryl-Substituted Dipyrrolylpyrazoles,” Chem. Eur. J. 21, 9520-9527, (2015), DOI: 10.1002/chem.201500681; *H. Maeda, T. Nishimura, A. Tsujii, K. Takaishi, M. Uchiyama, A. Muranaka, “Helical π-Systems of Bidipyrrin-Metal Complexes”, Chem. Lett., 43, 1078-1080, (2014), DOI: 10.1246/cl.140260; R. Sekiya, Y. Tsutsui, W. Choi, T. Sakurai, *S. Seki, Y. Bando, *H. Maeda, “Ion-based assemblies of planar anion complexes and cationic PtII complexes”, Chem. Commun., 50, 10615-10618, (2014), DOI: 10.1039/c4cc04565c; 【図書】; 前田大光, “π電子系の合成を基盤としたイオンペア集合体の創製」液晶（日本液晶学会設立20周年特集記事）”, 日本液晶学会 (Japan), 21(3), 317-320, (2017); Y. Haketa, H. Maeda, “π-Electronic Ion-Pairing Assemblies Providing Nanostructured Materials”, Functional Organic and Hybrid Nanostructured Materials: Fabrication, Properties, and Applications; Li, Q. Ed.; Wiley-VCH, 2017, in press. ISBN: 9783527342549; Y. Haketa, R. Yamakado, H. Maeda, “Supramolecular Assemblies of π-Electronic Charged Species”, Conjugated Objects: Developments, Synthesis, and Application, Nagai, A.; Takagi, K. Eds., Pan Stanford, 13, 349-379, (2017), ISBN: 9789814774031; *前田大光「イオンペアリングπ電子系超分子集合体」自己組織化マテリアルのフロンティア（エキゾチック自己組織化材料研究グループ編）フロンティア出版, pp 126-136, 2015, ISBN: 978-4-902410-26-6; H. Maeda, “Supramolecular Assemblies Based on Interionic Interactions”　In Synergy in Supramolecular Chemistry, 57-74 (2014). (T. Nabeshima Ed., CRC Press) ISBN: 978-1466595026; H. Maeda, “Ion-Based Liquid Crystals: From Well-Defined Self-Organized Nanostructures to Applications”　In Nanoscience with Liquid Crystals: From Self-Organized Nanostructures to Applications, Ch. 9, 281-299, (2014). (Li, Q. Ed. Springer) DOI: 10.1007/978-3-319-04867-3_9, ISBN: 978-3-319-04866-6; 前田大光「電荷を有するπ電子系の規則配列による次元制御型集合体の創製」高分子, 63 (12), 858-859, (2014); 前田大光「刺激応答性円偏光発光を示すπ電子系」光化学, 45 (2), 58–63 (2014)

日本学術振興会科学研究費補助金　新学術領域研究（平成25-29年度）
生命分子システムにおける動的秩序形成と高次機能発現
（略称：『動的秩序と機能』）

研究業績リスト

公募班A01：動的秩序の探査

公募班A02：動的秩序の創生

公募班A03：動的秩序の展開

班友

注目のコンテンツ

事後評価

中間評価

ニュースレター

日本学術振興会科学研究費補助金 新学術領域研究（平成25-29年度） 生命分子システムにおける動的秩序形成と高次機能発現 （略称：『動的秩序と機能』）

研究業績リスト

公募班A01：動的秩序の探査

公募班A02：動的秩序の創生

公募班A03：動的秩序の展開

班友

注目のコンテンツ

事後評価

中間評価

ニュースレター

日本学術振興会科学研究費補助金　新学術領域研究（平成25-29年度）
生命分子システムにおける動的秩序形成と高次機能発現
（略称：『動的秩序と機能』）