班 友


秋山 修志 ▲班員一覧に戻る▲
*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)
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, A. Mukaiyama, *S. Akiyama "Absolute slowness encoded in the circadian clock protein KaiC," SPring-8 Research Frontiers 2015, in press (2016)
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
秋山 良 ▲班員一覧に戻る▲
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
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▲
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
Masahiko Annaka “ Relaxation phenomena and development of structure in a physically cross-linked telechelic polymers, Soft Matter”,in press
池谷 鉄兵 ▲班員一覧に戻る▲
*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
岩田 耕一 ▲班員一覧に戻る▲
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
「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.
“Time-resolved Raman Spectroscopy”, Hiro-o Hamatuchi and Koichi Iwata, Encyclopedia of Spectroscopy and Spectrometry, 3rd Edition, Elsevier. 分担執筆 (in press).
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)
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▲
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)
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▲
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
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
*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
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▲
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., in press, 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
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▲
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
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
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
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
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
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
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▲
*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
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. 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
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
田中 良和 ▲班員一覧に戻る▲
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
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▲
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.
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., in press、DOI: 10.1016/j.molliq.2015.08.030
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
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, “揺らぎから観た生体分子科学”, Molecular Science, 7, (2013)
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・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▲
*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
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、“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
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▲
松村 浩由 ▲班員一覧に戻る▲
*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. 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
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
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 AureusFEBS 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▲
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▲
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
Y.Y. Yamamoto, M. Yohda.”Thermosome: A Group II Chaperonin of Archaea”,eLS. 1, (2016), DOI: 10.1002/9780470015902.a0026332
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


新井 亮一 ▲班員一覧に戻る▲
飯野 亮太 ▲班員一覧に戻る▲
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., online, (2016), DOI: 10.1038/nchembio.2028
*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 Iα and IIII”, 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
*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▲
上野 隆史 ▲班員一覧に戻る▲
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
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▲
片山 勉 ▲班員一覧に戻る▲
神谷 由紀子 ▲班員一覧に戻る▲
*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
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▲
*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)
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▲
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., in press (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., in press (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
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. 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
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
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).
澤田 知久 ▲班員一覧に戻る▲
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
杉安 和憲 ▲班員一覧に戻る▲
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, 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
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
*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▲
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, in press, (2016), DOI: 10.1021/acs.langmuir.6b00760
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
K. Horigome, T. Ueki, *D. Suzuki, “Direct Visualization of Swollen Microgels via Scanning Electron Microscopy Using Ionic Liquids”, Polym. J., in press, (2015), 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, in press, (2016), DOI: 10.1021/acs.langmuir.5b03698
*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, 65, (2016)
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
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▲
*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
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▲
*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▲
C. M, Backlund, T. Takeuchi, S. Futaki, *G. N. Tew. “Relating structure and internalization for ROMP-based protein mimics,” Biochim. Biophys. Acta, in press. DOI: 10.1016/j.bbamem.2016.03.024
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.. in press. DOI: 10.1021/acs.bioconjchem.6b00082
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, in press, (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
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▲
K. P. Huynh Nhat, T. Watanabe, K. Yoshikoshi, *T. Hohsaka“Antibody-based Fluorescent and Fluorescent Ratiometric Indicators for Detection of Phosphotyrosine”, J. Biosci. Bioeng., in press, (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., in press, (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
“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▲
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
三宅 弘之 ▲班員一覧に戻る▲
*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
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)
*H. Miyake, “Supramolecular Chirality in Dynamic Coordination Chemistry”, Symmetry, 6, 880-895, (2014), DOI: 10.3390/sym6040880
*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


稲垣 直之 ▲班員一覧に戻る▲
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▲
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
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, 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
K. Ishii, M. Noda, S. Uchiyama, “Mass Spectrometric Analysis of Protein-ligand Interaction”Biophys. Physicobiology, in press, (2016), DOI: 10.2142/biophysico.13.0_00
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
老木 成稔 ▲班員一覧に戻る▲
Y. Matsuki, M. Iwamoto, K. Mita, K. Shigemi, S. Matsunaga, *S. Oiki, “Rectified Proton Grotthuss Conduction Across a Long Water-Wire in the Test “Nano”-Tube of the Polytheonamide B Channel”, J. Am. Chem.Soc., ,138, 4168-4177 (2016), DOI: 10.1021/jacs.5b13377
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
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
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”, Biophysics and 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).
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▲
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
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
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
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
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
奥村 久士 ▲班員一覧に戻る▲
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.
*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 (2016) 印刷中
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
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
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
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▲
*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, in press (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
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
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
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
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)
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)
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
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▲
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, in press, (2016)
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▲
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
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▲
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., in press, (2016)
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
*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, ” 生物物理学324, in press (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
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
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▲
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▲
真行寺 千佳子 ▲班員一覧に戻る▲
*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
C. Shingyoji“Regulation of Dynein Activity in Oscillatory Movement of Sperm Flagella”, Muscle Contraction and Cell Motility, H. Sugi ed., Pan Stanford Publishing, (2016), in press
杉山 正明 ▲班員一覧に戻る▲
*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.
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
*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
*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*, 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▲
*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▲
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▲
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
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▲
*A. Oshima, T. Matsuzawa, K. Murata, K. Tani, Y. Fujiyoshi, “Hexadecameric Structure of an Invertebrate Gap Junction Channel”, J. Mol. Biol., (2016), online, 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
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▲


重田 育照 ▲班員一覧に戻る▲
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
T. Baba, T. Matsui, K. Kamiya, M. Nakano, *Y. Shigeta, “A Density Functional Study on pKa 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
*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
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
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▲
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
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, (2016), in press
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▲
濵田 大三 ▲班員一覧に戻る▲
原野 幸治 ▲班員一覧に戻る▲
前田 大光 ▲班員一覧に戻る▲
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, in press (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, in press, (2016), DOI: 10.1016/j.jphotochem.2015.10.013
*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
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“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
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)
*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
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)
*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