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Sugiyama, M., Arimura, Y., Shirayama, K., Fujita, R., Oba, Y., Sato, N., Inoue, R., Oda, T., Sato, M., Heenan, R. K. and Kurumizak, H. Distinct Features of the Histone Core Structure in Nucleosomes Containing the Histone H2A.B Variant. Biophysical J., 106, 2206-2213 (2014). PubMed
Walinda, E., Morimoto, D., Sugase, K., Konuma, T., Tochio, H. and Shirakawa, M. Solution structure of the ubiquitin-associated (UBA) domain of human autophagy receptor NBR1 and its interaction with ubiquitin and polyubiquitin. J. Biol. Chem. (2014). in press. PubMed
Nomura, K., Harada, E., Sugase, K. and Shimamoto, K. Solid-state NMR spectra of lipid-anchored proteins under magic angle spinning. J. Phys. Chem. B. 118, 2405-2413 (2014). PubMed
Sugase, K., Konuma, T., Lansing, JC. and , Wright, PE. Fast and accurate fitting of relaxation dispersion data using the flexible software package GLOVE. J. Biomol. NMR. 56, 275-283 (2013). PubMed
Ando, T., Uchihashi, T. and Scheuring, S. Filming biomoleculear processes by high-speed atomic force microscopy. Chem. Rev. 114, 3120-3188 (2014). PubMed
Nakamura, A., Watanabe, H., Ishida, T., Uchihashi, T., Wada, M., Ando, T., Igarashi, K. and Samejima, M. Trade-off between processivity and hydrolytic velocity of cellobiohydrolases at the surface of crystalline cellulose. J. Am. Chem. Soc. 136, 4584-4592 (2014). PubMed
Igarashi, K., Uchihashi, T., Uchiyama, T., Sugimoto, H., Wada, M., Suzuki, K., Sakuda, S., Ando, T., Watanabe, T. and Samejima, M. Two-way traffic of glycoside hydrolase family 18 processive chitinases on crystalline chitin. Nature Communications. in press.
Kodera, N. and Ando, T. The path to visualization of walking myosin V by high-speed atomic force microscopy. Biophy. Rev. (accepted).
Noi, K., Yamamoto, D., Nishikori, S., Arita-Morioka, K., Ando, T. and Ogura, T. High-Speed atomic force microscopic observation of ATP-dependent rotation of the AAA+ chaperone p97. Structure 21, 1992-2002 (2013). PubMed
Yilmaz, N., Yamada, T., Greimel, P., Uchihashi, T., Ando, T. and Kobayashi, T. Real-time visualization of assembling of a sphingomyelin-specific toxin. Biophys. J. 105, 1397-1405 (2013). PubMed
Fukuda, S., Uchihashi, T., Iino, R., Okazaki, Y., Yoshida, M., Igarashi, K. and Ando, T. High-speed atomic force microscope combined with single-molecule fluorescence microscope. Rev. Sci. Instrum. 84, 073706 (2013). PubMed
Watanabe, H., Uchihashi, T., Kobashi, T., Shibata, M., Nishiyama, J., Yasuda, R. and Ando, T. Wide-area scanner for high-speed atomic force microscopy. Rev. Sci. Instrum. 84, 053702 (10 pp) (2013). PubMed
Hashimoto, M., Kodera, N., Tsunaka, Y., Oda, M., Tanimoto, M., Ando, T., Morikawa, K. and Tate, S. Phosphorylation-coupled intramolecular dynamics of unstructured regions in chromatin remodeler FACT. Biophys. J. 104, 2222-2234 (2013). PubMed
Yamashita, H., Inoue, K., Shibata, M., Uchihashi, T., Sasaki, J., Kandori, H. and Ando, T. Role of trimer-trimer interaction of bacteriorhodopsin studied by high-speed atomic force microscopy. J. Struct. Biol. 184, 2-11 (2013). PubMed
Ando, T. Molecular machines directly observed by high-speed atomic force microscopy. FEBS Lett. 587, 997-1007 (2013). PubMed
Ando, T., Uchihashi, T. and Kodera, N. High-speed AFM and applications to biomolecular systems. Annu. Rev. Biophys. 42, 393-414 (2013). PubMed
Ando, T. High-speed atomic force microscopy. Microscopy 62, 81-93 (2013). PubMed
Ando, T., Uchihashi, T. and Kodera, N. High-speed atomic force microscopy. Jpn. J. Appl. Phys. 51, 08KA02 (15 pp) (2012).
Yamashita, H., Taoka, A., Uchihashi, T., Asano, T., Ando, T. and Fukumori, Y. Single molecule imaging on living bacterial cell surface by high-speed AFM. J. Mol. Biol. 422, 300-309 (2012). PubMed
Ando, T. High-speed atomic force microscopy coming of age. Nanotechnology. 23, 062001 (27 pp) (2012). PubMed
Igarashi, K., Uchihashi, T., Koivula, A., Wada, M., Kimura, S., Penttilä, M., Ando, T. and Samejima, M. Visualization of cellobiohydrolase I from Trichoderma reesei moving on crystalline cellulose using high-speed atomic force microscopy. Methods Enzymol. 510, 169-182 (2012). PubMed
Uchihashi, T., Kodera, N. and Ando, T. Guide to video recording of structure dynamics and dynamic processes of proteins by high-speed atomic force microscopy. Nature Protocols. 7, 1193-1206 (2012). PubMed
Ando, T. and Kodera, N. Visualization of mobility by atomic force microscopy. Methods Mol. Biol. 896, 57-69 (2012). PubMed
Uchihashi, T. and Ando, T. High-speed atomic force microscopy and biomolecular processes. Methods Mol. Biol. 736, 285-300 (2011). PubMed
Igarashi, K., Uchihashi, T., Koivula, A., Wada, M., Kimura, S., Okamoto, T., Penttilä, M., Ando, T. and Samejima, M. Traffic jams reduce hydrolytic efficiency of cellulase on cellulose surface. Science. 333, 1279-1282 (2011). PubMed
Laisne, A., Ewald, M., Ando, T., Lesniewska, E. and Pompon, D. Self-assembly properties and dynamic of synthetic proteo-nucleic building blocks in solution and on surfaces. Bioconjugate Chem. 22, 1824-1834 (2011). PubMed
Miyagi, A., Ando, T. and Lyubchenko, Y. L. Dynamics of nucleosomes assessed with time-lapse high speed atomic force microscopy. Biochemistry. 50, 7901-7908 (2011). PubMed
Uchihashi, T., Iino, R., Ando, T. and Noji, H. High-speed atomic force microscopy reveals rotary catalysis of rotorless F1-ATPase. Science. 333, 755-758 (2011). PubMed
Shibata, M., Uchihashi, T., Yamashita, H., Kandori, H. Ando, T. Structural changes in bacteriorhodopsin in response to alternate illumination observed by high-speed atomic force microscopy. Angew. Chem. Int. Ed. 50, 4410-4413 (2011). PubMed
Lyubchenko, Y. L., Shlyakhtenko, L. S. and Ando, T. Imaging of nucleic acids with atomic force microscopy. Methods. 54, 274-283 (2011). PubMed
Inoue, S., Uchihashi, T., Yamamoto, D. and Ando, T. Direct Observation of Surfactant Aggregate Behavior on a Mica Surface using High-Speed Atomic Force Microscopy. Chem. Commun. 47, 4974–4976 (2011). PubMed
Ando, T. and Uchihashi, T. High-speed AFM and imaging of biomoleculr processes. pp. 713-742 in Nanoscale Liquid Interfaces: Wetting, Patterning, and Force Microscopy at the Molecular Scale. Thierry Ondarçuhu, Jean-Pierre Aimé Ed., Pan Stanford Publishing (2013).
Uchihashi, T., Kodera, N. and Ando, T. Nanovisualization of proteins in action using high-speed AFM. pp 119-147, in "Single-molecule Studies of Proteins. Biophysics for the Life Sciences Vol 2". Andres Oberhauser Ed., Springer (2013).
Ando, T. and Kodera, N. Visualization of mobility of atomic force microscopy. pp 57-69, in Springer series Methods in Molecular Biology, vol. 897, part 1 "Experimental Tools for the Intrinsically Disordered Protein Analysis": Vladimir N. Uversky and A. Keith Dunker Ed., Springer (2012).
Ando, T. Techniques for developing high-speed AFM. pp. 1-16 in "Control Technologies for Emerging Micro and Nanoscale Systems" (Lecture Notes in Control and Information Sceinces, Vol.413). Eleftheriou, Evangelos; Moheimani, S.O. Reza, Ed., Springer (2011).
Ando, T., Uchihashi, T., Kodera, N., Shibata, M., Yamamoto, D. and Yamashita, H. High-speed AFM for observing dynamic processes in liquid. pp.189-210, in "Atomic force microscopy in liquid", Arturo M Baró and Donald Refenberger Ed., Wiley-VCH Verlag GmbH (2011)
T. Uchihashi, T. Ando, High-speed atomic force microscopy for dynamic biological imaging. pp. 163-184, in "Life at the Nanoscale - Atomic force microscopy of live cells", Yves Dufrene Ed., Pan Stanford Publishing Pte. Ltd. (2011).
Yokoyama, T., Kosaka, Y. and Mizuguchi, M. Crystal structures of human transthyretin complexed with glabridin. Journal of Medicinal Chemistry. 57, 1090-1096 (2014). PubMed
Yokoyama, T., Ostermann, A., Mizuguchi, M., Niimura, N., Schrader, T. E. and Tanaka, I. Crystallization and preliminary neutron diffraction experiment of human farnesyl pyrophosphate synthase complexed with risedronate. Acta Crystallographica Section F. 70, 470-472 (2014). PubMed
Mizuguchi, M., Obita, T., Serita, T., Kojima, R., Nabeshima, Y. and Okazawa, H. Mutations in the PQBP1 gene prevent its interaction with the spliceosomal protein U5-15kD. Nature Communications. 5, 3822 (2014).
Hayashi, T., Oshima, H., Mashima, T., Nagata, T., Katahira, M. and Kinoshita, M. Binding of an RNA aptamer and a partial peptide of a prion protein: Crucial importance of water entropy in molecular recognition. Nucleic Acids Res. (2014). in press.
Furukawa, A., Sugase, K., Morishita, R., Nagata, T., Kodaki, T., Takaori-Kondo, A., Ryo, A. and Katahira, M. Quantitative Analysis of Location- and Sequence-Dependent Deamination by APOBEC3G Using Real-Time NMR Spectroscopy. Angew Chem Int Ed Engl. 53, 2349-2352 (2014). PubMed
Mashima, T., Nishikawa, F., Kamatari, O. Y., Fujiwara, H., Saimura, M., Nagata, T., Kodaki, T., Nishikawa, S., Kuwata, K. and Katahira, M. Anti-prion activity of an RNA aptamer and its structural basis. Nucleic Acids Res. 41, 1355-1362 (2013). PubMed
Furukawa, A., Okamura, H., Morishita, R., Matsunaga, S., Kobayashi, N., Ikegami, T.,Kodaki, T., Takaori-Kondo, A., Ryo, A., Nagata, T. and Katahira, M. NMR study of xenotropic murine leukemia virus-related virus protease in a complex with amprenavir. Biochem. Biophys. Res. Commun. 425, 284-289 (2012). PubMed
Sugiyama, M., Yagi, H., Yamaguchi, T.,Kumoi, K., Hirai, M., Oba, Y., Sato, N., Porcar, L., Martel, A. and Kato, K. 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. Journal of Applied Crystallography. 47, 430-435 (2014).
Sugiyama, M., Sahashi, H., Kurimoto, E., Takata, S., Yagi, H., Kanai, K., Sakata, E., Minami, Y., Tanaka, K. and Kato, K. Spatial arrangement and functional role of α-subunits of proteasome activator PA28 in hetero-oligomer. Biochemical and Biophysical Research Communications. 432, 141-145 (2013). PubMed
Saikusa, K., Fuchigami, S., Takahashi, K., Asano, Y., Nagadoi, A., Tachiwana, H., Kurumizaka, H., Ikeguchi, M., Nishimura, Y. and Akashi, S. Gas-phase structure of the histone multimers characterized by ion mobility mass spectrometry and molecular dynamics simulation. Anal. Chem. 85, 4165-4171 (2013). PubMed
Saikusa, K., Kuwabara, N., Kokabu, Y., Inoue, Y., Sato, M., Iwasaki, H., Shimizu, T., Ikeguchi, M. and Akashi, S. Characterisation of an intrinsically disordered protein complex of Swi5-Sfr1 by ion mobility mass spectrometry and small-angle X-ray scattering. Analyst. 138, 1441-1449 (2013). PubMed
鎌形清人、「新規一分子蛍光観察法による蛋白質の構造変化の可視化」 化学と生物 51, 22-27 (2013).
Kamagata, K., Kawaguchi, T., Iwahashi, Y., Baba, A., Fujimoto, K., Komatsuzaki, T., Sambongi, Y., Goto, Y., Takahashi, S. Long-term observation of fluorescence of free single molecules to explore protein-folding energy landscapes. J. Am. Chem. Soc. 134, 11525-11532, (2012). PubMed
鎌形清人.「新技術によるタンパク質研究の新展開」生物物理 52, 104-105 (2012).
Downard, K.M., Maleknia, S.D. and Akashi, S. Impact of Limited Oxidation on Protein Ion Mobility and Structure of Importance to Footprinting by Radical Probe Mass Spectrometry. Rapid Commun. Mass Spectrom. 26, 226-230 (2012). PubMed
Kokabu, Y., Murayama, Y., Kuwabara, N., Oroguchi, T., Hashimoto, H., Tsutsui, Y., Nozaki, N., Akashi, S., Unzai, S., Shimizu, T., Iwasaki, H., Sato, M. and Ikeguchi, M. Fission yeast Swi5-Sfr1 complex, an activator of Rad51 recombinase, forms an extremely elongated Dogleg-shaped structure. J. Biol. Chem. 286, 43569-43576 (2011). PubMed
Downard, K.M., Kokabu, Y., Ikeguchi, M. and Akashi, S. Homology Modelled Structure of the βB2B3-Crystallin Heterodimer Studied by Ion Mobility and Radical Probe Mass Spectrometry. FEBS J. 278, 4044-4054 (2011). PubMed
Ikeda, K., Kameda, T., Harada, E., Akutsu, E. and Fujiwara, T. Combined use of replica-exchange molecular dynamics and magic-angle-spinning solid-state NMR spectral simulations for determining the structure and orientation of membrane-bound peptide. J. Phys. Chem. B. 115, 9327-9336 (2011). PubMed
Todokoro, Y., Kobayashi, M., Sato, T., Kawakami, T., Yumen, I., Aimoto, S., Fujiwara, T. and Akutsu, H. Structure analysis of membrane-reconstituted subunit c-ring of E. coli H+-ATP synthase by solid-state NMR under MAS. J. Biomol. NMR. 48, 1-11 (2010). PubMed
Iwasa, H., Meshitsuka, S., Hongo, K., Mizobata, T. and Kawata, Y. Covalent structural changes in unfolded GroES that lead to amyloid fibril formation detected by NMR: Insight into intrinsically disordered proteins. J. Biol. Chem. 286 (24), 21796-21805 (2011). PubMed
Seki, Y., Shimbo, Y., Nonaka, T. and Soda, K. A New Efficient Method for Generating Conformations of Unfolded Proteins with Diverse Main-Chain Dihedral-Angle Distributions Journal of Chemical Theory and Computation. American Chemical Society. 7, 2126-2136 (2011).
Tachiwana, H., Kagawa, W., Shiga, T., Osakabe, A., Miya, Y., Saito, K., Hayashi-Takanaka, Y., Oda, T., Sato, M., Park, S-Y., Kimura, H. and Kurumizaka, H. Crystal structure of the human centromeric nucleosome containing CENP-A. Nature. 476, 232-235 (2011). PubMed
Sugase, K. Elucidating slow binding kinetics of a protein without observable bound resonances by longitudinal relaxation NMR spectroscopy. J. Biomol. NMR. 50, 219-227 (2011). PubMed
Ikeda, K., Kameda, T., Harada, E., Akutsu, H. and Fujiwara, T. Combined Use of Replica-Exchange Molecular Dynamics and Magic-Angle-Spinning Solid-State NMR Spectral Simulations for Determining the Structure and Orientation of Membrane-Bound Peptide. J Phys Chem B. 115, 9327-9336 (2011). PubMed
Higo, J., Nishimura, Y. and Nakamura, H. A Free-energy Landscape for Coupled Folding and Binding of an Intrinsically Disordered Protein in Explicit Solvent from Detailed All-atom Computations. J Am Chem Soc.133, 10448-10458 (2011). PubMed
Yoshizawa, T., Shimizu, T., Yamabe, M., Taichi, M., Nishiuchi, Y., Shichijo, N., Unzai, S., Hirano, H., Sato, M. and Hashimoto, H. Crystal structure of basic 7S globulin, a xyloglucan-specific endo-β-1,4-glucanase inhibitor protein-like protein from soybean lacking inhibitory activity against endo-β-glucanase. FEBS J. 278, 1944-1954 (2011). PubMed
Oroguchi, T., Ikeguchi, M. and Sato, M. Towards the Structural Characterization of Intrinsically Disordered Proteins by SAXS and MD Simulation. J. Physics: Conference Series. 272, 012005 (2011).
Kawai, A., Hashimoto, H., Higuchi, S., Tsunoda M., Sato, M., Nakamura, KT. and Miyamoto, S. A novel heterotetrameric structure of the crenarchaeal PCNA2–PCNA3 complex. J. Struct. Biol. 174, 443-450 (2011). PubMed
苙口友隆, 池口満徳, 佐藤衛. 「天然変性タンパク質:タンパク質の構造・機能研究の新しいターゲット―X線小角散乱と分子動力学シミュレーションによる動的構造解析―」 実験医学. 29, 475-480 (2011).
Horikoshi, N., Tachiwana, H., Saito, K., Osakabe, A., Sato, M., Yamada, M., Akashi, S., Nishimura, Y., Kagawa, W. and Kurumizaka, H. Structural and biochemical analyses of the human PAD4 variant encoded by a functional haplotype gene. Acta Cryst. D 67, 112-118 (2011). PubMed
鎌形清人, 高橋聡. 「新しいタンパク質科学の可能性-新時代を切り拓くマルチタレントDavidBaker-」化学(化学同人). 1, 68-69 (2011).
Nomura, K., Maeda, M., Sugase, K. and Kusumoto, S. Lipopolysaccharide induces raft domain expansion in membrane composed of a phospholipid-cholesterol-sphingomyelin ternary system. Innate Immun. 17, 256-268 (2011). PubMed
Kurahashi, H., Pack, CG., Shibata, S., Oishi, K., Sako, Y. and Nakamura, Y. [PSI(+)] aggregate enlargement in rnq1 nonprion domain mutants, leading to a loss of prion in yeast. Genes Cells. 16, 576-589 (2011). PubMed
Kataoka, M. and Nakagawa, H. Effect of hydration on protein dynamics In "Water, The Forgotten Biological Molecule" (Eds. Le Bihan, D., Fukuyama, H.), pp. 49-62, Pan Stanford Publishing, Singapore (2011).
Kataoka, M. and Nakagawa, H. Protein dynamics studied by neutron incoherent scattering In "Neutrons in Soft Matter" (Eds. Imae, T., Kanaya, T., Furusaka, M., Torikai, N.), pp. 517-538, John Wiley, New Jersey (2011).
中川洋,片岡幹雄. 「中性子非弾性散乱による生体高分子ダイナミックスの研究」 高分子. 60, 195-196 (2011).
Soda, K., Shimbo, Y., Seki, Y. and Taiji, M. Structural Characteristics of Hydration Sites in Lysozyme. Biophysical Chemistry. 156, 31-42 (2011). PubMed
Nakamura, S., Seki, Y., Katoh, E. and Kidokoro, S.-i. Thermodynamic and Structural Properties of the Acid Molten Globule State of Horse Cytochrome c. Biochemistry, American Chemical Society. 50, 3116-3126 (2011). PubMed
Kodera, N.,Yamamoto, D., Ishikawa, R. and Ando T. Video imaging of walking myosin V by high-speed atomic force microscopy. Nature. 468, 72-76 (2010). PubMed ( 補足:関連記事が朝日新聞に掲載されました。)
Ishikawa, T. and Kuwata, K. Interaction Analysis of the Native Structure of Prion Protein with Quantum Chemical Calculations. J. Chem. Theory Comput. 6, 538–547 (2010).
Ishikawa, T. and Kuwata, K. Accerelation of monomer self-consistent charge process in fragment molecular orbital method. Chem-Bio Inform. J. 10, 24-31 (2010).
Yamamoto, N. and Kuwata, K. Redox behaviors of the neurotoxic portion in human prion protein, HuPrP (106-126), Chemical Physics Letters. doi:10.1016 / j.cplett, 2010.08.041 (2010).
Endo, S., Matsunaga, T., Kuwata, K., Zhao, HT., El-Kabbani, O., Kitade, Y. and Hara, A. Chromene-3-carboxamide derivatives discovered from virtual screening as potent inhibitors of the tumour maker, AKR1B10. Bioorg. Med. Chem. 18, 2485-2490 (2010). PubMed
Takahashi, S. and Kamagata, K. Staring at a Protein: Ensemble and Single Molecule Investigations on Protein Folding Dynamics. Single-Molecule Biophysics : Experiment and Theory in Adv. Chem. Phys. 146, 3-22 (2012).
Oda, T., Hashimoto, H., Kuwabara, N., Akashi, S., Hayashi, K., Kojima, C., Kawasaki, T., Shimamoto, K., Sato M. and Shimizu, T. Structure of the N-terminal regulatory domain of a plant NADPH oxidase and its functional implications. J. Biol. Chem. 285, 1435-1445 (2010). PubMed
Yanagihara, I., Nakahira, K., Yamane, T., Kaieda, S., Mayanagi, K., Hamada, D., Fukui, T., Ohnishi, K., Kajiyama, S., Shimizu, T., Sato, M., Ikegami, T., Ikeguchi, M., Honda, T. and Hashimoto, H. Structure and Functional Characterization of Vibrio parahaemolyticus Thermostable Direct Hemolysin. J. Biol. Chem. 285, 16267-16274 (2010). PubMed
Hara, K., Hashimoto, H., Murakumo, Y., Kobayashi, S., Kogame, T., Unzai, S., Akashi, S., Takeda, S., Shimizu T. and Sato, M. Crystal structure of human REV7 in complex with a human REV3 fragment and structural implication of the interaction between DNA polymerase zeta and REV1. J. Biol. Chem. 285, 12299-12307 (2010). PubMed
Yamamoto, D., Taoka, A., Uchihashi, T., Sasaki, H., Watanabe, H., Ando, T. and Fukumori, Y. Visualization and structural analysis of the bacterial magnetic organelle magnetosome using atomic force microscopy. Proc. Natl. Acad. Sci. USA 107, 9382-9387 (2010). PubMed
Shimoyama, S., Nagadoi, A., Tachiwana, H., Yamada, M., Sato, M., Kurumizaka, H., Nishimura, Y. and Akashi, S. Deimination stabilizes histone H2A/H2B dimers as revealed by electrospray ionization mass spectrometry. J. Mass. Spectrom. 45, 900-908 (2010). PubMed
佐藤衛.「中性子溶液散乱法による生体高分子の構造解析」 RADIOISOTOPES. 59, 367-378 (2010).
Sugimoto, S., Yamanaka, K., Nishikori, S., Miyagi, A., Ando, T. and Ogura, T. AAA+ chaperone ClpX regulates dynamics of prokaryotic cytoskeletal protein FtsZ. J. Biol. Chem. 285, 6648-6657 (2010). PubMed
Giocondi, M.-C., Yamamoto, D., Lesniewska, E., Milhiet, P.-E., Ando, T. and Grimellec, C.L. Surface topography of membrane domains. Biochim. Biophys. Acta.-Biomembranes 1978, 703-718 (2010). PubMed
Shibata, M., Yamashita, H., Uchihashi, T., Kandori, H. and Ando, T. High-speed atomic force microscopy shows dynamic molecular processes in photo-activated bacteriorhodopsin. Nature Nanotechnology 5, 208-212 (2010). PubMed
Yagi, H., Takeuchi, H., Ogawa, S., Ito, N., Sakane, I., Hongo, K., Mizobata, T., Goto, Y. and Kawata, Y. Isolation of short peptide fragments from alpha-synuclein fibril core identifies a residue important for fibril nucleation: A possible implication for diagnostic applications. Biochim. Biophys. Acta / Proteins and Proteomics 1804, 2077-2087 (2010). PubMed
Shimoyama, S., Nagadoi, A., Tachiwana, H., Yamada, M., Sato, M., Kurumizaka, H., Nishimura, Y. and Akashi, S. Deimination stabilizes histone H2A/H2B dimers as revealed by electrospray ionization mass spectrometry. J. Mass Spectrom. 45, 900-908 (2010). PubMed
Hiroshima, M. and Sako, Y. Single-molecule kinetic analysis of receptor protein tyrosine kinases. "Cell Signaling Reactions: Single-molecule Kinetic Analyses". Sako, Y. and Ueda, M. ed. Springer in press (2010).
Hibino, K. and Sako, Y. Single-molecule analysis of molecular recognition between signaling proteins Ras and RAF. "Cell Signaling Reactions: Single-molecule Kinetic Analyses". Sako, Y. and Ueda, M. ed. Springer in press (2010).
Hashimoto, H., Hara, K., Hishiki, A., Kawaguchi, S., Shichijo, N., Nakamura, K., Unzai, S., Tamaru, Y., Shimizu, T. and Sato, M. Crystal structure of zinc-finger domain of Nanos and its functional implications. EMBO Rep. 11, 848-853 (2010). PubMed
Kuwabara, N., Hashimoto, H., Yamada, N., Unzai, S., Ikeguchi, M., Sato, M., Murayama, Y., Iwasaki, H. and Shimizu, T. Expression, purification and crystallization of Swi5 and the Swi5-Sfr1 complex from fission yeast. Acta Cryst. F 66, 1124-1126 (2010). PubMed
Milhiet, PE., Yamamoto, D., Berthoumieu, O., Dosset, P., Le, Grimellec, C., Verdier, JM., Marchal, S. and Ando, T. Deciphering the structure, growth and assembly of amyloid-like fibrils using high-speed atomic force microscopy. PLos One. 5, e13240 (8 pp) (2010). PubMed
Yamamoto, D., Uchihashi, T., Kodera, N., Yamashita, H., Nishikori, S., Ogura, T., Shibata, M. and Ando, T. High-speed atomic force microscopy techniques for observing dynamic biomolecular processes. Methods Enzymol. 475 (B) 541-564 (2010). PubMed
安藤敏夫. 「歩くタンパク質 "ミオシンV" を捉えた!」 化学. 66, 55-59 (2010).
安藤敏夫, 古寺哲幸. 「高速原子間力顕微鏡によるタンパク質の動態撮影」 生物物理. 51, 22-25 (2010).
安藤敏夫. Visual Review「高速原子間力顕微鏡によるタンパク質の高解像・動画観察」 感染・炎症・免疫. 40, 31-37 (2010).
安藤敏夫. 「生体分子の動態を捉える高速原子間力顕微鏡」 表面科学. 31, 405-410 (2010).
安藤敏夫. 「生体分子の動的プロセスを直接可視化する高速AFM」 顕微鏡. 45, 22-30 (2010).
Domann, PJ., Akashi, S., Barbas, C., Huang, L., Lau, W., Legido-Quigley, C., McClean, S., Neusüss, C., Perrett, D., Quaglia, M., Rapp, E., Smallshaw, L., Smith, NW., Smyth, WF. and Taylor, CF. Minimum Information About a Proteomics Experiment (MIAPE). Guidelines for reporting the use of capillary electrophoresis in proteomics. Nat Biotechnol. 28, 654-655 (2010). PubMed
Tanaka, S., Kawata, Y., Otting, G., Dixon, NE., Matsuzaki, K. and Hoshino, M. Chaperonin-encapsulation of proteins for NMR. Biochim Biophys Acta. 1804, 866-8671 (2010). PubMed
日比野佳代, 白 燦基, 佐甲靖志. 「細胞内1分子計測とシステムズバイオロジー」 細胞工学. 29, 344-348 (2010).
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