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主要な論文
[Cytochrome c oxidase and cytochrome c] Distinguishing between Cl and O22- as the bridging element between Fe3+ and Cu2+ in resting-oxidized cytochrome c oxidase. Michihiro Suga, Naomine Yano, Kazumasa Muramoto, Kyoko Shinzawa-Itoh, Tomoko Maeda, Eiki Yamashita, Tomitake Tsukihara, and Shinya Yoshikawa, Acta Crystallographica Sect D Biological Crystallography, 67,742-744 (2011). Bovine cytochrome c oxidase structures enable O2 reduction with minimization of reactive oxygens and provide a proton-pumping gate. Kazumasa Muramoto, Kazuhiro Ohta, Kyoko Shinzawa-Itoh, Katsumasa Kanda, Maki Taniguchi, Hiroyuki Nabekura, Eiki Yamashita, Tomitake Tsukihara and Shinya Yoshikawa, Proc Natl Acad Sci U S A., 107, 7740-5(2010). X-ray structure of the NO-bound CuB in bovine cytochrome c oxidase. Kazuhiro Ohta, Kazumasa Muramoto, Kyoko Shinzawa-Itoh, Eiki Yamashita, Shinya Yoshikawa and Tomitake Tsukihara, Acta Cryst. F66, 251-253 (2010). A peroxide bridge between Fe and Cu ions in the O2 reduction site of fully oxidized cytochrome c oxidase could suppress the proton pump. Hiroshi Aoyama, Kazumasa Muramoto, Kyoko Shinzawa-Itoh, Kunio Hirata, Eiki Yamashita, Tomitake Tsukihara, Takashi Ogura and Shinya Yoshikawa, Proc. Natl. Acad. Sci. USA., 106, 2165-2169 (2009). Red-excitation resonance Raman analysis of the nu(Fe=O) mode of ferryl-oxo hemoprotein. Kenichiro Ikemura, Masahiro Mukai, Hideo Shimada, Tomitake Tsukihara, Satoru Yamaguchi, Kyoko Shinzawa-Itoh, Shinya Yoshikawa and Takashi Ogura, J. Am. Chem. Soc., 130, 14384-14385 (2008). A histidine residue as a controlling site for dioxygen reduction and proton pumping of cytochrome c oxidase. Kazumasa Muramoto, Kunio Hirata, Kyoko Shinzawa-Itoh, Shinji Yoko-o, Eiki Yamashita, Hiroshi Aoyama, Tomitake Tsukihara, and Shinya Yoshikawa, Proc. Natl. Acad. USA, 104, 7881-7886 (2007). Structures and physiological roles of all the integral lipids of bovine heart cytochrome c oxidase. Kyoko Shinzawa-Itoh, Hiroshi Aoyama, Kazumasa Muramoto, Hirohito Terada, Tsuyoshi Kurauchi, Yoshiki Tadehara, Akiko Yamasaki, Takashi Sugimura, Sadamu Kurono, Kazuo Tsujimoto, Tsunehiro Mizushima, Eiki Yamashita, Tomitake Tsukihara and Shinya Yoshikawa, EMBO J. 26, 1713-1725 (2007). The Proton-Pumping Pathway of Bovine Heart Cytochrome c Oxidase. Kunitoshi Shimokata, Yukie Katayama, Haruka Murayama, Makoto Suematsu, Tomitake Tsukihara, Kazumasa Muramoto, Shinya Yoshikawa and Hideo Shimada, Proc. Natl. Acad. USA, 104, 4200-4205 (2007). Proton pumping mechanism of bovine heart cytochrome c oxidase. Shinya Yoshikawa, Kazumasa Muramoto, Kyoko Shinzawa-Itoh, Hiroshi Aoyama, Tomitake Tsukihara, Kunitoshi Shimokata, Yukie Katayama, Hideo Shimada, Biochim Biophys Acta., 1757, 1110-1116 (2006). Reaction mechanism of bovine heart cytochrome c oxidase. Shinya Yoshikawa, Kazumasa Muramoto, Kyoko Shinzawa-Itoh, Hiroshi Aoyama, Tomitake Tsukihara, Takashii Ogura, Kunitoshi Shimokata, Yukie Katayama, Hideo Shimada, Biochim Biophys Acta., 1757, 395-400 (2006). Absolute configuration of the hydroxyfarnesylethyl group of haem A, determined by X-ray structural analysis of bovine heart cytochrome c oxidase using methods applicable at 2.8 Å resolution. Eiki Yamashita, Hiroshi Aoyama, Min Yao, Kazumasa Muramoto, Kyoko Shinzawa-Itoh, Shinya Yoshikawa and Tomitake Tsukihara, Acta Cryst. D61, 1373-1377 (2005). The low-spin heme of cytochrome c oxidase as the driving element of the proton-pumping process. Tomitake Tsukihara, Kunitoshi Shimokata, Yukie Katayama, Hideo Shimada, Kazumasa Muramoto, Hiroshi Aoyama, Masao Mochizuki, Kyoko Shinzawa-Itoh, Eiki Yamashita, Min Yao, Yuzuru Ishimura and Shinya Yoshikawa, Proc. Natl. Acad. Sci. U.S.A. 100, 15303-15309 (2003). X-ray structure and the reaction mechanism of bovine heart cytochrome c oxidase. Shinya Yoshikawa, Kyoko Shinzawa-Itoh, Tomitake Tsukihara, J. Inorg. Biochem., 82, 1-7 (2000). X-ray structure of azide bound fully oxidized cytrochrome c oxidase from bovine heart muscle at 2.9 Å resolution. Ming Jie Fei, Eiki Yamashita, Noriko Inoue, Min Yao, Hiroshi Yamaguchi, Tomitake Tsukihara, Kyoko Shinzawa-Itoh, Ryosuke Nakashima and Shinya Yoshikawa, Acta Cryst. D56, 529-535(2000). Quantitative Reevaluation of the Redox Active Sites of Crystalline Bovine Heart Cytochrome c Oxidase. Masao Mochizuki, Hiroshi Aoyama, Kyoko Shinzawa-Itoh, Toshihiro Usui, Tomitake Tsukihaera and Shinya Yoshikawa, J. Biol. Chem. 274, 33403-33411 (1999). Crystal Structure Analysis of Bovine Heart Cytochrome c Oxidase at 2.8 Å Resolution. T. Tomizaki, E. Yamashita, H. Yamaguchi, H. Aoyama, T. Tsukihara, K. Shinzawa-Itoh, R. Nakashima, R. Yaono and S. Yoshikawa, Acta Crystallogr., D55, 31-45 (1999). Crystal Structure of Bovine Heart Cytochrome c Oxidase at 2.8 Å Resolution. Shinya Yoshikawa, Kyoko Shinzawa-Itoh and Tomitake Tsukihara, J. Bioenerg. Biomembr., 30, 7-14 (1998 ). Crystal Structural Studies of a Membrane Protein Complex, Cytochrome c Oxidase from Bovine Heart. T. Tsukihara and S. Yoshikawa, Acta Crystallogr., A54, 895-904 (1998). Redox-Coupled Crystal Structural Change in Bovine Herart Cytochrome c Oxidase. S. Yoshikawa, K. Shinzawa-Itoh,, R. Nakashima, R. Yaono, E. Yamashita, N. Inoue, M. Yao, M. Fei, C. Peters Libeu, T. Mizushima, H. Yamaguchi, T. Tomizaki and T. Tsukihara, Science, 280, 1723-1729 (1998). Architecture of helix bundle membrane proteins: An analysis of cytochrome c oxidase from bovine mitochondria. Wallin, E., Tsukihara, T., Yoshikawa, S., Von Heijne, G., and Elofsson, A., Protein Science, 6, 808-815 (1997). The Whole Structure of the 13-Subinit Oxidized Cytochrome c Oxidase at 2.8 Å. T.Tsukihara, H. Aoyama, E.Yamashita, T. Tomizaki, H. Yamaguchi, K.Shinzawa-Itoh, R. Nakashima, R. Yaono and S.Yoshikawa, Science, 272, 1136-1144 (1996). Structure of Metal Sites of Oxidized Bovine Heart Cytochrome c Oxidase at 2.8 Å Resolution. T.Tsukihara, H. Aoyama, E.Yamashita, T. Tomizaki, H. Yamaguchi, K.Shinzawa-Itoh, R. Nakashima, R. Yaono and S.Yoshikawa, Science, 269, 1069-1074(1995). Effects of Ethyleneglycol Chain Length of Dodecyl Polyethylrneglycol Monoether on Crystallization of Bovine Heart Cytochrome c Oxidase. K.Shinzawa-Itoh, H. Ueda, S.Yoshikawa, H. Aoyama, E.Yamashita and T.Tsukihara, J. Mol. Biol., 246, 572-575(1995). Single Crystals of Bovine Heart Cytochrome c Oxidase at Fully Oxidized Resting, Fully Reduced and CO-bound Fully Reduced States are Isomorphous with Each other. K. Shinzawa-Itoh, H.Yamashita, S. Yoshikawa, Y. Fukumoto, T. Abe and T. Tsukihara, J.Mol.Biol., 228,987-990(1992). Strategies for Crystallization of Large Membrane Protein Complexes. S.Yoshikawa, K.Shinzawa-Itoh, H.Ueda, T.Tsukihara, Y.Fukumoto, T.Kubota, M.Kawamoto, K.Fukuyama and H.Matsubara, J.Crystal Growth, 122, 298-302(1992). Crystallization of Beef Heart Cytochrome c Oxidase. S. Yoshikawa, K. Shinzawa, T. Tsukihara, T. Abe and W. S. Caughey, J. Crystal Growth, 110, 247-251(1990). Crystalline Cytochrome c Oxidase of Bovine Heart Mitochondrial Membrane: Composition and X-ray Diffraction Studies. S. Yoshikawa, T. Tera, Y. Takahashi, T. Tsukihara and W. S. Caughey, Proc. Natl. Acad. Sci. USA, 85, 1354-1358(1988). The Crystal structure of Bonito (Katsuo) Ferrocytochrome c at 2.3 Å Resolution. II. Structure and Function. N. Tanaka, T. Yamane, T. Tsukihara, T. Ashida, and M. Kakudo, J. Biochem., 77, 147-162(1975). Oxidation of a Ferrocytochrome c in the Crystalline State---Structural Change and Anion Binding. T. Tsukihara, T. Yamane, N. Tanaka, T. Ashida, and M. Kakudo, J. Biochem., 73, 1163-1167(1973). The Cystal Structure of Bonito (Katsuo) Ferrocytochrome c at 2.3 Å Resolution. T. Ashida, N. Tanaka, T. Yamane, T. Tsukihara, and M. Kakudo, J. Biochem., 73, 463-465(1973). The Crystal Structure of Bonito (Katsuo) Ferrocytochrome c at 4 Å Resolution. T.Ashida, T.Ueki, T.Tsukihara, A.Sugihara, T.Takano and M.Kakudo, J. Biochem., 70, 913-924(1971). [Gap junction channels] Aspartic Acid Residue D3 Critically Determines Cx50 Gap Junction Channel Transjunctional Voltage-Dependent Gating and Unitary Conductance. Xin L, Nakagawa S, Tsukihara T, Bai D., Biophysical Journal, 102, 1022-1031 (2012). Asparagine175 of connexin32 is a critical residue for docking and forming functional heterotypic gap junction channels with connexin26. So Nakagawa, Xiang-Qun Gong, Shoji Maeda, Yuhua Dong, Yuko Misumi, Tomitake Tsukihara, Donglin Bai, J Biol Chem. 286,19672-19681 (2011). Structure of the gap junction channel and its implications for its biological functions. Maeda S, Tsukihara T., Cell Mol Life Sci. 2011 Apr;68(7):1115-29. Structural and functional studies of gap junction channels. Nakagawa S, Maeda S, Tsukihara T., Curr Opin Struct Biol. 2010 Aug;20(4):423-30. A description of the structural determination procedures of a gap junction channel at 3.5 Å resolution. Suga M, Maeda S, Nakagawa S, Yamashita E, Tsukihara T., Acta Crystallogr. D65, 758-766 (2009). Structure of the connexin-26 gap junction channel at 3.5 Å resolution. Shoji Maeda, So Nakagawa, Michihiro Suga, Eiki Yamashita, Atsunori Oshima, Yoshinori Fujiyoshi and Tomitake Tsukihara, Nature, 458, 597-602 (2009). [Vaults] The structure of rat liver vault at 3.5 angstrom resolution. H. Tanaka, K. Kato, E. Yamashita, T. Sumizawa, Y. Zhou, M. Yao, K. Iwasaki, M. Yoshimura and T. Tsukihara Science, 323, 384-388 (2009). A vault ribonucleoprotein particle exhibiting 39-fold dihedral symmetry. Koji Kato, Hideaki Tanaka, Tomoyuki Sumizawa, Masato Yoshimura, Eiki Yamashita, Kenji Iwasaki and Tomitake Tsukihara, Acta Crystallogr. D 64, 525-531 (2008). [Viruses] Crystallographic analysis reveals octamerization of viroplasm matrix protein P9-1 of Rice black streaked dwarf virus. Akita F, Higashiura A, Shimizu T, Pu Y, Suzuki M, Uehara-Ichiki T, Sasaya T, Kanamaru S, Arisaka F, Tsukihara T, Nakagawa A, Omura T., J Virol.,86, 746-56(2012). Viroplasm matrix protein Pns9 from rice gall dwarf virus forms an octameric cylindrical structure. Akita F, Miyazaki N, Hibino H, Shimizu T, Higashiura A, Uehara-Ichiki T, Sasaya T, Tsukihara T, Nakagawa A, Iwasaki K, Omura T., J Gen Virol., 92, 2214-21(2011). The crystal structure of a virus-like particle from the hyperthermophilic archaeon Pyrococcus furiosus provides insight into the evolution of viruses. Fusamichi Akita, Khoon Tee Chong, Hideaki Tanaka, Eiki Yamasita, Naoyuki Miyazaki, Yuichiro Nakaishi, Mamoru Suzuki, Kazuhiro Namba, Yasuko Ono, Tomitake Tsukihara, and Atsushi Nakagawa, J. Mol. Biol. 368, 1469-1483 (2007). Structure of the Central Hub of Bacteriophage Mu Baseplate Determined by X-ray Crystallography of gp44. Y. Kondou, D. Kitagawa, S. Takeda, Y. Tsuchiya, E. Yamashita, M. Mizuguchi, K. Kawano, and T. Tsukihara, J. Mol. Biol., 352, 976-985, (2005). Transcription and the conserved interactions of two major structural proteins of a pair of Phytoreoviruses confirm the mechanism of assembly of the outer capsid layer. Miyazaki, N., Hagiwara, K., Naitow, H., Higashi, T., Cheng, R. H., Tsukihara, T., Nakagawa, A., & Omura, T., J. Mol. Biol., 345, 229-237(2005). The aminoi-terminal region of major capsid protein P3 is essential for self-assembly of single-shelled core-like particles of Rice dwarf virus. Hagiwara, K.,Higashi, T., Miyazaki, N., Naitow, H., Cheng, R. H., Nakagawa, A.,Mizuno, H., Tsukihara, T., & Omura, T. , J. Virol., 78, 3145-3148 (2004). The atomic structure of Rice Dwarf Virus reveals the self-assembly mechanism of component proteins Atsushi Nakagawa, Naoyuki Miyazaki, Junichiro Taka, Hisashi Naitow, Akira Ogawa, Zui Fujimoto, Hiroshi Mizuno, Takahiko Higashi, Yasuo Watanabe, Toshio Omura, R. Holland Cheng, and Tomitake Tsukihara, Structure, 11, 1227-1238 (2003). Crystal Structure of Tobacco Necrosis Virus at 2.25 A Resolution. Y. Oda, K. Saeki, Y. Takahashi, T. Maeda, H. Naitow, T. Tsukihara and K. Fukuyama, J. Mol. Biol., 300, 153-169 (2000). Crystal Structure Analysis of Tobacco Necrosis Virus (TNV) at 5 Å Resolution. M.Bando, Y,Morimoto, T.Sato, T.Tsukihara, Y.Yokota, K.Fukuyama and H.Matsubara, Acta Crystallogr., D50, 878-883(1994). Crystallization and Preliminary X-ray Study of a Double-Shelled Spherical Virus, Rice Dwarf Virus. H.Mizuno, H.Kano, T.Omura, M.Koizumi, M.Kondoh and T.Tsukihara, J.Mol.Biol., 219, 665-669(1991). Symmetry and Subunit Arrangement of Tobacco Necrosis Virus (TNV). T. Tsukihara, Y. Yokota, T. Koyama, K. Fukuyama and H. Matsubara, Acta Crystallogr., B46,855-860(1990). Crystallization and Preliminary X-ray Diffraction Studies of Tobacco Necrosis Virus. K. Fukuyama, S. Hirota, and T. Tsukihara, J. Mol. Biol., 196, 961-962(1987). Crystallization and Preliminary Characterization of Arabis Mosaic Virus. Y. Takemoto, Y. Nagahara, K. Fukuyama, T. Tsukihara, and M. Iwaki, Virology, 145, 191-194(1985). A Description of Techniques Used in the Structure Determination of Southern Bean Mosaic Virus at 2.8A Resolution. C. Abad-Zapatero, S. S. Abdel-Meguid, J. E. Johnson, A.G. W. Leslie, I. Rayment, M. G. Rossmann, D. Suck, and T. Tsukihara, Acta Crystallogr., B37, 2002-2018(1981). Southern Bean Mosaic Virus at 2.8A Resolution. C. Abad-Zapatero, S. S. Abdel-Meguid, J. E. Johnson, A. G. W. Leslie, I. Rayment, M. G. Rossmann, D. Suck, and T. Tsukihara Struct. Aspects Recognit. Assem. Biol. Macromol., 2, 831-848(1981). Structure of Southern Bean Mosaic Virus at 2.8 A Resolution. C. Abad-Zapatero, S. S. Abdel-Meguid, J. E. Johnson, A.G.W. Leslie, I. Rayment, M. G. Rossmann, D. Suck, and T. Tsukihara, Nature, 286, 33-39(1980). A Structural Comparison of Concanavalin A and Tomato Bushy Stunt Virus Protein. P. Argos, T. Tsukihara, and M. G. Rossmann, J. Mol. Evol., 15, 169-179(1980). [Nuclear transport] Selective nuclear export mechanism of small RNAs. Lee SJ, Jiko C, Yamashita E, Tsukihara T., Curr Opin Struct Biol., 21, 101-8(2011). A high resolution structure of the pre-microRNA nuclear export machinery. Chimari Okada, Eiki Yamashita, Soo Jae Lee, Satoshi Shibata, Jun Katahira, Atsushi Nakagawa, Yoshihiro Yoneda, Tomitake Tsukihara, Science, 326, 1275-1279 (2009). The structure of importin-beta bound to SREBP-2: nuclear import of a transcription factor. S.J. Lee, E. Yamashita, A. Nakagawa, T. Tsukihara and Y. Yoneda , Science, 302, 1571-1575(2003). Crystallization and preliminary crystallographic analysis of importin-β-SREBP-2 complex. Soo Jae Lee, Toshihiro Sekimoto, Eiki Yamashita, Emi Nagoshi, Atsushi Nakagawa, Hideaki Tanaka, Yoshihiro Yoneda and Tomitake Tsukihara, Acta Crystallographica D59, 1866-1868 (2003). The adoption of a twisted structure of importin-beta is essential for the protein-protein interaction required for nuclear transport. S. J. Lee, N. Imamoto, H. Sakai, A. Nakagawa, S. Kose, M. Koike, M. Yamamoto, T. Kumasaka, Y. Yoneda and T. Tsukihara, J. Mol. Biol., 302, 251-264 (2000). [Proteasomes and related proteins] Structural basis of sugar-recognizing ubiquitin ligase. Mizushima, T., Hirao, T., Yoshida, Y., Lee, S.J., Chiba, T., Iwai, K., Yamaguchi, Y., Kato, K., Tsukihara, T., & Tanaka, K. , Nature Struc. Mol. Biol., 11, 365-370(2004). The Structure of the Mammalian 20S Proteasome at 2.75 Å Resolution. M. Unno, T. Mizushima, Y. Morimoto, Y. Tomisugi, K. Tanaka, N. Yasuoka, & T. Tsukihara, Structure 10, 609-618 (2002). Structure Determination of the Constitutive 20S Proteasome from Bovine Liver at 2.75 Å Resolution. M. Unno, T. Mizushima, Y. Morimoto, Y. Tomisugi, K. Tanaka, N. Yasuoka, & T. Tsukihara, J. Biochem. 131, 171-173 (2002). New Crystal Forms and Low Resolution Structure Analysis of 20S Proteasomes from Bovine Liver. Y. Tomisugi, M. Unnno, T. Mizushima, Y. Morimoto, N. Tanahashi, K. Tanaka, T. Tsukihara and N. Yasuoka, J. Biochem. 127, 941-943 (2000). Ordered Structure of the Crystallized Bovine 20S Proteasome. Y. Morimoto, T. Mizushima, A. Yagi, N. Tanahashi, K. Tanaka, A. Ichihara and T. Tsukihara, J. Biochem., 117, 471-474(1995). [Monoamine oxidases] Structure of human monoamine oxidase at 2.2 Å resolution: The control of opening the entry for substrates/inhibitors. Se-Young Son, Jichun Ma, Youhei Kondou, Masato Yoshimura, Eiki Yamashita, and Tomitake Tsukihara, Proc. Natl. Acad. USA, 105, 5739-5744 (2008). T. Structure of rat monoamine oxidase A and its specific recognitions for substrates and inhibitors. Ma, J, Yoshimura, M., Yamashita, E., Nakagawa, A., Ito, A., & Tsukihara, J. Mol. Biol., 338,103-114(2004). Crystallization and preliminary crystallographic analysis of rat monoamine oxidase A with complexed with clorgyline. Ma, J., Kubota, F., Yoshimura, M., Yamashita, E., Nakagawa, A., Ito, A., & Tsukihara, T. , Acta Cryst. D60, 317-319 (2004). [Ferredoxins] Tertiary Structure of [2Fe-2S] Ferredoxin from Spirulina platensis refined at 2.5 Å Resolution: Structural Comparison of Plant-type Ferredoxins and an Electrostatic Potential Analysis. K. Fukuyama, N. Ueki, H. Nakamura, T. Tsukihara and H. Matsubara, J. Biochem., 117, 1017-1023 (1995). Crystal Structural Analysis of [2Fe-2S] Ferredoxin I from Equistum arvense at 1.8 Å Resulution. S.Ikemizu, M.Bando, T.Sato, Y.Morimoto, T.Tsukihara and K.Fukuyama, Acta Crystallgr., D50, 167-174 (1994). Structure of the [2Fe-2S] Ferredoxin I from the Blue-green Alga, Aphanothece sacrum at 2.2 Å Resolution. T. Tsukihara, K. Fukuyama, M. Mizushima, T. Harioka, M. Kusunoki, Y. Katsube, T. Hase and H. Matsubara, J. Mol. Biol., 216,399-410(1990). Structure of [4Fe-4S] Ferredoxin from Bacillus thermoproteolyticus Refined at 2.3 Å Resolution: Structural Comparisons of Bacterial Ferredoxins. K. Fukuyama, H. Matsubara, T. Tsukihara and Y. Katsube, J. Mol. Biol., 210, 383-398(1989). Tertiary Structure of Bacillus thermoproteolyticus [4Fe-4S] Ferredoxin: Evolutionary Implications for Bacterial Ferredoxins. K. Fukuyama, Y. Nagahara, T. Tsukihara, Y. Katsube, T. Hase and H. Matsubara, J. Mol. Biol., 199, 183-193(1988). Synthesis of Tetrapeptide 2Fe-2S Complexes of Cys-X-Y-Cys Segments by a Ligand-Exchange Reaction. Peptide Models of 2Fe Ferredoxin Characterized by Electrochemistry and Spectroscopy. S. Ueno, N. Ueyama, A. Nakamura, and T. Tsukihara, Inorganic Chemistry, 25, 1000-1005(1986). Preliminary X-ray Diffraction Studies on a Ferredoxin from the Thermophilic Archaebacterium, Thermoplasma acidophilum. T. Tsukihara, K. Fukuyama, S. Wakabayashi, K. Wada, H. Matsubara, L. Kerscher, and D. Oesterhelt, J. Mol. Biol., 186, 481-482(1985).
Synthetic Analogue of the Active Site of Plant Type Ferredoxin. S. Ueno, N. Ueyama, A. Nakamura, K. Wada, H. Matsubara, S. Kumagai, S. Sakakibara, and T. Tsukihara, Pept. Chem., 22, 133-136(1985). Main Chain Fold of a [2Fe-2S] Ferredoxin I from Aphanothece Sacrum at 2.5Å Resolution. T. Tsutsui, T. Tsukihara, K. Fukuyama, Y. Katsube, T. Hase, H. Matsubara, Y. Nishikawa and N. Tanaka, J. Biochem., 94, 299-302(1983). Structure-function Relationship of [2Fe-2S] Ferredoxins and Design of a Model Molecule. T. Tsukihara, M. Kobayashi, M. Nakamura, Y. Katsube, K. Fukuyama, T. Hase, K. Wada, and H. Matsubara, BioSystems, 15, 243-257(1982). Preliminary X-ray Diffraction Studies on a [4Fe-4S] Ferredoxin from Bacillus thermoproteolyticus. T. Tsukihara, K. Homma, K. Fukuyama, Y. Katsube, T. Hase, H. Matsubara, N. Tanaka, and M. Kakudo, J. Mol. Biol., 152, 821-823(1981). X-ray Analysis of a [2Fe-2S] Ferredoxin from Spirulina platensis. Main Chain Fold and Location of Side Chains at 2.5 Å Resolution. T. Tsukihara, K. Fukuyama, M. Nakamura, Y. Katsube, N. Tanaka, M. Kakudo, K. Wada, T. Hase, and H. Matsubara, J. Biochem., 90, 1763-1773(1981). Structure of S. platensis [2Fe-2S] Ferredoxin and Evolution of Chloroplast-type Ferredoxins. K. Fukuyama, T. Hase, S. Matsumoto, T. Tsukihara, Y. Katsube, N. Tanaka, M. Kakudo, K. Wada, and H. Matsubara, Nature, 286, 522-524(1980). X-ray Analysis of Ferredoxin from Spirulina platensis. II. Chelate Structure of Active Center. T. Tsukihara, K. Fukuyama, H. Tahara, Y. Katsube, Y. Matsuura, N. Tanaka, M. Kakudo, K. Wada, and H. Matsubara, J. Biochem., 84, 1645-1647(1978). Crystallization and a 5 A X-ray Diffraction Study of Aphanothece sacrum Ferredoxin. A. Kunita, M. Koshibe, Y. Nishikawa, K. Fukuyama, T. Tsukihara, Y. Katsube, Y. Matsuura, N. Tanaka, M. Kakudo, T. Hase and H. Matsubara, J. Biochem., 84, 989-992(1978). Location of the Iron-sulfur Cluster in Spirulina platensis Ferredoxin by X-ray Analysis. K. Ogawa, T. Tsukihara, H. Tahara, Y. Katsube, Y. Matsuura, N. Tanaka, M. Kakudo, K. Wada, and H. Matsubara, J. Biochem., 81, 529-531(1977). [Other proteins] Structure of coenzyme A-disulfide reductase from Staphylococcus aureus at 1.54 Å resolution. Mallett TC, Wallen JR, Karplus PA, Sakai H, Tsukihara T, Claiborne A. Biochemistry. 45, 11278-11289 (2006). The asymmetric IscA homodimer with an exposed [2Fe-2S] cluster suggests the structural basis of the Fe-S cluster biosynthetic scaffold. Morimoto K, Yamashita E, Kondou Y, Lee SJ, Arisaka F, Tsukihara T, Nakai M., J Mol Biol. 360, 117-132 (2006). Preliminary crystallographic analysis of the antibiotic discharge outer membrane lipoprotein OprM of Pseudomonas aeruginosa with an exceptionally long unit cell and complex lattice structure. Akama H, Kanemaki M, Tsukihara T, Nakagawa A, Nakae T., Acta Crystallogr. F61, 131-133 (2005). Conformational Changes in the Tryptophan Synthase from a Hyperthermophile. S. J. Lee, K. Ogasahara, J. Ma, K. Nishio, M. Ishida, Y. Yamagata, T. Tsukihara, and K. Yutani., Biochemistry, 44, 11417-11427 (2005). Preliminary Crystallographic analysis of the antibiotic discharge outer membrane lipoprotein OprM of Pseudomonas aeruginosa with an exceptionally long unit cell and complex lattice structure. H. Akama, M. Kanemaki, T. Tsukihara, A. Nakagawa, & T. Nakae, Acta Cryst. F61, 131-133(2005). Conformational Changes in the R -Subunit Coupled to Binding of the â 2 -Subunit of Tryptophan Synthase from Escherichia coli: Crystal Structure of the Tryptophan Synthase R -Subunit Alone K. Nishio, Y. Morimoto, M. Ishizuka, K. Ogasawara, T. Tsukihara, & K. Yutani, Biochemistry, 44, 1184-1192 (2005). Crystal structure of the drug discharge outer membrane protein, OprM, of Pseudomonas aeruginosa. Akama, H., Kanemaki, M., Yoshimura, M., Tsukihara, T., Kashiwagi, S., Yoneyama, H., Narita, S., Nakagawa, A., & Nakae, T. , J. Biol. Chem., 279, 52816-52819 (2004). Crystal structure of the membrane fusion protein, MexA, of the multidrug transporter in Pseudomonas aeruginosa. Akama, H., Matsuura, T., Kashiwagi, S., Yoneyama, H., Narita, S., Tsukihara, T., Nakagawa, A., & Nakae, T. , J. Biol. Chem., 279, 25939-25942 (2004). Structure of the carboxyl-terminal Src kinase, Csk. Ogawa A, Takayama Y, Sakai H, Chong KT, Takeuchi S, Nakagawa A, Nada S, Okada M, Tsukihara T., J. Biol. Chem. 277, 14351-14354(2002). Roles of functional loops and the C-terminal segment of a single-stranded DNA binding protein elucidated by X-Ray structure analysis. T. Matsumoto,Y. Morimoto, N. Shibata, T. Kinebuchi, N. Shimamoto, T. Tsukihara and N. Yasuoka, J. Biochem., 127, 329-335 (2000). X-ray structure of b-carbonic anhydrase from the red alga, Porphyridium purpureum., reveals a novel catalytic site for CO2 hydration. S. Mitsuhashi, T. Mizushima, E. Yamashita, M. Matsumoto, T. Kumasaka, H. Moriyama, T. Ueki, S. Miyachi and T. Tsukihara, J. Biol. Chem. 275, 5521-5526 (2000). Crystal Structure of Methionine Aminopeptidase from Hyperthermophile, Pyrococcus furiosus. T. H. Tahirov, H. Oki, T. Tsukihara, K. Ogasawara, Y. Izu, S. Tsunasawa, I. Kato and K. Yutani, J. Mol. Biol., 284, 101-124 (1998). [Small molecules] The Crystal Structure of the Cupric Complex with Succinimide. II. Potassium Tetrakis(succinimidato)copper(II) Hexahydrate and Lithium Tetrakis(succinimidato)copper(II) Monohydrate. T. Tsukihara, Y. Katsube, K. Fujimori, K. Kawashima and Y. Kan-nan, Bull. Chem. Soc. Japan, 47, 1582-1585(1974). Structure and Absolute Configuration of (+)546-cis(o)-(sarcosinate-N-monopropionato) triamminecobalt(III) Ion. K. Okamoto, T. Tsukihara, J. Hidaka, and Y. Shimura, Chem. 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The Crystal Structure of Cupric Complex with Succinimide I. Cesium Tetrakis(succinimidato)copper(II) Dihydrate. T. Tsukihara, Y. Katsube, K. Fujimori and T. Ito, Bull. Chem. Soc. Japan, 45, 2959-2963(1972).
The Crystal Structures of L-Citrulline Hydrochloride and L-Homocitrulline Hydrochloride. T. Ashida, K. Funakoshi, T. Tsukihara, T. Ueki, and M. Kakudo, Acta Crystallogr., B28, 1367-1374(1972). The Crystal and Molecular Structure of Bis(L-prolinamidato)- nickel(II) Dihydrate. T. Tsukihara, Y. Katsube, K. Fujimori, and Y. Ishimura, Bull. Chem. Soc. Japan, 45, 1367-1371(1972). The Crystal Structure of 1-Ethyl-5-bromouracil. II. The Crystal Structure of the Form II Crystal of 1-Ethyl-5-bromouracil. T. Tsukihara, T. Ashida, and M. Kakudo, Bull. Chem. Soc. Japan, 45, 909-912(1972). The Crystal Structure of Two Forms of 1-Ethyl-5-bromouracil. H. Mizuno, N. Nakanishi, T. Fujiwara, K. Tomita, T. Tsukihara, T. Ashida, and M. Kakudo, Biochem. Biophys. Res. Commun., 41, 1161-1165(1970). [Methods] Ab initio crystal structure determination of spherical viruses that exhibit a centrosymmetric location in the unit cell. J. Taka, H. Naitow, M. Yoshimura, N. Miyazaki, A. Nakagawa, and T. Tsukihara, Acta Cryst. D61, 1099-1106 ,(2005). Scaling of one-shot oscillation images with a reference data set. Kunio Hirata, Eiki Yamashita, Hiroshi Aoyama, Kazumasa Muramoto, Kyoko Shinzawa-Itoh, Shinya Yoshikawa and Tomitake Tsukihara, J Synchrotron Radiat, 11, 60-63 (2004). Optimization of the energy constant of the methionine S -C bond for X-PLOR refinement of protein structure M. Odoko, M. Yao, E. Yamashita, R. Nakashima, K. Hirata, H. Aoyama, K. Muramoto, K. Shinzawa-Itoh, S. Yoshikawa and T. Tsukihara, J. Appl. Cryst., 34 80-81 (2001). A Low Resolution Crystal Structure of Rice Dwarf Virus Determined by Ab initio Phasing. H. Naitow, Y. Morimoto, H. Mizuno, H. Kano, T. Omura, M. Koizum and T. Tsukihara, Acta Crystallogr. D55, 77-84 (1999). A Strategy for Collecting Isomorphous Derivative Data with the Oscillation Method. A. G. W. Leslie and T. Tsukihara, J. Appl. Crystallogr., 13, 304-305(1980). Processing and Post-Refinement of Oscillation Camera Data. M. G. Rossmann, A. G. W. Leslie, S. S. Abdel-Meguid, and T. Tsukihara, J. Appl. Crystallogr., 12, 570-571(1979). |