「生体超分子構造」 A01：X 線及び電子線による超分子の構造解析法の研究 月原冨武 1. J. Taka, H. Naitow, M. Yoshimura, N. Miyazaki, A. Nakagawa and T.

Tsukihara. Ab initio crystal structure determination of spherical viruses that exhibit a centrosymmetric location in the unit cell. Acta Cryst. D 61, 1099-1106, 2005.

2. E. Yamashita, H. Aoyama, M. Yao, K. Muramoto, K. Shinzawa-Itoh, S.

Yoshikawa and T. Tsukihara. 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 A resolution. Acta Cryst. D61, 1373-1377, 2005.

3. Y. Kondou, D. Kitagawa, S. Takeda, Y. Tsuchiya, E. Yamashita, M.

Mizuguchi, K. Kawano, T. Tsukihara. Structure of the Central Hub of Bacteriophage Mu Baseplate Determined by X-ray Crystallography of gp44. J. Mol. Biol., 352, 976-985, 2005.

4. K. Nishio, Y. Morimoto, M. Ishizuka, K. Ogasawara, T. Tsukihara, & K. Yutani,

Conformational Change in the α-Subunit Coupled to Binding of the β2-Subunit of

Tryptophan Synthase from Escherichia coli: Crystal Structure of the Tryptophan

Synthase �-Subunit Alone. Biochemistry, 44, 1184-1192 (2005).

5. Miyazaki, N., Hagiwara, K., Naitow, H., Higashi, T., Cheng, R. H., Tsukihara, T.,

Nakagawa, A., & Omura, T. 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. J. Mol. Biol. 345, 229-237 (2005).

難波啓一 1. Yonekura, K., Maki-Yonekura, S. & Namba, K. (2005). Building the

atomic model for the bacterial flagellar filament by electron cryomicroscopy and image analysis. Structure 13, 407-412.

2. Samatey, F. A., Matsunami, H., Imada, K., Nagashima, S. & Namba K.

(2004). Crystallization of a core fragment of the flagellar hook protein, FlgE. Acta Crystallogr. D 60, 2078–2080.

3. Shailk T. R., Thomas D. R., Chen J. Z., Samatey F.A., Matsunami. H.,

Imada K., Namba K. & DeRosier D. J. (2005). A partial atomic structure for the flagellar hook of Salmonella typhimurium. Proc. Nat’l Acad. Sci. USA, 102, 1023-1028.

4. Samatey, F. A., Matsunami, H., Imada, K., Nagashima, S., Shaikh, T.

R., Thomas, D., Chen, J. Z., DeRosier, D. J., Kitao, A. & Namba K. (2004). Structure of the bacterial flagellar hook and implication for the molecular universal joint mechanism. Nature 431, 1062-1068.

5. Diószeghy, Z., Závodszky, P., Namba, K. & Vonderviszt, F. (2004).

Stabilization of flagellar filaments by HAP2 capping. FEBS Lett. 568, 105-109.

6. Saijo-Hamano, Y., Uchida, N., Namba, K. & Oosawa, K. (2004). In

vitro characterization of FlgB, FlgC, FlgF, FlgG, FliE, flagellar basal body proteins of Salmonella. J. Mol. Biol. 339, 423-435.

7. Minamino, T. & Namba, K. (2004). Self-assembly and type III protein

export of the bacterial flagellum. J. Mol. Microbiol. and Biotechnol. 7, 5-17.

8. Minamino, T., Saijo-Hamano, Y., Furukawa, Y., González, P. B.,

Macnab, R. M. & Namba, K. (2004). Domain organization and function of Salmonella FliK, a flagellar hook-length contorol protein. J. Mol. Biol. 341, 491-502.

9. Saijo-Hamano, Y., Minamino, T., Macnab, R. M. & Namba, K. (2004).

Structural and functional analysis of the C-terminal cytoplasmic domain of FlhA, an integral membrane component of the type III flagellar protein export apparatus in Salmonella J. Mol. Biol. 343, 457-466.

10. Saijo-Hamano, Y., Imada, K., Minamino, T., Kihara, M., Macnab, R.

M. & Namba, K. (2005). Crystallization and preliminary X-ray analysis of C-terminal cytoplasmic domain of FlhA, a membrane protein subunit of the bacterial flagellar type III protein export apparatus. Acta Crystallogr., F61, 599-602.

11. Iwase, R., Imada, K., Hayashi, F., Uzumaki, T., Namba, K. & Ishiura,

M. (2004)Crystallization and preliminary crystallographic analysis of the circadian clock protein KaiB from the thermophilic cyanobacterium Themosynechococus elongates BP-1. Acta Crystallogr. D60, 727-729.

12. Oda, T., Namba, K. & Maéda, Y. (2005)Position and orientation of

phalloidinin F-actin determinedby X-ray fiber diffraction analysis. Biophys. J. 88, 2727-2736.

13. Iwase, R., Imada, K., Hayashi, F., Uzumaki, T., Morishita, M., Onai,

K., Furukawa, Y., Namba, K. & Ishiura, M. (2005) Functionally important substructures of circadian clock protein KaiB in unique tetramer complex. J. Biol. Chem. 280, 43141-43149.

14. Yonekura, K., Yakushi, T., Atsumi, T., Maki-Yonekura, S., Homma, M.

& Namba, K. (2006) Electron cryomicroscopic visualization of PomA/B stator units of the sodium-driven flagellar motor in liposomes. J. Mol. Biol. in press

15. Ferris, H. U., Furukawa, Y., Minamino, T., Kroetz, M. B., Kihara, M.,

Namba, K. & Macnab, R. M. (2006) FlhB regulates ordered export of flagellar components via autocleavage mechanism. J. Biol. Chem. 280, 41236-41242.

16. Gonzalez-Pedrajo, B. et al. Interactions between C ring proteins and

export apparatus components: a possible promotion mechanism of flagellar type III protein export. Molecular Microbiology 2006 in press

17. Kishimoto, A.; Hasegawa, K.; Namba, K. (2005) β-Helix is a likely

core structure of yeast prion Sup35 amyloid fibers. Spring8 Research Frontiers. 28-29.

18. Minamino, T.; Pugsley, A. P. (2005) Measure for measure in the control

type III secretion hook and needle. Mol. Microbiol, 56, 303-308.

19. 今田勝己; サマティファデル; 松波秀行; 長島重広; 北尾彰朗;

米倉功治; 米倉さおり; 難波啓一. (2005） べん毛による細菌の

泳ぎと方向転換の分子機構. 蛋白質 核酸 酵素, 50, No.10,

1328-1334.

20. 北尾彰朗; サマティファデル; 松波秀行; 今田勝巳; 難波啓一.

(2005) 生体超分子のユニバーサルジョイント. In silico で探

る細菌べん毛フックのメカニズム. 蛋白質 核酸 酵素. 50,

No.10, 1335-1340.

佐藤主税 1. K.Mio, Y.Kubo, T.Ogura, T.Yamamoto and C.Sato: Biochem Biophys

Res Comm. 337, 998-1005, 2005 2. K.Mio, T.Ogura, Y.Hara, Y.Mori and C.Sato: Biochem Biophys Res

Comm. 333, 768-777, 2005 3. Toshihiko Ogura, Kazuhiro Mio, Ikuo Hayashi, Hiroyuki Miyashita,

Rie Fukuda, Raphael Kopan, Tatsuhiko Kodama, Takao Hamakubo, Takeshi Iwastubo, Taisuke Tomita and Chikara Sato. Three-dimensional structure of γ-secretase complex. Biochem. Biophys. Res. Comm. in press

北尾彰朗 1. F.A .Samatey, et al., Akio Kitao and Keiichi Namba, Structure of the

bacterial flagellar hook and implication for the molecular universal joint mechanism. Nature, 431, 1062-1068(2004)

2. Yasumasa Joti, Akio Kitao and Nobuhiro Go, Protein Boson Peak

Originated from Hydration-Related Multiple Minima Energy Landscape. J. Am. Chem. Soc., 127, 8705-8709 (2005)

3. 北尾彰朗; サマティファデル; 松波秀行; 今田勝巳; 難波啓一.

(2005) 生体超分子のユニバーサルジョイント. In silico で探

る細菌べん毛フックのメカニズム. 蛋白質 核酸 酵素. 50,

No.10, 1335-1340.

姚閔 1. LAFIRE : Software for automating the refinement process of protein structure analysis. Min Yao, Yong Zhou, and Isao Tanaka

Acta Cryst., D62, 189-196 (2006)

2. An algorithm for model building: expanding model in map segment. Yong Zhou, Min Yao, and Isao Tanaka, J. Appl. Cryst., 39, 57-63 (2006)

3. The CGL2612 protein from Corynebacterium glutamicum is a drug

resistance related transcriptional repressor: Structural and functional analysis on a newly identified transcription factor from genome DNA analysis. Hiroshi Itou, Ui Okada, Hiroaki Suzuki, Min Yao, Masaaki Wachi, Nobuhisa Watanabe and Isao Tanaka J. Boil. Chem. 280, 38711-38719 (2005)

4. Crystal structure of the putative RNA methyltransferase PH1948

from Pyrococcus horikoshii, in complex with the co-purified S-adenosyl-L-homocysteine. Yong-Gui Gao, Min Yao, Zhou Yong, and Isao Tanaka Proteins, 61, 1141-1145 (2005)

5. Crystal structure of the hypothetical protein ST2072 from Sulfolobus

tokodaii. Yoshikazu Tanaka, Kouhei Tsumoto, Eiki Tanabe, Yoshiaki Yasutake, Naoki Sakai, Min Yao, Isao Tanaka and Izumi Kumagai Proteins, 61, 1127-1131 (2005)

6. Molecular basis of alanine discrimination in editing site. Masaaki Sokabe, Ayuko Okada, Min Yao, Takashi Nakashima, Isao Tanaka PNAS, 102, 11669-11674 (2005)

7. Structure of the type I L-asparaginase from the hyperthermophilic archaea Pyrococcus horikoshii at 2.16 A resolution Min Yao, Yoshiaki Yasutake, Hazuki Morita, and Isao Tanaka Acta Cryst. D61, 294-301 (2005)

片山栄作 1. Iwaki M, Tanaka H, Iwane AH, Katayama E, Ikebe M, Yanagida T.

Cargo binding makes a wild-type single-headed myosin-VI move processively. Biophys. J. Epub ahead of print 2006

2. Morita-Ishihara T, Ogawa M, Sagara H, Yoshida M, Katayama E,

Sasakawa C. Shigella Spa33 is an essential C-ring component of type

III secretion machinery. J. Biol. Chem. 281（1）599-607 2006 3. Siddique MS, Mogami G, Miyazaki T, Katayama E, Uyeda TQ, Suzuki

M. Cooperative structural change of actin filaments interacting with activated myosin motor domain, detected with copolymers of pyrene-labeled actin and acto-S1 chimera protein. Biochem. Biophys. Res. Commun. 333（4）1185-1191 2005

4. Hagiwara K, Yonedu S, Saito K, Shiraishi T, Sugo T, Tojyo T,

Katayama E. High-performance purification of gelsolin from plasma using anion-exchange porous hollow-fiber membrane. J Chromatogr. B Analyt. Technol. Biomed. Life Sci. 821（2）153-158 2005

5. Siddique MS, Miyazaki T, Katayama E, Uyeda TQ, Suzuki M.

Evidence against essential roles for subdomain 1 of actin in actomyosin sliding movements. Biochem. Biophys. Res. Commun. 332（2）474-481 2005

［知的所有権］

6. 顕微鏡解析用プローブ及び顕微鏡解析方法 発明者：片山栄作

権利者：東京大学 特願 2005-168887 出願年月日：平成 17 年 6

月 8 日

大澤匡範 1. Osawa M, Dace A, Tong KI, Valiveti A, Ikura M, Ames JB. Mg2+ and

Ca2+ differentially regulate DNA binding and dimerization of DREAM. J Biol Chem. 2005 280(18):18008-14.

2. Mizukoshi Y, Takahashi H, Shimada I. Rapid Preparation of Stable

Isotope Labeled Peptides that Bind to Target Proteins by a Phage Library System. J Biomol NMR. 2006 34(1):23-30.

3. Sakakura M, Takahashi H, Terasawa H, Takeuchi K, Fujii I, Shimada I.

Backbone resonance assignments for the Fv fragment of catalytic antibody 6D9 complexed with a transition state analogue. J Biomol NMR. 2005 33(4):282.

4. Ueda T, Kato A, Kuramitsu S, Terasawa H, Shimada I. Identification

and characterization of a second chromophore of DNA photolyase from Thermus thermophilus HB27. J Biol Chem. 2005 280(43):36237-43.

5. Yokogawa M, Takeuchi K, Shimada I. Bead-linked proteoliposomes: a reconstitution method for nmr analyses of membrane protein-ligand interactions. J Am Chem Soc. 2005 127(34):12021-7.

6. Sakakura M, Noba S, Luchette PA, Shimada I, Prosser RS. An NMR

method for the determination of protein-binding interfaces using dioxygen-induced spin-lattice relaxation enhancement. J Am Chem Soc. 2005 127(16):5826-32.

7. Nakamura T, Takahashi H, Takeuchi K, Kohno T, Wakamatsu K,

Shimada I. Direct determination of a membrane-peptide interface using the nuclear magnetic resonance cross-saturation method. Biophys J. 2005 89(6):4051-5.

8. Nakasako M, Oka T, Mashumo M, Takahashi H, Shimada I,

Yamaguchi Y, Kato K, Arata Y. Conformational dynamics of complementarity-determining region H3 of an anti-dansyl Fv fragment in the presence of its hapten. J Mol Biol. 2005 19;351(3):627-40.

岩崎憲治 1. Iwasaki, K., Mitsuoka, K., Fujiyoshi, Y., Fujisawa, Y., Kikuchi, M.,

Sekiguchi, K. and Yamada, T. (2005). Electron tomography reveals diverse conformations of integrin αIIbβ3 in the active state. J. Struct. Biol. 150, 259-267.

2. 岩崎憲治；高木淳一. (2005). 電子顕微鏡を用いた蛋白質の高次

構造解析が開く世界 ―インテグリンレセプターの構造解析を

中心として―. 生化学, vol77, No.5, 400-410． 3. 岩崎憲治；宮澤淳夫．(2005). クライオ電子顕微鏡法と X 線結晶

構造解析のハイブリッドアプローチによって提案されたイノシ

トール 3 リン酸受容体の Ca2+放出のメカニズム． 生物物理, vol45，192-197．

4. 岩崎憲治．（2005）. 細胞内の分子を電子顕微鏡で見る．Bionics

（バイオニクス），１１月号，オーム社，p.p.38-43.

中村春木 1. I. Fukuda, H. Nakamura: Molecular dynamics sampling scheme

realizing multiple distributions. Phys. Rev. E (2005) 71 (4), 046708. 2. Y. S. Watanabe, Y. Fukunishi, H. Nakamura: Generation of a flexible

loop structural ensemble and its application to induced-fit structural changes following ligand binding. BIOPHYSICS (2006) 2 (1), 1-12.

3. I. Fukuda, H. Nakamura: Construction of an extended invariant for an

arbitrary ordinary differential equation with its development in a numerical integration algorithm. Phys. Rev. E. (2006) 73 (2), 026703.

安永卓生 1. Atomic model construction of protein complexes from electron

micrographs and visualization of their 3D structure using VR system, Noda, K., Nakamura, M., Nishida, R., Yamaguchi, Y., Tamura, Y., Nakamura, H., and Yasunaga, T., J. Plasma, Phys. (2006) in press.

2. An axonemal dynein particularly important for flagellar movement at

high viscosity: Implications from a new chlamydomonas mutant deficient in the dynein heavy chain gene DHC9. Yagi T., Minoura I, Fujiwara A., Saito R., Yasunaga T., Hirono M., and Kamiya R. J. Biol. Chem.,. 280, 41412-41420. (2005)

3. Structural basis for Ca2+-regulated muscle relaxation at interaction

sites of troponin with actin and tropomyosin. Murakami K, Yumoto F, Ohki SY, Yasunaga T, Tanokura M, Wakabayashi T. J Mol Biol. 352(1) 178-201 (2005)

4. Automatic Detecting Particles Approach Using Adaboost-SVM, Yang,

J., Ohashi, T., & Yasunaga, T. Wseas Transactinns on Biology and Biomedicine, 2, 163-168 (2005)

小倉尚志 1. Takahashi, T., Kuroiwa, S., Ogura, T. and Yoshikawa, S., Probing the

Oxygen Activation Reaction in Intact Whole Mitochondria through Analysis of Molecular Vibrations, J. Am. Chem. Soc., 2005, 127, 9970-9971.

2. 小倉尚志、高橋俊成、黒岩繁樹（2005）ミトコンドリア中のシト

クロム酸化酵素の in situ ラマン散乱、生物物理、実験技術、45、

272-275.

A02：鞭毛、ウイルスの構造形成と感染機構の研究 大村敏博 1. Hagiwara, K., Higashi, T., Takahashi, K., Hara, N., Aoki, H., Miyazaki,

N., Wang, W. Y., Zhu, Y., Yatou, O., Tanaka, H. and Omura, T. Encapsidation of the core of Rice gall dwarf virus by the outer capsid protein of Rice dwarf virus that was expressed in transgenic rice plants. Journal of General Plant Pathology 72(2) in press (2006).

2. Wei, T., Shimizu, T., Hagiwara, K., Kikuchi, A., Moriyasu, Y., Suzuki,

N., Chen, H. and Omura, T. The Pns12 protein of Rice dwarf virus is essential for formation and nucleation of viral assembly complexes. Journal of Generral Virology 87, 429-438 (2006).

3. Miyazaki, N., Hagiwara, K., Naitow, H., Higashi, T., Cheng, R. H.,

Tsukihara, T., Nakagawa, A., and Omura, T. Transcapsidaiton and the conserved interactions of two major structural proteins of a pair of phytoreoviruses confirm the mechanism of assembly of the outer capsid layer. Jouranal of Molecular Biology 345, 229-237 (2005).

4. Zhong, B., Shen, Y. and Omura, T. RNA-binding domain of the key

Structural protein P7 for the Rice dwarf virus particle assembly. Acta Biochemica et Biophysica Sinica 37, 55-60 (2005).

有坂文雄 1. Hitomi Takahashi, Eiji Inagaki, Yayoi Fujimoto, Chizu Kuroishi,

Yuichi Nodake, Yuki Nakamura, Fumio Arisaka, Katsuhide Yutani, Seiki Kuramitsu, Shigeyuki Yokoyama, Masaki Yamamoto, Masashi Miyano, and Tahir H. Tahirov: Structure and implications for the thermal stability of phosphopantetheine adenylyltransferase from Thermus thermophilus. Acta Cryst. D60: 97 - 104 (2004)

2. Michael G. Rossmann, Vadim V. Mesyanzhinov, Fumio Arisaka and

Petr G. Leiman: The bacteriophage T4 DNA injection machine. Current Opinion in Structural Biology 14: 171-180 (2004)

3. Shigeki Takeda, Makoto Suzuki, Takahito Yamada, Manabu

Kageyama, and Fumio Arisaka: Mapping of functional sites on the primary structure of the contractile tail sheath protein of bacteriophage T4 by mutation analysis. Biochim.Biophys.Acta 1699: (1-2) 163-171 (2004)

4. Shuji Kanamaru, Yasutaka Ishiwata, Toshiharu Suzuki, Michael G.

Rossmann and Fumio Arisaka: Control of Bacteriophage T4 Tail Lysozyme Activity During the Infection Process. J. Mol. Biol. 346:1013–1020 (2005)

5. Victor A. Kostyuchenko, Paul R. Chipman, Petr G. Leiman, Fumio

Arisaka, Vadim V. Mesyanzhinov, Michiael G. Rossmann. The tail structure of bacteriophage T4 and its mechanism of contraction. Nat Struct Mol Biol. 12:810-813 (2005)

6. Youske Shimizu, Hisayasu Mori, Fumio Arisaka, Masaru Tanokura:

Stalk region of kinesin-related protein Unc104 has moderate ability to form coiled-coil dimer Biochem. Biophys. Rres.Comm. 337:868-874 (2005)

7. Fumio Arisaka Assembly and Infection Process of Bacteriophage T4

Chaos 15:047502 (2005)

栗栖源嗣 1. Yan, J., Kurisu, G. and Cramer, W. A Intraprotein transfer of the quinine analogue inhibitor 2,5-dibromo-3-methyl-6-isopropyl-p-benzoquinone in the cytochrome b6f complex. Proc. Natl. Acad. Sci. U. S. A., 103, 69-74. 2006

2. Cramer, W. A., Yan, J. S., Zhang, H., Kurisu, G., Smith, J. L. Structure

of the cytochrome b6f complex: new prosthetic groups, Q-space, and the 'hors d'oeuvres hypothesis' for assembly of the complex. Photosynthesis Res., 85, 133-144. 2005.

3. Okutani, S., Hanke, G. T., Satomi, Y., Takao, T., Kurisu, G., Suzuki, A.,

Hase, T. Three Maize Leaf Ferredoxin:NADPH Oxidoreductases Vary in Subchloroplast Location, Expression, and Interaction with Ferredoxin. Plant Physiol., 139, 1451-1459. 2005.

4. 栗栖源嗣 光合成における電子伝達超分子系の役割 蛋白質・核

酸・酵素, 50, 1167-1173, 2005 5. 栗栖源嗣, Zakharov, S.D., Zhalnina, M. V., Cramer, W. A. 蛋白質・核

酸・酵素, 50, 356-361, 2005

薬師寿治 1. Yakushi T, Yang J, Fukuoka H, Homma M, Blair DF. Roles of charged residues of rotor and stator in flagellar rotation: comparative study using H+-driven and Na+-driven motors in Escherichia coli. J Bacteriol. 2006 Feb;188(4):1466-72.

2. Kusumoto A, Kamisaka K, Yakushi T, Terashima H, Shinohara A,

Homma M. Regulation of polar flagellar number by the flhF and flhG genes in Vibrio alginolyticus. J Biochem (Tokyo). 2006 Jan;139(1):113-21.

3. Yonekura K, Yakushi T, Atsumi T, Maki-Yonekura S, Homma M,

Namba K. Electron cryomicroscopic visualization of PomA/B stator units of the sodium-driven flagellar motor in liposomes. J Mol Biol. 2006 Mar 17;357(1):73-81.

4. Sowa Y, Rowe AD, Leake MC, Yakushi T, Homma M, Ishijima

A, Berry RM. Direct observation of steps in rotation of the bacterial flagellar motor. Nature. 2005 Oct 6;437(7060):916-9.

5. Fukuoka H, Yakushi T, Kusumoto A, Homma M. Assembly of motor

proteins, PomA and PomB, in the Na+-driven stator of the flagellar motor. J Mol Biol. 2005 Aug 26;351(4):707-17.

6. Okabe M, Yakushi T, Homma M. Interactions of MotX with MotY and

with the PomA/PomB sodium ion channel complex of the Vibrio alginolyticus polar flagellum. J Biol Chem. 2005 Jul 8;280(27):25659-64.

福山恵一 1. Crystal Structure of Escherichia coli YfhJ Protein, a Member of Isc

Machinery Involved in Assembly of Iron-Sulfur Clusters. Y.

Shimomura, Y. Takahashi, Y. Kakuta, and K. Fukuyama, Proteins: Struct. Funct. Bioinform. 60, 566-569 (2005).

2. Crystallization and preliminary X-ray diffraction study of BchU, a

methyltransferase from Chlorobium tepidum involved in bacteriochlorophyll c biosynthesis. J. Harada, K. Wada, H. Yamaguchi, H. Oh-oka, H. Tamiaki, and K. Fukuyama, Acta Crystallogr. Sect. F, 61, 712-714 (2005).

3. Identification of Variant Molecules of Bacillus thermoproteolyticus

Ferredoxin: Crystal Structure Reveals Bound Coenzyme A and an Unexpected [3Fe-4S] Cluster Associated with a Canonical [4Fe-4S] Ligand Motif. T. Shirakawa, Y. Takahashi, K. Wada, J. Hirota, T. Takao, D. Ohmori, and K. Fukuyama, Biochemistry 44, 12402-12410 (2005).

4. Crystal Structure of Escherichia coli SufA Involved in Biosynthesis of

Iron-sulfur Clusters: Implications for a functional dimer. K. Wada, Y. Hasegawa, Z. Gong, Y. Minami, K. Fukuyama, and Y. Takahashi, FEBS Lett. 579, 6543-6548 (2005).

5. Crystal structure of phycocyanobilin:ferredoxin oxidoreductase in

complex with biliverdin IXα: a key enzyme in biosynthesis of phycocyanobilin. Y. Hagiwara, M. Sugishima, Y. Takahashi, and K. Fukuyama, Proc. Natl. Acad. Sci. USA 103, 27-32 (2006).

6. Crystal structure of Escherichia coli SufC, an ABC-type ATPase

component of the SUF iron-sulfur cluster assembly machinery. S. Kitaoka, K. Wada, Y. Hasegawa, Y. Minami, K. Fukuyama, and Y. Takahashi, FEBS Lett. 580, 137-143 (2006).

A03：蛋白質複合体における高度な機能制御機構の研究 吉川信也 1. Kenji Oda, Takashi Ogura, Evan H. Appelman, Shinya Yoshikawa :The

intrinsic stability of the second intermediate following the dioxygen-bound form in the O2 reduction by cytochrome c oxidase, FEBS Lett. 570(2004) 161-165.

2. T. Takahashi, S. Kuroiwa, T. Ogura, S. Yoshikawa: Probing the oxygen

activation reaction in intact whole mitochondria through analysis of molecular vibrations, J. Am. Chem.. Soc. 127(2005) 9970-9971.

3. S. Yoshikawa: Mitochondrial cytochrome c oxidase in “Structures” B.

Lewin ed., Virtual Text, Ergito Cambridge MA USA, 2005 4. E. Yamashita, H. Aoyama, M. Yao, K. Muramoto, K. Shinzawa-Itoh, S.

Yoshikawa, T. Tsukihara: Absolute configuration of the hydroxyfarnesylethyl group of haem A, determined by X-ray structural analysis of bovine heart cytopchyrome c oxidase using methods applicable at 2.8 Å resolution, Acta Cryst. D61(2005),1373-1377.

5. S. Yoshikawa:Structural chemical studies on the reaction mechanism of

cytochrome c oxidase, in “Biophysical and Structural Aspects of Bioenrgetics” Marten Wikström ed., Royal Society of Chemistry, Cambridge UK, 2005, pp. 55 – 71.

6. S. Yoshikawa: Reaction mechanism and phospholipids structures of

bovine heart cytochrome c oxidase, Biochem. Soc. Trans. 33 (2005) 934 -937.

神谷信夫 1. Vasil'ev S, Shen JR, Kamiya N, Bruce D. (2004) "The orientations of

core antenna chlorophylls in photosystem II are optimized to maximize the quantum yield of photosynthesis", FEBS Lett., 561, 111-116.

2. Iwai, M., Katoh, H., Katayama, M. and Ikeuchi, M. (2004) " PSII-Tc

protein plays an important role in dimerization of Photosystem II", Plant Cell Physiol., 45, 1809-1816.

3. Nakazato K., Homma T., and Tomo T. (2004) "Rapid solubility

measurement of protein crystals as a function of precipitant concentration with micro-dialysis cell and two-beam interferometer", J. Synchrotron Rad., 11, 34-37.

4. Weng J., Tan C., Shen J.-R., Yu Y., Zeng X., Xu C.-H. and Ruan K

(2004) "pH-induced conformational changes in the soluble manganesestabilizing protein of photosystem II", Biochemistry, 43, 4855-4861.

5. Yamamoto Y., Sakuma S. and Shen J.-R. (2004) "Isolation o

photosystem II-enriched membranes and the oxygen-evolving complex(OEC) subunit proteins from higher plants", In Methods in MoleculaBiology: Photosynthesis Protocols (ed. by R. Carpentier), 274:29-36Humana Press.

6. Tan C.-Y., Xu C.-H., Wong J., Shen J.-R., Sakuma S., Yamamoto Y.

Lange R., Balny C., and Ruan K.-C. (2005) "Pressure Equilibrium andJump Study on Unfolding of 23kDa Protein from Spinach PhotosystemII", Biophys J. 88, 1264-1275.

7. Årsköld S. P., Smith P. J., Shen J.-R., Pace R. J. and Krausz E. (2005

"Key cofactors of photosystem II cores from four organisms identified by1.7-K absorption, CD and MCD", Photosynthesis Res. 84, 309-316.

8. Enami I., Suzuki T., Tada O., Nakada Y., Nakamura K., Tohri A., Ohta

H., Inoue I. and Shen J.-R. (2005) "Distribution of the extrinsic proteinas a potential marker for the evolution of photosyntheticoxygen-evolving photosystem II", FEBS Journal, 272, 5020-5030.

9. Kamata T., Hiramoto H., Morita N., Shen J.-R., Mann N. H. and

Yamamoto Y. (2005) "Quality control of photosystem II: An FtsHprotease plays an essential role in the turnover of the reaction center D1protein in Synechocystis PCC 6803 under heat stress as well as lighstress conditions", Photochemical & Photobiological Sciences, 4983-990.

10. Shen J.-R. and Kamiya N. (2005) "3D Crystal Structure of the

Photosystem II Core", In Photosystem II: The Light-DrivenWater:Plastoquinone Oxidoreductase, Edited by T.J. Wydrzynski and KSatoh, pp. 449-4677, 2005, Springer, The Netherlands.

11. 神谷 信夫、 沈 建仁 （2005） ”光化学系II複合体の構造と

機能”、「蛋白質 核酸 酵素」、Vol. 50, No. 10, 1174-1179.

12. Tomo T., Hirano E., Nagata J. & Nakazato K. (2005) "Pigment exchange of Phosystem II reaction center by chlorophyll d", Photosynthesis Research 84,77-83.

13. Iwai M, Katayama M, Ikeuchi M. (2006) "Absence of the psbH gene

product destabilizes the Photosystem II complex and prevents association of the Photosystem II-X protein in the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1", Photosynth Res. in press [Epub ahead of print]

大友征宇 1. Kobayashi, M., Fujioka, Y., Mori, T., Terashima, M., Suzuki, H.,

Shimada, Y., Saito, T., Wang, Z.-Y. & Nozawa, T. (2005). Reconstitution of photosynthetic reaction centers and core antenna-reaction center complexes in liposomes and their thermal stability. Biosci. Biotechnol. Biochem. 69, 1130-1136.

2. Kobayashi, M., Takaya, A., Kanai, N., Ota, Y., Saito, T., Wang, Z.-Y. &

Nozawa, T. (2004). Reconstitution and replacement of bacteriochlorophyll a molecules in photosynthetic reaction centers. J. Biochem. 136, 363-369(2004).

3. Suzuki, H., Shimada, Y., Kobayashi, M., Kudo, M., Nozawa, T. &

Wang, Z.-Y. (2005). Isotopic labeling of proteins by utilizing photosynthetic bacteria. Anal. Biochem. 347, 324-326.

4. Wang, Z.-Y., Gokan., Kobayashi, M. & Nozawa, T. (2005). Solution

structures of the core light-harvesting α and β polypeptides from Rhodospirillum rubrum: Implications for the pigment-protein and protein-protein interactions. J. Mol. Biol. 347, 465-477.

永田宏次 1. Kamo, M., Inouye, K., Nagata, K. and Tanokura, M. (2005).

Preliminary X-ray crystallographic analysis of thermolysin in the presence of 4 M NaCl. Acta Crystallogr. D61, 710-712.

2. Nagata, K., Sasaki, H., Ohtsuka, J., Ming, H., Okai, M., Kubota, K.,

Kamo, M., Ito, K., Ichikawa, T., Koyama, Y. and Tanokura, M. (2005).

Crystal structure of monomeric sarcosine oxidase from Bacillus sp. NS-129 reveals multiple conformations at the active-site loop. Proc. Japan Acad. B81, 220-224.

3. Okai, M., Kudo, N., Nagata, K., Lee, W. C., Kamo, M. and Tanokura,

M. (2005). Crystal structure of the short-chain flavin reductase HpaC from Sulfolobus tokodaii strain 7. Proc. Japan Acad. B81, 229-232.

4. Miyakawa, T., Hatano, K., Lee, W. C., Kato, Y., Sawano, Y., Yumoto,

F., Nagata, K. and Tanokura, M. (2005). Crystallization and preliminary X-ray analysis of the YjgF/YER057c/UK114-family protein ST0811 from Sulfolobus tokodaii strain7. Acta Crystallogr. F61, 828-830.

5. Yumoto, F., Lu, Q. W., Morimoto, S., Tanaka, H., Kono, N., Nagata,

K., Ojima, T., Takahashi-Yanaga, F., Miwa, Y., Sasaguri, T., Nishita, K., Tanokura, M. and Ohtsuki, I. (2005). Drastic Ca2+ sensitization of myofilament associated with a small structural change in troponin I in inherited restrictive cardiomyopathy. Biochem. Biophys. Res. Commun. 338, 1519-1526.

6. Kawaguchi, M., Yasumasu, S., Shimizu, A., Hiroi, J., Yoshizaki, N.,

Nagata, K., Tanokura, M. and Iuchi, I. (2005). Purification and gene cloning of Fundulus heteroclitus hatching enzyme. A hatching enzyme system composed of high choriolytic enzyme and low choriolytic enzyme is conserved between two different teleosts, Fundulus heteroclitus and medaka Oryzias latipes. FEBS J. 272, 4315-4326.

7. Maruoka, S., Lee, W. C., Kamo, M., Kudo, N., Nagata, K. and

Tanokura, M. (2005). Crystal structure of glutamine amidotransferase from Pyrococcus horikoshii OT3. Proc. Japan Acad. B81, 459-462.

8. Miyakawa, T., Lee, W. C., Hatano, K., Kato, Y., Sawano, Y., Miyazono,

K., Nagata, K. and Tanokura, M. (2006). Crystal Structure of the YjgF/YER057c/UK114 Family Protein from the hyperthermophilic archaeon Sulfolobus tokodaii strain 7. Proteins 62, 557-561.

9. Jia, M. Z., Ohtsuka, J., Lee, W. C., Nagata, K. and Tanokura, M. (2006). Crystallization and preliminary X-ray analysis of PH1566, a putative ribosomal RNA processing factor from the hyperthermophilic archaeon Pyrococcus horikoshii OT3. Acta Crystallogr. F62, 47-48.

10. Kato, Y., Hino, Y., Nagata, K. and Tanokura, M. (2006). Solution

structure and binding specificity of FBP11/HYPA WW domain as Group-II/III. Proteins 63, 227-234.

福森義宏 1. N.Numoto, T.Nakagawa, A.Kita, Y.Sasayama,Y.Fukumori and K.Miki

Structure of an extracellular giant hemoglobin of the gutless beard worm Oligobrachia mashikoi. Proc. Natl. Acad. Sci. USA, 102, 14521-14526, 2005.

2. N.Numoto, T.Nakagawa, A.Kita, Y.Sasayama,Y.Fukumori and K.Miki

Crystallization and preliminary X-ray crystallographic analysis of extracellular giant hemoglobin from pogonophoran Oligobrachia mashikoi. Biochim. Biophys. Acta, 1750, 173-176, 2005.

3. T.Nakagawa, S.Onoda, M.Kanemori, Y.Sasayama and Y.Fukumori

Purification, characterization and sequence analyses of the extracellular giant hemoglobin from Oligobrachia mashikoi. Zool. Sci. 22, 283-291, 2005.

4. H.Kumiota, K.Matsuura, T.Hino, S.Takahashi, H.Hori, Y.Fukumori,

I.Morisihima, Y. Shiro NO Reduction by Nitric-oxide Reductase from Denitrifying Bacterium Pseudomonas aeruginosa. J.Biol.Chem. 279, 55247-55254, 2004

5. M.Horikoshi, T.Yura, S.Tsuchimoto, Y.Fukumori, M.Kanemori

Conserved region 2.1 of Escherichia coli heat shock transcription factor σ32 is required for modulating both metabolic stability and transcriptional activity. J.Bact. 186, 7474-7480, 2004.

6. 沼本修孝、福森義宏、三木邦夫 巨大ヘモグロビンの謎に迫る—X

線結晶構造解析で構造と機能を解き明かせ！— 化学、61、30-34, 2006.

［新聞報道］ 論文（１）については下記の新聞に掲載されました。 京都新聞（１０／４）、産經新聞（１０／６）、日刊工業新聞（１０

／４）、日本経済新聞（１０／４）、毎日新聞（１０／４）、北国新聞

（１０／４）、北陸中日新聞（１０／４）

Boero Mauro

1. “Enol-to-Keto Tautomerism of Peptide Groups”, K. Kamiya, M. Boero, K. Shiraishi and A. Oshiyama, J. Phys. Chem. B 110, 4443 (2006).

2. “Double-Metal-Ion/Single-Metal-Ion Mechanisms of the Cleavage Reaction of Ribozymes”, M. Boero, M. Tateno, K. Terakura and A. Oshiyama, J. Chem. Theory and Computation, 1, 925 (2005).

3. “Charge Localization in DNA Fibers”, F. L. Gervasio, A. Laio, M. Parrinello and M. Boero, Phys. Rev. Lett. 94, 158103 (2005).

4. “Density and Temperature Dependence of Proton Diffusion in Water: a First Principles Molecular Dynamics Study”, M. Boero, T. Ikeshoji and K. Terakura, Chem. Phys. Chem. 6, 1775 (2005).

5. “Hydrophobic/hydrophilic Interactions of Water with Alkanethiolate Chains from First Principles Calculations”, P. L. Silvestrelli, F. Ancilotto, F. Toigo, C. Sbraccia, T. Ikeda and M. Boero, Chem. Phys. Chem. 6, 1889 (2005).

6. “Free Energy Molecular Dynamics Simulations of Pulsed-Laser-Irradiated SiO2”, M. Boero, A. Oshiyama, P. L. Silvestrelli and K. Murakami, Appl. Phys. Lett. 86, 201910 (2005).

7. “New Electron States that Float on semiconductor and Metal Surface”, S. Okada, Y. Enomoto, K. Shiraishi and A. Oshiyama, Surf. Sci. 585, L177 (2005).

8. “Carbon three-dimensional architecture formed by intersectional collision of graphite patches”, T. Kawai, S. Okada, Y. Miyamoto and A. Oshiyama, Phys. Rev. B 72, 035428 (2005).

仲本準 1. Kaneko, Y., R. Danev, K. Nagayama and H. Nakamoto Intact

Carboxysomes in a cyanobacterial cell visualized by Hilbert differential contrast transmission electron microscopy J. Bacteriol., 188 (2): 805-808, 2006.

深井周也 1. Watanabe, O. Nureki, S. Fukai, R. Ishii, H. Okamoto, S. Yokoyama, Y.

Endo, and H. Hori, Roles of conserved amino acid sequence motifs in the SpoU (TrmH) RNA methyltransferase family, J Biol Chem., 280,10368-10377 (2005)

2. K. Nakanishi, S. Fukai, Y. Ikeuchi, A. Soma, Y. Sekine, T. Suzuki, and

O. Nureki, Structural basis for lysidine formation by ATP pyrophosphatase accompanied with a lysine-specific loop and a tRNA-recognition domain, Proc. Natl. Acad.Sci. USA,21,7487-7492 (2005).

3. K. Nakanishi, Y. Ogiso, S. Fukai and O. Nureki , Structural basis for

anticodon recognition by methionyl-tRNA synthetase, Nat. Struct. Mol. Biol.,12,931-932 (2005).

4. T. Numata, S. Fukai, Y. Ikeuchi., T. Suzuki. and O. Nureki , Structural

basis for sulfur relay to RNA mediated by heterohexameric TusBCD complex, Structure, 14, 357-366 (2005).

川岸郁朗 1. Shiomi, D., Yoshimoto, M., Homma, M., and Kawagishi, I. (2006)

Helical distribution of the bacterial chemoreceptor via co-localization with the Sec protein translocation machinery. Mol. Microbiol., in press.

2. Hyakutake, A., Homma, M., Austin, M. J., Boin, M. A., Häse, C. C.,

and Kawagishi, I. (2005) Only one of the five CheY homologs of

Vibrio cholerae directly switches flagellar rotation. J. Bacteriol. 187: 8403-8410.

3. Shih, Y.-L., Kawagishi, I., and Rothfield, L. (2005) The MreB and

Min cytoskeletal-like systems play independent roles in prokaryotic polar differentiation. Mol. Microbiol. 58: 917-928.

4. Shiomi, D., Banno, S., Homma, M., and Kawagishi, I. (2005)

Stabilization of polar localization of a chemoreceptor via its covalent modifications and its communication with a different chemoreceptor. J. Bacteriol. 187: 7647-7654.

5. 川岸郁朗，入枝泰樹，坂野聡美 (2006) 大腸菌走化性シグナル

伝達機構――タンパク質局在と相互作用を中心に． 物性研究

85: 668-684.

6. 坂野聡美，川岸郁朗 (2005) 膜を介したシグナル伝達． 『リポ

ソーム応用の新展開 〜人工細胞の開発に向けて〜』（秋吉一成，

辻井薫 監修） エヌ・ティー・エス 257-266

水島恒裕 1. 糖鎖認識ユビキチンリガーゼの立体構造から明らかになった蛋

白質分解のための糖鎖の役割 水島恒裕 日本結晶学会誌,

47, 197-203.(2005) 2. The Crystal structure of human Atg4b, a processing and de-conjugating

enzyme for autophagosome-forming modifiers. Kumanomidou T, Mizushima T, Komatsu M, Suzuki A, Tanida I, Sou YS, Ueno T, Kominami E, Tanaka K, Yamane T, J Mol Biol. 355(4), 612-618. (2006)

森本幸生 1. Age related changes of alpha-crystallin aggregate in human lens

N.Fujii, Y.Shimmyo, M.Sakai, Y.Sadakane, T.Nakamura, Y.Morimoto, T.Kinouchi, Y.Goto and K.Lampi Amino Acids, accepted (2005)

2. Crystallization and preliminary X-ray diffraction study of L-lactate

oxidase (LOX), R181M mutant, from Aerococcus viridans Y.Umena, K. Yorita, T. Matsuoka, M. Abe, A. Kita, K. Fukui, T. Tsukihara and Y.

Morimoto Acta.Cryst., F61, 439-441 (2005) 3. Conformational Changes in the a-subunit coupled to binding of the

b2-subunit of tryptophan synthase from Escherichia coli: Crystal structure of tryptophan synthase a-subunit alone. K. Nishio, Y. Morimoto, M. Ishizuka, K. Ogasahara, K. Yutani, and T. Tsukihara Biochemistry, 44, 1184-1192 (2005)

北野健 1. Kitano, K., Kita, A., Hakoshima, T., Niimura, Y., and Miki, K.

(2005) ." Crystal structure of decameric peroxiredoxin (AhpC) from Amphibacillus xylanus." Proteins, 59(3):644-647.

2. Yanuar, A., Sakurai, S., Kitano, K.., and Hakoshima, T. (2005).

"Expression, purification, crystallization and preliminary crystallographic analysis of human Rad GTPase." Acta Crystallogr. F, 61(Pt 11):978-980.

松下一信 1. H. Toyama, W. Soenphol, D. Moonmangmee, O. Adachi, K.

Matsushita: Molecular properties of membrane-bound FAD-containing D-sorbitol dehydrogenase from thermotolerant Gluconobacter frateurii isolated from Thailand. Biosci. Biotechnol. Biochem. 69, 1120-1129 (2005) No.6, June

2. K. Matsushita, T. Inoue, O. Adachi, H. Toyama: Acetobacter aceti

possesses a proton motive force-dependent efflux system for acetic acid. J. Bacteriol., 187, 4346-4352 (2005) No. 13, July

3. K. Matsushita, T. Inoue, G. Theeragool, J. Trcek, H. Toyama, O.

Adachi: Acetic acid production in acetic acid bacteria leading to their "death" and survival. In: Survival and Death in Bacteria, Yamada M (ed), Research Signpost, Kerala, India; pp. 169-181 (2005) ISBN: 81-7736-236-4

4. Toyama H., Chen Z.W., Fukumoto M., Adachi O., Matsushita K.,

Mathews F.S.: Molecular cloning and structural analysis of quinohemoprotein alcohol dehydrogenase ADH-IIG from Pseudomonas putida HK5. J Mol Biol. 352, 91-104 (2005) No. 1, Spt.

9th 5. J. Trcek, H. Toyama, J. Czuba, A. Misiewicz, and K. Matsushita:

Correlation between acetic acid resistance and characteristics of PQQ-dependent ADH in acetic acid bacteria. Appl. Microbiol. Biotechnol. (2005) Aug 17;:1-8 [Epub ahead of print] PMID: 16133326

6. A. Deeraksa, S. Moonmangmee, H. Toyama, M. Yamada, O. Adachi,

K. Matsushita: Characterization and spontaneous mutation of a novel gene, polE, involved in pellicle formation in Acetobacter tropicalis SKU1100. Microbiology 151, 4111-4120 (2005) Part 12, Dec

7. Islam MM, Goto M, Miyahara I, Ikushiro H, Hirotsu K, Hayashi H.

Binding of C5-dicarboxylic substrate to aspartate aminotransferase: implications for the conformational change at the transaldimination step. Biochemistry, 44(23), 8218-8229 (2005).

8. Goto M, Miyahara I, Hirotsu K, Conway M, Yennawar N, Islam MM,

Hutson SM. Structural determinants for branched-chain aminotransferase isozyme specific inhibition by the anticonvulsant drug gabapentin. J. Biol. Chem., 280(44), 37246-37256 (2005).

9. Goto M, Muramatsu H, Mihara H, Kurihara T, Esaki N, Omi R,

Miyahara I, Hirotsu K. Crystal structures of Delta1-piperideine-2-carboxylate/Delta1-pyrroline-2-carboxylate reductase belonging to a new family of NAD(P)H-dependent oxidoreductases: conformational change, substrate recognition, and stereochemistry of the reaction. J. Biol. Chem., 280(49), 40875-40884 (2005).

10. Muramatsu H, Mihara H, Goto M, Miyahara I, Hirotsu K, Kurihara T,

Esaki N. A new family of NAD(P)H-dependent oxidoreductases distinct from conventional Rossmann-fold proteins. J. Biosci. Bioeng. 99(6), 541-547 (2005).

石野良純 1. Nishida, H., Ishino, S., Miyata, T., Morikawa, K., Ishino, Y (2005)

Identification of the critical region in Replication factor C from Pyrococcus furiosus for the stable complex formation with proliferating cell nuclear antigen and DNA. Genes Genet. Syst. 80, 83-93.

2. Namba, K., Hagiwara, K., Tanaka, H., Nakaishi, Y., Chong, K.T.,

Yamashita, E., Armah, G.E., Ono, Y., Ishino, Y., Omura, T., Tsukihara, T., Nakagawa, A. (2005) Expression and molecular characterization of spherical particles derived from the genome of the hyperthermophilic euryarchaeote Pyrococcus furiosus. J Biochem. 138, 193-199.

3. Miyata, T., Suzuki, H., Oyama, T., Mayanagi, K., Ishino, Y., Morikawa,

K. (2005) Open clamp structure in the clamp-loading complex visualized by electron microscopic image analysis. Proc Natl Acad Sci U S A. 102, 13795-13800.

4. Nishida, H., Tsuchiya, D., Ishino, Y., Morikawa, K. (2005)

Overproduction, purification and crystallization of an archaeal DNA ligase from Pyrococcus furiosus. Acta Cryst. F61, 1100-1102.

5. Fujikane, R., Shinagawa, H., Ishino, Y. (2006) The archaeal Hjm

helicase has recQ-like functions, and may be involved in repair of stalled replication fork. Genes Cells. 11, 99-110.

6. Ishino, Y., Nishino, T., Morikawa, K. (2006) Mechanisms of

Maintaining Genetic Stability by Homologous Recombination. Chem Rev. 106, 324-339.

北田栄 1. Kitada, S., Abe, Y., Ito, A., Kuge, O., Akao, T., Mizuki, E., and Ohba

M. Molecular identification and cytocidal action of parasporin, a protein group of novel crystal toxins targeting human cells. In Biotechnology of Bacillus thuringiensis and Its Environmental Impact. Proceedings of the 6th Pacific Rim Conference. Victoria BC, Canada. Minireview, in press.

2. Abe, Y., Kitada S., Kuge, O., Ohba M., and Ito, A Oligomerization of

parasporin-2, a new crystal protein from non-insecticidal Bacillus

thuringiensis, in lipid rafts. In Biotechnology of Bacillus thuringiensis and Its Environmental Impact. Proceedings of the 6th Pacific Rim Conference. Victoria BC, Canada., in press.

藤木幸夫 1. Miyata, N., and Fujiki, Y.: Shuttling mechanism of peroxisome

targeting signal type 1 receptor, Pex5: ATP-independent import and ATP-dependent export. Mol. Cell. Biol. 25: 10822-10832 (2005).

2. Matsuzono, Y., and Fujiki, Y.: In vitro transport of membrane proteins

to peroxisomes by shuttling receptor Pex19p. J. Biol. Chem. 281: 36-42 (2006).

3. Furuki, S., Tamura, S., Matsumoto, N., Miyata, N., Moser, A., Moser,

H.W., and Fujiki, Y.: Mutations in the peroxin Pex26p responsible for peroxisome biogenesis disorders of complementation group 8 impair its stability, peroxisomal localization, and interaction with Pex1p-Pex6p complex. J. Biol. Chem. 281: 1317-1323 (2006).

4. Itoh, R., and Fujiki, Y.: Functional domains and dynamic assembly of

the peroxin Pex14p, the entry site of matrix proteins. J. Biol. Chem. 281: in press (2006).

5. Tanaka, A., Kobayashi, S., and Fujiki, Y.: Peroxisome division is

impaired in a CHO cell mutant with an inactivating point-mutation in dynamin-like protein 1 gene. Exp. Cell Res.: in press (2006).

池水信二 1. Araki-Sasaki, K., Ando, Y., Nakamura, M., Kitagawa, K., Ikemizu, S.,

Kawaji, T., Yamashita, T., Ueda, M., Hirano, K., Yamada, K., Matsumoto, K., Kinoshita, S., and Tanihara. H. (2005) "Lactoferrin Glu561Asp Facilitates Secondary Amyloidosis in the Cornea" British J. Ophthalmology. 89, 684-688

2. Sato, T., Ando, Y., Susuki, S., Mikami, F., Ikemizu, S., Nakamura, M.,

Suhr, O., Anraku, M., Kai, T., Suico. M.A., Shuto, T., Mizuguchi, M., Yamagata, Y., and Kai, H. (2006) "Chromium (III) ion and thyroxine cooperate to stabilize the transthyretin tetramer and suppress in vitro amyloid fibril formation." FEBS Letters 580, 491-496

佐藤和彦 1. Tomoki Nishino, Yasuhiro Kashino, Hiroyuki Koike and Kazuhiko

Satoh Involvement of NADH and peripheral NADH dehydrogenase in the cyclic electron flow in higher plants. In Photosynthesis: Fundamental Aspects to Global Perspectives, Allen Press, Edited by van der Est and D. Bruce (2005) 20-22.

2. Hiroyuki Koike, Masashi Taniguchi and Kazuhiko Satoh Functional

Analysis of psbX Deletion Mutant in Synechocystis sp. PCC6803. . In Photosynthesis: Fundamental Aspects to Global Perspective, Allen Press, Edited by van der Est and D. Bruce (2005) 267-269.

3. Yohei Ikeda, Kazuhiko Satoh and Yasuhiro Kashino Characterization

of photosystem I complexes purified from a diatom, Chaetoceros gracilis. In Photosynthesis: Fundamental Aspects to Global Perspective, Allen Press, Edited by van der Est and D. Bruce (2005) 38-40.

4. Junko Ooyabu, Masako Ohtuka, Yasuhiro Kashino, Kazuhiko Satoh

and Hiroyuki Koike Changes in cyclic electron transport pathway of Synechocystis 6803 under various growth conditions. In Photosynthesis: Fundamental Aspects to Global Perspective, Allen Press, Edited by van der Est and D. Bruce (2005) 18-20.

5. Natsuko Inoue-Kashino, Yasuhiro Kashino, Kazuhiko Satoh, Ichiro

Terashima, and Himadri B. Pakrasi. PsbU Provides a Stable Architecture for the Oxygen-Evolving System in Cyanobacterial Photosystem II. Biochemistry 44 (2005) 12214-12228

6. Akiko Ban, Shimpei Aikawa, Hiroshi Hattori, Hiroshi Sasaki, Makoto

Sampei, Sakae Kudoh, Mitsuo Fukuchi, Kazuhiko Satoh and Yasuhiro Kashino. Comparative analysis of photosynthetic properties in ice algae and phytoplankton inhabiting Franklin Bay, the Canadian Arctic, with those in mesophilic diatoms during CASES 03-04. Polar Bioscience 19 (2006) 11-28.

若林健之 1. K. Murakami, F. Yumoto, S. Ohki, T. Yasunaga, M. Tanokura & T.

Wakabayashi (2005):Structural basis for Ca2+-regulated muscle relaxation at interaction sites of troponin with actin and tropomyosin. J. Mol. Biol., 352, 178-201.

鳥越秀峰 1. Torigoe, H., Katayama, T., Obika, S., Maruyama, A., and Imanishi, T.,

Nucleosides, Nucleotides & Nucleic Acids 24, 635-638 (2005). 2. Torigoe, H., Kawahashi, K., Takamori, A., and Ono, A., Nucleosides,

Nucleotides & Nucleic Acids 24, 915-917 (2005). 3. Torigoe, H., Kawahashi, K., and Tamura, Y., Nucleosides, Nucleotides

& Nucleic Acids 24, 1019-1021 (2005). 4. Furukawa, A., and Torigoe, H., Nucleic Acids Symp. Ser. 49, 63-64

(2005). 5. Torigoe, H., Kozasa, T., Takamori, A., and Ono, A., Nucleic Acids

Symp. Ser. 49, 217-218 (2005). 6. Torigoe, H., and Tsukamoto, Y., Nucleic Acids Symp. Ser. 49, 321-322

(2005).