P U B L I C A T I O N (1)
updated on: 28-May-2017

(116) Orii, R., Sakamoto, N., Fukami, D., Tsuda, S., Izumi, M., Kajihara, Y., Okamoto, R.: Total synthesis of O-GalNAcylated antifreeze glycoprotein using the switchable reactivity of peptidyl-N-pivaloylguanidine. Chemistry -A European Journal, 23 (39), 9253-9257 (2017).

(115) Mahatabuddin, S., Hanada, Y., Nishimiya, Y., Miura, A., Kondo, H., Davies, P.L., and Tsuda, S. : Concentration-dependent oligomerization of an alpha-helical antifreeze polypeptide makes it hyperactive. Scientific Reports 7, 42501 (2017).

(114) Cheng, J., Hanada, Y., Miura, A., Tsuda, S., and Kondo, H.: Hydrophobic Ice-Binding Sites confer Hyperactivity of an Antifreeze Protein from a Snow Mold Fungus. Biochem. J. 473 (21), 4011-26 (2016).

(113) Tsuda, S.: Mass preparation of fish antifreeze protein. J. Bioprocess Biotechniq.6 (7), 30 (2016).

(112) Mahatabuddin S., Nishimiya, Y., Miura, A., Kondo, H., and Tsuda, S.: Critical Ice Shaping Concentration (CISC): A New Parameter to Evaluate the Activity of Antifreeze Proteins. Cryobiology and Cryotechnology 62 (2), 95-103 (2016).

(111) Arai, A., Cheng, J., Mahatabuddin, S., Kondo, H., and Tsuda, S.: Observation of Inhibitory Effect of Antifreeze Protein on Progressive Freeze-Concentration. Cryobiology and Cryotechnology 61 (2) 121-124 (2015).

(110) Ideta, A., Aoyagi, Y., Tsuchiya, K., Nakamura, K., Shirasawa, A., Sakaguchi, K., Tominaga, N., Nishimiya, Y., and Tsuda, S. : Prolonging hypothermic storage (4oC) of bovine embryos with fish antifreeze protein. J. Reprod. Dev., 61, 1-6 (2015).

(109) Hanada, Y., Nishimiya Y., Miura, A., Tsuda, S., and Kondo, H. : Hyperactive antifreeze protein from an Antarctic sea ice bacterium Colwellia sp. has a compound ice-binding site without repetitive sequences. FEBS J. 281 3576-3590 (2014).

(108) Xiao, N., Hanada, Y., Seki, H., Kondo, H., Tsuda, S., and Hoshino, T. : Annealing condition influences thermal hysteresis of fungal type ice-binding proteins. Cryobiology 68 159-161 (2014).

(107) Singh, P., Hanada, Y., Singh, S., and Tsuda, S. : Antifreeze protein activity in Arctic Cryoconite bacteria. FEMS Microbiol Lett. 351, 14-22 (2014).

(106) Sakaki, K., Cristov N., Tsuda, S., and Imai, R. : Identification of a novel LEA protein involved in freezing tolerance in wheat. Plant and Cell Physiology, 55 (1) 136-147 (2014).

(105) Basu, K., Garnham, C.P., Nishimiya, Y., Tsuda, S., Braslavsky, I., and Davies, P.L. : Determining the ice-binding planes of antifreeze proteins by fluorescence-based ice plane affinity. Journal of Visualized Experiments 83, e51185 (2014).

(104) Tsuchiya, K., Ideta, A., Nishimiya, Y., and Tsuda, S. and Aoyagi, Y. : Artificial dormancy of bovine embryos for a maximum of 7 days using a simple medium. Reproduction, Fertility and Development, 26 (1) 139-140 (2013).

(103) Fukami, D., Hanada, Y., Cheng, J., Tsuda, S., and Kondo, H. : Functional Analysis of Antifreeze Protein from Ascomycete. Cryobiology and Cryotechnology 59 (2) 157-160 (2013).

(102) Tsuda, S. : Antifreeze Proteins from Japanese organisms: Functional analyses for their general use. Cryobiology 67 (3), 415 (2013).

(101) Kamijima, T, Sakashita, M., Miura, A., Nishimiya, Y., and Tsuda, S. : Antifreeze Protein Prolongs the Life-Time of Insulinoma Cells during Hypothermic Preservation. PLoS ONE 8 (9), e73643 (2013).

(100) Tsuji, M., Fujiu, S., Xiao N, Hanada, Y., Kudoh, S., Kondo, H., Tsuda, S.,and Hoshino, T. : Cold adaptation of fungi obtained from soil and lake sediment in the Skarvsnes ice-free area, Antarctica. FEMS Microbiol Lett 346 121-130 (2013).

(99) Ideta, A., Aoyagi, Y., Tsuchiya, K., Kamijima, T., Nishimiya, Y., and Tsuda, S. : A simple medium enables bovine embryos to be held for seven days at 4 oC. Scientific Reports, 3 (1173) 1-5 (2013).

(98) Fukushima, M., Tsuda, S., and Nishizawa, Y.-I. : Fabrication of highly porous alumina prepared by gelation freezing route with antifreeze protein. J. Am. Ceram. Soc., 96 (4), 1029-1031 (2013).

(97) Kumeta, H., Ogura, K., Nishimiya, Y., Miura, A., Inagaki, F., and Tsuda, S. : A defective isoform and its activity-improved variant of a type III antifreeze protein from Zoarces elongatus Kner. J. Biomol. NMR, 55 (2), 225-230 (2013).

(96) Izumi, R., Matsushita, T., Ohyabu, N., Fujitani, N., Naruchi, K., Shimizu, H., Tsuda, S., Hinou, H., and Nishimura, S.-I. : Microwave-assisted solid-phase synthesis of antifreeze glycopeptides. Chem. Eur. J.,19, 3913-3920 (2013).

(95) Yamanouchi, T., Xiao, N., Hanada, Y., Kamijima, T., Sakashita, M., Nishimiya, Y., Miura, A., Kondo, H., and Tsuda, S. : Dependence of freeze-concentration inhibition on antifreeze protein. Low Temperature Science 71, 91-96 (2013).

(94) Kondo, H., Hanada, Y., and Tsuda, S. : Fungal Antifreeze Protein Consists of a Unique beta-Solenoid Structure. Photon Factory Activity Report, Part A, 58-59 (2012). ISSN 1344-6320.

(93) Tsuda, S. : Antifreeze proteins from Japanese fish. Journal of Japanese society for extremophiles 11 (2), 64-69 (2012).

(92) Garnham, C.P., Nishimiya, Y., Tsuda, S., and Davies, P.L. : Engineering a naturally inactive isoform of type III antifreeze protein into one that can stop the growth of ice. FEBS Letters, 586, 3876-3881 (2012).

(91) Sakashita, M. and Tsuda, S. : Function of antifreeze protein and its application to food industry. Food and Science, 54 (5), 15-18 (2012). ISSN 0037-4105.

(90) Kondo, H., Hanada, Y., Hoshino, T., Garnham, C.P., Davies, P.L., and Tsuda, S. : Ice-binding site of snow mold fungus antifreeze protein deviates from structural regularity and high conservation. Proc. Natl. Acad. Sci., 109 (24), 9360-9365 (2012).

(89) Sakashita, M., Nishimiya, Y., Kondo, H., and Tsuda, S. : Cold-adapted fishes and antifreeze proteins. Biological Science, 63 (4), 214-221 (2012).

(88) Kiga, A., Kurita, K., Nishimura, M., Higashi, K., Nakagawa, T., Kishi, M., Kamijima, T., Nishimiya, Y., Tsuda, S., Hosoi, Y., and Anzai, M. : Short term storage of Mouse epididymal spermatozoa by Antifreeze protein addeition at cold temperature. Mem. Inst. of Adv. Technol. (Kinki Univ.) 16, 51-58.

(87) Ishiwata, A., Sakurai, A., Nishimiya, Y., Tsuda, S., and Ito, Y. : Synthetic study and structural analysis of the antifreeze agent xylomannan from Upis ceramboides. J. Am. Chem. Soc., 133, 19524-19535 (2011).

(86) Kondo, H. and Tsuda, S. : Types of antifreeze protein and their activity in freeze inhibition. Refrigeration, 86 (1005), 557-561 (2011). ISSN 0453-073X.

(85) Nishimiya, Y. and Tsuda, S. : Technological developments utilizing antifreeze protein. Refrigeration, 86 (1005), 551-556 (2011). ISSN 0034-3714.

(84) Xiao, N., Suzuki, K., Nishimiya, Y., Kondo, H., Miura, A., Tsuda, S., and Hoshino, T. : Comparison of functional properties of two fungal antifreeze proteins from Antarctomyces psychrotrophicus and Typhula ishikariensis. FEBS J., 277, 394-403 (2010).

(83) Nishimiya, Y., Kondo, H., Sakashita, M., and Tsuda, S. : Antifreeze protein - their structure and function-. Chemistry and Science, 48 (6), 381-388 (2010). ISSN 0453-073X.

(82) Yaoi, K., Kondo, H., Hiyoshi, A., Noro, N., Sugimoto, H., Tsuda, S., and Miyazaki, K. : The crystal structure of a xyloglucan-specific endo-beta-1,4-glucanase from Geotrichum sp. M128 xyloglucanase reveals a key amino acid residue for substrate specificity. FEBS J., 276, 5094-5100 (2009).

(81) Hachisu, M., Hinou, H., Takamichi, M., Tsuda, S., Koshida, S., and Nishimura, S.-I.. : One-pot synthesisof cyclic antifreeze glycopeptides. Chem. Commun., 1641-1643 (2009).

(80) Takamichi, M., Nishimiya, Y., Miura, A., and Tsuda, S. : Fully active QAE isoform confers thermal hysteresis activity on a defective SP isoform of type III antifreeze protein. FEBS J., 276 1471-1479 (2009).

(79) Kodama, Y., Masaki, K., Kondo, H., Suzuki, M., Tsuda, S., Nagura, K., Shimba, N., Suzuki, E. and Iefuji, H. : Crystal Structure and Enhanced Activity of a Cutinase-like Enzyme from Cryptococcus sp. Strain S-2. Proteins, 77 (3), 710-717 (2009).

(78) Nishimiya, Y., Kondo, H., Sugimoto, H., Suzuki, M., Takamichi, M., Miura, A., and Tsuda, S. : Crystal Structure and Mutatiuonal Analysis of Ca2+-independent Type II Antifreeze Protein from Longsnout poacher, Brachyopsis rostatus. J. Mol. Biol., 382 (3), 734-746 (2008).

(77) Hirano, Y., Nishimiya, Y., Kowata, K., Mizutani, F., Tsuda, S., and Komatsu, Y. : Construction of Time-Lapse Scanning Electrochemical Microscopy with Temperature Control and Its Application to Evaluate the Preservation Effects of Antifreeze Proteins on Living Cells. Anal. Chem., 80, 9349-9354 (2008).

(76) Warashina, A., Hirano, Y., Takamichi, M., Nishimiya, Y., Kondo, H., and Tsuda, S. : Hypothermic preservation of cultured cells with using fish type III antifreeze protein from Notched-fin eelpout. Cryobiology and Cryotechnology, 54 (2). 93-96 (2008).

(75) Iwasaki, K., Kondo, H., Nishimiya, Y., Takamichi, M., Miura, A., and Tsuda, S. : Enhancement of the activity of antifreeze protein by addition of a water-soluble polymer. Cryobiology and Cryotechnology, 54 (2). 89-92 (2008).

(74) Hirano, Y., Nishimiya, Y., Matsumoto, S., Matsushita, M., Todo, S., Miura, A., Komatsu, Y., and Tsuda, S. : Hypothermic preservation effect on mammalian cells of type III antifreeze proteins from notched-fin eelpout. Cryobiology, 57, 46-51 (2008).

(73) Nishimiya, Y., Mie, Y., Hirano, Y., Kondo, H., Miura, A., and Tsuda, S. : Mass preparation and technological development of an antifreeze protein - Toward a practical use of biomolecules - Synthesiology, 1 (1), 7-14 (2008).

(72) Yasui, M., Takamichi, M., Miura, A., Nishimiya, Y., Kondo, H., and Tsuda, S. : Hydroxyl groups of threonines contribute to the activity of Ca2+-dependent type II antifreeze protein. Cryobiology and Cryotechnology, 54 (1). 1-8 (2008).

(71) Takamichi, M., Nishimiya, Y., Miura, A., and Tsuda, S. : Effect of annealing time of an ice crystal on the activity of type III antifreeze protein. FEBS J., 274, 6469-6476 (2007).

(70) Matsumoto, S., Matsushita, M., Nishimiya, Y., Hirano, Y., Tsuda, S. and Todo, S. : Type III antifreeze protein extremely enhances viability of cultured endothelial cells during hypothermic preservation. Am. J. Transplant, 7, 506 (2007).

(69) Yaoi, K., Kondo, H., Hiyoshi, A., Noro, N., Sugimoto, H., Tsuda, S., Mitsuishi, Y., and Miyazaki, K. : The Structural Basis for the Exo-mode of Action in GH74 Oligoxyloglucan Reducing End-speicific Cellobiohydrolase.  J. Mol. Biol., 370, 53-62 (2007).

(68) Uchida, T., Ikeda, I.Y., Ohmura, R., and Tsuda, S. : Effects of additives on formation rates of CO2 hydrate Films. Proceedings of 11th International Conference of Physical Chemistry of Ice, 609-618 (2007).

(67) Holland, N.B., Nishimiya, Y., Tsuda, S., and Sonnichsen, F.D. : Activity of a Two-domain Antifreeze Protein is Not Dependent on Linker Sequence. Biophys. J., 46, 11-22 (2007).

(66) Nishimiya, Y., Kondo, H., Yasui, M., Sugimoto, H., Noro, N., Sato, R., Suzuki, M., Miura, A., and Tsuda, S. : Crystallization and preliminary X-ray crystallographic analysis of Ca2+-independent and Ca2+-dependent species of the type II antifreeze protein.  Acta Crystallographica., F62, 538-541 (2006).

(65) Tsuda, S., Miura, A., and Nishimiya, Y. : Antifreeze protein from Japanese fish. Koubunshi, 55 (7), 494-495 (2006).

(64) Miyazaki, K., Takenouchi M., Kondo, H., Noro, N., Suzuki, M., and Tsuda, S. : Thermal Stabilization of Bacillus Subtilis Family-11 Xylanase by Directed Evolution.  J. Biol. Chem., 281, 10236-10242 (2006).

(63) Kobashigawa, Y., Nishimiya, Y., Miura, K., Ohgiya, S., Miura, A., and Tsuda, S. : A part of ice nucleation protein exhibits the ice-binding ability. FEBS Letters., 579 (6), 1493-1497 (2005).

(62) Nishimiya, Y., Sato, R., Takamichi, M., Miura, A., and Tsuda, S. : Co-operative effect of the isoforms of type III antifreeze protein expressed in Notched-fin eelpout, Zoarces elongatus Kner. FEBS J. (Eur. J. Biochem.), 272, 482-492 (2005).

(61) Yaoi, K., Kondo, H., Noro, N., Suzuki, M., Tsuda, S., and Mitsuishi, Y. : Tandem Repeat of a Seven-Bladed beta-Propeller Domain in Oligoxyloglucan Reducing-End-Specific Cellobiohydrolase. Structure, 12 (7), 1209-1217 (2004).

(60) Tachibana, Y., Fletcher, G.L., Fujitani, N., Tsuda, S., Monde, K., and Nishimura, S.-I.: Antifreeze Glycoproteins: Elucidation of the Structural Motifs That Are Essential for Antifreeeze Activity. Angew. Chem. Int. Ed., 43, 856-862 (2004).

(59) Yaoi, K., Kondo, H., Suzuki, M., Noro, N., Tsuda, S., and Mitsuishi, Y. : A novel xyloglucan-specific glycosidase, olygoxyloglucan reducing end-specific cellobiohydrolase. Biotech. Lignocel. Degrade Utilization (UNI Publishers, Co. Ltd.) (2004).

(58) Tanaka, S., Kobashigawa, Y., Miura, K., Nishimiya, Y., Miura, A., and Tsuda, S. : Antifreeze protein. Seibutsubutsuri, 43 (3), 130-135 (2003).

(57) Hoshino, T., Kiriaki, M., Ohgiya, S., Fujiwara, M., Kondo, H., Nishimiya, Y., Yumoto, I., and Tsuda, S. : Antifreeze proteins from snow mold fungi. Can J. Bot., 81, 1175-1181 (2003).

(56) Nishimiya, Y., Ohgiya, S., and Tsuda, S. : Artificial Multimers of The Type III Antifreeze Protein: Effects on Thermal Hysteresis and Ice Crystal Morphology. J. Biol. Chem., 278 (34), 32307-32312 (2003).

(55) Yaoi, K., Kondo, H., Suzuki, M., Noro, N., Tsuda, S., and Mitsuishi, Y. : Crystallization and Preliminary X-Ray Crystallographic Study on Xyloglucan-Specific exo-beta-glycosidase, oligoxyloglucan reducing-end specific cellobiohydrolase. Acta Crystal., D59, 1838-1839 (2003).

(54) Yamashita, Y., Miura, R., Takemoto, Y., Tsuda, S., Kawahara, H., and Obata, H. : Type II Antifreeze Protein from a Mid-Latitude Freshwater Fish, Japanese Smelt (Hypomesus nipponesis). Biosci. Biotech. Biochem., 67 (3), 461-466 (2003).

(53) Kumeta, H., Miura, A., Kobashigawa, Y., Miura, K., Oka, C., Nemoto, N., Nitta, K., and Tsuda, S : Low-Temperature-Induced Structural Changes in Human Lysozyme Elucidated by Three-Dimensional NMR Spectroscopy. Biochemistry, 42 (5), 1209-1216 (2003).

(52) Tachibana, Y., Matsubara, N., Nakajima, F., Tsuda, T., Tsuda, S., Monde, K., and Nishimura, S-I. : Efficient and versatile synthesis of mucin-like glycoprotein mimics. Tetrahedron, 58, 10213-10224 (2002).

(51) Koike, M., Okamoto, T., Tsuda, S., and Imai, R. : A novel plant defensin-like gene of winter wheat is specifically induced during cold acclimation. Biochecm. Biophys. Res. Commun., 298, 46-53 (2002).

(50) Suetake, T., Aizawa, T., Koganesawa, N., Osaki, T., Kobashigawa, Y., Demura, M., Kawabata, S., Kawano, K., Tsuda, S., and Nitta, K. : Production and Characterization of Recombinant tachycitin, the Cys-rich chitin-binding protein. Protein Engineering, 15 (9), 763-769 (2002).

(49) Kawasaki, K., Kondo, H., Suzuki, M., Ohgiya, S., and Tsuda, S. : Alternate conformations observed in catalytic serine of Bacillus subtilis lipase determined at 1.3 angstrome resolution. Acta Cryst., D58, 1168-1174 (2002).

(48) Kumeta, H., Kobashigawa, Y., Miura, K., Nishimiya, Y., Oka, C., Nemoto, N., Miura, A., Nitta, K., and Tsuda, S : Assignment of 1H, 13C, and 15N resonances of human lysozyme at 4oC. J. Biomol. NMR, 22 (3), 183-184 (2002).

(47) Uedaira Hisashi, Okouchi S., Tsuda, S., and Uedaira Hatsuho. : Hydration of Glucose and Galactose Derivatives. Bull. Chem. Soc. Jpn., 74, 1857-1861 (2001).

(46) Kobashigawa, Y., Miura, K., Demura, M., Nemoto, N., Koshiba, T., Nitta, K., and Tsuda, S. : Assignment of 1H, 13C, and 15N resonances of canine milk lysozyme. J. Biomol. NMR, 19 (4), 387-388 (2001).

(45) Miura, K., Ohgiya, S., Hoshino, T., Nemoto, N., Suetake, T., Miura, A., Spyracopoulos, L., and Tsuda, S. : NMR Analysis of Type III Antifreeze Protein Intramolecular Dimer: Structural Basis for Enhanced Activity. J. Biol. Chem., 276 (2), 1304-1310 (2001).

(44) Miura, K., Ohgiya, S., Hoshino, T., Nemoto, N., Nitta, K., and Tsuda, S. : Assignments of 1H, 13C, and 15N NMR resonances of intramolecular dimer antifreeze protein RD3. J. Biomol. NMR, 16, 273-274 (2000).

(43) Odaira, M., Hoshino, T., Yoshida, M., Jin S., Tsuda, S., Ohgiya, S., and Ishizaki, K. : p-Coumaric Acid from Wheat Inactivates Ice-Nucleating Activity by Ice-Nucleating Bacterium. Plant Cell Physiology, 41, s50 (2000).

(42) Suetake, T., Tsuda, S., Kawabata, S., Kawano, K., Miura, K., Iwanaga, S., Hikichi, K., and Nitta, K. : Chitin-binding Proteins in Invertebrates and Plants Comprise a Common Chitin-binding Structural Motif. J. Biol. Chem., 275 (24), 17929-17932 (2000).

(41) Hoshino, T., Odaira, T., Yoshida, M., and Tsuda, S. : Physiological and biochemical significance of antifreeze substances in plants. J. Plant Res., 112, 255-261 (1999).

(40) Miura, K., Ohgiya, S., Hoshino, T., Nemoto, N., Nitta, K., and Tsuda, S. : Determination of the solution structure of the N-domain plus linker of antarctic eel pout antifreeze protein RD3. J. Biochem., 126, 387-394 (1999).

(39) Tsuda, S., Miura, A., Gagne, S.M., Spyracopoulos, L., and Sykes, B.D. : Low-Temperature-Induced Structural Changes in The Apo Regulatory Domain of Skeletal Muscle Troponin C. Biochemistry, 38 (18), 5693-5700 (1999).

(38) Suetake, T., Tsuda, S., Kawabata, S., Kawano, K., Miura, K., Hikichi, K., and Nitta, K. : Three-Dimensional Structure of Tachycitin in Solution Determined by 1H NMR. Rept. Progr. Polym. Phys. Jpn. 41, 67-69 (1998).

(37) Gagne, S.M., Tsuda, S., Spyracopoulos, L., Kay, L.E., and Sykes, B.D. : Backbone and Methyl Dynamics of the Regulatory Domain of Troponin C: Anisotropic Rotational Diffusion and Contribution of Conformational Entropy to Calcium Affinity. J. Mol. Biol., 278, 667-686 (1998).

(36) Miura, K., Ohgiya, S., Hoshino, T., Nemoto, N., Hikichi, K., and Tsuda, S. : Solution Structure of the N-domain with A Linker Portion of Antarctic Eel Pout Antifreeze Protein RD3. Rept. Progr. Polym. Phys. Jpn. 41, 71-74 (1998).

(35) Tsuda, S., Ito, A., and Matsushima, N. : A hairpin-loop conformation in tandem repeat sequence of the ice nucleation protein revealed by NMR spectroscopy. FEBS Letters, 409, 227-231 (1997).

(34) John, G., Tsuda, S., and Morita, M. : Synthesis and Modification of New Biodegradable Co-polymers: Serine/Glycolic acid Alternating Polymer abd Copolymers of L-Lactide or e-Caprolactone. J. Polym. Sci., A62, 1901-1907 (1997).

(33) Service R.F. : Flexing Muscle With Just One Amino Acid, Science, 271, 31. (1996). *Interview News

(32) Ohki, S., Miura, K., Saito, M., Nakashima, K., Maekawa, H., Yazawa, M., Tsuda, S., and Hikichi, K. : Secondary Structure and Ca2+-Binding Property of the N-Terminal Half Domain of Calmodulin from Yeast Saccaromyces cerevisiae as Studied by NMR. J. Biochem., 119, 1045-1055 (1996).

(31) Tsuda, S. : Modern NMR spectroscopy and X-ray crystallography: a different approach to study the structure and its function of a protein. Nihon Kessho Gakkaishi, 38 (1), 84-88 (1996).

(30) Sykes, B.D., Audette, G., Gagne, S.M., Li, M.X., Slupsky, C.M., and Tsuda, S. : NMR Studies of the Calcium-Induced Structural lChanges that Triggers Muscle Contraction. Proceedings of 34th. Hanford Symposium on Health and the Environment, "Biomolecules: From 3-D Structure to Applications"(ed. Ornstein, R.L.) pp. 11-19, Pasco, Washington (1995).

(29) Tsuda, S., Aimoto, S., and Hikichi, K. : Interaction between Troponin-C and Inhibitory Region Peptide of Troponin-I as Studied by 1H-NMR. Rept. Progr. Polym. Phys. Jpn. 35, 583-584 (1995).

(28) Miura, K., Saito, M., Ohki, S., Tsuda, S., Nakashima, K., Yazawa, M., and Hikichi, K. : Secondary Structure of N-Terminal-Half Domain of Yeast Calmodulin in the Presence of Ca2+ as Studied by 1H-NMR. Rept. Progr. Polym. Phys. Jpn. 38, 501-502 (1995).

(27) Gagne, S.M., Tsuda, S., Li, M.X., Smillie, L.B., and Sykes, B.D. : Structures of the troponinC regulatory domains in the apo and calcium-saturated states. Nature Struct. Biol., 2, 784-789 (1995).

(26) Li, M.X., Gagne, S.M., Tsuda, S., Kay, C.M., Smillie, L.B., and Sykes, B.D. : Calcium Binding to the Regulatory N-Domain of Skeletal Muscle Troponin C Occurs in a Stepwise manner. Biochemistry, 34, 8330-8440 (1995).

(25) Tsuda, S., Matsuda, S., Izumi, Y., Hikichi, K., and Matsushima, N. : Structural Features of Bovine Brain S100b as Studied by 1H-NMR Spectroscopy. Rept. Progr. Polym. Phys. Jpn. 38, 509-510 (1995).

(24) Gagne, S.M., Tsuda, S., Li, M.X., Chandra, M., Smillie, L.B., and Sykes, B.D. : Quantification of the calcium-induced secondary structural changes in the regulatory domain of troponin-C. Protein Sci., 3, 1961-1974 (1994).

(23) Hojo, H., Kwon, Y., Kakuta, Y., Tsuda, S., Tanaka, I., Hikichi, K., and Aimoto, S. : Development of a Linker with an Enhanced Stability for the Preparation of a Peptide Thioesters and Its Application to the Systhesis of a Stable-Isotope-Labeled HU-Type DNA-Binding Protein. Bull. Chem. Soc. Jpn., 66, 2700-2706 (1993).

(22) Nishihira, J., Ishibashi, T., Sakai, M., Tsuda, S., and Hikichi, K. : Identification of the Hydrophobic Ligand-Binding Region in Recombinant Glutathione S-Transferase P and Its Binding Effect on the Conformational State of the Enzyme. Arch. Biochem. Biophys., 302, 128-133 (1993).

(21) Nishihira, J., Ishibashi, T., Sakai, M., Nishi, S., Kumazaki, T., Hatanaka, Y., Tsuda, S., and Hikichi, K. : Characterization of Cystein Residues of Glutathione S-Transferase P: Evidence For Steric Hindrance of Substrate Binding by A Bulky Adduct to Cystein 47. Biochem. Biophys. Res. Commun., 188, 424-432 (1992).

(20) Moriyasu, M., Ohki, S., Tsuda, S., and Hikichi, K. : The Ca2+-Binding Property of Carp Parvalbumin 5a as Studied by 1H-NMR Spectroscopy. Rept. Progr. Polym. Phys. Jpn. 35, 579-580 (1992).

(19) Tsuda, S., Aimoto, S., and Hikichi, K. : 1H-NMR Study of Ca2+- and Mg2+-Dependent Interaction between Troponin C and Troponin I Inhibitory Peptide (96-116). J. Biochem., 112, 665-670 (1992).

(18) Tsuda, S. and Hikichi, K. : 1H-NMR study of rabbit skeletal muscle troponin C: Ca2+-dependent interaction with mastoparan. Biophys. Biochim. Acta, 1121, 213-220 (1992).

(17) Ohki, S., Tsuda, S., Joko, S., Yazawa, M., Yagi, K., and Hikichi, K. : 1H-NMR Study on Amide Proton Exchange of Calmodulin-Mastoparan Complex. J. Biochem., 109, 234-237 (1991).

(16) Tsuda, S., Niki, R., Kuwata, T., Tanaka, I., and Hikichi, K. : 1H-NMR Study of Casein Phosphopeptide (1-25): Assignment and Conformation. Magn. Reson. Chem., 28, 1097-1102 (1991).

(15) Kumaki, Y., Tsuda, S., Hikichi, K., Hojo, H., Aimoto, S., and Matsushima, N. : Two-Dimensional NMR Studies of the synthetic repeat pentapeptide. Rept. Progr. Polym. Phys. Jpn. 34, 475-478 (1991).

(14) Tsuda, S., Kakita, S., and Hikichi, K. : Analysis of Ca2+-binding to Troponin-C as Studied by 1H-NMR. Rept. Progr. Polym. Phys. Jpn. 34, 461-462 (1991).

(13) Sasaki, T., Iwai, S., Tsuda, S., Hikichi, K., and Ohtsuka, E. : Chemical synthesis of oligoribonucletides for structural studies. Nucleic Acids Research, 22, 43-44 (1990).

(12) Tsuda, S., Sasaki, T., Ohtsuka, E., and Hikichi, K. : 1H-NMR Spectral Assignment of RNA HexamerGGICCC. Rept. Progr. Polym. Phys. Jpn. 33, 583-584 (1990).

(11) Tsuda, S., Ogura, K., Hasegawa, Y., Yagi, K., and Hikichi, K. : 1H NMR Study of Rabbit Skeletal Muscle Troponin C: Mg2+-Induced Conformational Change. Biochemistry, 29, 4951-4958 (1990).

(10) Tsuda, S., Hasegawa, Y., Yoshida, M., Yagi, K., and Hikichi, K. : Interaction between mastoparan and Troponin-C as Studied by Nuclear Magnetic Resonance. Rept. Progr. Polym. Phys. Jpn. 32, 583-584 (1990).

(9) Tsuda, S., Yazawa, M., Yagi, K., and Hikichi, K. : Interaction between mastoparan and Troponin-C as Studied by Nuclear Magnetic Resonance. Rept. Progr. Polym. Phys. Jpn. 32, 583-584 (1990).

(8) Uedaira, H., Ishimura, M., Tsuda, S., and Uedaira, H. : Hydration of Oligosaccharides. Bull. Chem. Soc. Jpn., 63, 3376-3379 (1990).

(7) Tsuda, S., Yazawa, M., Yagi, K., and Hikichi, K. : Interaction between mastoparan and Troponin-C as Studied by Nuclear Magnetic Resonance. Rept. Progr. Polym. Phys. Jpn. 32, 583-584 (1990).

(6) Takegoshi, K., Tsuda, S., and Hikichi, K. : Practical Implementation of the Self-Refocused 1331 Solvent Suppression. J. Magn. Reson., 89, 399-405 (1990).

(5) Yamazaki, Y., Tsuda, S., Yagi, K., and Hikichi, K. : A 1H-NMR Study on Hydrogen Exchange of Rabbit Skeletal Muscle Troponin-C. Rept. Progr. Polym. Phys. Jpn. 32, 531-532 (1989).

(4) Takegoshi, K., Tsuda, S., and Hikichi, K. : Self-Refocused Binominal Pulse Sequence for Solvent Suppression. J. Magn. Reson., 85, 198-202 (1989).

(3) Tsuda, S., Ogura, K., Hasegawa, Y., Yagi, K., and Hikichi, K. : Magnesium Binding to the Low Affinity Calcium Sites of Troponin C as determined by Nuclear Magnetic Resonance. Rept. Progr. Polym. Phys. Jpn. 31, 565-566 (1988).

(2) Tsuda, S., Hasegawa, Y., Yoshida, M., Yagi, K., and Hikichi, K. : Nuclear Magnetic Resonance Study on Rabbit Skeletal Troponin C: Calcium-Induced Conformational Change. Biochemistry, 27, 4120-4126 (1988).

(1) Tsuda, S., Ikura, M., Hasegawa, Y., Yoshida, M., Yagi, K., and Hikichi, K. : The Interaction between the N and C-terminal Domains of Troponin-C. Rept. Progr. Polym. Phys. Jpn. 30, 673-674 (1987).

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