Achievements

Biomolecular Engineering Research Group

Recent publications

2023

  1. Akiyama, K., Okabe, H., Motomura, T., Matsuda N. and Mie, Y.: Efficacy of AuNP film electrode fabricated with surfactant-free solution for direct electron transfer control of redox protein. Electrochem. Commun., inpress. DOI:10.2139/ssrn.4643727. (2023).
  2. Shiraki, Y., Mitsuma, M., Takada, R., Hata, S., Kitamura, A., Takada, S., Kinjo, M., Taru, H., Müller, U.C., Yamamoto, T., Sobu, Y. and Suzuki, T.: Axonal transport of Frizzled5 by Alcadein α-containing vesicles is associated with kinesin-1. Mol. Biol. Cell, 34, 11, ar110. DOI:10.1091/mbc.E22-10-0495. (2023).
  3. Hata, S., Saito, H., Kakiuchi, T., Fukumoto, D., Yamamoto, S., Kasuga, K., Kimura, A., Moteki, K., Abe, R., Adachi, S., Kinoshita, S., Kumagaye, K.Y., Nishio, H., Saito, T., Saido, T.C., Yamamoto, T., Nishimura, M., Taru, H., Sobu, Y., Ohba, H., Nishiyama, S., Harada, H., Ikeuchi, T., Tsukada, H., Ouchi, Y. and Suzuki, T.: Brain p3-Alcβ peptide restores neuronal viability impaired by Alzheimer’s amyloid β-peptide. EMBO Mol Med, 15, 5. DOI:10.15252/emmm.202217052. (2023).
  4. Honda, K., Saito, Y., Saito, H., Toyoda, M., Abe, R., Saito, T., Saido, T.C., Michikawa, M., Taru, H., Sobu, Y., Hata, S., Nakaya, T. and Suzuki, T.: Accumulation of amyloid-β in the brain of mouse models of Alzheimer’s disease is modified by altered gene expression in the presence of human apoE isoforms during aging, Neurobiol. Aging, 123, 63. DOI:10.1016/j.neurobiolaging.2022.12.003. (2023).
  5. Nishimiya, Y., Morita, Y., Wu, C., Ohyama, Y., Tochigi, Y., Okuzawa, T., Sakashita, M., Asakawa, A., Irie, T., Ohmiya, Y., Ohgiya, S. and Morita, N.: Molecular evolution of Cypridina noctiluca secretory luciferase for production of spectrum-shifted luminescence-emitting mutants and their application in nuclear receptor–reporter assays, Photochem. Photobiol., . DOI:10.1111/php.13857. (2023).

  1. Suzuki, T., Sobu, Y. and Hata, S.: γ-Secretase structure and activity are modified by alterations in its membrane localization and ambient environment, J. Biol. Chem., 171, 253. DOI:10.1093/jb/mvab132. (2022).
  2. Doi, M., Morita, N., Okuzawa, T., Ohgiya, S., Okamoto, D., Sato, K., Ito, Y., Matsuura, H. and Hashidoko, Y.: Pinellic Acid Isolated from Quercetin-rich Onions has a Peroxisome Proliferator-Activated Receptor-Alpha/Gamma (PPAR-α/γ) Transactivation Activity. Planta Med., 88, 440. DOI:10.1055/a-1345-9471. (2022).
  3. Mie, Y., Okabe, H., Mikami, C., Motomura, T. and Matsuda, N.: Nanostructured gold thin film electrode derived from surfactant-free gold nanoparticles for enhancement in electrocatalysis. Electrochem. Commun., 16, 107415. DOI:10.1016/j.elecom.2022.107415. (2023).
  4. Hirano, Y., and Komatsu, Y.: Promotion of cytoplasmic localization of oligonucleotides by connecting cross-linked duplexes. RSC Adv., 12, 24471. DOI:10.1039/D2RA04375K. (2022).
  5. Abdelhady, A. M., Hirano, Y., Onizuka, K., Okamura, H., Komatsu, Y., and Nagatsugi, F.: Synthesis of Crosslinked 2′-OMe RNA Duplexes Using 2-Amino-6-Vinylpurine and Their Application for Effective Inhibition of miRNA Function. Current Protocols. 2 e386. DOI:10.1002/cpz1.386. (2022)

2021

  1. Hata, S., Kano, K., Kikuchi, K., Kinoshita, S., Sobu, Y., Saito, H., Saito, T., Saido, T.C., Sano, Y., Taru, H., Aoki, J., Komano, H., Tomita, T., Natori, S. and Suzuki, T.: Suppression of amyloid-β secretion from neurons by cis-9, trans-11-octadecadienoic acid, an isomer of conjugated linoleic acid, J. Neurochem, 159, 603. DOI:10.1111/jnc.15490. (2021).
  2. Shiraki, Y., Mitsuma, M., Takada, R., Hata, S., Kitamura, A., Takada, S., Kinjo, M., Taru, H., Müller, U.M., Yamamoto, T., Sobu, Y. and Suzuki, T.: Extracellular Release of ILEI/FAM3C and Amyloid-β Is Associated with the Activation of Distinct Synapse Subpopulations, J. Alzheimer’s Dis., 34, 11. DOI:10.3233/JAD-201174. (2021).
  3. Haga, S., Kanno, A., Morita, N., Jin, A., Matoba, K., Ozawa, T., and Ozaki, M.: Poly(ADP-ribose) polymerase (PARP) is critically involved in liver ischemia/reperfusion-injury, J. Surg. Res., 270, 124. DOI:10.1016/j.jss.2021.09.008. (2021).
  4. Mie Y., Katagai, S. and Mikami, C.: Electrochemical Molecular Conversion of α-Keto Acid to Amino Acid at a Low Overpotential Using a Nanoporous Gold Catalyst. Int. J. Mol. Sci., 22, 9442. DOI:10.3390/ijms22179442. (2021).
  5. Abdelhady, A. M., Hirano, Y., Onizuka, K., Okamura, H., Komatsu, Y., and Nagatsugi, F.: Synthesis of crosslinked 2′-OMe RNA duplexes and their application for effective inhibition of miRNA function. Bioorganic and Medicinal Chemistry Letters. 48, 128257. DOI:10.1016/j.bmcl.2021.128257. (2021)
  6. Khan, N.M.M.U., Arai, T., Tsuda, S., and Kondo, H.: Characterization of microbial antifreeze protein with intermediate activity suggests that a bound-water network is essential for hyperactivity. Scientific Reports 11, 5971. DOI:10.1038/s41598-021-85559-x. (2021).
  7. Arai T., Yamauchi, A., Miura, A., Kondo, H., Nishimiya Y., Sasaki, Y.C., and Tsuda, S.: Discovery of Hyperactive Antifreeze Protein from Phylogenetically Distant Beetles Questions Its Evolutionary Origin. Int. J. Mol. Sci. 22, 3637. DOI:10.3390/ijms22073637. (2021).
  8. Okumura, S., Hirano, Y., and Komatsu, Y.: Stable duplex-linked antisense targeting miR-148a inhibits breast cancer cell proliferation. SCI REP. 11(1), 11467. doi:10.1038/s41598-021-90972-3 (2021).

2020

  1. Kakuda, N., Yamaguchi, H., Akazawa, K., Hata, S., Suzuki, T., Hatsuta, H., Murayama, S., Satoru, Funamoto, S. and Ihara, Y.: γ-Secretase Activity Is Associated with Braak Senile Plaque Stages, Am. J. Pathol., 109, 1323. DOI:10.1016/j.ajpath.2020.02.009. (2020).
  2. Gotoh, N., Saito, Y., Hata, S., Saito, H., Ojima, D., Murayama, C., Shigeta, M., Abe, T., Konno, D., Matsuzaki, F., Suzuki, T. and Yamamoto, T.: Amyloidogenic processing of amyloid β protein precursor (APP) is enhanced in the brains of alcadein α–deficient mice, J. Biol. Chem. 295, 9650. DOI:10.1074/jbc.RA119.012386. (2020).
  3. Umeno A., Sakashita, M., Sugino, S., Murotomi, K., Okuzawa, T., Morita, N., Tomii, K., Tsuchiya, Y., Yamasaki, K., Horie, M., Takahara, K., and Yoshida, Y.: Comprehensive analysis of PPARγ agonist activities of stereo-, regio-, and enantio-isomers of hydroxyoctadecadienoic acids, Biosci. Rep., 40, (4). DOI:10.1042/BSR20193767. (2020).
  4. Mie, Y., Katagai, S. and Ikegami, M.: Electrochemical Oxidation of Monosaccharides at Nanoporous Gold with Controlled Atomic Surface Orientation and Non-Enzymatic Galactose Sensing, Sensors 20 (19), 5632. doi:10.3390/s20195632 (2020).
  5. Mie, Y., Takayama, H. and Hirano, Y.:, Facile Control of Surface Crystallographic Orientation of Anodized Nanoporous Gold Catalyst and its Application for Highly Efficient Hydrogen Evolution Reaction, J. Catal., 389, 476-482. doi:doi.org/10.1016/j.jcat.2020.06.023 (2020).
  6. Mie, Y., Takahashi, K., Torii, R., Jingkai, S., Tanaka, T., Sueyoshi, K., Tsujino, H. and Yamashita, T.: Redox State Control of Human Cytoglobin by Direct Electrochemical Method to Investigate its Function in Molecular Basis.Chem. Pharm. Bull., 68, 806-809. doi:10.1248/cpb.c20-00175 (2020).
  7. Mie, Y., Yasutake, Y., Takayama, H. and Tamura, T.: Electrochemically boosted cytochrome P450 reaction that efficiently produces 25-hydroxyvitamin D-3. Journal of Catalysis 384, 30-36. doi:10.1016/j.jcat.2020.02.012 (2020).
  8. Mie, Y., Takahashi, K., Itoga, Y., Sueyoshi, K., Tsujino, H. and Yamashita, T.: Nanoporous gold based electrodes for electrochemical studies of human neuroglobin. Electrochemistry Communications 110. doi:10.1016/j.elecom.2019.106621 (2020).
  9. Yamauchi, A., Arai, T., Kondo, H., Sasaki, Y.C., and Tsuda, S.: An ice-binding protein from an Antarctic ascomycete is fine-tuned to bind to specific water molecules located in the prism planes. Biomolecules 10 (5), 759. doi:10.3390/biom10050759 (2020).
  10. Tsuda, S., Yamauchi, A., Khan, U. N.M.-M., Arai, T., Mahabuddin, S., Miura, A., and Kondo, H.: Fish-derived antifreeze proteins and antifreeze glycoprotein exhibit a different ice-binding property with increasing concentration. Biomolecules 10 (3), 423. doi:10.3390/biom10030423 (2020).

2019

  1. Hata, S., Hu, A., Piao, Y., Nakaya, T., Taru, H., Kawashima, M.M., Murayama, S., Nishimura, M. and Suzuki, T.: Enhanced amyloid-β generation by γ-secretase complex in DRM microdomains with reduced cholesterol levels, Hum. Mol. Genet., 29, 382. DOI:10.1093/hmg/ddz297. (2019)
  2. Kato, S., Tobe, H., Matsubara, H., Sawada, M., Sasaki, Y., Fukiya, S., Morita, N., and Yokota, A.: The membrane phospholipid cardiolipin plays a pivotal role in bile acid adaptation by Lactobacillus gasseri JCM1131T. Biochim Biophys Acta Mol Cell Biol Lipids, 1864, 403. DOI:10.1016/j.bbalip.2018.06.004. (2019).
  3. Makino, M., Sahara, T., Morita, N. and Ueno, H.: Carboxypeptidase Y activity and maintenance is modulated by a large helical structure. FEBS Open Bio, 9, (7), 1337. DOI:10.1002/2211-5463.12686. (2019).
  4. Haga, S., Yimin, Yamaki, H., Jin, S., Sogon, T., Morita, N. and Ozaki, M.: Extracts of bilberry (Vaccinium myrtillus L.) fruits improve liver steatosis and injury in mice by preventing lipid accumulation and cell death. Biosci. Biotechnol. Biochem., 83, (11), 2110. DOI:10.1080/09168451.2019.1634514. (2019).
  5. Arai, T., Nishimiya, Y., Ohyama, Y., Kondo, H., and Tsuda, S.: Calcium-Binding Generates the Semi-Clathrate Waters on a Type II Antifreeze Protein to Adsorb onto an Ice Crystal Surface. Biomolecules, 9, 162. DOI:10.3390/biom9050162. (2019).
  6. Arai, T., Fukami, D., Hoshino, T., Kondo, H., and Tsuda, S.: Ice‐binding proteins from the fungus Antarctomyces psychrotrophicus possibly originate from two different bacteria through horizontal gene transfer. FEBS J., 286, 946. DOI:10.1111/febs.14725. (2019).
  7. Rahman, A., Arai T., Yamauchi, A., Miura A., Kondo, H., Ohyama, Y., and Tsuda, S.: Ice recrystallization is strongly inhibited when antifreeze proteins bind to multiple ice planes. Sci. Rep., 9, 2212. DOI:10.1038/s41598-018-36546-2. (2019).
  8. Aohara, T., Furukawa J., Miura, K., Tsuda, S., Poisson J.S., Ben R.N., Wilson P.W., and Satoh S.: Presence of a basic secretory protein in xylem sap and shoots of poplar in winter and its physicochemical activities against winter environmental conditions. J. Plant Res., 132, 655. doi:10.1007/s10265-019-01123-9 (2019).
  9. Kuramochi, M., Takanashi, C., Yamauchi, A., Doi, M., Mio, K., Tsuda, S., and Sasaki, Y.: Expression of ice-binding proteins in Caenorhabditis elegans improves the survival rate upon cold shock and during freezing. Scientific Reports, 9, 6246. doi:10.1038/s41598-019-42560-8 (2019).
  10. Ikegami, M., Hirano, Y., Mie, Y. and Komatsu, Y.: Adsorptive Stripping Voltammetry for the Determination of Dissolved Oxygen Using a Mesoporous Pt Microelectrode. J. Electrochem. Soc., 166(6), B542-B546. doi:10.1149/2.0021908jes (2019).
  11. Mie, Y., Yasutake, Y., Ikegami, M. and Tamura, T.: Anodized gold surface enables mediator-free and low-overpotential electrochemical oxidation of NADH: A facile method for the development of an NAD(+)-dependent enzyme biosensor. SENSORS AND ACTUATORS B-CHEMICAL, 288, 512. doi:10.1016/j.snb.2019.03.039 (2019).
  12. Yamazaki, A., Nishimiya, Y., Tsuda, S., Togashi, K. and Munehara, H.: Freeze tolerance in sculpins (Pisces; Cottoidea) inhabiting north pacific and Arctic oceans: Antifreeze activity and gene sequences of the antifreeze protein. Biomolecules, 9(4), 139. doi:10.3390/biom9040139 (2019).

2018

  1. Kondo, H., Mochizuki, K., and Bayer-Giraldi, M. : Multiple binding modes of a moderate ice-binding protein from a polar microalga. Phys. Chem. Chem. Phys., 20, 25295-25303 DOI:10.1039/c8cp04727h. (2018).
  2. Nakamura, A., Wang, D. and Komatsu, Y. Biochemical analysis of human tRNAHis guanylyltransferase in mitochondrial tRNAHis maturation. Biochem. Biophys. Res. Commun., 503, 2015 doi:10.1016/j.bbrc.2018.07.150 (2018).
  3. Nakamura, A., Wang, D. and Komatsu, Y. Molecular mechanism of substrate recognition and specificity of tRNAHis guanylyltransferase during nucleotide addition in the 3′-5′ direction. RNA, 24, 1583 doi:10.1261/rna.067330.118 (2018).
  4. Mie, Y., Hirano, Y., Kowata, K., Nakamura, A., Yasunaga, M., Nakajima, Y., Komatsu, Y. Function Control of Anti-microRNA Oligonucleotides Using Interstrand Cross-Linked Duplexes. Mol. Ther. Nucleic Acids., 10, 64–74 doi:10.1016/j.omtn.2017.11.003 (2018)
  5. Hirano, Y., Kojima, N. and Komatsu, Y. Synthesis and Application of Interstrand Cross-Linked Duplexes by Covalently Linking a Pair of Abasic Sites. CURR. PROTOC. NUCLEIC ACID CHEM., 75, e63 doi:10.1002/cpnc.63 (2018).
  6. Okumura, S., Hirano, Y., Maki, Y. and Komatsu, Y. Analysis of time-course drug response in rat cardiomyocytes cultured on a pattern of islands. Analyst., 143 4083-4089 doi:10.1039/c8an01033a (2018).
  7. Mahatabuddin, S., Fukami, D., Arai, T., Nishimiya, Y., Shimizu, R., Shibazaki, C., Kondo, H., Adachi, M. and Tsuda, S. Polypentagonal ice-like water networks emerge solely in an activity-improved variant of ice-binding protein. Proc. Natl. Acad. Sci. USA, 115 (21), 5456-5461 doi:10.1073/pnas.1800635115 (2018).
  8. Yamazaki, A., Nishimiya, Y., Tsuda, S., Togashi, K. and Munehara, H. Gene expression of antifreeze protein in relation to historical distributions of Myoxocephalus fish species. Marine Biology, 165 181 doi:10.1007/s00227-018-3440-x (2018).

2017

  1. Suzuki, T., Imada, T., Komatsu, Y. and Kamiya, H. Comparison of DNA fragments as donor DNAs upon sequence conversion of cleaved target DNA. Nucleosides, nucleotides & nucleic acids., 36, 1-7 doi:10.1080/15257770.2017.1310385 (2017).
  2. Chen, MR., Kato, K., Kubo, Y., Tanaka, Y., Liu, YC., Long, F., Whitman, WB., Lill, P., Gatsogiannis, C., Raunser, S., Shimizu, N., Shinoda, A., Nakamura, A., Tanaka, I. and Yao, M. Structural basis for tRNA-dependent cysteine biosynthesis Nat. Commun., 8, 1521 doi:10.1038/s41467-017-01543-y (2017).
  3. 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 doi:10.1038/srep42501 (2017).
  4. Hirano, Y., Ikegami, M., Kowata, K. and Komatsu, Y. Bienzyme reactions on cross-linked DNA scaffolds for electrochemical analysis. Bioelectrochemistry., 113, 15-19 doi:10.1016/j.bioelechem.2016.08.005 (2017).

2016

  1. Ikegami, M., Hirano, Y., Mie, Y. and Komatsu, Y. Fabrication and characterization of nanoporous gold on microelectrode. Journal of Electroanalytical Chemistry., 783, 188-191 doi:10.1016/j.jelechem.2016.11.023 (2016).
  2. 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), 4011-4026 doi:10.1042/BCJ20160543 (2016).
  3. Tsuda, S. Mass preparation of fish antifreeze protein. J. Bioprocess Biotechniq.., 6 (7), 30, ISSN:2155-9821, (2016).
  4. 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 doi:10.20585/cryobolcryotechnol.62.2_95 (2016).
  5. Mie, Y., Ikegami, M. and Komatsu, Y. Nanoporous structure of gold electrode fabricated by anodization and its efficacy for direct electrochemistry of human cytochrome P450. Chem. Lett., 45,640-642 doi:10.1246/cl.160164 (2016).
  6. Kowata, K., Kojima, N. and Komatsu, Y. Development of a 3′-amino linker with high conjugation activity and its application to conveniently cross-link blunt ends of a duplex. Bioorg. Med. Chem., 24, 2108-2113 doi:10.1016/j.bmc.2016.03.039 (2016).
  7. Kimura, K., Suzuki, T., Chen, M., Kato, K., Yu, J., Nakamura, A., Tanaka, I. and Yao, M. Template-dependent nucleotide addition in the reverse (3′–5′) direction by Thg1-like protein. Sci. Adv.2(3), dio:10.1126/sciadv.1501397 (2016)

2015

  1. 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).
  2. 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).
  3. Englert, M., Nakamura, A., Wang, Y-S., Eiler, D., Söll, D. and Guo, L-T. Probing the active site tryptophan of Staphylococcus aureus thioredoxin with an analog. Nucl. Acid Res. 43, 11061-11067 (2015)
  4. Nakamura, A., Tamura, N. and Yasutake, Y. Structure of the HIV-1 reverse transcriptase Q151M mutant: insights into the inhibitor resistance of HIV-1 reverse. Acta Cryst. F., 71, 1384-1390 (2015)
  5. Tarashima, N., Komatsu, Y., Furukawa, K. and Minakawa, N. Faithful PCR amplification of an unnatural base-pair analogue with four hydrogen bonds. Chem. Eur. J., 21, 10688-10695 (2015).
  6. Suzuki, Y. and Komatsu, Y. Environmentally responsive and bright fluorescent probes possessing dansyl-modified oligonucleotides under hybridization of DNA and RNA. RNA and DNA Diagnostics (Springer series). 145-159 (2015).
  7. Asano, N., Kato, K., Nakamura, A., Komoda, K., Tanaka, I. and Yao, M. Structural and functional analysis of the Rpf2-Rrs1 complex in ribosome biogenesis. Nucl. Acid Res. 43, 4746-4757 (2015).

〜2014

  1. Hanada, Y., Nishimiya, Y., Tsuda, S., Miura, A., 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 DOI:10.1111/febs.12878 (2014).
  2. Hirano, Y., Kodama, M., Shibuya, M., Maki, Y. and Komatsu, Y. Analysis of beat fluctuations and oxygen consumption in cardiomyocytes by scanning electrochemical microscopy. Anal. Biochem., 447C, 39-42 (2014).
  3. Mie, Y., Tateyama, E. and Komatsu, Y. p-Aminothiophenol modification on gold surface improves stability for electrochemically driven cytochrome P450 microsome activity. Electrochim. Acta, 115, 364-369 (2014).
  4. 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, 159-261 DOI:10.1016/j.cryobiol.2013.10.008 (2013).
  5. 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 DOI:10.1111/1574-6968.12217 (2013).
  6. Ikegami, M., Mie, Y., Hirano, Y. and Komatsu, Y. Direct Electrochemistry of Microsomal Human Flavin-containing Monooxygenases 1 and 3 on Naphthalenethiol Thin Films. Ecs Electrochemistry Letters, 2, G5-G7 (2013).
  7. Suzuki, Y., Kowata, K. and Komatsu, Y. Development of dansyl-modified oligonucleotide probes responding to structural changes in a duplex. Bioorg. Med. Chem. Lett., 23, 6123-6126 (2013).
  8. Hirano, Y., Kowata, K., Kodama, M. and Komatsu, Y. Development of a scanning electrochemical microscopy-based micropipette and its application to analysis of topographic change of single-cell. Bioelectrochemistry, 92C, 1-5 (2013).
  9. Mie, Y., Kowata, K., Kojima, N. and Komatsu, Y. Electrochemical properties of interstrand cross-linked DNA duplexes labeled with Nile blue. Langmuir, 28, 17211-17216 (2012).
  10. Tarashima, N., Higuchi, Y., Komatsu, Y. and Minakawa, N. A practical post-modification synthesis of oligodeoxynucleotides containing 4,7-diaminoimidazo[5′,4′:4,5]pyrido[2,3-d]pyrimidine nucleoside. Bioorg.Med. Chem., 20, 7095-7100 (2012).
  11. Mie, Y., Kojima, N., Kowata, K. and Komatsu, Y. End-tether Structure of DNA Alters Electron-transfer Pathway of Redox-labeled Oligo-DNA Duplex at Electrode Surface. Chem. Letters, 41, 62-64 (2012).
  12. Ichikawa, K., Kojima, N., Hirano, Y., Takebayashi, T., Kowata, K. and Komatsu, Y. Interstrand cross-link of DNA by covalently linking a pair of abasic sites. Chem. Commun., 48, 2143-2145 (2012).
  13. Yokoyama, H., Mizutani, R., Satow, Y., Sato, K., Komatsu, Y., Ohtsuka, E. and Nikaido, O. Structure of the DNA (6-4) photoproduct dTT(6-4)TT in complex with the 64M-2 antibody Fab fragment implies increased antibody-binding affinity by the flanking nucleotides. Acta Crystallogr.D Biol. Crystallogr., 68, 232-238 (2012).
  14. Ikegami, M., Mie, Y., Hirano, Y., Suzuki, M. and Komatsu, Y. Size-controlled fabrication of gold nanodome arrays and its application to enzyme electrodes. Colloids and Surfaces A: Physicochemical and Engineering Aspects, 384, 388-392 (2011).
  15. Mie, Y., Ikegami, M. and Komatsu, Y. Gold sputtered electrode surfaces enhance direct electron transfer reactions of human cytochrome P450s. Elect. Comm., 12, 680-683 (2010).
  16. Kojima, N. and Komatsu, Y. Hydroxylamine, Oxime and Hydroxamic Acid Derivatives of Nucleic Acids. The Chemistry of Hydroxylamines, Oximes and Hydroxamic Acids, Vol 2, 807-851, WILEY (2010).
  17. Kojima N., Takebayashi T., Mikami A., Ohtsuka E, Komatsu Y. Construction of Highly Reactive Probes for Abasic Site Detection by Introduction of an Aromatic and a Guanidine Residue into an Aminooxy Group J. Am. Chem. Soc., 131, 13208-13209 (2009).
  18. Mie, Y., Suzuki, M. and Komatsu, Y. Electrochemically Driven Drug Metabolism by Membranes Containing Human Cytochrome P450 J. Am. Chem. Soc., 131, 6646-6647 (2009).
  19. Kojima N., Takebayashi T., Mikami A., Ohtsuka E, Komatsu Y. Efficient synthesis of oligonucleotide conjugates on solid-support using an (aminoethoxycarbonyl)aminohexyl group for 5′-terminal modification Bioorg. Med. Chem. Lett., 19, 2144-2147 (2009).
  20. Mizutani, F., Ohta, E., Mie, Y., Niwa, O. and Yasukawa, T. Enzyme immunoassay of insulin at picomolar levels based on the coulometric determination of hydrogen peroxide. Sens. Actuator B-chem., 135, 304-308(2008).
  21. Mizutani, F., Kato, D., Kurita, R., Mie, Y., Sato, Y. and Niwa, O. Highly-sensitive biosensors with chemical-amplified responses. Electrochemistry , 76, 515- 521(2008).
  22. Mie, Y., Kisita, M., Nishiyama, K. and Taniguchi, I. Interfacial electron transfer kinetics of myoglobins modified with succinic anhydride at an indium oxide electrode. J. Electroanal. Chem. , 624,305-309 (2008).
  23. 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).
  24. Komatsu, Y., Kojima, N., Sugino, M., Mikami, A., Nonaka, K., Fujinawa, Y., Sugimoto, T., Sato, K., Matsubara, K. and Ohtsuka, E. Novel amino linkers enabling efficient labeling and convenient purification of amino-modified oligonucleotides. Bioorg. Med. Chem. , 16, 941-949 (2008).
  25. Mie Y., Kowata K., Hirano Y., Niwa O. and Mizutani F. Comparison of Enzymatic Recycling Electrodes for Measuring Aminophenol: Development of a Highly Sensitive Natriuretic Peptide Assay Syste. Analytical Sciences , 24, 577-582 (2008).
  26. 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).
  27. Saito, Y., Kon, S., Fujiwara, Y., Nakayama, Y., Kurotaki, D., Fukuda, N., Kimura, C., Kanayama, M., Ito, K., Diao, H., Matsui, Y., Komatsu, Y., Ohtsuka, E. and Uede, T.　Osteopontin small interfering RNA protects mice from fulminant hepatitis. Hum Gene Ther , 18, 1205-1214 (2007).
  28. Inoue K., Ferrante P., Hirano Y., Yasukawa T., Shiku H. and Matsue T. A competitive immunochromatographic assay for testosterone based on electrochemical detection. TALANTA , 73, 886-892 (2007).
  29. Yasukawa T., Hirano Y., Motochi N., Shiku H. and Matsue T. Enzyme immunosensing of pepsinogens 1 and 2 by scanning electrochemical microscopy. Biosensors and Bioelectronics , 22, 3099-3104 (2007).
  30. Kojima, N., Sugino, M., Mikami, A., Nonaka, K., Fujinawa, Y., Muto, I., Matsubara, K., Ohtsuka, E. and Komatsu, Y. Enhanced reactivity of amino-modified oligonucleotides by insertion of aromatic residue. Bioorg. Med. Chem. Lett, 16, 5118-5121 (2006).
  31. Mie, Y., Kato, D., Niwa, O. and Mizutani, F. A highly sensitive assay to determine atrial natriuretic peptide by electrochemical enzyme immunoassays. Electrochemistry., 74, 138-140 (2006).
  32. Mie, Y., Kishita, M., Neya, S., Funasaki, N., Mizutani, F., Nishiyama, K. and Taniguchi, I. Electrochemical analysis of heme functions of myoglobin using semi-artificial mioglobins. J. Electroanal. Chem., 588, 226-234 (2006).
  33. Takahashi Y., Hirano Y., Yasukawa T., Shiku H., Yamada H. and Matsue T. Topographic, electrochemical, and optical mages captured using standing approach mode scanning electrochemical/optical microscopy. Langmuir., 22, 10299-10306 (2006).
  34. Ogasawara D., Hirano Y., Yasukawa T., Shiku H., Kobori K., Ushizawa K., Kawabata S., and Matsue T., Electrochemical microdevice with separable electrode and antibodychips for simultaneous detection of pepsinogens 1 and 2. Biosensors and Bioelectronics, 21, 1784-1790 (2006)
  35. Kojima, N., Sugino, M., Mikami, A., Nonaka, K., Fujinawa, Y., Ueda, Y., Satou, K., Ohtsuka, E., Matsubara, K. and Komatsu, Y. High throughput purification of amino-modified oligonucleotides and its application to novel detection system of gene expression. Nucleic Acids Sym. Ser., 49, 181-182 (2005).
  36. Kato, Y., Minakawa, N., Komatsu, Y., Kamiya, H., Ogawa, N., Harashima, H. and Matsuda, A. New NTP analogs: the synthesis of 4′-thioUTP and 4′-thioCTP and their utility for SELEX. Nucleic Acids Res. 33, 2942-51 (2005).
  37. Kojima, N., Sugino, M., Mikami, A., Ohtsuka, E. and Komatsu, Y. Generation of an abasic site in an oligonucleotide by using acid-labile 1-deaza-2′-deoxyguanosine and its application to postsynthetic modification. Org. Lett., 7, 709-712 (2005).
  38. Mie, Y., Yamada, C., Uno, T., Neya, S., Mizutani, F., Nishiyama, K. and Taniguchi, I. Notable deuterium effect on the electron transfer rate of myoglobin. Chem. Commun., 250-252, (2005).
  39. Mie, Y., Mizutani, F., Uno, T., Yamada, C., Nishiyama, K. and Taniguchi, I. Direct electrochemistry of cytochrome b562 molecules with a ligand binding pocket. J. Inorg. Biochem., 99,1245-1249 (2005).
  40. Nishiyama, K., Mie, Y., Kishita, M., Yamada, C., Kitagawa, R. and Taniguchi, I. Phototriggered chemical reduction of NADP+ by Zn-reconstituted myoglobin and triethanolamine as a sacrificial donor. Chem. Lett., 1032-1033 (2005).
  41. Komatsu, Y., Kojima, N., Fujinawa, Y., Nonaka, K., Sugino, M., Mikami, A., Hashida, J., Ohtsuka, E. and Matsubara, K. Synthesis and application of new amino modification analogues for functional oligonucleotide. Nucleic Acids Sym. Ser., 48, 21-22 (2004).
  42. Yamamoto, Y., Shuto, S., Tamura, Y., Ohtsuka, E., Komatsu, Y. and Matsuda, A. Oligodeoxynucleotides having a loop consisting of 3′-deoxy-4′-C-(2-hydroxyethyl)thymidines form stable hairpins. Biochemistry, 43, 8690-8699 (2004).
  43. Komatsu, Y. Regulation of ribozyme activity with short oligonucleotides. Biol Pharm Bull., 27, 457-462 (2004).
  44. Mie, Y., Yamada, C., Hareau, G., Neya, S., Uno, T., Funasaki, N. and Taniguchi, I. Functional evaluation of heme vinyl groups in myoglobin with symmetric protoheme isomers. Biochemistry, 43, 13149-13155 (2004).
  45. Xu, G., Ikegami, M., Honma, S., Ikeda, K., Dietrich, L., D. and Struk, M., P. Sooting Characteristics of Isolated Droplet Burning in Heated Ambients under Microgravity. Int. J. Heat and Mass Trans, 47, 5807-5821 (2004).
  46. Xu, G., Ikegami, M., Honma, S., Ikeda, K., Dietrich, L., D. and Struk, M., P. Interactive influences of convective flow and initial droplet diameter on isolated droplet burning rate. Int. J. Heat and Mass Trans, 47, 2029-2035 (2004).
  47. Hirano Y., Oyamatsu D., Yasukawa T., Shiku H., and Matsue T., Scanning Electrochemical Microscopy for Protein Chip Imaging and Shear Force Feedback Regulation of Substrate-Probe Distance. Electrochemistry, 72, 137-142 (2004).
  48. Ito, T., Ueno, Y., Komatsu, Y. and Matsuda, A. Synthesis, thermal stability and resistance to enzymatic hydrolysis of the oligonucleotides containing 5-(N-aminohexyl)carbamoyl-2′-O-methyluridines. Nucleic Acids Res., 31, 2514-2523, (2003).
  49. Sakamoto S, Tamura T, Furukawa T, Komatsu Y, Ohtsuka E, Kitamura M, Inoue H. Highly efficient catalytic RNA cleavage by the cooperative action of two Cu(II) complexes embodied within an antisense oligonucleotide. Nucleic Acids Res., 31, 1416-1425, (2003).
  50. Kojima, N., Inoue, K., Nakajima-S. R., Kawahara, S., Ohtsuka, E. New, but old, nucleoside analogue: The first synthesis of 1-deaza-2′-deoxyguanosine and its properties as a nucleoside and as oligodeoxynucleotides. Nucleic Acids Res., 31(24), 7175-7188 (2003).
  51. Minakawa, N., Kojima, N., Hikishima, S., Sasaki, T., Kiyosue, A., Atsumi, N., Ueno, Y., Matsuda, A. New base pairing motifs. The synthesis and thermal stability of oligodeoxynucleotides containing imidazopyrido-pyrimidine nucleosides with the ability to form four hydrogen bonds. J. Am. Chem. Soc., 125(33), 9970-9982 (2003).
  52. Ikegami, M., Xu, G., Ikeda, K., Honma, S., Nagaishi, H., Dietrich, L., D. and Takeshita, Y. Distinctive Combustion Stages of Single Heavy Oil Droplet under Microgravity. Fuel., 82, 293-304 (2003).
  53. Xu, G., Ikegami, M., Honma, S., Ikeda, K., Ma, X., Nagaishi, H., Dietrich, L., D. and Struk, P., M. Inverse Influences of Initial Diameter on Droplet Burning Rate in Cold and Hot Ambiences: a thermal action of flame in balance with heat loss. Int. J. Heat and Mass Trans., 46, 1155-1169 (2003).
  54. Xu, G., Ikegami, M., Honma, S., Ikeda, K., Ma, X. and Nagaishi, H. Burning Droplets of Heavy Oil Residual Blended with Diesel Light Oil: Distinction of Burning Phases. Comb. Sci.Tech., 175, 1-26 (2003).
  55. Xu, G., Ikegami, M., Honma, S., Sasaki, M., Ikeda, K., Nagaishi, H. and Takeshita, Y. Combustion characteristics of droplets composed of light cycle oil and diesel light oil in a hot-air chamber. Fuel., 82, 319-330 (2003).
  56. Hirano Y., Mitsumori Y., Oyamatsu D., Nishizawa M., and Matsue T., Imaging of Immobilized Enzyme Spots by Scanning Chemiluminescence Microscopy with Electrophoretic Injection. Biosensors and Bioelectronics, 18, 587-590 (2003).
  57. Oyamatsu D., Hirano Y., Kanaya N., Mase Y., Nishizawa M., and Matsue T., Imaging of Enzyme Activity by Scanning Electrochemical Microscope Equipped with a Feedback Control for Substrate-Probe Distance. Bioelectrochemistry, 60, 115-121 (2003).
  58. Oyamatsu D., Kanaya N., Hirano Y., Nishizawa M., and Matsue T., Area-selective immobilization of multi enzymes by using the reductive desorption of self-assembled monolayer. Electrochemistry, 71, 232-234 (2003).
  59. Komatsu, Y., Nobuoka, K., Karino-Abe, N., Matsuda, A. and Ohtsuka, E. In vitro selection of hairpin ribozymes activated with short oligonucleotides. Biochemistry, 41, 9090-9098, (2002).
  60. Kojima, N., Szabo, I. F., Bruice, T. C. Synthesis of ribonucleic guanidine: replacement of the negative phosphodiester linkages of RNA with positive guanidinium linkages. Tetrahedron, 58(5), 867-879 (2002).
  61. Xu, G., Ikegami, M., Honma, S., Ikeda, K., Nagaishi, H., Dietrich, L., D. and Takeshita, Y. Burning Droplets Composed of Light Cycle Oil and Diesel Light Oil. Energy & Fuels, 16, 366-378 (2002).
  62. Xu, G., Ikegami, M., Honma, S., Ikeda, K. and Nagaishi, H. Burning Droplets of Heavy Oil Residual Blended with Diesel Light Oil; Characterization of Burning Steps. Comb. Sci. Tech., 174, 115-145 (2002).
  63. Kasai S., Hirano Y., Motochi N., Nishizawa M., and Matsue T., Simultaneous detection of uric acid and glucose on a dual-enzyme chip using scanning electrochemical microscopy/scanning chemiluminescence microscopy. Anal. Chim. Acta, 458, 263-270 (2002).
  64. Hirano Y., Kasai S., Nishizawa M., and Matsue T., Chemiluminescence Imaging of Localized Bi-enzyme by Scanning Chemiluminescence Microscopy. Electrochemistry, 69, 946-948 (2001).
  65. Yokoyama, H., Mizutani, R., Satow, Y., Komatsu, Y., Ohtsuka, E. and Nikaido, O. Crystal Structure of the 64M-2 Antibody Fab Fragment in Complex with a DNA dT(6-4)T Photoproduct Formed by Ultraviolet Radiation. J. Mol. Biol. 299, 711-723, (2000).
  66. Torizawa, T., Yamamoto, N., Suzuki, T., Nobuoka, K., Komatsu, Y., Morioka, H., Nikaido, O., Ohtsuka, E., Kato, K. and Shimada, I. DNA binding mode of the Fab fragment of a monoclonal antibody specific for cyclobutane pyrimidine dimer. Nucleic Acids Res 28, 944-951, (2000).
  67. Sato, K., Komatsu, Y., Torizawa, T., Kato, K., Shimada, I., Nikaido, O. and Ohtsuka, E. Efficient chemical synthesis of a pyrimidine (6-4) pyrimidone photoproduct analog and its properties. Tetrahedron Lett. 41, 2175-2179, (2000).
  68. Komatsu, Y., Yamashita, S., Kazama, N., Nobuoka, K. and Ohtsuka, E. Construction of new ribozymes requiring short regulator oligonucleotides as a cofactor. J. Mol. Biol. 299, 1231-1243, (2000).
  69. Kojima, N., Minakawa, N., Matsuda, A. Studies in the chemical conversion of the 4-carboxamide group of 5-amino-1-b-D-ribofuranosylimidazole-4-carboxamide (AICA-riboside). Application for the synthesis of 1-deazaguanosine. Tetrahedron, 56(40), 7909-7914 (2000).
  70. Kojima, N., Bruice, T. C. Replacement of the phosphodiester linkages of RNA with guanidinium linkages: The solid-phase synthesis of ribonucleic guanidine, Org. Lett., 2(1), 81-84 (2000).
  71. Komatsu, Y., Kanzaki, I., Shirai, M., Kumagai, I., Yamashita, S. and Ohtsuka, E. Functional Domain-Assembly in Hairpin Ribozymes. J Biochem (Tokyo) 127, 531-536, (2000). Review.

Peer-reviewed Articles (AFP project)

(92) Yamauchi, A., Arai, T., Kondo, H., Sasaki, Y.C., and Tsuda, S. : An ice-binding protein from an Antarctic ascomycete is fine-tuned to bind to specific water molecules located in the prism planes. Biomolecules 10 (5), 759, doi: 10.3390/biom10050759 (2020).

(91) Tsuda, S., Yamauchi, A., Khan, U. N.M.-M., Arai, T., Mahabuddin, S., Miura, A., and Kondo, H.: Fish-derived antifreeze proteins and antifreeze glycoprotein exhibit a different ice-binding property with increasing concentration. Biomolecules 10 (3), 423. doi: 10.3390/biom10030423 (2020).

(90) Aohara, T., Furukawa J., Miura, K., Tsuda, S., Poisson J.S., Ben R.N., Wilson P.W., and Satoh S.: Presence of a basic secretory protein in xylem sap and shoots of poplar in winter and its physicochemical activities against winter environmental conditions. J. Plant Res. doi: doi.org/10.1007/s10265-019-01123-9 (2019).

(89) Kuramochi, M., Takanashi, C., Yamauchi, A., Doi, M., Mio, K., Tsuda, S., and Sasaki, Y.: Expression of ice-binding proteins in Caenorhabditis elegans improves the survival rate upon cold shock and during freezing. Scientific Reports, 9, 6246, doi: 10.1038/s41598-019-42560-8 (2019).

(88) Arai, T., Nishimiya, Y., Ohyama, Y., Kondo, H., and Tsuda, S.: Calcium-binding generates the semi-clathrate waters on a type II antifreeze protein to adsorb onto an ice crystal surface. Biomolecules, 9, 162, doi:10.3390/biom9050162 (2019).

(87) Yamazaki, A., Nishimiya, Y., Tsuda, S., Togashi, K., Munehara, H.: Freeze tolerance in sculpins (Pisces; Cottoidea) inhabiting north pacific and Arctic oceans: Antifreeze activity and gene sequences of the antifreeze protein. Biomolecules, 9, 139, doi:10.3390/biom9040139 (2019).

(86) Rahman, A.T., Arai, T., Yamauchi, A., Miura, A., Kondo, H., Ohyama, Y., and Tsuda, S.: Ice recrystallization is strongly inhibited when antifreeze proteins bind to multiple ice planes. Sci Rep, 9 (1): 2212. doi: 10.1038/s41598-018-36546-2 (2019).

(85) Arai, T., Fukami, D., Hoshino, T., Kondo, H., and Tsuda, S.: Ice-binding proteins from the fungus Antarctomyces psychrotropicus possibly originate from two different bacteria through horizontal gene transfer. FEBS J. doi: 10.1111/febs.14725 (2018).

(84) Yamazaki, A., Nishimiya, Y., Tsuda, S., Togashi, K., Munehara, H.: Gene expression of antifreeze protein in relation to historical distributions of Myoxocephalus fish species. Marine Biology, 165: 181. doi: https://doi.org/10.1007/s00227-018-3440-x (2018).

(83) Mahatabuddin, S. and Tsuda, S.: Applications of Antifreee Proteins: Practical Use of the Quality Products from Japanese Fishes. Adv. Exp. Med. Biol., 1081, 321-327. doi: 10.1007/978-981-13-1244-1_17 (2018).

(82) Azuma, N., Miyazaki Y., Nakano, M., and Tsuda, S.: Unexpected Rise of Glass Transition Temperature of Ice Crystallized from Antifreeze Protein Solution. J. Phys. Chem. Lett. 9, 4512-4515 (2018).

(81)Mahatabuddin S., Fukami, D., Arai,T., Nishimiya, Y., Shimizu, R., Shibazaki, C., Kondo, H., Adachi, M., and Tsuda, S.: Polypentagonal ice-like water networks emerge solely in an activity-improved variant of ice-binding protein. Proc. Natl. Acad. Sci. USA,115 (21), 5456-5461 (2018).

(80) Orii, R., Sakamoto, N., Fukami, D., Tsuda, S., Izumi, M., Kajihara, Y., and Okamoto, R. Total Synthesis of O-GalNAcylated Antifreeze Glycoprotein using the Switchable Reactivity of Peptidyl-N-pivaloylguanidine. Chem. Eur. J., 9253-9257 (2017).

(79) 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).

(78) 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).

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

(76) 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).

(75) 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).

(74) 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).

(73) 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).

(72) 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).

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

(70) 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).

(69) 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).

(68) 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).

(67) 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).

(66) 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).

(65) 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).

(64) 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 ℃. Scientific Reports, 3 (1173) 1-5 (2013).

(63) 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).

(62) 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).

(61) 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).

(60) 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).

(59) 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).

(58) 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).

(57) 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).

(56) 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).

(55) Yamawaki, H., Fujihisa, H., Sakashita, M., Honda, K., and Gotoh, Y. : Vibration and structural study in phase I of Rb3H(SO4)2. Physica B-Condensed Matter, 405, 291-295 (2010).

(54) 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).

(53) Yasuda, K., Takeya, S., Sakashita, M., Yamawaki, H., and Ohmura, R. : Binary Ethanol-Methane Clathrate Hydrate Formation in the System CH4-C2H5OH-H2O: Confirmation of Structure II Hydrate Formation. J. Phys. Chem. C, 113, 12598-12601 (2009).

(52) Yasuda, K., Takeya, S., Sakashita, M., Yamawaki, H., and Ohmura, R. : Characterization of the Clathrate Hydrate Formed with Methane and Propan-1-ol. Ind. Eng. Chem. Res. 48, 9335-9337 (2009).

(51) 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).

(50) Sakae, Y., Matsubara, T., Aida, M., Kondo, H., Masaki. K., and Iefuji, H. : ONIOM Study of the Mechanism of the Enzymatic Hydrolysis of Biodegradable Plastics. Bull. Chem. Soc. Jpn. 82 (3), 338-346 (2009).

(49) 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).

(48) 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).

(47) 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).

(46) 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).

(45) 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).

(44) 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).

(43) 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).

(42) 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).

(41) Nakanishi, T., Tsumoto, K., Yokota, A., Kondo, H., and Kumagai, I. : Critical contribution of VH-VL interaction to rehaping of an antibody: The case of humanization of anti-lysozyme antibody, HyHEL-10. Protein Sci. 17 (2), 261-270 (2008).

(40) Makabe, K., Nakanishi, T., Tsumoto, K., Tanaka, Y., Kondo, H., Umezu, M., Sone, Y., Asano, R., and Kumagai, I. : Thermodynamic consequences of mutations in Vernier Zone residues of a humanized anti-human epidermal growth factor receptor (EGFR) murine antibody, 528. J. Biol. Chem. 283 (2), 1156-1166 (2008).

(39) Sakashita, M., Fujihisa, H., Suzuki, K., Hayashi, S., and Honda, K. : Using X-ray diffraction to study thermal phase transitions in CS5H3(SO4)4 xH2O. Solid State Ionics, 178, 1262-1267 (2007).

(38) 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).

(37) 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).

(36) 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).

(35) Shiroishi, M., Tsumoto, K., Tanaka, Y., Yokota, A., Nakanishi, T., Kondo, H., and Kumagai, I. : Structural consequences of mutations in interfacial Tyr residues of a protein antigen-antibody complex: The case of HyHEL-10-HEL. J. Biol. Chem. 282, 6783-6791 (2007).

(34) Hara, I., Ichise, N., Kojima, K., Kondo,H., Ohgiya, S., Matsuyama, H., and Yumoto, I. : Relationship between Size of Bottleneck 15 Angstrome Away from Iron in Main Channel and Reactivity of Catalase Corresponding to Molecular Size of Substrates. Biochemistry, 46, 11-22 (2007).

(33) 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).

(32) 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).

(31) 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).

(30) 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).

(29) 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).

(28) 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).

(27) Yaoi, K., Kondo, H., Noro, N., Suzuki, M., Tsuda, S., and Mitsuishi, Y. : A part of ice nucleation protein exhibits the ice-binding ability. FEBS Letters., 579(6), 1493-1497 (2005).

(26) 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).

(25) 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).

(24) 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).

(23) 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).

(22) 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).

(21) 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).

(20) 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).

(19) 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).

(18) 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).

(17) 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).

(16) 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).

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

(14) 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).

(13) 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).

(12) 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).

(11) 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).

(10) 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).

(9) 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).

(8) 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).

(7) Gagne, S.M., Tsuda, S., Spyracopoulos, L., 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).

(6) 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).

(5) 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).

(4) 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).

(3) 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).

(2) 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).

(1) 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).

Inviting and keynote Lectures (AFP project)

(53) Sakae Tsuda: Molecular function and application of Antifreeze protein. Annual meeting at Ishikawa Prefectural University, Kanazawa, JPN. Dec 4th, 2017.

(52) Sakae Tsuda: Antifreeze proein – from functional analysis to industrial applications -. Inviting lecture at National Defense Academy, Yokosuka, JPN. Nov.28th, 2017.

(51) Sakae Tsuda： Molecular function and application of antifreeze proteins. 15th Annual meeting of Spring-8 advanced research workshop. Kyoto, JPN. Aug 24th, 2017.

(50) Sakae Tsuda: Molecular biology of antifreeze protein. 2017 Annual meeting of the Ichthyological Society of Japan. Hakodate, JPN. Sep 18th, 2017.

(49) Sakae Tsuda: A new type I antifreeze protein BpAFP undergoes oligomerization to bind to whole surface of an ice crystal. 2nd International Conference on Bioscience. London, UK (2017/6/19).

(48)　Sakae Tsuda: Antifreeze Science. 3rd meeting of the Low- temperature science community, Tokyo, JPN. Jan 20th, 2017.

(47)　Sakae Tsuda: Antifreeze Science. New cell-preservation technique utilizing extremely purified antifreeze protein. Cryopreservation Conference 2016, Okazaki, JPN. Nov.10th, 2016.

(46) Sakae Tsuda: Mass preparation of fish antifreeze protein. 4th International conference on Bioprocess and Bio Therapeutics (Bioprocess2016). Houston, USA. Oct 21st, 2016.

(45) Sakae Tsuda: Structure of antifreeze protein –Ice binding mechanism and its application-. 2016 Annual meeting of the vacuum society of Japan. Sapporo, JPN. Oct 6th, 2016.

(44) Sakae Tsuda: What is antifreeze protein? – Ice binding function operated by different structural motifs –. Special seminar at the Osaka University. Osaka, JPN. Nov 5th, 2016.

(43) Sakae Tsuda: Development of cell-preservation technique on the basis of the functional analysis of antifreeze protein. Cryopreservation Conference 2014, Okazaki, JPN. Oct.24th, 2014.

(42) Sakae Tsuda* : The membrane-binding ability of fish IBP prolongs the life-time of a cell dramatically. 2nd International Ice-Binding Protein (IBP) Conference, Sapporo, JPN. Aug.7th. 2014. (* ST is the host-organizer of this conference).

(41) Sakae Tsuda: Development of new cryotechnology utilizing the antifreeze protein. 1st Open facility symposium of Hokkaido University. Sapporo, JPN. Mar 10th, 2014.

(40) Sakae Tsuda: Analysis of molecular mechanism of antifreeze protein for its application. Training for technical staffs employed in Universities & Institutes of Hokkaido in 2013. Sapporo, JPN. Aug 27th 2013.

(39)○Tsuda, S., Kondo, H., Ideta, A., Aoyagi, Y., and Nishimiya, Y. Antifreeze Protein from Japanese Organisms: Functional Analyses for the General Use. 50th Annual meeting of the society for cryobiology (CRYO2013), Washingon D.C. USA (2013/7/29).

(38) Sakae Tsuda: Antifreeze protein -Applicational aspect in cryotechnlogy, The Science Forum in Tokyo, “Application of antifreeze protein in industry – Milestone for the practical use of the protein -. JPN. Feb.14th. 2013.

(37) Sakae Tsuda: Analysis of structure and function of a new fungal antifreeze protein, 2012 Industrial technology seminar in Hirosaki. JPN. Dec. 13th. 2012.

(36) Sakae Tsuda: Functional analysis of antifreeze protein and its industrial appications, 2012 Industrial technology seminar in Yonago. JPN. Dec. 7th. 2012.

(35) Sakae Tsuda: Study of antifreeze protein and its industrial appications, 9th Meeting of industrial innovation utilizing Methane-hydrate. JPN. Nov. 5th. 2012.

(34) Sakae Tsuda: Applications of antifreeze proteins in food industry, Nihon-Syokuhin-Kougyou Club. JPN. Apr.24th. 2012.

(33) Sakae Tsuda: Mass preparation and technological developments of antifrreze protein, 2012 training for new AIST researchers, Tsukuba, JPN. Apr.11th. 2012.

(32) Sakae Tsuda: Recent technological developments utilizing antifreeze protein, 1st International Ice-Binding Protein (IBP) conference and workshop, Kingston (ON), CAN. Aug.6th, 2011.

(31) Hidemasa Kondo: Crystal structure of antifreeze protein from a snow mold fungus, 1st International Ice-Binding Protein (IBP) conference and workshop, Kingston (ON), CAN. Aug.5th, 2011.

(30) Sakae Tsuda: New technologies utilizing the functions of antifreeze protein, 12th Annual Meeting of Japanese Society of Extremophiles, Tsukuba, JPN. Jun.13th, 2011.

(29) Sakae Tsuda: Functional analyses of antifreeze protein and its practical applications, 65th Annual Meeting of Japanese Society of Enzyme Engineering, Kyoto, JPN. Apr.22th, 2011.

(28) Sakae Tsuda: New technologies utilizing antifreeze protein, 12th. International Conference on the Physics and Chemistry of Ice (PCI-2010), Sapporo, JPN. Sep.10th, 2010.

(27) Mami Sakashita, Yoshiyuki Nishimiya, Hidemasa Kondo, and Sakae Tsuda: Interaction between ice and a type III antifreeze protein under high pressure, 12th International Conference on the Physics and Chemistry of Ice (PCI-2010), Sapporo, JPN. Sep.10th, 2010.

(26) Sakae Tsuda: Molecular analyses of antifreeze protein for its industrial applications, 5th alliance seminar for methane-hydrate research laboratory of AIST, Sapporo, JPN. Sep.2nd, 2010.

(25) Sakae Tsuda: Functional analyses of antifreeze protein for a new technology, 10th annual meeting of protein science society of Japan, Sapporo, JPN. Jun.16th, 2010.

(24) Sakae Tsuda: Structure and function analyses of antifreeze protein for a novel technology, Annual Seminar for the national newtron diffraction center of Ibaraki prefecture, Ibaraki, JPN. Mar.25th, 2010.

(23) Yoshiyuki Nishimiya: A protein that ineteracts with ice – application of neutron diffraction-, Annual Seminar for the national newtron diffraction center of Ibaraki prefecture, Ibaraki, JPN. Jan.15th, 2010.

(22) Sakae Tsuda: Analysis of antifreeze function for technological application, Annual seminar held at Division of Engineering for Composite Functions in Muroran Institute of Technology, Muroran, JPN. Nov.11th, 2009.

(21) Sakae Tsuda: Functional analysis of antifreeze protein and its application to food technologies, 56th Annual Meeting of the Japanese Society for Food Science and Technology, Nagoya, JPN. Sep.12th, 2009.

(20) Sakae Tsuda: New technologies developed for practical use of antifreeze protein, 46th Annual Meeting of the Society for Cryobiology (CRYO2009), Sapporo, JPN. Jul 20th. 2009.

(19) Yoshiyuki Nishimiya: Purification and functional analysis of antifreeze protein from Japanese fish, Dou-ou bioresearch community, Eniwa, JPN. Feb 27th. 2009.

(18) Yoshiyuki Nishimiya: Mass-purification of antifreeze proteins from fish muscles, AIST-Fair, Hakodate, JPN. Jan 23rd. 2007.

(17) Sakae Tsuda: Development of practical freezing techniques by using antifreeze protein, AIST Forum in Nagoya, JPN. Dec.5th, 2007.

(16) Sakae Tsuda: Saving of the freezing energy by utilizing antifreeze protein, Kyusyu University WS-Forum “Current situation and future aspects of protein and peptides, Fukuoka, JPN. Nov.2nd,2007.

(15) Sakae Tsuda: Antifreeze Protein from Japanese Fish: An epoch in biotechnology, The 234th American Chemical Society Meeting – Antifreeze Proteins: A Memorial Synposium for Robert Feeney. (*Program assigned to ‘Division of Computers in Chemistry’), Boston, USA. Aug.19th, 2007.

(14) Sakae Tsuda: Antifreeze Protein – from functional analysis to technological applications-, 2nd International Symposium on the Environmental Physiology of Ectotherms and Plants (ISEPEP2) . Duniden, NZ. Jul.2nd, 2007.

(13) Sakae Tsuda: Functions of antifreeze protein (AFP) and its practical use in industry, Food Technology Forum, Tokyo, JPN. Apr.21st, 2006.

(12) Sakae Tsuda: A special gift from nothern nature – antifreeze protein -, A forum for the citizen of Sapporo, Sapporo, JPN. Nov.26th, 2005.

(11) Sakae Tsuda: Biotechnology utilizing Japan-original antifreeze protein, 2005 AIST Life Science Meeting, Fukuoka, JPN. Mar.3rd, 2005.

(10) Sakae Tsuda: Antifreeze Protein – from structural basis to industrial application -, Hokkaido University Sousei-kagaku seminar, Sapporo, JPN. Oct.12th, 2004.

(9) Katsuro Yaoi, Hidemasa Kondo, Mamoru Suzuki, Natsuko Noro, Sakae Tsuda, and Yasushi Mitsuishi : Structure and Function of xyloglucan hydrolases belonging to Glycoside Hydrolase Family 74, 12th symposium of applied glycoscience, Kagoshima, JPN. Sep.17th, 2004.

(8) Sakae Tsuda: Antifreeze Protein – from structural basis to industrial application -, AIST-Korea Joint Workshop, Sapporo, JPN. Jun.29th, 2004.

(7) Sakae Tsuda: Antifreeze Protein from Japanese Fish, The 30th. Annual Meeting of the Japan Society for Low Temperature Medicine, Sapporo, JPN. Nov.29th, 2003.

(6) Sakae Tsuda: Antifreze Protein from Japanese Fish – application for tissue preservation -, 2nd Hokkaido Marine Bioscience Symposium, Sapporo, JPN. Oct.31st, 2003.

(5) Sakae Tsuda: Three-Dimensional Structure of Fish Antifreeze Protein and its Industrial Applications, 2003 AIST Life Science Meeting, Sapporo, JPN. Sep.18th, 2003.

(4) Sakae Tsuda: Antifreeze Protein – from structural basis to industrial application -, 2003 Annual Meeting of Japanese Society for Cryobiology and Cryotechnology, Sapporo, JPN. Jun.26th, 2003.

(3) Sakae Tsuda: Antifreeze Protein from Japanese Organisms, 3rd Annual meeting of Japanese Society for Protein Science, Sapporo, JPN. Jun.24th, 2003.

(2) Sakae Tsuda: Japanese Antifreeze Proteins, Symposium on Stress Proteins: From Antifreeze to Heat Shock.California, USA. Jun.26th, 2003.

(1) Sakae Tsuda and Yoshiyuki Nishimiya: Cold Adaptation of Arctic Fish – Expression of Ice binding Protein -, Seminar at the Institute for Protein Research in Osaka University, Osaka, JPN. Mar.11th, 2003.