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.inpressDOI: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. Cell34, 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 Med15, 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. Aging123, 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 Protocols2 e386. DOI:10.1002/cpz1.386. (2022)


  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. Neurochem159, 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 Letters48, 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. Sci22, 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 REP11(1), 11467. doi:10.1038/s41598-021-90972-3 (2021).


  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 110doi: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).


  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 JCM1131TBiochim Biophys Acta Mol Cell Biol Lipids1864, 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 Bio9, (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. Biomolecules9, 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 Reports9, 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-CHEMICAL288, 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. Biomolecules9(4), 139. doi:10.3390/biom9040139 (2019).



  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. RNA24, 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. USA115 (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 Biology165 181 doi:10.1007/s00227-018-3440-x (2018).


  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).


  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)
  8. 小松康雄:オリゴヌクレオチドの合成後の化学修飾,  「核酸医薬の創製と応用展開」(シーエムシー出版)p104 ISBN:978-4-7813-1138-8 (2016)


  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).


  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. Acta115, 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. Cryobiology68, 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 Letters2, 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. Bioelectrochemistry92C, 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. Langmuir28, 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. Letters41, 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 Aspects384, 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 AcidsVol 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. Lett16, 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 Bioelectronics21, 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 Res33, 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. Biochemistry43, 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. Biochemistry43, 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 Trans47, 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 Trans47, 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. Electrochemistry72, 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 Bioelectronics18, 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. Bioelectrochemistry60, 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. Electrochemistry71, 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. Biochemistry41, 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. Tetrahedron58(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 & Fuels16, 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. Acta458, 263-270 (2002).
  64. Hirano Y., Kasai S., Nishizawa M. and Matsue T., Chemiluminescence Imaging of Localized Bi-enzyme by Scanning Chemiluminescence Microscopy. Electrochemistry69, 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. Biol299, 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 Lett41, 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. Biol299, 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. Tetrahedron56(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.


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