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  4. 誌上発表(国際誌・査読有)2014年





  • Kato, YS., Yagi, T., Harris, SA., Ohki, S., Yura, K., Shimizu, Y., Honda, S., Kamiya, R., Burgess, SA., Tanokura, M.: Structure of the microtubule-binding domain of flagellar dynein. Structure (2014).
  • Kaishima, M., Fukuda, N., Ishii, J., Kondo, A.: Desired alteration of protein affinities: competitive selection of protein variants using yeast signal transduction machinery. PLoS One, 9(9), 108229 (2014).
  • Tsukamoto, M., Watanabe, H., Ooishi, A., Honda, S.: Engineered protein A ligands, derived from a histidine-scanning library, facilitate the affinity purification of IgG under mild acidic conditions. J. Biol. Engineering., 8(15) (2014).
  • Shibakami, M., Tsubouchi, G., Hayashi, M.: Thermoplasticization of euglenoid beta-1,3-glucans by mixed esterification. Carbohydr. Polym., 105, 90-96 (2014).
  • Oshiro, S., Honda, S.: Imparting Albumin-Binding Affinity to a Human Protein by Mimicking the Contact Surface of a Bacterial Binding Protein. ACS Chem. Biol., 9(4), 1052-1060(2014).
  • Watanabe, H., Yamasaki, K., Honda, S.: Tracing primordial protein evolution through structurally guided stepwise segment elongation. J. Biol. Chem., 289(6), 3394-3404 (2014).


  • Muraki, M.: Improved production of recombinant human Fas ligand extracellular domain in Pichia pastoris: Yield enhancement using disposable culture-bag and its application to site-specific chemical modifications. BMC Biotechnol., 14, 19 (2014).


  • Nishiyama, H., Koizumi, M., Ogawa, K., Kitamura, S., Konyuba, Y., Watanabe, Y., Ohbayashi, N., Fukuda, M., Suga, M., Sato, C.: Atmospheric scanning electron microscope system with an open sample chamber: configuration and applications. Ultramicroscopy, 147, 86-97 (2014).
  • Ogura, T., Yajima, H., Nitta, R., Hirokawa, N., Sato, C.: New simulated annealing approach considering helix bending applied to determine the 8.8 A structure of 15-protofilament microtubules. J. Struct. Biol., 188(2), 165-176 (2014).
  • Ogura, T.: Non-destructive observation of intact bacteria and viruses in water by the highly sensitive frequency transmission electric-field method based on SEM. Biochem. Biophys. Res. Commun., 450(4), 1684-1689 (2014).
  • Kato, Y., Fujiwara, T., Komeiji, Y., Nakano, T., Mori, H., Okiyama, K., Mochizuki, Y.: Fragment molecular orbital;based molecular dynamics (FMO-MD) simulations on hydrated Cu(II) ion. CBI Journal, 14(1), 1-13 (2014).
  • Hirano, K., Kinoshita, T., Uemura, T., Motohashi, H., Watanabe, Y., Ebihara, T., Nishiyama, H., Sato, M., Suga, M., Maruyama, Y., Tsuji, N.M., Yamamoto, M., Nishihara, S., Sato, C.: Electron microscopy of primary cell cultures in solution and correlative optical microscopy using ASEM. Ultramicroscopy, 143, 52-66 (2014).
  • Kinoshita, T., Mori, Y., Hirano, K., Sugimoto, S., Okuda, K., Matsumoto, S., Namiki, T., Ebihara, T., Kawata, M., Nishiyama, H., Sato, M., Suga, M., Higashiyama, K., Sonomoto, K., Mizunoe, Y., Nishihara, S., Sato. C.: Immuno-electron microscopy of primary cell cultures from genetically modified animals in liquid by atmospheric scanning electron microscopy. Microsc. Microanal., 20, 469-483 (2014).
  • Fukuzawa, K., Watanabe, C., Kurisaki, I., Taguchi, N., Mochizuki, Y., Nakano, T., Tanaka, S., Komeiji, Y.: Accuracy of the fragment molecular orbital (FMO) calculations for DNA: total energy, molecular orbital, and inter-fragment interaction energy. Comput. Theor. Chem., 1034(1), 7-16 (2014).
  • Ogura, T.: Direct observation of unstained biological specimens in water by the frequency transmission electric-field method using SEM. PLoS One, 9(3), e92780-6 (2013).
  • Matsui, E., Matsui, I.: Serial intermediates with a 1 nt 3′-flap and 5′ variable length flaps are formed by cooperative functioning of Pyrococcus horikoshii FEN-1 with either B or D DNA polymerases. Extremophiles, 18(2), 415-427 (2014).
  • Nishiyama, H., Teramoto, K., Suga, M., Sato, T.: Positively Charged Nanogold Label Allows the Observation of Fine Cell Filopodia and Flagella in Solution by Atmospheric Scanning Electron Microscopy. Microsc. Res. Tech., 77(2), 153-160 (2013).


  • Takahashi, T., Ohnishi, H., Sugiura, Y., Honda, K., Suematsu, M., Kawasaki, T., Deguchi, T., Fujii, T., Orihashi, K., Hippo, Y., Watanabe, Y., Yamagaki, T., Yuba, S.:Non-neuronal acetylcholine as an endogenous regulator of proliferation and differentiation of Lgr5-positive stem cells in mice. FEBS J., 281(20), 4672-4690 (2014).
  • Kawata, Y., Ando, H., Matsushita, I., Tsubota, J.: Efficient secretion of (R)-3-hydroxybutyric acid from Halomonas sp. KM-1 by nitrate fed-batch cultivation with glucose under microaerobic conditions. Bioresour. Technol., 156, 400-403 (2014).


  • Yamano, N., Kawasaki, N., Oshima, M., Nakayama, A.: Polyamide 4 with long-chain fatty acid groups - suppressing the biodegradability of biodegradable polymers. Polym. Degrad. Stabil., 108, 116-122 (2014).
  • Mine, S., Niiyama, M., Hashimoto, W., Ikegami, T., Koma, D., Ohmoto, T., Fukuda, Y., Inoue, T., Abe, Y., Ueda, T., Morita, J., Uegaki, K., Nakamura, T.: Expression from engineered Escherichia coli chromosome and crystallographic study of archaeal N,N'-diacetylchitobiose deacetylase. FEBS J., 281(11), 2584-2596 (2014).
  • Mine, S., Nakamura, T., Sato, T., Ikegami, T., Uegaki, K.: Solution structure of the chitin-binding domain 1 (ChBD1) of a hyperthermophilic chitinase from Pyrococcus furiosus. J. Biochem., 155(2), 115-122 (2014).



  • Kondoh, D., Tateno, H., Hirabayashi, J., Yasumoto, Y., Oishi, K.: The molecular clock regulates circadian variations in a1-2 fucosylation within mouse secondary olfactory neurons. J. Biol. Chem. (2014).
  • Yasumoto, Y., Nakao, R., Oishi, K.: Free access to a running-wheel advances the phase of behavioral and physiological circadian rhythms and peripheral molecular clocks in mice. PLoS One (2014).
  • Tomita, S., Nemoto, T., Matsuo, Y., Shoji, T., Tanaka, F., Nakagawa, H., Ono, H., Kikuchi, J., Ohnishi-Kameyama, M., Sekiyama, Y.: A NMR-based, non-targeted multistep metabolic profiling revealed L-rhamnitol as a metabolite that characterised apples from different geographic origins. Food Chem., 174, 163-172 (2014).
  • Oishi, K., Higo-Yamamoto, S.: Disrupted daily light-dark cycles induce physical inactivity and enhance weight gain in mice depending on dietary fat intake. Neuroreport., 25(11), 865-869 (2014).
  • Kondoh, D., Yamamoto, S., Tomita, T., Miyazaki, K., Itoh, N., Yasumoto, Y., Oike, H., Doi, R., Oishi, K.: Harmine lengthens circadian period of the Mammalian molecular clock in the suprachiasmatic nucleus. Biol Pharm. Bull., 37(8), 1422-1427 (2014).
  • Oishi, K., Yamamoto, S., Itoh, N., Miyazaki, K., Nemoto, T., Nakakita, Y., Kaneda, H.: Disruption of behavioral circadian rhythms induced by psychophysiological stress affects plasma free amino acid profiles without affecting peripheral clock gene expression in mice. Biochem. Biophys. Res. Commun., 450(1), 880-884 (2014).
  • Nakao, R., Yamamoto, S., Yasumoto, Y., Kadota, K., Oishi, K.: Impact of denervation-induced muscle atrophy on housekeeping gene expression in mice. Muscle. Nerve., DOI: 10.1002/mus.24310. (2014).
  • Wang, Q.,Hanatani, I., Takeda, M., Oishi, K., Sakamoto, K.: D2-like dopamine receptors mediate regulation of pupal diapause in the Chinese oak silkmoth Antheraea pernyi. Entomol.Sci., DOI: 10.1111/ens.12099. (2014).
  • Nakao, R., Yamamoto, S., Yasumoto, Y., Oishi, K.: Dosing schedule-dependent attenuation of dexamethasone-induced muscle atrophy in mice. Chronobiol. Int., 31(4), 506-514 (2014).
  • Oike, H., Oishi, K., Kobori, M.: Nutrients, Clock Genes, and Chrononutrition. Curr. Nutr. Rep., 3(3), 204-212 (2014).
  • Wang, Q., Takeda, M., Oishi, K., Sakamoto, K.: Melatonin pathway transmits information to terminate pupal diapause in the Chinese oak silkmoth, Antheraea pernyi, and through reciprocated inhibition of dopamine pathway functions as a photoperiodic counter. Entomol. Sci. (2014).


  • Miyazaki, K., Itoh, N., Yamamoto, S., Higo-Yamamoto, S., Nakakita, Y., Kaneda, H., Shigyo, T., Oishi, K.: Dietary heat-killed Lactobacillus brevis SBC8803 promotes voluntary wheel-running and affects sleep rhythms in mice. Life Sci., 111(1-2), 47-52 (2014).
  • Higo, K., Oda, M., Morii, H., Takahashi, J., Harada, Y., Ogawa, S., Abe, R.: Quantitative analysis by surface plasmon resonance of CD28 interaction with cytoplasmic adaptor molecules Grb2, Gads and p85 PI3K. Immunol. Invest., 43(3), 278-291 (2014).
  • Ogawa, Y., Kawano, Y., Yamazaki, Y, Onishi, Y.: Shikonin shortens the circadian period: possible involvement of Top2 inhibition. Biochem. Biophys. Res. Commun., 443, 339-343 (2014).


  • Kwon, H.J., Ohmiya, Y., Yasuda, K.: Simultaneous monitoring of intracellular ATP and oxygen levels in chondrogenic differentiation using a dual-color bioluminescence reporter. Luminescence, 29(8), 1194-1198 (2014).
  • Gao, R., Shah, N., Lee, JS., Katiyar, S.P., Li, L., Oh, E., Sundar, D., Yun, C-O., Wadhwa, R., Kaul, SC.: Withanone-rich combination of ashwagandha withanolides restricts metastasis and angiogenesis through hnRNP-K. Mol. Cancer Ther., 13(12), 2930-2940 (2014).
  • Dhanjal, JK., Nigam, N., Sharma, S., Chaudhary, A., Kaul, SC., Grover, A., Wadhwa, R.: Embelin inhibits TNF-α converting enzyme and cancer cell metastasis: molecular dynamics and experimental evidence. BMC Cancer, 14(1), 775 (2014).
  • Ryu, J., Kaul, Z., Yoon, A.R., Liu, Y., Yaguchi, T., Na, Y., Ahn, H.M., Gao, R., Choi, I.K., Yun, C.O., Kaul, S.C., Wadhwa, R.: Identification and functional characterization of nuclear mortalin in human carcinogenesis. J. Biol. Chem., 289(36), 24832-24844 (2014).
  • Kwon, HJ., Kurono, S., Kaneko, Y., Ohmiya, Y., Yasuda, K.: Analysis of proteins showing differential changes during ATP oscillations in chondrogenesis. Cell Biochem. Funct., 32(5), 429-437 (2014).
  • Cheung, C.T., Singh, R., Kalra, R.S., Kaul, S.C., Wadhwa, R.: Collaborator of ARF (CARF) regulates proliferative fate of human cells by dose-dependent regulation of DNA damage signaling. J. Biol. Chem., 289(26), 18258-18269 (2014).
  • Gao, R., Singh, R., Kaul, Z., Kaul, S.C., Wadhwa, R.: Targeting of DNA damage signaling pathway induced senescence and reduced migration of cancer cells. J. Gerontol. Ser. A-Biol. Sci. Med. Sci. (2014).
  • Sato, M., Nakanishi, K., Haga, S., Fujiyoshi, M., Baba, M., Mino, K., Yimin, Niwa, H., Yokoo, H., Umezawa, K., Ohmiya, Y., Kamiyama, T., Todo, S., Taketomi, A., Ozaki, M.: Anoikis induction and inhibition of peritoneal metastasis of pancreatic cancer cells by a nuclear factor-kappa B inhibitor, (-)-DHMEQ. Oncol. Res., 21(6), 333-343 (2014).
  • Ohtsuki, H., Yokoyama, J., Ohba, N., Ohmiya, Y., Kawata, M.: Expression of the nos gene and firefly flashing: A test of the nitric-oxide-mediated flash control model. J Insect Sci. 14(56) (2014).
  • Kwon, HJ., Yasuda, K., Gong, JP., Ohmiya, Y.: Polyelectrolyte hydrogels for replacement and regeneration of biological tissues. Macromol. Res., 22(3), 227-235 (2014).
  • Singh, R., Kalra, R.S., Hasan, K., Kaul, Z., Cheung, C.T., Huschtscha, L., Reddel, R.R., Kaul, S.C., Wadhwa, R.: Molecular characterization of collaborator of ARF (CARF) as a DNA damage response and cell cycle checkpoint regulatory protein. Exp. Cell Res., 322(2), 324-334 (2014).


  • Mizukami, M., Tokunaga, H., Onishi, H., Ueno, Y., Hanagata, H., Miyazaki, N., Kiyose, N., Ito, Y., Ishibashi, M., Hagihara, Y., Arakawa, T., Miyauchi, A., Tokunaga, M.: Highly efficient production of VHH antibody fragments in Brevibacillus choshinensis expression system. Protein Expr. Purif., 105, 23-32 (2015).
  • Kubo, I., Kanamatsu, T., Furutani, S.: Microfluidic device for enzyme-linked immunosorbent assay (ELISA) and its application to bisphenol a sensing. Sens. Mater., 26(8), 615-621 (2014).
  • Furutani, S., Shozen, N., Nagai, H., Aoyama, Y., Kubo, I.: Development of a detection system for expressed genes in isolated single jurkat cells. Sens. Mater., 26(8), 623-635 (2014).
  • Minamiki, T., Minami, T., Kurita, R., Niwa, O., Wakida, S., Fukuda, K., Kumaki, D., Tokito. S.: A label-free immunosensor for IgG based on an extended-gate type organic field effect transistor. Materials, 7(9), 6843-6852 (2014).
  • Miyashita, H., Chikazawa, M., Otaki, N., Hioki, Y., Shimozu, Y., Nakashima, F., Shibata, T., Hagihara, Y., Maruyama, S., Matsumi, N., Uchida, K.: Lysine pyrrolation is a naturally-occurring covalent modification involved in the production of DNA mimic proteins. Sci Rep., 4, 5343 (2014).
  • Minamiki, T., Minami, T., Kurita, R., Niwa, O., Wakida, S., Fukuda, K., Kumaki, D., Tokito, S.: Accurate and reproducible detection of proteins in water using an extended-gate type organic FET biosensor. Appl. Phys. Lett., 104, 243703 (2014).
  • Furutani, S., Naruishi, N., Saito, M., Tamiya, E., Fuchiwaki, Y., Hidenori, N.: Rapid and highly sensitive detection by a real-time polymerase chain reaction using a chip coated with its reagents. Anal. Sci., 30(5), 569-574 (2014).
  • Akazawa-Ogawa, Y., Takashima, M., Lee, Y-H., Ikegami, T., Goto, Y., Uegaki, K., Hagihara, Y.: Heat-induced irreversible denaturation of the camelid single domain VHH antibody is governed by chemical modifications. J. Biol. Chem., 289(22), 15666-15679 (2014).
  • Kurinomaru, T., Tomita, S., Hagihara, Y., Shiraki, K.: Enzyme hyperactivation system based on a complementary charged pair of polyelectrolytes and substrates. Langmuir, 30(13), 3826-3831 (2014).
  • Yamazoe, H., Sugiyama, Y., Omri, A.E., Hagihara, Y., Okada, T.: Facile immunostaining and labeling of nonadherent cells using a microfluidic device to entrap the cells. J. Biosci. Bioeng., 117(3), 375-378 (2014).
  • Horie, M., Nishio, K., Kato, H., Endoh, S., Fujita, K., Nakamura, A., Hagihara, Y., Yoshida, Y., Iwahashi, H.: Evaluation of cellular effects of silicon dioxide nanoparticles. Toxicol. Mech. Methods, 24(3), 196-203 (2014).
  • Horie, M., Nishio, K., Kato, H., Endoh, S., Fujita, K., Nakamura, A., Kunugasa, S., Hagihara, Y., Yoshida, Y., Iwahashi, H.: Evaluation of cellular influences caused by calcium carbonate nanoparticles. Chem.-Biol. Interact., 210, 64-76 (2014).



  • Ohtsuka, Y., Matsumoto, J., Katsuyama, Y., Okamura, Y.: Nodal signaling regulates specification of ascidian peripheral neurons through control of the BMP signal. Development., 141(20), 3889-3899 (2014).


  • Nakayama, T., Sakuraba, T., Tomita, S., Kaneko, A., Takai, E., Shiraki, K., Tashiro, K., Ishii, N., Hasegawa, Y., Yamada, Y., Kumai, R., Yamamoto, Y.: Charge-separated fmoc-peptide β-sheets: Sequence-secondary structure relationship for arranging charged side chains on both sides. Asian J. Org. Chem., 3(11), 1182-1188 (2014).
  • Ishii, N.: Two-dimensional crystalline array formations of proteins by use of the self-assembled monolayer at the air/water interface. Microscopy: advances in scientific research and education, 6(2), 929-935 (2014).
  • Takeshita, D., Yamashita, S., Tomita, S.: Molecular insights into replication initiation by Qβ replicase using ribosomal protein S1. Nucl. Acids Res., 42(16), 10809-10822 (2014).
  • Yamamoto, YY., Abe, Y., Moriya, K., Arita, M., Noguchi, K., Ishii, N., Sekiguchi, H., Sasaki, YC., Yohda, M.: Inter-ring communication is dispensable in the reaction cycle of group II chaperonins. J. Mol. Biol., 426(14), 2667-2678 (2014).
  • Murakami, K., Miyagishi, M.: Tiny masking LNAs effectively bind to mRNA and inhibit binding of microRNAs in relation to thermo dynamical stability. Biomedical Reports, 2(4), 509-512 (2014).
  • Ohnuma, T., Umemoto, N., Nagata, T., Shinya, S., Numata, T., Taira, T., Fukamizo, T.: Crystal structure of a "loopless" GH19 chitinase in complex with chitin tetrasaccharide spanning the catalytic center. BBA-Proteins Proteomics, 1844(4), 793-802 (2014).
  • Arano, T., Fujisaki, S., Ikemoto, MJ.: Identification of tomoregulin-1 as a novel addicsin-associated factor. Neurochem. Int., 71, 22-35(2014).
  • Tong,L., Kushida,S., Kuwabara,J., Kanbara,T., Ishii,N., Saeki,A., Seki,S., Furumi,S., Yamamoto,Y.:Tetramethylbithiophene in π-conjugated alternating copolymers as an effective structural component for the formation of spherical assemblies. Polym. Chem., 5, 3583-3587 (2014).
  • Yamashita, S., Takeshita, D., Tomita, K.: Translocation and rotation of tRNA during template-independent RNA polymerization by tRNA nucleotidyltransferase. Structure, 22(2), 315-325 (2014).
  • Garzoni, M., Okuro, K., Ishii, N., Aida, T., Pavan, G.M.: Structure and shape effects of molecular glue on supramolecular tubulin assemblies. ACS Nano, 8(1), 904-914 (2014).


  • Wada, S., Kato, Y., Sawada, S., Aizawa, K., Park, J.H., Russell, A.P., Ushida, T., Akimoto, T.: MicroRNA-23a has minimal effect on endurance exercise-induced adaptation of mouse skeletal muscle. Pflugers Arch., 467(2), 389-398 (2014).
  • Shimbo, K., Miyaki, S., Ishitobi, H., Kato, Y., Kubo, T., Shimose, S., Ochi, M.: Exosome-formed synthetic microRNA-143 is transferred to osteosarcoma cells and inhibits their migration. Biochem. Biophys. Res. Commun., 445(2), 381-387 (2014).


  • Mine, S., Kado, Y., Watanabe, M., Fukuda, Y., Abe, Y., Ueda, T., Kawarabayasi, Y., Inoue, T., Ishikawa, K.: The structure of hyperthermophilic β-N-acetylglucosaminidase reveals a novel dimer architecture associated with the active site. FEBS J., 281(22), 5092-5103 (2014).
  • Okayama, T., Yokoi, S., Abe, H., Isoe, Y., Suehiro, Y., Imada, H., Tanaka, M., Kawasaki, T., Yuba, S., Taniguchi, Y., Kamei, Y., Okubo, K., Shimada, A., Naruse, K., Takeda, H., Oka, Y., Kubo, T., Takeuchi, H.: A neural mechanism underlying mating preferences for familiar individuals in medaka fish. Science, 343(6166), 91-94 (2014).



  • Kiyama, R., Zhu, Y., Kawaguchi, K., Iitake, N., Wada-Kiyama, Y., Dong, S.: Estrogen-responsive genes for environmental studies. Env. Tech. Innovation., 1-2, 16-28 (2014).
  • Yoo, H.B., Oh, D., Song, J.Y., Kawaharasaki, M., Hwang, J., Yang, I.C., Park, S.R.: A candidate reference method for quantification of low concentrations of plasmid DNA by exhaustive counting of single DNA molecules in a flow stream. Metrologia, 51(5), 491-502 (2014).
  • Gopinath, SC., Kumar, P.K.R.: Biomolecular discrimination analyses by surface plasmon resonance. Analyst. 139(11), 2678-2682 (2014).
  • Kiyama, R., Zhu, Y.: DNA microarray-based gene expression profiling of estrogenic chemicals. Cell. Mol. Life Sci., 71(11), 2065-2082 (2014).
  • Wuxiuer, D. Zhu, Y., Ogaeri, T., Mizuki, K., Kashiwa, Y., Nishi, K., Isobe, S., Aoyagi, T., Kiyama, R.: Development of pathological diagnostics of human kidney cancer by multiple staining using new fluorescent Fluolid dyes. Biomed Res. Int., 2014, 437871 (2014).
  • Soo, R.M., Skennerton, C.T., Sekiguchi, Y., Imelfort, M., Paech, S.J., Dennis, P.G., Steen, J.A., Parks, D.H., Tyson, G.W., Hugenholtz, P.: An expanded genomic representation of the phylum cyanobacteria. Genome. Biol. Evol., 6(5), 1031-1045 (2014).
  • Qiu, Y.L., Hanada, S., Kamagata, Y., Guo, R.B., Sekiguchi, Y.: Lactivibrio alcoholicus gen. nov., sp. nov., an anaerobic, mesophilic lactate-, alcohol-, carbohydrate- and amino-acid-degrading bacterium in Aminobacteria classis nov. within the phylum Synergistetes. Int. J. Syst. Evol. Microbiol., 64, 2137-2145 (2014).
  • Kumar, P.K.R., Mizuno, H.: Metal ion-dependent anti-termination of transcriptional regulation of ribonucleoprotein complexes. Biophys. Rev. 6(2), 215-226 (2014).
  • Harada, K., Aoyama, S., Matsugami, A., Kumar, P.K.R., Katahira, M., Kato, N., Ohkanda, J.: RNA-directed amino acid coupling as a model reaction for primitive coded translation. ChemBioChem., 15(6), 794-798 (2014).
  • Suenaga, E., Penmetcha K.R. Kumar.: An aptamer that binds efficiently to the hemagglutinins of highly pathogenic avian influenza viruses (H5N1 and H7N7) and inhibits hemagglutinin?glycan interactions. Acta Biomater., 10(3), 1314-1323 (2014).
  • Hayashi, K., Onoue, H., Sasaki, K., Lee, J.B., Kumar, P.K.R., Gopinath, S.C.B., Maitani, Y., Kai, T., Hayashi, T.: Topical application of polyethylenimine as a candidate for novel prophylactic therapeutics against genital herpes caused by herpes simplex virus. Arch. Virol., 159(3), 425-435 (2014).
  • Nakamoto, H., Fujita, K., Ohtaki, A., Watanabe, S., Narumi, S., Maruyama, T., Suenaga, E., Misono, TS., Kumar, P.K.R., Goloubinoff, P., Yoshikawa, H.: Physical interaction between bacterial heat shock protein (Hsp) 90 and Hsp70 chaperones mediates their cooperative action to refold denatured proteins. J. Biol. Chem., 289(9), 6110-6119 (2014).
  • Hanazato, M., Nakato, G., Nishikawa, F., Hase, K., Nishikawa, S., Ohno, H.: Selection of an aptamer against mouse GP2 by SELEX. Cell Struct. Funct., 39(1), 23-29 (2014).


  • Moritomo, H., Yamada, K., Kojima, Y., Suzuki, Y., Tani, S., Kinoshita, H., Sasaki, A., Mikuni, S., Kinjo, M., Kawamata, J.: A biphenyl type two-photon fluorescence probe for monitoring the mitochondrial membrane potential. Cell Struct. Funct., 39(2), 125-133 (2014).
  • Takei, H., Morishita, S., Araki, M., Edahiro, Y., Sunami, Y., Hironaka, Y., Noda, N., Sekiguchi, Y., Tsuneda, S., Ohsaka, A., Komatsu, N.: Detection of MPLW515L/K mutations and determination of allele frequencies with a single-tube PCR assay. PLoS ONE, 9(8), e104958. (2014).
  • Kishida, N., Noda, N., Haramoto, E., Kawaharasaki, M., Akiba, M., Sekiguchi, Y.: Quantitative detection of human enteric adenoviruses in river water by microfluidic digital polymerase chain reaction. Water Sci. Technol., 70(3), 555-560 (2014).
  • Edahiro, Y., Morishita, S., Takahashi, K., Hironaka, Y., Yahata, Y., Sunami, Y., Shirane, S., Tsutsui, M., Noguchi, M., Koike, M., Imai, K., Kirito, K., Noda, N., Sekiguchi, Y., Tsuneda, S., Ohsaka, A., Araki, M., Komatsu, N.: JAK2V617F mutation status and allele burden in classical Ph-negative myeloproliferative neoplasms in Japan. Int. J. Hematol., 99(5), 625-634 (2014).
  • Salam, KA., Furuta, A., Noda, N., Tsuneda, S., Sekiguchi, Y., Yamashita, A., Moriishi, K., Nakakoshi, M., Tani, H., Roy, SR., Tanaka, J., Tsubuki, M., Akimitsu, N.: PBDE: structure-activity studies for the inhibition of hepatitis C virus NS3 helicase. Molecules., 19(4), 4006-4020 (2014).
  • Furuta, A., Kazi Abdus Salam, Idam Hermawan, Akimitsu, N., Tanaka, J., Tani, H., Yamashita, A., Moriishi, K., Nakagoe, M., Tsubuki, M., Poh Wee Peng, Suzuki, Y., Yamamoto, N., Sekiguchi, Y., Tsuneda, S., Noda, N.: Identification and Biochemical Characterization of Halisulfate 3 and Suvanine as Novel Inhibitors of Hepatitis C Virus NS3 Helicase from a Marine Sponge. Mar. Drugs, 12, 462-476 (2014).


  • Tomita, S., Soejima, T., Shiraki, K., Yoshimoto, K.: Enzymatic fingerprinting of structurally similar homologous proteins using polyion complex library constructed by tuning PEGylated polyamine functionalities. Analyst, 139(23), 6100-6103 (2014).
  • Yanagisawa, H., Kurita, R., Kamata, T., Kato, D., Niwa, O.: Anodic stripping voltammetric determination of Cd and Pb with nanocarbon film electrode fabricated by unbalanced magnetron sputtering. Electrochemistry, 82(11), 949-953 (2014).
  • Kamata,T., Katoa, D., Ida, H., Niwa, O. : Structure and electrochemical characterization of carbon films formed by unbalanced magnetron (UBM) sputtering method. Diam. Relat. Mat., 49, 25-32 (2014).
  • Sato, Y., Yoshioka, K., Murakami, T., Tanaka, M., Niwa, O.: Thick-matrix-free interface for highly effective protein detection and sufficient signal enhancement. Compos. Interfaces, 21(7), 631-638 (2014).
  • Guo, Q., Liu, D., Zhang, X., Li, L., Hou, H., Niwa, O., You, T. : Pd-Ni alloy nanoparticle/carbon nanofiber composites: preparation, structure, and superior electrocatalytic properties for sugar analysis. Anal. Chem. , 86(12), 5898-5905 (2014).
  • Yosioka, K., Kato, D., Kamata, T., Niwa, O.: High performance of DET-type bioelectrocatalysis of cytochrome c on indium tin oxide film electrode with enzyme-sized nanostructure. Electrochemistry, 82(5), 322-324 (2014).
  • Liu, D., Guo, Q., Hou, H., Niwa, O., and You, T. : PdxCoy nanoparticle/carbon nanofiber composites with enhanced electrocatalytic properties. ACS Catal., 4(6), 1825-1829(2014).
  • Kato, D., Oda, A., Tanaka, M., Iijima, S., Kamata, T., Todokoro, M., Yoshimi, Y., Niwa, O.: Poly-ε-Lysine Modified Nanocarbon Film Electrodes for LPS Detection. Electroanalysis, 26, 618-624 (2014).


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