Journal (年をクリックで表示/非表示切替え)
  1. Tsugita, A., Uehara, S., Matsui, T., Yokoyama, T., Ostash, I., Deneka, M., Yalamanchili, S., Bennett, C. S., Tanaka, Y., and Ostash, B.
    The carbohydrate tail of landomycin A is responsible for its interaction with the repressor protein LanK
    FEBS J., in press(2022)[link]
  2. Ghanem, N., Kanagami, N., Matsui, T., Takeda, K., Kaneko, J., Shiraishi, Y., Choe, C. A., Uchikubo-Kamo, T., Shirouzu, M., Hashimoto, T., Ogawa, T., Matsuura, T., Po-Ssu, H., Yokoyama, T., and Tanaka, Y.
    Chimeric mutants of staphylococcal hemolysin, which act as both one-component and two-component hemolysin, created by grafting the stem domain
    FEBS J., in press(2022)[link]
  3. Tagami, T., Chen M., Furunaga Y., Kikuchi A., Sadahiro J., Lang W., Okuyama M., Tanaka Y., Iwasaki T., Yao M., and Kimura A.
    Structural insights reveal the second base catalyst of isomaltose glucohydrolase
    FEBS J., 2891118-1134 (2022) [link]
  1. Ishida, K., Tsukamoto, Y., Horitani, M., Ogawa, T., and Tanaka, Y.
    Biochemical properties of CumA multicopper oxidase from plant pathogen, Pseudomonas syringae
    Biosci. Biotech. Biochem., 85 1995-2002 (2021) [link]
  2. Makabe, K., Yokoyama, T., Uehara, S., Uchikubo-kamo, T., Shirouzu, M., Kimura, K., Tsumoto, K., Asano, R., Tanaka, Y., and Kumagai, I.
    Anti-EGFR antibody 528 binds to domain Ⅲ of EGFR at a site shifted from the cetuximab epitope
    Sci. Rep., 11 5790 (2021) [link]
  3. Makabe, K., Hirota, R., Shiono, Y., Tanaka, Y., and Koseki, T.
    Biochemical and structural investigation of rutinosidase from Aspergillus oryzae
    Appl. Env. Microbiol., 15, e02438-20 (2021) [link]
  1. Takeda, K., Tanaka, Y., Kaneko, J.
    The N-terminal amino-latch region of Hlg2 component of staphylococcal bi-component γ-haemolysin is dispensable for prestem release to form β-barrel pores
    J. Biochem., 168 349-354 (2020) [link]
  2. Nakazawa, H., Onodera-Sugano, T., Sugiyama, A., Tanaka, Y., Hattori, T., Niide, T., Ogata, H., Asano, R., Kumagai, I., and Umetsu, M.
    Association behavior and control of the quality of cancer therapeutic bispecific diabodies expressed in Escherichia coli
    Biochem. Eng. J., 160, 107636 (2020) [link]
  3. Wakui, H., Tanaka, Y., Ose, T., Matsumoto, I., Kato, K., Min, Y., Tachibana, T., Sato, M., Naruchi, K., Martin F., Hinou, H., and Nishimura, S-I.
    A straightforward approach to antibodies recognising cancer specific glycopeptidic neoepitopes
    Chemical Sci., 11 4999-5006 (2020) [PubMed]
  4. Chen, M., Ishizaka, M., Narai, S., Horitani, M., Shigi, N., Yao, M., and Tanaka, Y.
    The [4Fe-4S] cluster of sulfurtransferase TtuA desulfurizes TtuB during tRNA modification in Thermus thermophilus
    Commun. Biol., 3, 168 (2020) [PubMed]
  1. Yano, S., Suyotha, W., Oguro, N., Matsui, T., Shiga, S., Itoh, T., Hibi, T., Tanaka, Y., Wakayama, M., Makabe, K.
    Crystal structure of the catalytic unit of GH 87-type α-1,3-glucanase Agl-KA from Bacillus circulans
    Sci.Rep., 9, 15295 (2019) [PubMed]
  2. Ogawa, T., Oda-Ueda, N., Hisata, K., Nakamura, N., Chijiwa, T., Hattori, S., Isomoto, A., Yugeta, H., Yamasaki, S., Fukumaki, Y., Ohno, M, Satoh, N., Shibata, H.
    Alternative mRNA Splicing in Three Venom Families Underlying a Possible Production of Divergent Venom Proteins of the Habu Snake, Protobothrops flavoviridis
    Toxins, 11, 581 (2019) [PubMed]
  3. Ogawa, T., Sato, R., Naganuma, T., Liu, K., Lakudzala, AE, Muramoto, K., Osada, M., Yoshimi, K., Hiemori, K., Hirabayashi, J., Tateno, H.
    Glycan Binding Profiling of Jacalin-Related Lectins from the Pteria Penguin Pearl Shell.
    Int. J. Mol. Sci., 20, 4629 (2019) [PubMed]
  4. Hashimoto, T., Ye, Y., Ui, M., Ogawa, T., Matsui, T., and Tanaka, Y.
    Protein encapsulation in the hollow space of hemocyanin crystals containing a covalently conjugated ligand
    Biochem. Biophys. Res. Commun., 51, 31-36 (2019) [PubMed]
  5. Tanaka Y., Kato S., Stabrin S., Raunser S., Matsui T., Gatsogiannis C.
    CryoEM reveals the asymmetric assembly of squid hemocyanin
    IUCrJ, 6, 426-437 (2019) [PubMed]
  6. Shibata, H., Oda-Ueda, N., Chijiwa, T., Nakamura, H., Yamaguchi,K., Hattori, S., Matsubara, K., Matsuda, K., Isomoto, A, Koyanagi, R., Hisata, K., Fukumaki, Y., Ohno, M., Shoguchi, E., Satoh, N., Ogawa, T.
    Whole genome sequencing of a Japanese endemic pit viper, habu, Protobothrops flavoviridis reveals accelerated evolution of venom protein genes enriched in microchromosomal regions
    Toxincon, 159, S9 (2019) [PubMed]
  7. Nakae.S., Shionyu M., Ogawa.T., Shirai T.
    Crystallization of Pearl Biomineralization Protein in Microgravity Environments.
    Int. J. Microgravity Sci. Appl., 36, 360105 (2019) [link]

  8. Matsui T., Kamata S., Ishii K., Maruno T., Ghanem N., Uchiyama S., Kato K., Suzuki A., Oda-Ueda N., Ogawa T. and Tanaka, Y.
    SDS-induced oligomerization of Lys49-phospholipase A2 from snake venom
    Sci. Rep., 9, 2330 (2019) [PubMed]
  9. Hashimoto T., Ye Y., Matsuno A.,Ohnishi Y., Kitamura A., Kinjo M., Abe S., Ueno T., Yao M., Ogawa T., Matsui T., and Tanaka, Y.
    Encapsulation of biomacromolecules by soaking and co-crystallization into porous protein crystals of hemocyanin
    Biochem. Biophys. Res. Commun., 509, 577?584 (2019) [PubMed]

  1. Ogawa.T., Sekikawa A., Sato H., Muramoto K., Shibata H., Hattori S.
    Proteomic Analysis of Venomous Fang Matrix Proteins of Protobothrops flavoviridis (Habu) Snake.
    In: Biomineralization. From Molecular and Nano-structural Analyses to Environmental Science. [link]

  2. Nakae S., Shionyu M., Ogawa.T., Shirai T.
    Structures of jacalin-related lectin PPL3 regulating pearl shell biomineralization.
    PROTEINS: Structure, Function, and Bioinformatics, 86, 644-653 (2018) [PubMed]
  3. Shibata.H., Chijiwa.T., Oda-Ueda N., Nakamura H., Yamaguchi K., Hattori S., Matsubara K., Matsuda Y., Yamashita A., Isomoto A., Mori K., Tashiro K., Kuhara S., Yamasaki S., Fujie M., Goto H., Koyanagi R., Takeuchi T., Fukumaki Y., Ohno M., Shoguchi E., Hisata K., Satoh N., Ogawa.T.
    The habu genome reveals accelerated evolution of venom protein genes.
    Sci.Rep., 8, 10.1038 (2018) [PubMed]
  4. Takeda K., Tanaka, Y., Abe N., and Kaneko J.
    Intermolecular ionic interactions serve as a possible switch for stem release in the staphylococcal bi-component toxin for β-barrel pore assembly
    Toxicon, 151, 43-48 (2018) [PubMed]
  5. Fujii, H., Tanaka, Y., Nakazawa, H., Sugiyama, A., Manabe, N., Shinoda, A., Shimizu, N., Hattori, T., Hosokawa, K., Sujino, T., Ito, T., Niide, T., Asano, R., Kumagai, I., and Umetsu, M.
    Compact Seahorse-Shaped T Cell-Activating Antibody for Cancer Therapy
    Adv. Therapeut., 1, 1700031 (2018) [Wiley]

  6. Peng, Z., Takeshita, M., Shibata, N., Tada, H., Tanaka, Y., and Kaneko, J.
    Rim domain loops of Staphylococcal β-pore forming bi-component toxin S-components 3 recognize target human erythrocytes in a coordinated manner,
    J. Biochem., 164, 93-102 (2018) [PubMed]
  7. Uchida, T., Funamizu, T., Chen, M., Tanaka, Y., and Ishimori, K.
    Heme Binding to Porphobilinogen Deaminase from Vibrio cholerae Decelerates the Formation of 1-Hydroxymethylbilane
    ACS Chem. Biol., 13, 750-760 (2018) [PubMed]
  1. Ogawa.T., Hirakakiuchi I., Tsubono M., Sato R., Yukawa M., Muramoto K. Shirai T.
    Molecular mechanism of derivation of anti-cancer peptide, lunasin, from 2S albumin, and its application to the processed foods of soybean.
    Soy Protein Res, 20, 47-51 (2017) [link]
  2. Chen, M., Kubo, M., Kato, K., Tanaka, Y., Liu, Y., Long, F., Whitman, W., Lill, P., Gatsogiannis, C., Raunser, S., Shimizu, N., Shinoda, A., Nakamura, A., Tanaka, I., and Yao, M.
    Structural basis for tRNA-dependent cysteine biosynthesis
    Nature Commun., 8, 1512 (2017) [PubMed]
  3. Kunthic, T., Watanabe, H., Kawano, R., Tanaka,Y., Promdonkoy, B., Yao, M., and Boonserm, P.
    pH Regulates Pore Formation of a Protease Activated Vip3Aa from Bacillus thuringiensis.
    BBA Biomembranes, 1859, 2234-2241 (2017) [PubMed]
  4. Chen, M., Asai, S., Narai, S., Nambu, S., Omura, N., Sakaguchi, Y., Suzuki, T., Ikeda-Saito, M., Watanabe, K., Yao, M., Shigi, N., and, Tanaka, Y.
    Biochemical and structural characterization of oxygen-sensitive 2-thiouridine synthesis catalyzed by the iron-sulfur protein TtuA.
    Proc. Natl. Acad. Sci. USA, 114, 4954-4959 (2017) [PubMed]
  5. Miyabe, Y., Furuta, T., Takeda, T., Kanno, G., Shimizu, T., Tanaka, Y., Gai, Z., Yasui, H., and Kishimura, H.
    Structural properties of phycoerythrin from dulse palmaria palmata.
    J. Food Biochem., 41, e12301 (2017) [Wiley]

  6. Katow H., Kanaya T., Ogawa T., Egawa R., Yawo H.
    Regulation of axon arborization pattern in the developing chick ciliary ganglion: Possible involvement of caspase 3.
    Dev. Growth Differ., 59, 115-128 (2017) [PubMed]
  7. Kuroishi T., Bando K., Tanaka Y., Shishido K., Kinbara M., Ogawa T., Muramoto K., Endo Y., Sugawara S.
    CXCL4 is a novel nickel-binding protein and augments nickel allergy.
    Clin. Exp. Allergy, 2017, 1-10 (2017) [PubMed]

  8. Matsui T., Kodama T., Mori T., Tadakoshi T., Noguchi H., Abe I., Morita H.
    2-Alkylquinolone alkaloid biosynthesis in the medicinal plant Evodia rutaecarpa involves collaboration of two novel type III polyketide synthases.
    J. Biol. Chem., 292, 9117-9135 (2017) [PubMed]

  9. Matsui T., Lallo S., Nisa K., Morita H.
    Filamenting temperature-sensitive mutant Z inhibitors from Glycyrrhiza glabra and their inhibitory mode of action.
    Bioorg. Med. Chem. Lett., 27, 1420-1424 (2017) [PubMed]

  1. Chen, M., Narai, S., Omura, N., Shigi, N., Chimnaronk, S., Tanaka, Y., and Yao, M., Crystallographic Study of Two-Thiouridine Synthetic Complex TtuA-TtuB from Thermus thermophilus. Acta Crystallogr. F., F72, 777-781 (2016)
  2. Oshima, K., Kakiuchi, Y., Tanaka, Y., Ueda, T., Nakashima, T., Kimura, M., and Yao, M., Structural basis for recognition of a kink-turn motif by an archaeal homologue of human RNase P protein Rpp38. Biochem. Biophys. Res. Commun., 474, 541-546 (2016)
  3. Sekine, Y., Tanzawa, T., Tanaka, Y., Ishimori, K., and Uchida, T., Cytoplasmic Heme-binding Protein (HutX) from Vibrio cholerae is an Intracellular Heme Transport Protein for the Heme-degrading Enzyme, HutZ. Biochemistry, 55, 884-893 (2016)
  4. Yamazaki T., Ogawa T., Muramoto K., Nakahigashi J., Takeuchi A., Ueda H., Isolation and Biochemical Characterization of Mucus Proteins in Japanese Bunching Onion (Allium fistulosum) Green Leaves. Food Sci. Technol. Res., 22, 235-243 (2016)
  5. Win NN., Ito T., Matsui T., Aimaiti S., Kodama T., Ngwe H., Okamoto Y., Tanaka M., Asakawa Y., Abe I., Morita H., Isopimarane diterpenoids from Kaempferia pulchra rhizomes collected in Myanmar and their Vpr inhibitory activity. Bioorg. Med. Chem. Lett., 26, 1789-1793 (2016)
  6. Nisa K., Ito T., Matsui T., Kodama T., Morita H., New acylphloroglucinol derivatives from the leaves of Baeckea frutescens. Phytochem. Lett., 15, 42-45 (2016)
  7. Yang X., Matsui T., Kodama T., Mori T., Zhou X., Taura F., Noguchi H., Abe I., Morita H., Structural basis for olivetolic acid formation by a polyketide cyclase from Cannabis sativa. FEBS J., 283, 1088-1106 (2016)
  1. Uchida, T., Sasaki, M., Tanaka, Y., and Ishimori, K., A dye-decolorizing peroxidase from Vibrio cholera. Biochemistry, 54, 6610-6621 (2015)
  2. Sugawara, T., Yamashita, D., Kato, K., Peng, Z., Ueda, J., Kaneko, J., Kamio, Y., Tanaka, Y., and Yao, M., Structural basis for pore-forming mechanism 1 of staphylococcal α-hemolysin. Toxicon, 108, 226-231 (2015)
  3. Gai, Z., Matsuno, A., Kato, K., Kato, S.,Khan, R.I., Shimizu, T., Yoshioka, T., Kato, Y., Kishimura, H., Kanno, G., Miyabe, Y., Terada, T., Tanaka, Y., and Min Yao, Crystal structure of the 3.8 MDa respiratory supermolecule hemocyanin at 3.0 angstrom resolution. Structure, 23, 2204-2212 (2015)
  4. Sasaki, R., Kitazawa, S., Kitahara, R., Nakazawa, H., Tanaka, Y., Kumagai, I., Umetsu, M., and Makabe, K., Zinc ion-binding activity of an anti-ZnO VHH antibody, 4F2. Chem. Letters, 44, 1309-1311 (2015)
  5. Matsuno, A., Gai, Z., Tanaka, M., Kato, K., Kato, S., Katoh, T., Shimizu, T., Yoshioka, T., Kishimura, H., Tanaka, Y., and Yao, M., Crystallization and preliminary X-ray crystallographic study of a 3.8-MDa respiratory supermolecule hemocyanin. J. Struct. Biol., 190, 379-382 (2015)
  6. Ohashi Y., Onuma R., Naganuma T., Ogawa T., Naude R., Nokihara K., Muramoto K., Antioxidant Properties of Tripeptides Revealed by a Comparison of Six Different Assays. Food Sci. Technol. Res., 21, 685-693 (2015)
  7. Nemoto R., Yamamoto S., Ogawa T., Naude R., Muramoto K., Effect of Chum Salmon Egg Lectin on Tight Junctions in Caco-2 Cell Monolayers. Molecules, 20, 8094-8098 (2015)
  8. Kenmochi K., Kabir SR., Ogawa T., Naude R., Tateno H., Hirabayashi J., Muramoto K., Isolation and Biochemical Characterization of Apios Tuber Lectin. Molecules, 20, 987-1002 (2015)
  9. Yang X., Matsui T., Mori T., Taura F., Noguchi H., Abe I., Moriat H., Expression, purification and crystallization of a plant polyketide cyclase from Cannabis sativa. Acta Crystallogr. F., F71, 1470-1474 (2015)
  10. Mori T., Hoshino S., Sahashi S., Wakimoto T., Matsui T., Morita H., Abe I., Structural basis for β-carboline alkaloid production by the microbial homodimeric enzyme McbB. Chem. & Biol., 22, 898-906 (2015)
  11. Mori T., Yang D., Matsui T., Hashimoto M., Morita H., Fujii I., Abe I., Structural basis for the formation of acylalkylpyrones from two β-ketoacyl units by the fungal type III polyketide synthase CsyB. J. Biol. Chem., 290, 5214-5225 (2015)
  12. Noike M., Matsui T., Ooya K., Sasaki I., Ohtaki S., Hamano Y., Maruyama C., Ishikawa J., Satoh Y., Ito H., Morita H., Dairi T., A peptide ligase and the ribosome cooperate to synthesize the peptide pheganomycin. Nature Chem. Biol., 11, 71-76 (2015)
  1. Ito, S., Horikawa, S., Suzuki, T., Kawauchi, H., Tanaka, Y., Suzuki, T., and Suzuki, T., Human NAT10 is an ATP-dependent RNA acetyltransferase responsible for N4-acetylcytidine formation in 18S rRNA. J. Biol. Chem., 289, 35724-35730 (2014)
  2. Yamashita, D., Sugawara, T., Takeshita, M., Kaneko, J., Kamio, Y., Tanaka, I., Tanaka, Y., and Yao, M., Molecular basis of transmembrane beta-barrel formation of staphylococcal pore-forming toxins. Nature Commun., 5, 4897 (2014)
  3. Hayashi, T., Tanaka, Y., Sakai, N., Okada, U., Yao, M., Watanabe, N., Tamura, T., and Tanaka, I., Structural and genomic DNA analysis of the putative TetR transcriptional repressor SCO7518 from Streptomyces coelicolor A3(2). FEBS Letters, 588, 4311-4318 (2014)
  4. Shinoda, A., Tanaka, Y., Yao, M., and Tanaka, I., Anchoring protein crystals to mounting loops with hydrogel using inkjet technology. Acta Cryst. D., D70 2794-2799 (2014)
  5. Ushijima, Y., Ohniwa, R., Maruyama, A., Saito, S., Tanaka, Y., and Morikawa, K., Nucleoid compaction by MrgAAsp56Ala/Glu60Ala does not contribute to staphylococcal cell survival against oxidative stress and phagocytic killing by macrophage. FEMS Microbiol. Letters, 360, 144-151 (2014)
  6. Suzuki, T., Yamashita, K., Tanaka, Y., Tanaka, I., and Yao, M., Crystallization and preliminary X-ray crystallographic analysis of a bacterial Asn-transamidosome. Acta Cryst. F., F70, 790-793 (2014)
  7. Asano, N., Atsuumi, H., Nakamura, A., Tanaka, Y., Tanaka, I., and Yao, M., Direct interaction between EFL1 and SBDS is mediated by an intrinsically disordered insertion domain. Biochem. Biophys. Res. Commun., 443, 1251-1256 (2014)
  8. Naganuma T., Hoshino W., Shikanai Y., Sato R., Liu K., Sato S., Muramoto K., Osada M., Yoshimi K., Ogawa T., Novel Matrix Proteins of Pteria penguin Pearl Oyster Shell Nacre Homologous to the Jacalin-Related β-Prism Fold Lectins. PLos ONE, 9 e112326 (2014)
  9. Frank OA., Frost C., Smith N, Ogawa T., Muramoto K., Oliva MLV., Graf L., Naude R., Biochemical characterization of Acacia schweinfurthii serine proteinase inhibitor. J. Enz. Inh. Med. Chem., 29 633-638 (2014)
  10. Yang D., Mori T., Matsui T., Hashimoto M., Morita H., Fujii I., Abe I., Expression, purification and crystallization of a fungal type III polyketide synthase that produces the csypyrones. Acta Crystallogr. F., F70 730-733 (2014)
  11. Matsui T., Han X., Yu J., Yao M., Tanaka I., Structural Change in FtsZ Induced by Intermolecular Interactions between Bound GTP and the T7 loop. J. Biol. Chem., 289 3501-3509 (2014)
  1. Miyafusa, T., Caaveiro, J.M., Tanaka, Y., and Tsumoto, K., Dynamic elements govern the catalytic activity of CapE, a capsular polysaccharide-synthesizing enzyme from Staphylococcus aureus. FEBS Letters, 587, 3824-3830 (2013)
  2. Matsumoto, K., Tanaka, Y., Watanabe, T., Motohashi, R., Ikeda, K., Tobitani, K., Yao, M., Tanaka, I., and Taguchi, S., Directed evolution and structural analysis of NADPH-dependent acetoacetyl-CoA reductase from Ralstonia eutropha reveals two mutations responsible for enhanced kinetics. Appl. Env. Microb., 79, 6134-6139 (2013)
  3. Gai, Z., Nakamura, A., Tanaka, Y., Hirano, N., Tanaka, I., and Yao, M., Crystal structure analysis, overexpression and refolding behavior of a DING protein with single mutation. J. Synchrotron Rad., 20, 854-858 (2013)
  4. Chen, M., Yu, J., Tanaka, Y., Tanaka, M., Tanaka, I., and Yao, M., Crystal structure of dihydrouridine synthase C (DusC) from Escherichia coli. Acta Cryst. F., F69, 834-838 (2013)
  5. Sugawara, T., Yamashita, D., Tanaka, Y., Kaneko, J., Kamio, Y., Tanaka, I., and Yao, M., Preliminary X-ray crystallographic study of staphylococcal α-hemolysin monomer. Acta Cryst. F., F69, 868-870 (2013)
  6. Hayashi, T., Tanaka, Y., Sakai, N., Okada, U., Yao, M., Watanabe, N., Tamura, T., and Tanaka, I., SCO4008, a putative TetR transcriptional repressor from Streptomyces coelicolor A3(2), regulates transcription of sco4007 by multidrug recognition. J. Mol. Biol., 425, 3289-3300 (2013)
  7. Miyafusa, T., Caaveiro, JM., Tanaka, Y., Tanner, ME., and Tsumoto, K., Crystal structure of the capsular polysaccharide synthesizing protein CapE of Staphylococcus aureus. Biosci. Rep., 33, 463-474 (2013)
  8. Hayashi, T., Tanaka, Y., Sakai, N., Watanabe, N., Tamura, T., Tanaka, I., and Yao, M., Structural and genomic DNA analysis of a putative transcription factor SCO5550 from Streptomyces coelicolor A3(2): regulating the expression of gene sco5551 as a transcriptional activator with a novel dimer shape. Biochem. Biophys. Res. Commun., 435, 28-33 (2013)
  9. Kita, S., Tanaka, Y., Hirano, N., Kimura, S., Suzuki, T., Suzuki, T., Yao, M., and Tanaka. I., Crystal structure of a putative methyltransferase SAV1081 from Staphylococcus aureus. Protein & Pept. Lett., 20, 530-537 (2013)
  10. Yamamoto S., Tomiyama M., Nemoto R., Naganuma T., Ogawa T., Muramoto K., Effects of Food Lectins on the Transport System of Human Intestinal Caco-2 Cell Monolayers. Biosci. Biotechnol. Biochem., 77, 1917-1924 (2013)
  11. Watanabe Y., Chang YH., Nakamura O., Naganuma T., Ogawa T., Muramoto K., Rhamnose-binding lectins induce respiratory burst activity in macrophage cells from rainbow trout. Fisheries Sci., 79, 513-519 (2013)
  12. Mori T., Shimokawa Y., Matsui T., Kinjo K., Kato R., Noguchi H., Sugio S., Morita H., Abe I., Cloning and structure-function analyses of quinolone-and acridone-producing novel type III polyketide synthases from Citrus microcarpa. J. Biol. Chem., 288, 28845-28858 (2013)
  13. Kawashima Y., Satoh M., Saito T., Matsui T., Nomura F., Matsumoto H., Kodera Y., Cyclic sample pooling using two‐dimensional liquid chromatography system enhances coverage in shotgun proteomics. Biomed. Chromatogr., 27, 691-694 (2013)
  14. Saito T., Kawashima Y., Minamida S., Matsumoto K., Araki K., Matsui T., Satoh M., Nomura F., Iwamura M., Maeda T., Baba S., Kodera Y., Establishment and application of a high-quality comparative analysis strategy for the discovery and small-scale validation of low-abundance biomarker peptides in serum based on an optimized novel peptide extraction method. J. Electrophr., 57, 1-9 (2013)
  1. Gai, Z., Kitagawa, Y., Tanaka, Y., Shimizu, N., Komoda, K., Tanaka, I., and Yao, M., The binding mechanism of eIF2{beta} with its partner proteins, eIF5 and eIF2B{epsilon}. Biochem. Biophys. Res. Commun., 423, 515-519 (2012)
  2. Tsukamoto, K., Arimitsu, H., Ochi, S., Nakamura, K., Tanaka, Y., Nuemket, N., Taniguchi, K., Kozaki, S., and Tsuji, T., P19 embryonal carcinoma cells exhibit high sensitivity to botulinum type C and D/C mosaic neurotoxins. Microbiol. and Immunol., 56, 664-672 (2012)
  3. Ui, M., Tanaka, Y., Araki, Y., Wada, T., Takei, T., Tsumoto, K., Endo, S., and Kinbara, K., Application of photoactive yellow protein as a photoresponsive module for controlling hemolytic activity of staphylococcal α-hemolysin. Chem. Commun. 48, 4737-4739 (2012)
  4. Miyafusa T, Caaveiro JM, Tanaka Y, Tsumoto K. Crystal Structure of Enzyme CapF of Staphylococcus aureus Reveals a Unique Architecture Composed of Two Functional Domains. Biochem J., 443, 671-680 (2012)
  5. Yoshimura S., Komatsu M., Kaku K., Hori M., Ogawa T., Muramoto K., Kazama T., Ito Y., Toriyama K., Production of transgenic rice plants expressing Dioscprea batatus tuber lectin 1 to confer resistance against brown plant hopper. Plant Biotechnol., 29, 501-504 (2012)
  6. Nakamura O., Watanabe M., Ogawa T., Muramoto K., Ogawa K., Tsutsui S., Kamiya H., Galectins in the abdominal cavity of conger eel, Conger myriaster, participate in the cellular encapsulation of parasitic nematode by host cells. FIsh & Shellfish Immun., 33, 780-787 (2012)
  7. Watanabe M., Nakamura O., Muramoto K., Ogawa T., Allosteric regulation of the carbohydrate-binding ability of a novel conger Eel galectin by D-mannoside. J. Biol. Chem., 287, 31061-31072 (2012)
  8. Matsui T., Yamane J., Mogi N., Yamaguchi H., Takemoto H., Yao M., Tanaka I., Structural reorganization of the bacterial cell-division protein FtsZ from Staphylococcus aureus. Acta Crystallogr. D., D68, 1175-1188 (2012)
  1. Yu, F., Tanaka, Y., Yamashita, K., Suzuki, T., Nakamura, A., Hirano, N., Suzuki, T., Yao, M., and Tanaka, I., Molecular basis of dihydrouridine formation on tRNA. Proc. Natl. Acad. Sci. USA, 108, 19593-19598 (2011)
  2. Yamashita, K., Kawai, Y., Tanaka, Y., Hirano, N., Kaneko, J., Tomita, N., Ohta, M., Kamio, Y., Yao, M., and Tanaka, I., Crystal Structure of the Octameric Pore of Staphylococcal γ-hemolysin Reveals the β-barrel Pore Formation Mechanism by Two Components. Proc. Natl. Acad. Sci. USA, 108, 17314-17319 (2011)
  3. Moriwaki, Y., Caaveiro, JM., Tanaka, Y., Tsutsumi, H., Hamachi, I., Tsumoto K. Molecular Basis of Recognition of Antibacterial Porphyrins by Heme-Transporter IsdH-NEAT3 of Staphylococcus aureus. Biochemistry., 50, 7311-7320 (2011)
  4. Nuemket, N., Tanaka, Y., Tsukamoto, K., Tsuji, T., Nakamura, K., Kozaki, S., Yao, M., Tanaka, I., Structural and Mutational Analyses of the Receptor Binding Domain of Botulinum D/C Mosaic Neurotoxin: Insight into the Ganglioside Binding Mechanism. Biochem. Biophys. Res. Commun. , 411, 433-439 (2011)
  5. Yu, F., Tanaka, Y., Yamamoto, S., Nakamura, A., Kita, S., Hirano, N., Tanaka, I., and Yao, M., Crystallization and preliminary X-ray crystallographic analysis of dihydrouridine synthase from Thermus thermophilus and its complex with tRNA. Acta Cryst. F., F67, 685-688 (2011)
  6. Tanaka, Y., Hirano, N., Kaneko, J., Kamio, Y., Yao, M., and Tanaka, I., 2-Methyl-2,4-pentanediol induces spontaneous assembly of staphylococcal alpha-hemolysin into heptameric pore structure. Protein Science , 20, 448-456 (2011)
  7. Matsuoka, E., Tanaka, Y., Kuroda, M., Shouji, Y., Ohta, T., Tanaka, I., and Yao, M., Crystal structure of the functional region of Uro-adherence factor A (UafA) from Staphylococcus saprophyticus reveals participation of the B domain in ligand binding. Protein Science , 20, 406-416 (2011)
  8. Ui, M., Tanaka, Y., Tsumuraya, T., Fujii, I., Inoue, M., Hirama, M., and Tsumoto, K., Structural and Energetic Hot-Spots for the Interaction between a Ladder-like Polycyclic Ether and the Anti-Ciguatoxin Antibody 10C9Fab. Molecular BioSystems, 7, 793-798 (2011)
  9. Konno A., Kitagawa A., Watanabe M., Ogawa T., Shirai T., Tracing Protein Evolution through Ancestral Structures of Fish Galectin. Structure, 19, 711-721 (2011)
  10. Krause J., Tshidino SC., Ogawa T., Watanabe Y., Oosthuizen V., Somai B., Muramoto K., Naudea RJ., Purification and partial characterization of ostrich skeletal muscle cathepsin D and its activity during meat maturation. Meat Sci., 87, 196-201 (2011)
  1. Morikawa, K., Ohniwa, R. L., Ohta, T., Tanaka, Y., Takeyasu, K., and Msadek, T., Adaptation beyond the Stress Response: Cell Structure Dynamics and Population Heterogeneity in Staphylococcus aureus. Microbes and Environments , 25, 75-82 (2010)
  2. Nuemket, N., Tanaka, Y., Tsukamoto, K., Tsuji, T., Nakamura, K., Kozaki, S., Yao, M., and Tanaka, I., Preliminary X-ray crystallographic study of the receptor binding domain of the D/C mosaic neurotoxin from Clostridium botulinum. Acta Cryst. F., F66, 608-610 (2010)
  3. Nagatoishi, S., Tanaka, Y., Kudou, M., and Tsumoto, K., Temperature and salt concentration alter base-sequence selectivity of a duplex DNA-binding protein, Mol. Biosyst., 6, 98-101 (2010)
  4. Yanaka, S., Kudou, M., Tanaka, Y., Sasaki, T., Takemoto, S., Sakata, A., Hattori, Y., Koshi, T., Futaki, S., Tsumoto, K., and Nakashima, T., Contribution of the flexible loop region to the function of Staphylococcal enterotoxin B (SEB), Protein Eng. Des. Select., 23, 415-421 (2010)
  5. Kato T., Hori M., Ogawa T., Muramoto K., Toriyama K., Expression of gene for Dioscorea batatas tuber lectin 1 in transgenic tobacco confers resistance to green-peach aphid, Plant Biotechnol., 27, 141-145 (2010)
  6. Kanno A., Yonemaru S., Kitagawa A., Muramoto K., Shirai T., Ogawa T., Protein engineering of conger eel galectins by tracing of molecular evolution using probable ancestral mutants, BMC Evol. Biol., 10, (2010)
  1. Tanaka, Y., Yamagata, S., Kitago, Y., Yamada, Y., Chimnaronk, S., Yao, M., and Tanaka, I., Deduced RNA binding mechanism of ThiI based on structural and binding analyses of a minimal RNA ligand, RNA, 15, 1498-1506 (2009)
  2. Nagatoishi, S., Tanaka, Y., Kudou, M., and Tsumoto, K., The interaction of hyperthermophilic TATA-box binding protein with single-stranded DNA is entropically favorable and exhibits a large negative heat capacity change at high salt concentration, Mol. BioSyst., 5, 957-961 (2009)
  3. Sakamoto, S., Caaveiro, J. M., Sano, E., Tanaka, Y., Kudou, M., and Tsumoto, K., Contributions of interfacial residues of human Interleukin15 to the specificity and affinity for its private alpha-receptor, J. Mol. Biol., 389, 880-894 (2009)
  4. Abe, R., Kudou, M., Tanaka, Y., Arakawa, T., and Tsumoto, K., Immobilized metal affinity chromatography in the presence of arginine, Biochem. Biophys. Res. Commun., 381, 306-310 (2009)
  5. Konno A., Suzuki Y., Ogawa T., Taniuchi T., Irradiation Promotes the Accumulation of Triglyceride in Lipomyces lipofer, Biosci. Biotechnol. Biochem., 73, 2474-2477 (2009)
  6. Watanabe Y., Abolhassani M., Tojo Y, Sudab Y., Miyazawa K., Igarashi Y., Sakuma K., Ogawa T.,, Muramoto K., Evaluation of silica gel-immobilized phosphorylcholine columns for size exclusion chromatography and their application in the analysis of the subunit structures of fish-egg lectins, J. Chromatogr. A., 1216, 8563-8566 (2009)
  7. Shirai T., Watanabe Y., Lee MS., Ogawa T., Muramoto K., Structure of Rhamnose-binding Lectin CSL3: Unique Pseudo-tetrameric Architecture of a Pattern Recognition Protein, J. Mol. Biol., 391, 390-403 (2009)
  8. Ohizumi Y., Gaidamashvili M., Ohwada S., Matsuda K., Kominami J., Nakamura-Tsuruta S., Hirabayashi J., Naganuma T., Ogawa T., Muramoto K., Mannose-binding lectin from yam (Dioscorea batatas) tubers with insecticidal properties against Helicoverpa armigera (Lepidoptera: Noctuidae), J. Agr. Food Chem., 57, 2896-2902 (2009)
  9. Watanabe Y., Nakamura O., Watanabe T., Kamiya H., Naganuma T., Ogawa T., Naude RJ., Muramoto K., The function of rhamnose-binding lectin in innate immunity by restricted binding to Gb3, Dev. Comp. Immunol., 33, 187-197 (2009)
  10. Yamamoto S., Naganuma T., Ogawa T., Muramoto K., Proteomic analysis of Caco-2 cells treated with food lectins, J. Clin. Biochem. Nutr., , (2009)
  11. Matsui T., Tanaka T., Endoh H., Sato K., Tanaka H., Miyauchi E., Kawashima Y., Nagai-Makabe M., Komatsu H., Kohno T., Maeda T., Kodera Y., The RNA recognition mechanism of human immunodeficiency virus (HIV) type 2 NCp8 is different from that of HIV-1 NCp7, Biochemistry, 48, 4314-4323 (2009)
  12. Kawashima Y., Fukuno T., Satoh M., Takahashi H., Matsui T., Maeda T., Kodera Y., A simple and highly reproducible method for discovering potential disease markers in low abundance serum proteins, J. Electrophor., 53, 13-18 (2009)
  1. Gao, Y.-G., Suzuki, H., Itou, H., Zhou, Y., Tanaka, Y., Wachi, M., Watanabe, N., Tanaka, I., and Yao, M., Structural and Functional Characterization of the LidR from Corynebacterium glutamicum: a Transcriptional Repressor Involved in L-Lactate and Sugar Utilization, Nucleic Acids Res., 36, 7110-7123 (2008)
  2. Kuroda, M., Ito, R., Tanaka, Y., Yao, M., Matoba, K., Saito, S., Tanaka, I., and Ohta, T., Staphylococcus aureus Surface Protein SasG Contributes to Intercellular Autoaggregation of Staphylococcus aureus, Biochem. Biophys. Res. Commun., 377, 1102-1106 (2008)
  3. Sakamoto, S., Tanaka, Y., Tanaka, I., Takei, T., Yu, J., Kuroda, M., Yao, M., Ohta, T., and Tsumoto, K., Electron Microscopy and Computational Studies of Ebh, a Giant Cell-wall-associated Protein from Staphylococcus aureus, Biochem. Biophys. Res. Commun., 376, 261-266 (2008)
  4. Watanabe, M., Tanaka, Y., Suenaga, A., Kuroda, M., Yao, M., Watanabe, N., Arisaka, F., Ohta, T., Tanaka, I., and Tsumoto, K., Structural basis for multimeric heme complexation through a specific protein-heme interaction: the case of the third NEAT domain of IsdH from Staphylococcus aureus, J. Biol. Chem.,283, 28649-28659 (2008)
  5. Nakakido, M., Tanaka, Y., Mitsuhori, M., Kudou, M., Ejima, D., Arakawa, T., and Tsumoto, K., Structure-based analysis reveals hydration changes induced by arginine hydrochloride, Biophys. Chem., 137, 105-109 (2008)
  6. Kuroda, M., Tanaka, Y., Aoki, R., Shu, D., Tsumoto, K., and Ohta, T., Staphylococcus aureus Giant Protein Ebh is Involved in Tolerance to Transient Hyperosmotic Pressure Biochem. Biophys. Res. Comm., 374, 237-241 (2008)
  7. Ui, M., Tanaka, Y., Tsumuraya, T., Fujii, I., Inoue, M., Hirama, M., and Tsumoto, K., How Protein Recognizes Ladder-Like Polycyclic Ethers: Interactions Between Ciguatoxin (CTX3C) Fragments and Its Specific Antibody 10C9 J. Biol. Chem., 283, 19440-19447 (2008)
  8. Nakakido, M., Tanaka, Y., Sokabe, M., and Tsumoto, K., Thermodynamic Analysis Reveals that GTP Binding Affects the Interaction between the alpha- and gamma-subunits of Translation Initiation Factor 2. Biochem. Biophys. Res. Comm., 371, 596-599 (2008)
  9. Miyafusa, T., Tanaka, Y., Kuroda, M., Ohta, T., and Tsumoto, K., Expression, Purification, Crystallization, and Primary Diffraction Analysis of CapF, a Capsular Polysaccharide Synthesis Enzyme from Staphylococcus aureus. Acta Cryst. F., F64, 512-515 (2008)
  10. Tsumoto, K., Yokota, A., Tanaka, Y., Ui, M., Tsumuraya, T., Fujii, I., Kumagai, I., Nagumo, Y., Oguri, H., Inoue, M., and Hirama, M., Critical contribution of aromatic rings to specific recognition of polyether rings: the case of ciguatoxin CTX3C and its specific antibody 1C49. J. Biol. Chem., 283, 512259-12266 (2008)
  11. Tanaka, Y., Sakamoto, S., Kuroda, M., Goda, S., Gao, Y.-G., Tsumoto, K., Hiragi, Y., Yao, M., Watanabe, N., Ohta, T., and Tanaka, I., A helical string of alternately connected two three-helix bundles for the 1.1-Megadalton cell wall-associated adhesion protein Ebh from Staphylococcus aureus. Structure, 16, 488-496, (2008)
  12. Makabe, K., Nakanishi, T., Tsumoto, K., Tanaka, Y., Kondo, H., Umetsu, 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 murine antibody, 528. J. Biol. Chem., 283, 1156-1166 (2008)
  13. Adebiyi AP., Adebiyi AO., Yamashita J., Ogawa T., Muramoto K., Purification and characterization of antioxidative peptides derived from rice bran protein hydrolysates. Eur. Food. Res. Technol., 228, 553-563 (2008)
  14. Adebiyi AP., Adebiyi AO., Hasegawa Y., Ogawa T., Muramoto K., Isolation and characterization of protein fractions from deoiled rice bran. Eur. Food. Res. Technol., 228, 391-401 (2008)
  15. Seto M., Ogawa T., Kodama K., Muramoto K., Kanayama Y., Sakai Y., Chijiwa T., Ohno M., A novel recombinant system for functional expression of myonecrotic snake phospholipase A2 in Escherichia coli using a new fusion affinity tag. Protein Expr. Purif., 58, 194-202 (2008)
  16. Watanabe Y., Shiina N., Shinozaki F., Yokoyama H., Kominami J., Nakamura-Tsuruta S., Hirabayashi J., Sugahara K., Kamiya H., Matsubara H., Ogawa T., Muramoto K., Isolation and characterization of l-rhamnose-binding lectin, which binds to microsporidian Glugea plecoglossi, from ayu (Plecoglossus altivelis) egg. Dev. Comp. Immun., 32, 487-499 (2008)
  17. Oshi Y., Nakata E., Miyagawa M., Tsukiji S., Ogawa T., Hamachi I., Target-Specific Chemical Acylation of Lectins by Ligand-Tethered DMAP Catalysts. J. Am. Chem. Soc., 130, 245-251 (2008)
  1. Tanaka, Y., Morikawa, K., Ohki, Y., Yao, M., Tsumoto, K., Watanabe, N., Ohta, T., and Tanaka, I., Structural and mutational analyses of Drp35 from Staphylococcus aureus: a possible mechanism for its lactonase activity. J. Biol. Chem., 282, 5770-5780 (2007)
  2. 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)
  3. Nagatoishi, S., Tanaka, Y., and Tsumoto, K., Circular dichroism spectra demonstrate formation of the thrombin-binding DNA aptamer G-quadruplex under stabilizing-cation-deficient conditions. Biochem. Biophys. Res. Comm., 352, 812-817 (2007)
  4. Arakawa, T., Ejima, D., Tsumoto, K., Obeyama, N., Tanaka, Y., Kita, Y., and Timasheff, S. N., Suppression of protein interactions by arginine: A proposed mechanism of arginine effects. Biophys. Chem., 127, 1-8 (2007)
  5. Tanaka, Y., Sasaki, T., Kumagai, I., Yasutake, Y., Yao, M., Tanaka, I., and Tsumoto, K., Molecular properties of two proteins homologous to PduO-type ATP:cob(I)alamin adenosyltransferase from Sulfolobus tokodaii, Proteins: Structure, Function, and Bioinformatics, 68, 446-457 (2007)
  6. Tanaka, Y., Kuroda, M., Yasutake, Y., Yao, M., Tsumoto, K., Watanabe, N., Ohta, T., and Tanaka, I., Crystal structure analysis reveals a novel forkhead-associated (FHA) domain of ESAT-6 secretion system C (EssC) protein in Staphylococcus aureus. Proteins: Structure, Function, and Bioinformatics, 69, 659-664 (2007)
  7. Nakakido, M., Tanaka, Y., and Tsumoto, K., The N-terminal domain of elastin-binding protein of Staphylococcus aureus changes its secondary structure in a membrane-mimetic environment. J. Biochem. (Tokyo), 142, 131-134 (2007)
  8. Adebiyi AP., Adebiyi AO., Ogawa T., Muramoto K., Rice bran protein-based edible films. Int. J. Food Sci. Technol., 43, 35-43 (2007)
  9. Konno A., Ogawa T., Shirai T., Muramoto K., Reconstruction of a Probable Ancestral Form of Conger Eel Galectins Revealed. Mol. Biol. Evol., 24, 2504-2514 (2007)
  10. Terada T., Watanabe Y., Tateno H., Naganuma T., Ogawa T., Muramoto K., Kamiya H., Structural characterization of a rhamnose-binding glycoprotein (lectin) from Spanish mackerel (Scomberomorous niphonius) eggs. Biochim. Biophys. Acta., 1770, 617-629 (2007)
  11. Matsubara H., Nakamura-Tsuruta S., Hirabayashi J., Jimbo M., Kamiya H., Ogawa T., Muramoto K., Diverse Sugar-Binding Specificities of Marine Invertebrate C-Type Lectins. Biosci. Biotechol. Biochem., 71, 513-519 (2007)
  12. Matsui T., Kodera Y., Miyauchi E., Tanaka H., Endoh H., Komatsu H., Tanaka T., Kohno T., Maeda T., Structural role of the secondary active domain of HIV-2 NCp8 in multi-functionality. Biochem. Biophys. Res. Commun., 358, 673-678 (2007)
  13. Matsui T., Kodera Y., Endoh H., Miyauchi E., Komatsu H., Sato K., Tanaka T., Kohno T., Maeda T., RNA recognition mechanism of the minimal active domain of the human immunodeficiency virus type-2 nucleocapsid protein. J. Biochem. (Tokyo), 141, 269-277 (2007)
  1. Matsubara H., Ogawa T., Muramoto K., Structures and Functions of C-type Lectins in marine Invertebrates. Tohoku J. Agr. Res., 57, 71-86 (2006)
  2. Shirai T., Shionyu-Mitsuyama C., Ogawa T., Muramoto K., Structure based studies of the adaptive diversification process of congerins. Mol. Divers., 10, 567-573 (2006)
  3. Naganuma T., Ogawa T., Hirabayashi J., Kasai K., Hamiya H., Muramoto K., Isolation, characterization and molecular evolution of a novel pearl shell lectin from a marine bivalve, Pteria penguin. Mol. Divers., 10, 607-618 (2006)
  4. Chijiwa T., Tokunaga E., Ikeda R., Terada K., Ogawa T., Oda-Ueda N., Hattori S., Nozaki M., Ohno M, Discovery of novel [Arg(49)]phospholipase A(2) isozymes from Protobothrops elegans venom and regional evolution of Crotalinae snake venom phospholipase A(2) isozymes in the southwestern islands of Japan and Taiwan. Toxicon, 48, 672-682 (2006)
  5. Konno A., Ogawa T., Muramoto K., Shirai T., Reconstraction of Ancestral Conger Eel Galectins Have Revealed Their Molecular Diversification Process by Accelerated Evolution. Pep. Sci., 2006, 138-139 (2006)
  6. Nakamura O., Matsuoka H., Ogawa T., Muramoto K., Kamiya H., Watanabe H., Opsonic effect of congerin, a mucosal galectin of the Japanese conger, Conger myriaster (Brevoort). Fish Shellfish Immunol., 20, 433-435 (2006)
  7. Ohno Y., Naganuma T., Ogawa T., Muramoto K., Watanabe H., Effect of lectins on the transport of food factors in Caco-2 cell monolayers. J. Agr. Food Chem., 54, 548-553 (2006)
  1. Umetsu, M., Kadota, T., Wang, Z.-Y., Tanaka, Y., Adschiri, T., and Nozawa, T., Selective detection of the dolid-state NMR signals from the bacteriochlorophyll a dimers in a reconstituted light-harvesting 1 complex, Chemistry Letters, 34, 940-941, (2005).
  2. Tanaka, Y., Tsumoto, K., Tanabe, E., Yasutake, Y., Sakai, N., Yao, M., Tanaka, I., and Kumagai, I., Crystal structure of the hypothetical protein ST2072 from Sulfolobus tokodaii. Proteins: Structure, Function, and Bioinformatics, 61, 1127-1131 (2005).
  3. Matsubara H., Kabuto S., Nakahara N., Ogawa T., Muramoto K., Jimbo M., Kamiya H., Structure and possible function of N-glycans of an invertebrate C-type lectin from the acorn barnacle Megabalanus rosa. Fisheries Sci., 71, 931-940 (2005).
  4. Chijiwa T., Abe K., Ogawa T., Nikandrov N.N., Hattori S., Oda-Ueda N., Ohno M., Amino acid sequence of a basic aspartate-49-phospholipase A2 from Trimeresurus flavoviridis venom and phylogenetic analysis of Crotalinae venom phospholipases A2. Toxicon, 46, 185-195 (2005).
  5. Shionyu-Mitsuyama C., Ito Y., Konno A., Miwa Y., Ogawa T., Muramoto K., Shirai T., In vitro evolutionary thermostabilization of congerin II: A limited reproduction of natural protein evolution by artificial selection pressure. J. Mol. Biol., 347, 385-397 (2005).
  6. Adebiyi AP., Jin DH., Ogawa T., Muramoto K., Acid hydrolysis of protein in a microcapillary tube for the recovery of tryptophan. Biosci. Biotechnol. Biochem., 69, 255-257 (2005).
  7. Ogawa T., Chijiwa T., Oda-Ueda N., Ohno M., Molecular diversity and accelerated evolution of C-type lectin-like proteins from snake venom. Toxicon, 45, 1-14 (2005).
  1. Tanaka, Y., Tsumoto, K., Yasutake, Y., Umetsu, M., Yao, M., Fukada, H., Tanaka, I., and Kumagai, I., How oligomerization contributes to the thermostability of an archaeon protein: Protein L-Isoaspartyl-O-methyltransferase from Sulfolobus tokodaii. J. Biol. Chem., 279, 32957-32967 (2004).
  2. Tanaka, Y., Tsumoto, K., Nakanishi, T., Yasutake, Y., Sakai, N., Yao, M., Tanaka, I., and Kumagai, I., Structural implications for heavy metal-induced reversible assembly and aggregation of a protein: the case of Pyrococcus horikoshii CutA. FEBS Letters, 556, 167-174 (2004).
  3. Tanaka, Y., Tsumoto, K., Umetsu, M., Nakanishi, T., Yasutake, Y., Sakai, N., Yao, M., Tanaka, I., Arakawa, T., and Kumagai, I., Structural evidence for guanidine- protein side chain interactions: crystal structure of CutA from Pyrococcus horikoshii in 3M guanidine hydrochloride. Biochem. Biophys. Res. Commun., 323, 185-191 (2004).
  4. Tajika, Y., Sakai, N., Tanaka, Y., Yao, M., Watanabe, N., and Tanaka, I., Crystal structure of conserved protein PH1136 from Pyrococcus horikoshii. Proteins: Structure, Function, and Bioinformatics, 55, 210-213 (2004).
  5. Umetsu, M., Tsumoto, K., Ashish, K., Nitta, S., Tanaka, Y., Adschiri, T., and Kumagai, I., Structural characteristics and refolding of in vivo aggregated hyperthermophilic archaeon proteins. FEBS Letters, 557, 49-56 (2004).
  6. Ohno Y., Naganuma T., Ogawa T., Muramoto K., Effect of lectins on the transport of food ingredients in Caco-2 cell cultures. Biofactors, 21, 399-401 (2004).
  7. Kimura T., Nakano T., Yamaguchi T., Sato M., Ogawa T., Muramoto K., Yokoyama T., Kan-no N., Nagahisa E., Janssen F., Grieshaber MK., Complementary DNA cloning and molecular evolution of opine dehydrogenases in some marine invertebrates. Marine Biotechnol., 6, 493-502 (2004).
  8. Hayashi MAF., Ligny-Lemaire C., Wollberg Z., Wery M., Galat A., Ogawa T., Muller BH., Lamthanh H., Doljansky Y., Bdolah A., Stocklin R., Ducancel F., Long-sarafotoxins: characterization of a new family of endothelin-like peptides. Peptides, 25, 1243-1251 (2004).
  9. Gaidamashvili M., Ohizumi Y., Iijima S., Takayama T., Ogawa T., Muramoto K., Characterization of the yam tuber storage proteins from Dioscorea batatas exhibiting unique lectin activities. J. Biol. Chem., 279, 26028-26035 (2004).
  10. Yoshimi K., Shoji M., Ogawa T., Yamauchi A., Naganuma T., Muramoto K., Hanada S., Microstructure and orientation distribution of aragonite crystals in nacreous layer of pearl shells. Materials Transactions, 45, 999-1004 (2004).
  11. Ogawa T., Shirai T., Shionyu-Mitsuyama C., Yamane T., Kamiya H., Muramoto K., The speciation of conger eel galectins by rapid adaptive evolution. Glycoconjugate J., 19, 451-458 (2004).
  1. 松井崇,加藤早苗,田中良和,クライオ電子顕微鏡で明らかになった超巨大酸素運搬タンパク質ヘモシアニンの会合構造,生化学 Vol 92, 113-119 (2020)
  2. 松井崇,加藤早苗,田中良和,クライオ電子顕微鏡で明らかになったスルメイカヘモシアニン(TpH)の立体構造,日本結晶学会誌 Vol 61, 211-212 (2019) [link]
  3. Chen M., and Tanaka Y., Sulfur transferase TtuA, Encyclopedia of Inorganic and Bioinorganic Chemistry (2019)
  4. Kato S., Matsui T., Gatsogiannis C., Tanaka, Y., Molluscan Hemocyanin: Structure, Evolution, and Physiology, Biophys. Review, 10, 191-202 (2018) [PubMed]
  5. 加藤早苗, 松井崇, 田中良和, 3.8 MDaの超巨大酸素運搬タンパク質ヘモシアニン会合体の結晶構造, 生化学 90(2), 238-243 (2018)
  6. 松井崇, リボソーム由来ペプチドのN末端をキャッピングする新規ペプチドリガーゼの構造基盤, 日本結晶学会誌 59, 96-101 (2017)
  7. 松野明日香,田中良和, 超巨大蛋白質会合体ヘモシアニンのX線結晶構造解析, 日本結晶学会誌 58,91-95(2016)
  8. Tanaka, Y., and Yao, M, Pore formation mechanism of staphylococcal pore forming toxin, PF activity report part A, 2014 Highlight, 46-47 (2015)
  9. 田中良和, 黄色ブドウ球菌が産生する膜孔形成毒素の作用機構, Isotope News 736, 7-11(2015)
  10. 田中良和, 黄色ブドウ球菌の2成分性膜孔形成毒素γヘモリジンの膜孔形成メカニズム 失敗から明らかになった毒素の戦略, 化学と生物 53(3),136-137(2015)
  11. 小川智久, マベ真珠バイオミネラリゼーション:マトリックスタンパク質による結晶界面制御, C & I Commun. 40, 27-30(2015)
  12. 田中良和,陳明皓,姚閔, tRNAジヒドロウリジン合成酵素の分子機構, 生化学 86(3),395-399(2014)
  13. 松井崇, HIVヌクレオキャプシド蛋白質の立体構造とRNA認識機構, ペプチドニュースレター 88,1-4(2013)
  14. 田中良和, 黄色ブドウ球菌の膜孔形成毒素の分子機構, 生物物理 52(6),293-295(2012)
  15. 小川智久, ベノミクス:毒生物ゲノムプロジェクト, BIO Clinica 24(6),65-71(2009)
  16. 田中良和, 高度好熱古細菌Sulfolobus tokodaii由来protein L-isoaspartyl-O-methyltransferaseの多量体化による耐熱性獲得機構, 生物物理 46(4),209-213(2006)
  17. Ogawa T., Molecular diversity of proteins in biological offense and defense systems, Molecular Diversity 2006,138-139(2006)
  1. 田中良和, Essential タンパク質科学 第2章 タンパク質のドメイン, p59-94 南江堂(2016)
  2. 左巻健男, 一色健司, 浅賀宏昭, 池田圭一, 大庭義史, 小川智久, 貝沼関志, 嘉村均, 滝澤昇, 中山榮子, 藤村陽, 保谷彰彦, 山本文彦, 和田重雄, 知っておきたい化学物質の常識84, SBクリエイティブ(2016)
  3. 小川智久 (分担), 左巻健男, 池田圭一編著, 知っていると安心できる成分表示の知識 その食品、その洗剤、本当に安全なの?, SBクリエイティブ(2016)
  4. 田中良和, 環境と微生物の事典 第6章 135 人体環境での鉄の獲得, 朝倉書店(2014)
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