論文発表

解析拠点 制御拠点 情報拠点
2015 2014 2013 2012

謝辞について

1. 解析拠点

解析領域

  1. Structural basis of starvation-induced assembly of the autophagy initiation complex. Fujioka, Y., Suzuki, S.W., Yamamoto, H., Kondo-Kakuta, C., Kimura, Y., Hirano, H., Akada, R., Inagaki, F., Ohsumi, Y. and Noda, N.N. J. Phys.: Conf. Ser., 21, 513-521, 2014. (DOI:10.1038/nsmb.2822)(PubMed:24793651)
  2. X-ray crystallographic structure of RNase Po1 that exhibits anti-tumor activity. Kobayashi, H., Katsutani, T., Hara, Y., Motoyoshi, N., Itagaki, T., Akita, F., Higashiura, A., Yamada, Y., Inokuchi, N., Suzuki, M. J Synchrotron Radiat., 20, 838-42, 2014. (DOI:10.1248/bpb.b13-00929)(PubMed:24882409)
  3. S46 peptidases are the first exopeptidases to be members of clan PA. Sakamoto,Y., Suzuki, Y., Iizuka, I., Tateoka, C., Roppongi, S., Fujimoto, M., Inaka, K., Tanaka, H., Masaki, M., Ohta, K., Okada, H., Nonaka, T., Morikawa, Y., T. Nakamura, K., Ogasawara, W., Tanaka, N. J Synchrotron Radiat., 20, 938-42, 2014. (DOI:10.1038/srep04977)(PubMed:24827749)
  4. Structural basis of Sec-independent membrane protein insertion by YidC. Kumazaki, K., Chiba, S., Takemoto, M., Furukawa, A., Nishiyama, K., Sugano, Y., Mori, T., Dohmae, N., Hirata, K., Nakada-Nakura, Y., Maturana, A.D., Tanaka, Y., Mori, H., Sugita, Y., Arisaka, F., Ito, K., Ishitani, R., Tsukazaki, T., Nureki, O. J Synchrotron Radiat., 20, 890-3, 2014. (DOI:10.1038/nature13167)(PubMed:24739968)
  5. Crystal structure of a claudin provides nsight into the architecture of tight junctions. Suzuki, H., Nishizawa, T., Tani, K., Yamazaki, Y., Tamura, A., Ishitani, R., Dohmae, N., Tsukita, S., Nureki, O., Fujiyoshi, Y. Biophys. Res. Commun., 447, 32-37, 2014. (DOI:10.1126/science.1248571)(PubMed:24744376)
  6. Crystal structure of Cas9 in complex with guide RNA and target DNA. Nishizawa, T., Kita, S., Maturana, A.D., Furuya, N., Hirata, K., Kasuya, G., Ogasawara, S., Dohmae, N., Iwamoto, T., Ishitani, R., Nureki, O. Science, 341, 168-72, 2014. (DOI:10.1016/j.cell.2014.02.001)(PubMed:24529477)
  7. Structural basis for gating mechanisms of a eukaryotic P-glycoprotein homolog. Kodan, A., Yamaguchi, T., Nakatsu, T., Sakiyama, K., Hipolito, C.J., Fujioka, A., Hirokane, R., Ikeguchi, K., Watanabe, B., Hiratake, J., Kimura, Y., Suga, H., Ueda, K., Kato, H. Nature, 496, 247-51, 2014. (DOI:10.1073/pnas.1321562111)(PubMed:24591620)
  8. Structural insights into the epimerization of beta-1,4-linked oligosaccharides catalyzed by cellobiose 2-epimerase, the sole enzyme epimerizing non-anomeric hydroxyl groups of nnmodified sugars. Fujiwara, T., Saburi, W., Matsui, H., Mori, H., Yao, M. J.Biol. Chem., 289, 3405-3415, 2014. (DOI:10.1074/jbc.M113.531251)(PubMed:24362032)
  9. Current status and future prospects of an automated sample exchange system PAM for protein crystallography. Hiraki, M., Yamada, Y., Chavas, L.M., Matsugaki, N., Igarashi, N., Wakatsuki, S. J. Phys.: Conf. Ser., 425, e012014, 2013. (DOI:10.1088/1742-6596/425/1/012014)
  10. Data Management System at the Photon Factory Macromolecular Crystallography Beamline. Yamada, Y., Matsugaki, N., Chavas, L.M., Hiraki, M., Igarashi, N., Wakatsuki, S. J. Phys.: Conf. Ser., 425, e012017, 2013. (DOI:10.1088/1742-6596/425/1/012017)
  11. New methodologies at PF AR-NW12A: the implementation of high-pressure macromolecular crystallography. Chavas, L.M., Nagae, T., Yamada, H., Watanabe, N., Yamada, Y., Hiraki, M., Matsugaki, N. J. Synchrotron Rad., 20, 838-842, 2013. (DOI:10.1107/S0909049513020797)(PubMed:24121324)
  12. Improvements toward highly accurate diffraction experiments at the macromolecular micro-crystallography beamline BL-17A. Yamada, Y., Chavas, L.M., Igarashi, N., Hiraki, M., Wakatsuki, S., Matsugaki, N. Nature, 509, 516-520, 2013. (DOI:10.1107/S0909049513022875)(PubMed:24121344)
  13. Improvement of an automated protein crystal exchange system PAM for high-throughput data collection. Yamada, Y., Chavas, L.M., Igarashi, N., Hiraki, M., Wakatsuki, S., Matsugaki, N. Science, 344, 304-307, 2013. (DOI:10.1107/S0909049513021067)(PubMed:24121334)
  14. Crystal structure of glycoside hydrolase family 127 β-L-arabinofuranosidase from Bifidobacterium longum. Ito, T., Saikawa, K., Kim, S., Fujita, K., Ishiwata, A., Kaeothip, S., Arakawa, T., Wakagi, T., Beckham, G.T., Ito, Y., Fushinobu, S. J. Biol. Chem., 289, 3501-3509 , 2013. (DOI:10.1016/j.bbrc.2014.03.096)(PubMed:24680821)
  15. Crystallization and preliminary X-ray analysis of human leukocyte cell-derived chemotaxin 2 (LECT2). Zheng, H., Miyakawa, T., Sawano, Y, Yamagoe, S, Tanokura, M. Acta Cryst., F69, 316-319, 2013. (DOI:10.1107/S1744309113003758)(PubMed:23519812)
  16. Structural basis for the counter-transport mechanism of a H+/Ca2+ exchanger. Nishizawa, T., Kita, S., Maturana, A.D., Furuya, N., Hirata, K., Kasuya, G., Ogasawara, S., Dohmae, N., Iwamoto, T., Ishitani, R., Nureki, O. Science, 34, 168-172, 2013. (DOI:10.1126/science.1239002)(PubMed:23704374)
  17. Structural basis for the drug extrusion mechanism by a MATE multidrug transporter. Tanaka, Y., Hipolito, C. J., Maturana, A. D., Ito, K., Kuroda, T., Higuchi, T., Katoh, T., Kato, H. E., Hattori, M., Kumazaki, K., Tsukazaki, T., Ishitani, R., Suga, H., Nureki, O. Nature, 496, 245-251, 2013. (DOI:10.1038/nature12014)(PubMed:23535598)
  18. Crystal structures of an archaeal oligosaccharyltransferase provide insights into the catalytic cycle of N-linked protein glycosylation. Matsumoto, S., Shimada, A., Nyirenda, J., Igura, M., Kawano, Y., Kohda, D. Proc. Natl. Acad. Sci., 111, 17868-17873, 2013. (DOI:10.1073/pnas.1309777110.)(PubMed:24127570)
  19. 3D Manipulation of protein microcrystals with optical tweezers for X-ray crystallography. Hikima, T., Hashimoto, K., Murakami, H., Ueno, G., Kawano, Y., Hirata, K., Hasegawa, K., Kumasaka, T., & Yamamoto, M. J. Phys.: Conf. Ser., 425, e012011, 2013. (DOI: 10.1088/1742-6596/425/1/012011)
  20. Achievement of protein micro-crystallography at SPring-8 beamline BL32XU. Hirata, K., Kawano, Y., Ueno, G., Hashimoto, K., Murakami, H., Hasegawa, K., Hikima, T., Kumasaka, T., & Yamamoto, M. J. Phys.: Conf. Ser., 425, e012002, 2013. (DOI: 10.1088/1742-6596/425/1/012002)
  21. SPring-8 BL41XU, a high-flux macromolecular crystallography beamline. Hasegawa, K., Shimizu, N., Okumura, H., Mizuno, N., Baba, S., Hirata, K., Takeuchi, T., Yamazaki, H., Senba, Y., Ohashi, H., Yamamoto, M., Kumasaka, T. J. Synchrotron Radiat., 20, 910-913, 2013. (DOI:10.1107/S0909049513022176.)(PubMed:24121338)

生産領域

  1. Making things better. Takagi, J., Tate, C.G. Current Opin. Struct. Biol., in press, 2015.
  2. Structural basis of the divergent oxygenation reactions catalyzed by the rieske nonheme iron oxygenase carbazole 1,9a-dioxygenase. Inoue, K., Usami, Y., Ashikawa, Y., Noguchi, H., Umeda, T., Yamagami-Ashikawa, A., Horisaki, T., Uchimura, H., Terada, T., Nakamura, S., Shimizu, K., Habe, H., Yamane, H., Fujimoto, Z., Nojiri, H. Appl. Environ Microbiol., 80, 2821-2832, 2014. (DOI:10.1128/AEM.04000-13)(PubMed:24584240)
  3. In vitro synthesis of the E. coli sec translocon from DNA. Matsubayashi, H., Kuruma, Y., Ueda, T. Angew Chem Int Ed Engl., in press, 2014. (DOI:10.1002/anie.)(PubMed:24894900)
  4. X-ray crystallographic structure of RNase Po1 that exhibits antitumor activity. Kobayashi, H., Katsutani, T., Hara, Y., Motoyoshi, N., Itagaki, T., Akita, F., Higashiura, A., Yamada, Y., Inokuchi, N., Suzuki, M. Biol. Pharm. Bull., 37, 968-978, 2014. (DOI:10.1248/bpb.b13-00929)(PubMed:24882409)
  5. The phosphorylation of HIV-1 Gag by atypical protein kinase C facilitates viral infectivity by promoting Vpr incorporation into virions. Kudoh, A., Takahama, S., Sawasaki, T., Ode, H., Yokoyama, M., Okayama, A., Ishikawa, A., Miyakawa, K., Matsunaga, S., Kimura, H., Sugiura, W., Sato, H., Hirano, H., Ohno, S., Yamamoto, N., Ryo, A. Retrovirology, 11, 9, 2014. (DOI:10.1186/1742-4690-11-9)(PubMed:24447338)
  6. Suppression of LUBAC-mediated linear ubiquitination by a specific interaction between LUBAC and the deubiquitinases CYLD and OTULIN. Takiuchi, T., Nakagawa, T., Tamiya, H., Fujita, H., Sasaki, Y., Saeki, Y., Takeda, H., Sawasaki, T., Buchberger, A., Kimura, T., Iwai, K. Genes Cells, 19, 254-272, 2014. (DOI:10.1111/gtc.12128)(PubMed:24461064)
  7. Involvement of Hepatitis C virus NS5A hyperphosphorylation mediated by casein kinase I-α in infectious virus production. Masaki, T., Matsunaga, S., Takahashi, H., Nakashima, K., Kimura, Y., Ito, M., Matsuda, M., Murayama, A., Kato, T., Hirano, H., Endo, Y., Lemon, S.M., Wakita, T., Sawasaki, T., Suzuki, T. J Virol., 88, 7541-7555, 2014. (PubMed:24760886)
  8. Retroviral vectors for homologous recombination provide efficient cloning and expression in mammalian cells. Kobayashi, E., Kishi, H., Ozawa, T., Horii, M., Hamana, H., Nagai, T., Muraguchi, A. Biochem. Bioph. Res. Co., 444, 319, 2014. (DOI:10.1016/j.bbrc.2014.01.049)(PubMed:24462869)
  9. Structural basis for potent inhibition of SIRT2 deacetylase by a macrocyclic peptide inducing dynamic structural change. Yamagata, K., Goto, Y., Nishimasu, H., Morimoto, J., Ishitani, R., Dohmae, N., Takeda, N., Nagai, R., Komuro, I., Suga, H., Nureki, O. Structure, 22, 345-352, 2014. (DOI:10.1016/j.str.2013.12.001)(PubMed:24389023)
  10. Structural basis for gating mechanisms of a eukaryotic P-glycoprotein homolog. Kodan, A., Yamaguchi, T., Nakatsu, T., Sakiyama, K., Hipolito, C.J., Fujioka, A., Hirokane, R., Ikeguchi, K., Watanabe, B., Hiratake, J., Kimura, Y., Suga, H., Ueda, K., Kato, H. Pro. Nat. Acad. Sci., 111, 4049-4054, 2014. (DOI:10.1073/pnas.1321562111)(PubMed:24591620)
  11. Protein cocrystallization molecules originating from in vitro selected macrocyclic peptides. Hipolito, C.J., Bashiruddin, N.K., Suga, H. Curr Opin Struct Biol., 26, 24-31, 2014. (DOI:10.1016/j.sbi.2014.03.001)(PubMed:24681557)
  12. PA tag: a versatile protein tagging system using a super high affinity antibody against a dodecapeptide derived from human podoplanin. Fujii, Y., Kaneko, M., Neyazaki, M., Nogi, T., Kato, Y., Takagi, J. Protein Exp. Pur., 95, 240-247, 2014. (DOI:10.1016/j.pep.2014.01.009)(PubMed:24480187)
  13. Lysosomal sorting of amyloid-β by the SORLA receptor is impaired by a familial Alzheimer's disease mutation. Caglayan, S., Takagi-Niidome, S., Liao, F., Carlo, A-S., Schmidt, V., Burgert, T., Kitago, Y., Fuchtbauer, E-M., Fuchtbauer, A., Holtzman, D.M., Takagi, J., Wilnow, T.E. Science Transl. Med., 6, 223ra20, 2014. (DOI:10.1126/scitranslmed.3007747)(PubMed:24523320)
  14. PA tag: a versatile protein tagging system using a super high affinity antibody against a dodecapeptide derived from human podoplanin. Fujii, Y., Kaneko, M., Neyazaki, M., Nogi, T., Kato, Y. and Takagi, J. Protein Exp. Pur., 95, 240-7, 2014. (DOI:10.1016/j.pep.2014.01.009)(PubMed:24480187)
  15. IDH2 mutation is frequently observed in giant cell tumor of bone. Kaneko, M., Liu, X., Oki, H., Ogasawara, S., Nakamura, T., Saidoh, N., Tsujimoto, Y., Matsuyama, Y., Uruno, A., Sugawara, M., Tsuchiya, T., Yamakawa, M., Yamamoto, M., Takagi, M., Kato, Y. Cancer Sci., 105, 744-8, 2014. (DOI:10.1111/cas.12413)(PubMed:24898068)
  16. PA tag: a versatile protein tagging system using a super high affinity antibody against a dodecapeptide derived from human podoplanin. Fujii, Y., Kaneko, M., Neyazaki, M., Nogi, T., Kato, Y., Takagi, J. Protein Exp. Pur., 95, 240-247, 2014. (DOI:10.1016/j.pep.2014.01.009)(PubMed:24480187)
  17. Distinct Features of the Histone Core Structure in Nucleosomes Containing the Histone H2A.B Variant. Sugiyama, M., Arimura, Y., Shirayama, K., Fujita, R., Oba, Y., Sato, N., Inoue, R., Oda, T., Sato, M., Heenan, R.K., Kurumizaka, H. Biophysical journal, 106, 2206-2213, 2014. (DOI:10.1016/j.bpj.2014.04.007.)(PubMed:24853749)
  18. Purification, crystallization and preliminary X-ray crystallographic analysis of a rice Rac/Rop GTPase, OsRac1. Kosami, K-I., Ohki, I., Hayashi, K., Tabata, R., Usugi, S., Kawasaki, T., Fujiwara, T., Nakagawa, A., Shimamoto, K., Kojima, C. Acta Crystallographica Section F, 70, 113-115, 2014. (DOI:10.1107/S2053230X13033645)(PubMed:24419631)
  19. Active-site structure of thermophilic Foc subunit ring in membranes elucidated by solid-state NMR. Kang, S-J., Todokoro, Y., Yumen, I., Shen, B., Iwasaki, I., Suzuki, T., Miyagi, A., Yoshida, M., Fujiwara, T., Akutsu, H. Biophysical J., 106, 390-398, 2014. (DOI:10.1016/j.bpj.2013.12.005)(PubMed:24461014)
  20. 1H, 15N and 13C resonance assignments of the conserved region in the middle domain of S. pombe Sin1 protein. Kataoka, S., Furuita, K., Hattori, Y., Kobayashi, N., Ikegami, T., Shiozaki, K., Fujiwara, T., Kojima, C. Biomolecular NMR Assignments, in press, 2014. (DOI:10.1007/s12104-014-9550-6)
  21. Cell-free expression of protein complexes for structural biology. Terada, T., Murata, T., Shirouzu, M., Yokoyama, S. Methods Mol. Biol. , 1091, 151-159, 2014. (DOI:10.1007/978-1-62703-691-7_10)(PubMed:24203330)
  22. Cell-free membrane protein expression. Kimura-Someya, T., Shirouzu, M., Yokoyama, S. Methods Mol. Biol., 1118 , 267-273, 2014. (DOI:10.1007/978-1-62703-782-2_18)(PubMed:24395423)
  23. Dimer-dimer interaction of the bacterial selenocysteine synthase SelA promotes functional active-site formation and catalytic specificity. Itoh, Y., Brocker, M.J., Sekine, S-I., Soll, D., Yokoyama, S. J. Mol. Biol., 8, 1723-1735, 2014. (DOI:10.1016/j.jmb.2014.01.003)(PubMed:24456689)
  24. Crystal structure of the eukaryotic translation initiation factor 2A from Schizosaccharomyces pombe. Kashiwagi, K., Ito, T., Yokoyama, S. J. Struct. Funct. Genomics, 15, 125-130, 2014. (DOI:10.1007/s10969-014-9177-y)(PubMed:24569939)
  25. MicroRNA-mediated deadenylation in a mammalian cell-free system. Wakiyama, M., Yokoyama, S. Methods Mol. Biol., 1125 , 341-351, 2014. (DOI:10.1007/978-1-62703-971-0_27)(PubMed:24590801)
  26. MicroRNA-mediated deadenylation in a mammalian cell-free system. Wakiyama, M., Yokoyama, S. Methods Mol. Biol., 1118 , 257-266, 2014. (DOI:10.1007/978-1-62703-782-2_17)(PubMed:24395422)
  27. Translation enhancer improves the ribosome liberation from translation initiation. Takahashi, S., Furusawa,H., Ueda,T., Okahata, Y. Journal of the American Chemical Society, 135, 13096-13106, 2013. (DOI:10.1021/ja405967h)(PubMed:23927491)
  28. A novel mode of ferric ion coordination by the periplasmic ferric ion-binding subunit FbpA of an ABC-type iron transporter from Thermus thermophilus HB8. Wang, S., Ogata, M., Horita, J., Ohtsuka, S., Nagata, K., Tanokura, M. Acta Crystallography, D70, 196-202 , 2013. (DOI:10.1107/S1399004713026333)(PubMed:24419392)
  29. Expression, high-pressure refolding and purification of human leukocyte cell-derived chemotaxin 2 (LECT2). Zheng, H., Miyakawa, T., Sawano, Y., Yamagoe, S., Tanokura, M. Protein Expression and Purification, 88, 221-9, 2013. (DOI:10.1016/j.pep.2013.01.008)(PubMed:23337084)
  30. Complex structure of the DNA-binding domain of AdpA, the global transcription factor in Streptomyces griseus, and a target duplex DNA reveals the structural basis of its tolerant DNA sequence specificity. Yao, M.D., Ohtsuka, J., Nagata, K., Miyazono, K., Zhi, Y., Ohnishi, Y., Tanokura, M. The Journal of Biological Chemistry, 288, 31019-29, 2013. (DOI:10.1074/jbc.M113.473611)(PubMed:24019524)
  31. Structural units important for activity of a novel-type phosphoserine phosphatase from Hydrogenobacter thermophilus TK-6 revealed by crystal structure analysis. Chiba, Y., Horita, S., Ohtsuka, J., Arai, H., Nagata, K., Igarashi, Y., Tanokura, M., Ishii, M. The Journal of Biological Chemistry, 288, 11448-58, 2013. (DOI:10.1074/jbc.M112.449561)(PubMed:23479726)
  32. Integrated database of information from structural genomics experiments. Asada, Y., Sugahara, M., Mizutani, H., Naitow, H., Tanaka, T., Matsuura, Y., Agari, Y., Ebihara, A., Shinkai, A., Kuramitsu, S., Yokoyama, S., Kaminuma, E., Kobayashi, N., Nishikata, K., Shimoyama, S., Toyoda, T., Ishikawa, T., Kunishima, N. Acta Crystallographica Section D, 69, 914-919, 2013. (DOI:10.1107/S0907444913001728)(PubMed:23633602)
  33. Structure and function of a TetR family transcriptional regulator, SbtR, from Thermus thermophilus HB8. Agari, Y., Sakamoto, K., Yutani, K., Kuramitsu, S., Shinkai, A. Proteins, 81, 1166-1178, 2013. (DOI:10.1002/prot.24266)(PubMed:23408580)
  34. Loose binding of the DF axis with the A3B3 complex stimulates the initial activity of enterococcus hirae V1-ATPase. Alam, M.J., Satoshi, A., Saijo, S., Suzuki, K., Mizutani, K., Ishizuka-Katsura, Y., Ohsawa, N., Terada, T., Shirouzu, M., Yokoyama, S., Iwata, S., Kakinuma, Y., Yamato, I., Murata, T. PLoS ONE, 8, e74291, 2013. (DOI:10.1371/journal.pone.0074291)(PubMed:24058539)
  35. Mutant LV476-7AA of A-subunit of Enterococcus hirae V1-ATPase: High affinity of A3B3 complex to DF axis and low ATPase activity. Alam, M.J., Yamato, I., Arai, S., Saijo, S., Mizutani, K., Ishizuka-Katsura, Y., Ohsawa, N., Terada, T., Shirouzu, M., Yokoyama, S., Iwata, S., Kakinuma, Y., Murata, T. SpringerPlus, 2, 689, 2013. (DOI:10.1186/2193-1801-2-689)(PubMed:24404436)
  36. Myosin phosphatase is inactivated by caspase-3 cleavage and phosphorylation of myosin phosphatase targeting subunit 1 during apoptosis. Iwasaki, T., Katayama, T., Kohama, K., Endo, Y., Sawasaki, T. Mol Biol Cell, 24, 748-756, 2013. (DOI:10.1091/mbc.E11-08-0740)(PubMed:23345589)
  37. Suppression of DS1 phosphatidic acid phosphatase confirms resistance to Ralstonia solanacearum in Nicotiana benthamiana. Nakano, M., Nishihara, M., Yoshioka, H., Takahashi, H., Sawasaki, T., Ohnishi, K., Hikichi, Y., Kiba, A. PLoS One, 8, e75124, 2013. (DOI:10.1371/journal.pone.0075124.)(PubMed:24073238)
  38. Anti-interleukin-5 and multiple autoantibodies are associated with human atherosclerotic diseases and serum interleukin-5 levels. Ishigami, T., Abe, K., Aoki, I., Minegishi, S., Ryo, A., Matsunaga, S., Matsuoka, K., Takeda, H., Sawasaki.?T., Umemura, S., Endo, Y. The FASEB Journal, 9, 3437-3445, 2013. (DOI:10.1096/fj.12-222653)(PubMed:23699176)
  39. Nek5, a novel substrate for caspase-3, promotes skeletal muscle differentiation by up-regulating caspase activity. 2013 Jul 11;587(14):2219-25.. Shimizu, K., Sawasaki, T. FEBS Lett., 587, 2219-2225, 2013. (DOI:10.1016/j.febslet.2013.05.049.)(PubMed:23727203)
  40. Interaction between RB protein and NuMA is required for proper alignment of spindle microtubules. Uchida, C., Hattori, T., Takahashi, H., Yamamoto, N., Kitagawa, M., Taya, Y. Genes Cells, 19, 89-96, 2013. (DOI:10.1111/gtc.12119)(PubMed:24350565)
  41. Ca2+ spiking activity caused by the activation of store-operated Ca2+ channels mediates TNF-α release from microglial cells under chronic purinergic stimulation. Ikeda, M., Tsuno, S., Sugiyama, T., Hashimoto, A., Yamoto, K., Takeuchi, K., Kishi, H., Mizuguchi, H., Kohsaka, S-I., Yoshioka, T. Biochim. Biophys. Acta., 1833, 2573, 2013. (DOI:10.1016/j.bbamcr.2013.06.022)(PubMed:23830920)
  42. Polymeric microfluidic devices exhibiting sufficient capture of cancer cell line for isolation of circulating tumor cells.. Ohnaga, T., Shimada, Y., Moriyama, M., Kishi, H., Obata, T., Takata, K., Okumura, T., Nagata, A., Muraguchi, A., Tsukada, K. Biomed. Microdevices, 15, 611, 2013. (DOI:10.1007/s10544-013-9775-7)(PubMed:23666489)
  43. A novel cloning and expression system yields and validates TCRs from blood lymphocytes of cancer patients within 10 days. Kobayashi, E., Mizukoshi, E., Kishi, H., Ozawa, T., Hamana, H., Nagai, T., Nakagawa, H., Jin, A., Kaneko, S., Muraguchi, A. Nature Medicine, 19, 1542, 2013. (DOI:10.1038/nm.3358)(PubMed:24121927)
  44. Structural basis for the drug extrusion mechanism by a MATE multidrug transporter. Tanaka, Y., Hipolit, C.J., Maturana, A., Ito, K., Kuroda, T., Higuchi, Katoh, T., Kato, H.E., Hattori, M., Kumazaki, K., Tsukazaki, T., Ishitani, R., Suga, H., Nureki, O. Nature, 496, 247-251, 2013. (DOI:10.1038/nature12014)(PubMed:23535598)
  45. A macrocyclic peptide that serves as a cocrystallization ligand and inhibits the function of a MATE family transporter. Hipolito, C.J., Tanaka, Y., Katoh, T., Nureki, O., Suga, H. Molecules, 18, 10514-30, 2013. (DOI:10.3390/molecules180910514)(PubMed:23999725)
  46. A multi-purpose fusion tag derived from an unstructured and hyper-acidic region of the amyloid precursor protein. Sangawa, T., Tabata, S., Suzuki, K., Saheki, Y., Tanaka, K., Takagi, J. Protein Science, 22: 840-850, 2013. (DOI:10.1002/pro.2254)(PubMed:23526492)
  47. 動物細胞発現系を用いた細胞外タンパク質の試料調製. 禾 晃和、三原 恵美子、高木 淳一 「タンパク質結晶の最前線」(シー・エム・シー出版), 第Ⅱ編第1章, 25-31, 2013.
  48. Establishment of novel monoclonal antibodies KMab-1 and MMab-1 specific for IDH2 mutations. Kaneko, M.K., Morita, S., Tsujimoto, Y., Yanagiya, R., Nasu, K., Sasaki, H., Hozumi, Y., Goto, K., Natsume, A., Watanabe, M., Kumabe, T., Takano, S., Kato, Y. Biochem Biophys Res Commun., 432, 40-5, 2013. (DOI:10.1016/j.bbrc.2013.01.088.)(PubMed:23376717)
  49. A novel monoclonal antibody GMab-m1 specifically recognizes IDH1-R132G mutation. Kato, Y., Natsume, A., Kaneko, M.K. Biochem Biophys Res Commun., 432, 564-7., 2013. (DOI:10.1016/j.bbrc.2013.02.049.)(PubMed:23485467)
  50. Generation of a novel monoclonal antibody WMab-1 specific for IDH2-R172W mutation. Kato, Y., Kaneko, M.K. Biochem Biophys Res Commun., 433, 374-8, 2013. (DOI:10.1016/j.bbrc.2013.02.106)(PubMed:23524262)
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  5. Ligand heterogeneity of the cysteine protease binding protein family in the parasitic protist Entamoeba histolytica. Marumo, K., Nakada-Tsukui, K., Tomii, K., Nozaki, T. Int. J. Parasitol., 14, 120-129, 2014. (DOI:10.1016/j.ijpara.2014.04.008)(PubMed:24907554)
  6. Ubiquitin is phosphorylated by PINK1 to activate parkin. Koyano, F., Okatsu, K., Kosako, H., Tamura, Y., Go, E., Kimura, M., Kimura, Y., Tsuchiya, H., Yoshihara, H., Hirokawa, T., Endo, T., Fon, E.A., Trempe, J.F., Saeki, Y., Tanaka, K., Matsuda, N. Nature, 510, 162-166, 2014. (DOI:10.1038/nature13392)(PubMed:24784582)
  7. Blockade of TLR3 protects mice from lethal radiation-induced gastrointestinal syndrome. Takemura, N., Kawasaki, T., Kunisawa, J., Sato, S., Lamichhane, A., Kobiyama, K., Aoshi, T., Ito, J., Mizuguchi, K., Karuppuchamy, T., Matsunaga, K., Miyatake, S., Mori, N., Tsujimura, T., Satoh, T., Kumagai, Y., Kawai, T., Standley, D.M., Ishii, K.J., Kiyono, H., Akira, S., Uematsu, S.. Nat. Commun., 5, e3492, 2014. (DOI:10.1038/ncomms4492)(PubMed:24637670)
  8. Differential roles of epigenetic changes and Foxp3 expression in regulatory T cell-specific transcriptional regulation. Morikawa, H., Ohkura, N., Vandenbon, A., Itoh, M., Nagao-Sato, S., Kawaji, H., Lassmann, T., Carninci, P., Hayashizaki, Y., Forrest, A.R., Standley, D.M., Date, H., Sakaguchi, S., Consortium, F. Proc. Natl. Acad. Sci., 111, 5289-5294, 2014. (DOI:10.1073/pnas.1312717110)(PubMed:24706905)
  9. Intrinsic Disorder Mediates Cooperative Signal Transduction in STIM1. Furukawa, Y., Teraguchi, S., Ikegami, T., Dagliyan, O., Jin, L., Hall, D., Dokholyan, N.V., Namba, K., Akira, S., Kurosaki, T., Baba, Y., Standley, D.M. J. Mol. Biol., 426, 2082-2097, 2014. (DOI:10.1016/j.jmb.2014.03.006)(PubMed:24650897)
  10. High-resolution structural model building of antibodies by combination of bioinformatics, expert knowledge and molecular simulations. Shirai, H., Ikeda, K., Yamashita, K., Tsuchiya, Y., Sarmiento, J., Liang, S., Morokata, T., Mizuguchi, K., Higo, J., Standley, D.M., Nakamura, H. Proteins, 82, 1624-1635, 2014. (DOI:10.1002/prot.24591)(PubMed:24756852)
  11. MAFFT: iterative refinement and additional methods. Katoh, K., Standley, D.M. Methods Mol. Biol., 1079, 131-146, 2014. (DOI:10.1007/978-1-62703-646-7_8)(PubMed:24170399)
  12. LEAP: highly accurate prediction of protein loop conformations by integrating coarse-grained sampling and optimized energy scores with all-atom refinement of backbone and side chains. Liang, S., Zhang, C., Zhou, Y. J. Comput. Chem., 5, 335-341, 2014. (DOI:10.1002/jcc.23509)(PubMed:24327406)
  13. Molecular modeling and molecular dynamics simulations of recombinase Rad51. Kokabu, Y., Ikeguchi, M. Biophys. J., 104, 1556-1565, 2013. (DOI:10.1016/j.bpj.2013.02.014)(PubMed:23561532)
  14. Gas-phase structure of the histone multimers characterized by ion mobility mass spectrometry and molecular dynamics simulation. Saikusa, K., Fuchigami, S., Takahashi, K., Asano, Y., Nagadoi, A., Tachiwana, H., Kurumizaka, H., Ikeguchi, M., Nishimura, Y., Akashi, S. Anal. Chem., 85, 4165-4171, 2013. (DOI:10.1021/ac400395j)(PubMed:23485128)
  15. Functional rotation induced by alternating protonation states in the multidrug transporter AcrB: All-atom molecular dynamics simulations. Yamane, T., Murakami, S., Ikeguchi, M. Biochemistry, 52, 7648-7658, 2013. (DOI:10.1021/bi400119v)(PubMed:24083838)
  16. Selective binding of antimicrobial porphyrins to the heme-receptor IsdH-NEAT3 of Staphylococcus aureus. Vu, N.T., Moriwaki, Y., Caaveiro, J.M., Terada, T., Tsutsumi, H., Hamachi, I., Shimizu, K., Tsumoto, K. Protein Sci., 22, 942-953, 2013. (DOI:10.1002/pro.2276)(PubMed:23649633)
  17. Heme-binding mechanism of structurally similar Isd NEAT domains of Staphylococcus aureus exhibiting different affinities for heme Biochem. Moriwaki, Y., Terada, T., Caaveiro, J., Takaoka, Y., Hamachi, I., Tsumoto, K., Shimizu, K. Biochemistry, 52, 8866-8877, 2013. (DOI:10.1021/bi4008325)(PubMed:24245481)
  18. Creating a TALE protein with unbiased 5'-T binding. Tsujii, S., Futaki, S., Imanishi, M. Biochem. Biophys. Res. Commun., 441, 262-265, 2013. (DOI:10.1016/j.bbrc.2013.10.060)(PubMed:24148249)
  19. Tam41 is a CDP-diacylglycerol synthase required for cardiolipin biosynthesis in mitochondria. Tamura, Y,, Harada, Y., Nishikawa, S., Yamano, K., Kamiya, M., Shiota, T., Kuroda, T., Kuge, O., Sesaki, H., Imai, K., Tomii, K., Endo, T. Cell Metab., 17, 709-718, 2013. (DOI:10.1016/j.cmet.2013.03.018)(PubMed:23623749)
  20. Revisiting amino acid substitution matrices for identifying distantly related proteins. Yamada, K., Tomii, K. Bioinformatics, 30, 317-325, 2013. (DOI:10.1093/bioinformatics/btt694)(PubMed:24281694)
  21. Solution structure of the Q41N variant of ubiquitin as a model for the alternatively folded N2 state of ubiquitin. Kitazawa, S., Kameda, T., Yagi-Utsumi, M., Sugase, K., Baxter, N.J., Kato, K., Williamson, M.P., Kitahara, R. Biochemistry, 52, 1874-1885, 2013. (DOI:10.1021/bi301420m)(PubMed:23421577)
  22. Design and synthesis of cyclic ADP-4-thioribose as a stable equivalent of cyclic ADP-ribose, a calcium ion-mobilizing second messenger. Tsuzuki, T., Sakaguchi, N., Kudoh, T., Takano, S., Uehara, M., Murayama, T., Sakurai, T., Hashii, M., Higashida, H., Weber, K., Guse, A.H., Kameda, T., Hirokawa, T., Kumaki, Y., Potter, B.V., Fukuda, H., Arisawa, M., Shuto, S. Angew. Chem. Int. Ed. Engl., 52, 6633-6637, 2013. (DOI:10.1002/anie.201302098)(PubMed:23670921)
  23. Investigation of the noncovalent binding mode of covalent proteasome inhibitors around the transition state by combined use of cyclopropylic strain-based conformational restriction and computational modeling. Kawamura, S., Unno, Y., Tanaka, M., Sasaki, T., Yamano, A., Hirokawa, T., Kameda, T., Asai, A., Arisawa, M., Shuto, S.. J. Med. Chem., 56, 5829-5842, 2013. (DOI:10.1021/jm400542h)(PubMed:23837692)
  24. Rational hopping of a peptidic scaffold into non-peptidic scaffolds: structurally novel potent proteasome inhibitors derived from a natural product, belactosin A. Kawamura, S., Unno,Y., Hirokawa, T., Asai, A., Arisawa, M., Shutoa, S. Chem. Comm., 50, 2445-2447. , 2013. (DOI:10.1039/c3cc48818g)(PubMed:24452398)
  25. Tertiary structure prediction of RNA-RNA complexes using secondary structure and fragment based method. Yamasaki, S., Hirokawa, T., Asai, K., Fukui, K. J. Chem. Inf. Model., 54, 672-682, 2013. (DOI:10.1021/ci400525t)(PubMed:24479711)
  26. A Pyrrolo-Pyrimidine Derivative Targets Human Primary AML Stem Cells in Vivo. Saito, Y., Yuki, H., Kuratani, M., Hashizume, Y., Takagi, S., Honma, T. Tanaka, A., Shirouzu, M., Mikuni, J., Handa, N., Ogahara, I., Sone, A., Najima, Y., Tomabechi, Y., Wakiyama, M., Uchida, N., Tomizawa-Murasawa, M., Kaneko, A., Tanaka, S., Suzuki, N., Kajita, H., Aoki, Y., Ohara, O., Shultz, L. D., Fukami, T., Goto, T., Taniguchi, S. Yokoyama, S., Ishikawa, F. Sci. Transl. Med., 5, e181ra52, 2013. (DOI:10.1126/scitranslmed.3004387)
  27. Biochemical characterization of highly active Trypanosoma brucei gambiense glycerol kinase, a promising drug target. Balogun, E. O., Inaoka, D. K., Shiba, T. Kido, Y., Nara, T.; Aoki, T., Honma, T., Tanaka, A., Inoue, M., Matsuoka, S., Michels, P. A., Harada, S., Kita, K. J. Biochem., 154, 77-84, 2013. (DOI:10.1093/jb/mvt037)(PubMed:23620597)
  28. Blind prediction of interfacial water positions in CAPRI. Lensink, M.F., Moal, I.H., Bates, P.A., Kastritis, P.L., Melquiond, A.S., Karaca, E., Schmitz, C., van Dijk, M., Bonvin, A.M., Eisenstein, M., Jimenez-Garcia, B., Grosdidier, S., Solernou, A., Perez-Cano, L., Pallara, C., Fernandez Recio J., Xu, J., Muthu, P., Praneeth Kilambi, K., Gray, J.J., Grudinin, S., Derevyanko, G., Mitchell, J.C., Wieting, J., Kanamori, E., Tsuchiya, Y., Murakami, Y., Sarmiento, J., Standley, D.M., Shirota, M., Kinoshita, K., Nakamura, H., Chavent, M., Ritchie, D.W., Park, H., Ko, J., Lee, H., Seok, C., Shen, Y., Kozakov, D., Vajda, S., Kundrotas, P.J., Vakser, I.A., Pierce, B.G., Hwang, H., Vreven, T., Weng, Z., Buch, I., Farkash, E., Wolfson, H.J., Zacharias, M., Qin, S., Zhou, H.X., Huang, S.Y., Zou, X., Wojdyla, J.A., Kleanthous, C., Wodak, S.J. Proteins, 82, 620-632, 2013. (DOI:10.1002/prot.24439)(PubMed:24155158)
  29. Structures and interface mapping of the TIR domain-containing adaptor molecules involved in interferon signaling. Enokizono, Y., Kumeta, H., Funami, K., Horiuchi, M., Sarmiento, J., Yamashita, K., Standley, D.M., Matsumoto, M., Seya, T., Inagaki, F. Proc. Natl. Acad. Sci., 110, 19908-19913, 2013. (DOI:10.1073/pnas.1222811110)(PubMed:24255114)
  30. The second messenger phosphatidylinositol-5-phosphate facilitates antiviral innate immune signaling. Kawasaki, T., Takemura, N., Standley, D.M., Akira, S., Kawai, T. Cell Host Microbe, 14, 148-158, 2013. (DOI:10.1016/j.chom.2013.07.011)(PubMed:23954154)
  31. Malt1-induced cleavage of regnase-1 in CD4(+) helper T cells regulates immune activation. Uehata, T., Iwasaki, H., Vandenbon, A., Matsushita, K., Hernandez-Cuellar, E., Kuniyoshi, K., Satoh, T., Mino, T., Suzuki, Y., Standley, D.M., Tsujimura, T., Rakugi, H., Isaka, Y., Takeuchi, O., Akira, S. Cell, 153, 1036-1049, 2013. (DOI:10.1016/j.cell.2013.04.034)(PubMed:23706741)
  32. MAFFT multiple sequence alignment software version 7: improvements in performance and usability. Katoh, K., Standley, D.M. Mol. Biol. Evol., 30, 772-780, 2013. (DOI:10.1093/molbev/mst010)(PubMed:23329690)
  33. Community-wide evaluation of methods for predicting the effect of mutations on protein-protein interactions. Moretti, R., Fleishman, S. J., Agius, R., Torchala, M., Bates, P. A., Kastritis, P. L., Rodrigues, J. P., Trellet, M., Bonvin, A. M., Cui, M., Rooman, M., Gillis, D., Dehouck, Y., Moal, I., Romero-Durana, M., Perez-Cano, L., Pallara, C., Jimenez, B., Fernandez-Recio, J., Flores, S., Pacella, M., Praneeth Kilambi, K., Gray, J. J., Popov, P., Grudinin, S., Esquivel-Rodriguez, J., Kihara, D., Zhao, N., Korkin, D., Zhu, X., Demerdash, O. N., Mitchell, J. C., Kanamori, E., Tsuchiya, Y., Nakamura, H., Lee, H., Park, H., Seok, C., Sarmiento, J., Liang, S., Teraguchi, S., Standley, D.M., Shimoyama, H., Terashi, G., Takeda-Shitaka, M., Iwadate, M., Umeyama, H., Beglov, D., Hall, D. R., Kozakov, D., Vajda, S., Pierce, B. G., Hwang, H., Vreven, T., Weng, Z., Huang, Y., Li, H., Yang, X., Ji, X., Liu, S., Xiao, Y., Zacharias, M., Qin, S., Zhou, H.X., Huang, S. Y., Zou, X., Velankar, S., Janin, J., Wodak, S.J.,Baker, D. Proteins, 81, 1980-1987, 2013. (DOI:10.1002/prot.24356)(PubMed:23843247)
  34. A novel function prediction approach using protein overlap networks. Liang, S., Zheng, D., Standley, D.M., Guo, H., Zhang, C. BMC Syst. Biol., 7, e61, 2013. (DOI:10.1186/1752-0509-7-61)(PubMed:23866986)
  35. aLeaves facilitates on-demand exploration of metazoan gene family trees on MAFFT sequence alignment server with enhanced interactivity. Kuraku, S., Zmasek, C.M., Nishimura, O., Katoh, K. Nucleic Acids Res., 41, W22-W28, 2013. (DOI:10.1093/nar/gkt389)(PubMed:23677614)
  36. Deconstructing RNA: optical measurement of composition and structure. Hobro, A.J., Standley, D.M., Ahmad, S., Smith, N.I. Phys. Chem. Chem. Phys., 15, 13199-13208, 2013. (DOI:10.1039/c3cp52406j)(PubMed:23824161)
  37. Molecular dynamics simulations of yeast F1-ATPase before and after 16° rotation of the γ subunit. Ito, Y., Yoshidome, T., Matubayasi, N., Kinoshita, M., Ikeguchi, M. J. Phys. Chem. B, 117, 3298-3307, 2012. (DOI:10.1021/jp312499u)(PubMed:23452086)
  38. MICAN: a protein structure alignment algorithm that can handle Multiple-chains, inverse alignments, Ca only models, Alternative alignments, and Non-sequential alignments. Minami, S., Sawada, K., Chikenji, G. BMC Bioinformatics, 18,14-24, 2012. (DOI:10.1186/1471-2105-14-24)(PubMed:23331634)
  39. Substrate-shielding and hydrolytic reaction in hydrolases. Kanematsu, Y., Koike, R., Amemiya, T., Ota, M. Proteins, 81, 926-932, 2012. (DOI:10.1002/prot.24253)(PubMed:23345013)
  40. A new method for evaluating the specificity of indirect readout in protein-DNA recognition. Yamasaki, S., Terada, T., Shimizu, K., Kono, H., Sarai, A. Nucleic Acids Res., 40, e129, 2012. (DOI:10.1093/nar/gks462)(PubMed:22618872)
  41. Blind prediction of quaternary structures of homo-oligomeric proteins from amino acid sequences based on templates. Morita, M., Kakuta, M., Shimizu, K., Nakamura, S. J. Proteome. Sci. Comput. Biol., 1, e, 2012. (DOI:10.7243/2050-2273-1-1)
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  43. A new entropy model for RNA: part II, Persistence-related entropic contributions to RNA secondary structure free energy calculation. Dawson, W., Yamamoto,K., Shimizu, K., Kawai, G. J. Nucleic. Acids. Investig., 3, 4-18, 2012. (DOI:10.4081/jnai.2013.e2)
  44. Small-angle X-ray scattering constraints and local geometry like secondary structures can construtct a coarse-grained protein model at amino acid residue resolution. Morimoto, Y., Nakagawa, T., Kojima, M. Biochem. Biophys. Res. Commun., 431, 65-69, 2012. (DOI:10.1016/j.bbrc)(PubMed:23291239)
  45. Structure of the trypanosome cyanide-insensitive alternative oxidase. Shiba, T., Kido, Y., Sakamoto, K., Inaoka, D. K., Tsuge, C., Tatsumi, R., Takahashi, G., Balogun, E. O., Nara, T., Aoki, T., Honma, T., Tanaka, A., Inoue, M., Matsuoka, S., Saimoto, H., Moore, A. L., Harada, S., Kita, K. Proc. Natl. Acad. Sci., 110, 4580-4585, 2012. (DOI:10.1073/pnas.1218386110)(PubMed:23487766)
  46. Prediction of ligand-induced structural polymorphism of receptor interaction sites using machine learning. Takaya, D., Sato, T., Yuki, H., Sasaki, S., Tanaka, A., Yokoyama, S., Honma, T. J. Chem. Inf. Model., 53, 704-716, 2012. (DOI:10.1021/ci300458g)(PubMed:23351076)
  47. Protein loop modeling with optimized backbone potential functions. Liang, S., Zhang, C., Sarmiento, J., Standley, D.M. J. Chem. Theory Comput., 8, 1820-1827, 2012. (DOI:10.1021/ct300131p)
  48. The transcription factor Jdp2 controls bone homeostasis and antibacterial immunity by regulating osteoclast and neutrophil differentiation. Maruyama, K., Fukasaka, M., Vandenbon, A., Saitoh, T., Kawasaki, T., Kondo, T., Yokoyama, K.K., Kidoya, H., Takakura, N., Standley, D., Takeuchi, O., Akira, S. Immunity, 37, 1024-1036, 2012. (DOI:10.1016/j.immuni.2012.08.022. )(PubMed:23200825)

機能ゲノミクス領域(A、B)

2. 制御拠点

ライブラリー・スクリーニング領域

  1. Structural basis for simultaneous recognition of an O-glycan and its attached peptide of mucin family by immune receptor PILRα. Kuroki, K., Wangb, J., Ose, T., Yamaguchi, M., Tabata, S., Maita, N., Nakamura, S., Kajikawa, M., Kogure, A., Satoh, T., Arase H., Maenaka K. Proc. Natl. Acad. Sci. , 111, 8877-8882, 2015. (DOI:10.1073/pnas.1324105111 )(PubMed:24889612)
  2. Thermodynamic and structural characterization of the specific binding of Zn(II) to human protein DJ-1. Tashiro, S., Caaveiro, J.M., Wu, C.X., Hoang, Q.Q., Tsumoto, K. Biochemistry, 53, 2218-2220, 2014. (DOI:10.1021/bi500294h)(PubMed:24697266)
  3. Selective inhibitors of a PAF biosynthetic enzyme lysophosphatidylcholine acyltransferase 2. Tarui, M., Shindou, H., Kumagai, K., Morimoto, R., Harayama, T., Hashidate, T., Kojima, H., Okabe,T., Nagano, T., Nagase, T., Shimizu, T. J. Lipid Res., 55, 1386-1396, 2014. (DOI:10.1194/jlr.M049205 )(PubMed:24850807)
  4. Rational Hopping of a Peptidic Scaffold into Non-Peptidic Scaffolds: Structurally Novel Potent Proteasome Inhibitors Derived from a Natural Product, Belactosin A. Kawamura, S., Unno, Y., Hirokawa, T., Asai, A., Arisawa, M., Shuto, S. Chem. Commun., 50, 2445-2447 , 2014. (DOI:10.1039/c3cc48818g.)(PubMed:24452398)
  5. Structurally novel highly potent proteasome inhibitors created by the structure-based hybridization of nonpeptidic belactosin derivatives and peptide boronates. Kawamura, S., Unno, Y., Asa,i A., Arisawa, M., Shuto, S. J. Med. Chem., 57, 2726-2735 , 2014. (DOI:10.1021/jm500045x.)(PubMed:24524217)
  6. Total synthesis of syringolin?a and improvement of its biological activity. Chiba, T., Hosono, H., Nakagawa, K., Asaka, M., Takeda, H., Matsuda, A., Ichikawa, S. Angew. Chem. Int. Ed., 53, 4836-4839, 2014. (DOI:10.1002/anie.201402428)(PubMed:24668894)
  7. Synthesis and Biological Evaluation of Quinaldopeptin. Katayama, K., Okamura, T., Sunadome, T., Nakagawa, K., Takeda, H., Shiro, M., Matsuda, A., Ichikawa, S. J. Org. Chem., 79, 2580-2590, 2014. (DOI:10.1021/jo500039d)(PubMed:24555872)
  8. Development of Diversity-enhanced Extracts of Curcuma zedoaria and Their New Sesquiterpene-like Compounds. Kikuchi, H., Sakura, K., Oshima, Y. Org. Lett., 16, 1916-1919, 2014. (DOI:10.1021/ol5004324)(PubMed:24646363)
  9. Total syntheses of leuconoxine, leuconodine B, and melodinine E by oxidative cyclic aminal formation and diastereoselective ring-closing metathesis. Umehara, A., Ueda, H., Tokuyama, H. Org. Lett., 16, 2526-2529, 2014. (DOI:10.1021/0l500903e)(PubMed:24754345)
  10. The effect of podoplanin inhibition on lymphangiogenesis under pathological conditions. Maruyama, Y., Maruyama, K., Kato, Y., Kajiya, K., Moritoh, S., Yamamoto, K., Matsumoto, Y., Sawane, M., Kerjaschiki, D., Nakazawa, T., Kinoshita, S. Invest. Ophthalmol. Vis. Sci., 55, 4813-4822, 2014. (DOI:10.1167/iovs.13-13711.)(PubMed:24985477)
  11. Synthesis of functionalized polycyclic aromatic compounds via a formal [2+2]-cycloaddition. Nagamoto, Y., Yamaoka, Y., Fujimura, S., Takemoto, Y., Takasu, K. Org. Lett. , 16, 1008-1011, 2014. (DOI:10.1021/ol403757e.)(PubMed:24437688)
  12. Optimization of diaryl amine derivatives as kinesin spindle protein inhibitors. Takeuchi, T., Oishi, S., Kaneda, M., Misu, R., Ohno, H., Sawada, J., Asai, A., Nakamura, S., Nakanishi, I., Fujii, N. Bioorg. Med. Chem., 22, 3171-3179, 2014. (DOI:10.1016/j.bmc.2014.04.008)(PubMed:24794744)
  13. Design and synthesis of fluorescent probes for GPR54. Kaneda, M., Misu, R., Ohno, H., Hirasawa, A., Ieda, N., Uenoyama, Y., Tsukamura, H., Maeda, K., Oishi, S., Fujii, N. Bioorg. Med. Chem., 22, 3325-3330, 2014. (DOI:10.1016/j.bmc.2014.04.052)(PubMed:24857775)
  14. Gold-catalyzed cascade cyclization of (azido)ynamides: an efficient strategy for the construction of indoloquinolines. Tokimizu, Y., Oishi, S., Fujii, N., Ohno, H. Org. Lett. , 16, 3138-3141, 2014. (DOI:10.1021/ol5012604)(PubMed:24874723)
  15. Discovery of protein disulfide isomerase P5 inhibitors that reduce the secretion of MICA from cancer cells. Horibe, T., Torisawa, A., Okuno, Y., Kawakami, K. Chem. Bio. Chem., 15, 1599-1606, 2014. (DOI:10.1002/cbic.201400050)(PubMed:24920482)
  16. Dynamic kinetic resolution of racemic allylic alcohols via hydrolaseMetal combo catalysis: An effective method for the synthesis of optically active compounds. Akai, S. Chemistry Letters, 43, 746?754, 2014. (DOI:10.1246/cl.140223)
  17. Enantiospecific synthesis and cytotoxicity evaluation of ligudentatol: a programmed aromatization approach to the 2,3,4-trisubstituted phenolic motif via visible-light-mediated group transfer radical cyclization. Moustafa, G.A.I., Suizu, H., Aoyama, H., Arai, M., Akai, S., Yoshimitsu, T. Chemistry-An Asian Journal , 9, 1506 ? 1510, 2014. (DOI:10.1002/asia.201400110)(PubMed:19755802)
  18. Development of a highly sensitive, high-throughput assay for glycosyltransferases using enzyme-coupled fluorescence detection. Kumagai, K., Kojima, H., Okabe, T., Nagano, T. Anal. Biochem., 447, 146-155, 2013. (DOI:10.1016/j.ab.2013.11.025)(PubMed:24299989)
  19. Dynamic elements govern the catalytic activity of CapE, a capsular polysaccharide-synthesizing enzyme from Staphylococcus aureus. Miyafusa, T., Caaveiro, J.M., Tanaka, Y., Tsumoto, K. FEBS Lett., 587, 3824-3830, 2013. (DOI:10.1016/j.febslet.2013.10.009)(PubMed:24157361)
  20. Structure-activity relationship study of novel iminothiadiazolo-1 pyrimidinone antimicrobial agents. Paudel, A., Kaneko, K., Watanabe, A., Matsunaga, S., Kanai, M., Hamamoto, H., Sekimizu, K. J. Antibiotics, 66, 663-667, 2013. (DOI:10.1038/ja.2013.69)(PubMed:23820613)
  21. Identification of Novel Small Compounds that Restore E-cadherin Expression and Inhibit Tumor Cell Motility and Invasiveness. Hirano, T., Satow, R., Kato, A., Tamura, M., Murayama, Y., Saya, H., Kojima, H., Nagano, T., Okabe, T., Fukami, K. Biochem. Pharmacol., 86, 1419-1429, 2013. (DOI:10.1016/j.bcp.2013.09.001)(PubMed:24035834)
  22. Structural analysis for glycolipid recognition by the C-type lectins Mincle and MCL. Furukawa, A., Kamishikiryo, J., Mori, D., Toyonaga, K., Okabe, Y., Toji, A., Kanda, R., Miyake, Y., Ose, T., Yamasaki, S., Maenaka, K. Proc. Natl. Acad. Sci., 110, 17438-17443, 2013. (DOI:10.1073/pnas.1312649110.)(PubMed:24101491)
  23. Conformational restriction approach to b-secretase (BACE1) inhibitors III: Effective investigation of the binding mode by combinational use of X-ray analysis, isothermal titration calorimetry and theoretical calculations. Yonezawa, S., Fujiwara, K., Yamamoto, T., Hattori, K., Yamakawa, H., Muto, C., Hosono, M., Tanaka, Y., Nakano, T., Takemoto, H., Arisawa, M., Shuto, S. Bioorg. Med. Chem., 21, 6506-6522 , 2013. (DOI:10.1016/j.bmc.2013.08.036.)(PubMed:24051074)
  24. Investigation of the Non-Covalent Binding Mode of Covalent Proteasome Inhibitors around the Transition State by Combined Use of Cyclopropylic Strain-Based Conformational Restriction and Computational Modeling. Kawamura, S., Unno, Y., Tanaka, M., Sasaki, T., Yamano, A., Hirokawa, T., Kameda, T., Asai, A., Arisawa, M., Shuto, S. J. Med. Chem., 56, 5829-5842 , 2013. (DOI:10.1021/jm400542h.)(PubMed:23837692)
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合成領域

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3. 情報領域

情報領域
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  5. Identification of functionally important residues of the silkmoth pheromone biosynthesis-activating neuropeptide receptor, an insect ortholog of the vertebrate neuromedin U receptor. Kawai, T., Katayama, Y., Guo, L., Liu, D., Suzuki, T., Hayakawa, K., Lee, J. M., Nagamine, T., Hull, J. J., Matsumoto, S., Nagasawa, H., Tanokura, M., Nagata, K. J. Biol. Chem., 289, 19150-19163, 2014. (DOI:10.1074/jbc.M113.488999)(PubMed:24847080)
  6. Structural insights of post-translational modification sites in the proteome of Thermus thermophilus. Masui, R., Takahata, Y., Inoue, M., Iio, Y., Okanishi, H., Kim, K., Nakagawa, N., Yura, K., Kuramitsu, S. Struct. Funct. Genomics., 15, 137-151, 2014. (DOI:10.1007/s10969-013-9169-3)(PubMed:24407378)
  7. Protein experimental information management system (PREIMS) based on ontology: development and applications. Sato,J., Kozaki, K., Handa, S., Ikeda, T., Saka, R., Tomizuka, K., Nishiyama, Y., Okumura, T., Hirai, S., Ohno, T., Ohta, M., Date, S., Nakamura, H. IPSJ Transactions on Bioinformatics, 6, 9-17, 2013. (DOI:10.2197/ipsjtbio.6.9)
  8. Exhaustive comparison and classification of ligand-binding surfaces in proteins. Murakami, Y., Kinoshita, K., Kinjo, A. R., Nakamura, H. Protein Sci., 22, 1379-1391, 2013. (DOI:10.1002/pro.2329)(PubMed:23934772)
  9. Molecular dynamics simulations of a double-stranded DNA in an explicit solvent model with zero-dipole summation method. Arakawa, T., Kamiya, N., Nakamura, H., Fukuda, I. Plos One, 8, e76606, 2013. (DOI:10.1371/journal.pone.0076606)(PubMed:24124577)
  10. Community-wide evaluation of methods forpredicting the effect of mutations on protein?protein interactions. Moretti, R., Fleishman, S.J., Agius, R., Torchala, M., Bates, P.A., Kastritis, P.L., Rodrigues, J.P., Trellet, M., Bonvin, A.M., Cui, M., Rooman, M., Gillis, D., Dehouck, Y., Moal, I., Romero-Durana, M., Perez-Cano, L., Pallara, C., Jimenez, B., Fernandez-Recio, J., Flores, S., Pacella, M., Praneeth Kilambi, K., Gray, J.J., Popov, P., Grudinin, S., Esquivel-Rodriguez, J., Kihara, D., Zhao, N., Korkin, D., Zhu, X., Demerdash, O.N., Mitchell, J.C., Kanamori, E., Tsuchiya, Y., Nakamura, H., Lee, H., Park, H., Seok, C., Sarmiento, J., Liang, S., Teraguchi, S., Standley, D.M., Shimoyama, H., Terashi, G., Takeda-Shitaka, M,, Iwadate, M., Umeyama, H., Beglov, D., Hall, D.R., Kozakov, D., Vajda, S., Pierce, B.G., Hwang, H., Vreven, T., Weng, Z., Huang, Y., Li, H., Yang, X., Ji, X., Liu, S., Xiao, Y., Zacharias, M., Qin, S., Zhou, H.X., Huang, S.Y., Zou, X., Velankar, S., Janin, J., Wodak, S.J., Baker, D. Proteins, 81, 1980-1987, 2013. (DOI:10.1002/prot.24356)(PubMed:23843247)
  11. ATTED-II in 2014: Evaluation of Gene Coexpression in Agriculturally Important Plants. Obayashi, T., Okamura, Y., Ito, S., Tadaka, S., Aoki, Y., Shirota, M., Kinoshita, K. Plant Cell Physiol., 55, e6, 2013. (DOI:10.1093/pcp/pct178)(PubMed:24334350)
  12. Blind prediction of interfacial water positions in CAPRI. Lensink, M.F., Moal, I.H., Bates, P.A., Kastritis, P.L., Melquiond, A.S., Karaca, E., Schmitz, C., van Dijk, M., Bonvin, A.M., Eisenstein, M., Jimenez-Garcia, B., Grosdidier, S., Solernou, A., Perez-Cano, L., Pallara, C., Fernandez Recio J., Xu, J., Muthu, P., Praneeth Kilambi, K., Gray, J.J., Grudinin, S., Derevyanko, G., Mitchell, J.C., Wieting, J., Kanamori, E., Tsuchiya, Y., Murakami, Y., Sarmiento, J., Standley, D.M., Shirota, M., Kinoshita, K., Nakamura, H., Chavent, M., Ritchie, D.W., Park, H., Ko, J., Lee, H., Seok, C., Shen, Y., Kozakov, D., Vajda, S., Kundrotas, P.J., Vakser, I.A., Pierce, B.G., Hwang, H., Vreven, T., Weng, Z., Buch, I., Farkash, E., Wolfson, H.J., Zacharias, M., Qin, S., Zhou, H.X., Huang, S.Y., Zou, X., Wojdyla, J.A., Kleanthous, C., Wodak, S.J.. Proteins, 82, 620-632, 2013. (DOI:10.1002/prot.24439)(PubMed:24155158)
  13. Targeting BIG3-PHB2 interaction to overcome tamoxifen resistance in breast cancer cells. Yoshimaru, T., Komatsu, M., Matsuo, T., Chen, Y.A., Murakami, Y., Mizuguchi, K., Mizohata, E., Inoue, T., Akiyama, M., Yamaguchi, R., Imoto, S., Miyano, S., Miyoshi, Y., Sasa, M., Nakamura, Y., Katagiri, T. Nat. Communi., 4, e2443, 2013. (DOI:10.1038/ncomms3443)(PubMed:24051437)
  14. Exhaustive comparison and classification of ligand-binding surfaces in proteins. . Murakami, Y., Kinoshita, K., Kinjo, A.R., Nakamura, H.. Protein Sci., 22, 1379-1391, 2013. (DOI:10.1002/pro.2329)(PubMed:23934772)
  15. Accidental interaction between PDZ domains and diclofenac revealed by NMR-assisted virtual screening. Tenno, T., Goda, N., Umetsu, Y., Ota, M., Kinoshita, K., Hiroaki, H. Molecules, 18, 9567-9581, 2013. (DOI:10.3390/molecules18089567)(PubMed:23966078)
  16. Analyses of the general rule on residue pair frequencies in local amino acid sequences of soluble, ordered proteins. Shirota, M., Kinoshita, K. Protein Sci., 22, 725-733, 2013. (DOI:10.1002/pro.2255)(PubMed:23526551)
  17. Crystal structure and site-directed mutagenesis analyses of haloalkane dehalogenase LinB from Sphingobium sp. MI1205. Okai, M., Ohtsuka, J., Imai, F. L., Mase, T., Moriuchi, R., Tsuda, M., Nagata, K., Nagata, Y., Tanokura, M. J. Bacteriol., 195, 2642-2651, 2013. (DOI:10.1128/JB.02020-12)(PubMed:23564170)
  18. Crystal structure of conjugated polyketone reductase (CPRC1) from Candida parapsilosis IFO 0708 complexed with NADPH. Qin, H.-M., Yamamura, A., Miyakawa, T., Kataoka, M., Maruoka, S., Ohtsuka, J., Nagata, K., Shimizu, S., Tanokura, M. Proteins, 81, 2059-2063, 2013. (DOI:10.1002/prot.24363)(PubMed:23852710)
  19. Complex structure of the DNA-binding domain of AdpA, the global transcription factor in Streptomyces griseus, and a target duplex DNA reveals the structural basis of its tolerant DNA sequence specificity. Yao, M.D., Ohtsuka, J., Nagata, K., Miyazono, K., Zhi, Y., Ohnishi, Y., Tanokura, M. J. Biol. Chem., 288, 31019-31029, 2013. (DOI:10.1074/jbc.M113.473611)(PubMed:24019524)
  20. A novel mode of ferric ion-coordination of the periplasmic ferric ion-binding subunit, FbpA, of an ABC-type iron transporter from Thermus thermophiles HB8. Wang, S., Ogata, M., Horita, S., Ohtsuka, J., Nagata, K., Tanokura, M. Acta Crystallogr. D Biol. Crystallogr., 70, 196-202, 2013. (DOI:10.1107/S1399004713026333)(PubMed:24419392)
  21. Distinct Conformation of ATP Molecule in Solution and on Protein. Kobayashi, E., Yura, K., Nagai, Y. Biophysics, 9, 1-12, 2013. (DOI:10.2142/biophysics.9.1)
  22. CoDP: predicting the impact of unclassified genetic variants in MSH6 by the combination of different properties of the protein. Terui, H., Akagi, K., Kawame, H., Yura, K. J. Biomed. Sci., 20, e25, 2013. (DOI:10.1186/1423-0127-20-25)(PubMed:23621914)
  23. Molecular and clinical characteristics of MSH6 germline variants detected in colorectal cancer patients. Terui, H., Tachikawa, T., Kakuta, M., Nishimura, Y., Yatsuoka, T., Yamaguchi, K., Yura, K., Akagi, K., Oncology Reports, 30, 2909-2916, 2013. (DOI:10.3892/or.2013.2781)(PubMed:24100870)
  24. Human origin recognition complex binds preferentially to G-quadruplex-preferable RNA and single-stranded DNA. Hoshina, S., Yura, K., Teranishi, H., Kiyasu, N., Tominaga, A., Kadoma, H., Nakatsuka, A., Kunichika, T., Obuse, C., Waga, S. J. Biol. Chem., 288, 30161-30171, 2013. (DOI:10.1074/jbc.M113.492504)(PubMed:24003239)
  25. Cephalopod eye evolution was modulated by the acquisition of Pax-6 splicing variants. Yoshida, M., Yura, K., Ogura, A. Sci. Rep., 4, e4256, 2013. (DOI:10.1038/srep04256)(PubMed:24594543)
  26. Application of zero-dipole summation method to molecular dynamics simulations of amembrane protein system. Kamiya, N., Fukuda, I., Nakamura, H. Chem. Phys. Lett., 568-569, 26-32, 2012. (DOI:10.1016/j.cplett.2013.03.014)
  27. Ion concentration-dependent ion conduction mechanism of a voltage-sensitive potassium channel. Kasahara, K., Shirota, M., Kinoshita, K. PLoS One, 8, e56342, 2012. (DOI:10.1371/journal.pone.0056342)(PubMed:23418558)
  28. COXPRESdb: a database of comparative gene coexpression networks of eleven species for mammals. Obayashi, T., Okamura, Y., Ito, S., Tadaka, S., Motoike, I.N., Kinoshita, K. Nucleic Acids Res., 41, D1014-1020, 2012. (DOI:10.1093/nar/gks1014. )(PubMed:23203868)
  29. Comprehensive classification and diversity assessment of atomic contacts in protein-small ligand interactions. Kasahara, K., Shirota, M., Kinoshita, K. J. Chem. Inf. Model, 53, 241-248, 2012. (DOI:10.1021/ci300377f)(PubMed:23186137)
  30. The structure of brazzein, a sweet-tasting protein from the wild African plant Pentadiplandra brazzeana.. Nagata, K., Hongo, N., Kameda, Y., Yamamura, A., Sasaki, H., Lee, W. C., Ishikawa, K., Suzuki, E.I., Tanokura, M. Acta Crystallogr. D Biol. Crystallogr., 69, 642-647, 2012. (DOI:10.1107/S0907444913001005)(PubMed:23519673)
  31. Development of a peptide antagonist against fsr quorum sensing of Enterococcus faecalis. Nakayama, J., Yokohata, R., Sato, M., Suzuki, T., Matsufuji, T., Nishiguchi, K., Kawai, T., Yamanaka, Y., Nagata, K., Tanokura, M., Sonomoto, K. ACS Chem. Biol., 8, 804-811, 2012. (DOI:10.1021/cb300717f)(PubMed:23362999)
  32. Structural units important for activity of a novel-type phosphoserine phosphatase from Hydrogenobacter thermophilus TK-6 revealed by crystal structure analysis. Chiba, Y., Horita, S., Ohtsuka, J., Arai, H., Nagata, K., Igarashi, Y., Tanokura, M., Ishii, M. J. Biol. Chem., 288, 11448-11458, 2012. (DOI:10.1074/jbc.M112.449561)(PubMed:23479726)
  33. Tuning glycosidase inhibition through aglycone interactions: pharmacological chaperones for Fabry disease and GM1 gangliosidosis. Aguilar-Moncayo, M., Takai, T., Higaki, K., Mena-Barragan T., Hirano, Y., Yura, K., Li, L., Yu, Y., Ninomiya, H., Garcia-Moreno, M.I., Ishii, S., Sakakibara, Y., Ohno, K., Nanba, E., Mellet, C.O., Fernandez, J.M.G., Suzuki, Y. Chemical Communications, 48, 6514-6516, 2012. (DOI:10.1039/C2CC32065G )(PubMed:22618082)
  34. A bicyclic 1-deoxygalactonojirimycin derivative as a novel pharmacological chaperone for GM1 gangliosidosis. Takai, T., Higaki, K., Aguilar-Moncayo, A., Mena-Barragan, T., Hirano, Y., Yura, K., Yu, L., Ninomiya, H., Garcia-Moreno, M.I., Sakakibara, Y., Ohno, K., Nanba, E., Mellet, C.O., Fernandez, J.M.G., Suzuki, Y. Molecular Therapy, 21, 526-532, 2012. (DOI:10.1038/mt.2012.263)(PubMed:23337983)

年度別

2015
  1. Crystal structures of the human adiponectin receptors. Tanabe, H., Fujii, Y., Okada-Iwabu, M., Iwabu, M., Nakamura, Y., Hosaka, T., Motoyama, K., Ikeda, M., Wakiyama, M., Terada, T., Ohsawa, N., Hato, M., Ogasawara, S., Hino, T., Murata, T., Iwata, S., Hirata, K., Kawano, Y., Yamamoto, M., Kimura-Someya, T., Shirouzu, M., Yamauchi, T., Kadowaki, T., Yokoyama, S. Nature, 520, 312-316, 2015. (DOI:doi:10.1038/nature14301)(PubMed:25855295)
  2. Making things better. Takagi, J., Tate, C.G. Current Opin. Struct. Biol., in press, 2015.
  3. Structural basis for simultaneous recognition of an O-glycan and its attached peptide of mucin family by immune receptor PILRα. Kuroki, K., Wangb, J., Ose, T., Yamaguchi, M., Tabata, S., Maita, N., Nakamura, S., Kajikawa, M., Kogure, A., Satoh, T., Arase H., Maenaka K. Proc. Natl. Acad. Sci., 111, 8877-8882, 2015. (DOI:10.1073/pnas.1324105111 )(PubMed:24889612)
2014
  1. Structural basis of starvation-induced assembly of the autophagy initiation complex. Fujioka, Y., Suzuki, S.W., Yamamoto, H., Kondo-Kakuta, C., Kimura, Y., Hirano, H., Akada, R., Inagaki, F., Ohsumi, Y. and Noda, N.N. J. Phys.: Conf. Ser., 21, 513-521, 2014. (DOI:10.1038/nsmb.2822)(PubMed:24793651)
  2. X-ray crystallographic structure of RNase Po1 that exhibits anti-tumor activity. Kobayashi, H., Katsutani, T., Hara, Y., Motoyoshi, N., Itagaki, T., Akita, F., Higashiura, A., Yamada, Y., Inokuchi, N., Suzuki, M. J Synchrotron Radiat., 20, 838-42, 2014. (DOI:10.1248/bpb.b13-00929)(PubMed:24882409)
  3. S46 peptidases are the first exopeptidases to be members of clan PA. Sakamoto,Y., Suzuki, Y., Iizuka, I., Tateoka, C., Roppongi, S., Fujimoto, M., Inaka, K., Tanaka, H., Masaki, M., Ohta, K., Okada, H., Nonaka, T., Morikawa, Y., T. Nakamura, K., Ogasawara, W., Tanaka, N. J Synchrotron Radiat., 20, 938-42, 2014. (DOI:10.1038/srep04977)(PubMed:24827749)
  4. Structural basis of Sec-independent membrane protein insertion by YidC. Kumazaki, K., Chiba, S., Takemoto, M., Furukawa, A., Nishiyama, K., Sugano, Y., Mori, T., Dohmae, N., Hirata, K., Nakada-Nakura, Y., Maturana, A.D., Tanaka, Y., Mori, H., Sugita, Y., Arisaka, F., Ito, K., Ishitani, R., Tsukazaki, T., Nureki, O. J Synchrotron Radiat., 20, 890-3, 2014. (DOI:10.1038/nature13167)(PubMed:24739968)
  5. Crystal structure of a claudin provides nsight into the architecture of tight junctions. Suzuki, H., Nishizawa, T., Tani, K., Yamazaki, Y., Tamura, A., Ishitani, R., Dohmae, N., Tsukita, S., Nureki, O., Fujiyoshi, Y. Biophys. Res. Commun., 447, 32-37, 2014. (DOI:10.1126/science.1248571)(PubMed:24744376)
  6. Crystal structure of Cas9 in complex with guide RNA and target DNA. Nishizawa, T., Kita, S., Maturana, A.D., Furuya, N., Hirata, K., Kasuya, G., Ogasawara, S., Dohmae, N., Iwamoto, T., Ishitani, R., Nureki, O. Science, 341, 168-72, 2014. (DOI:10.1016/j.cell.2014.02.001)(PubMed:24529477)
  7. Structural basis for gating mechanisms of a eukaryotic P-glycoprotein homolog. Kodan, A., Yamaguchi, T., Nakatsu, T., Sakiyama, K., Hipolito, C.J., Fujioka, A., Hirokane, R., Ikeguchi, K., Watanabe, B., Hiratake, J., Kimura, Y., Suga, H., Ueda, K., Kato, H. Nature, 496, 247-51, 2014. (DOI:10.1073/pnas.1321562111)(PubMed:24591620)
  8. Structural insights into the epimerization of beta-1,4-linked oligosaccharides catalyzed by cellobiose 2-epimerase, the sole enzyme epimerizing non-anomeric hydroxyl groups of nnmodified sugars. Fujiwara, T., Saburi, W., Matsui, H., Mori, H., Yao, M. J.Biol. Chem., 289, 3405-3415, 2014. (DOI:10.1074/jbc.M113.531251)(PubMed:24362032)
  9. Structural basis of the divergent oxygenation reactions catalyzed by the rieske nonheme iron oxygenase carbazole 1,9a-dioxygenase. Inoue, K., Usami, Y., Ashikawa, Y., Noguchi, H., Umeda, T., Yamagami-Ashikawa, A., Horisaki, T., Uchimura, H., Terada, T., Nakamura, S., Shimizu, K., Habe, H., Yamane, H., Fujimoto, Z., Nojiri, H. Appl. Environ Microbiol., 80, 2821-2832, 2014. (DOI:10.1128/AEM.04000-13)(PubMed:24584240)
  10. In vitro synthesis of the E. coli sec translocon from DNA. Matsubayashi, H., Kuruma, Y., Ueda, T. Angew Chem Int Ed Engl., 53, 7535-7538, 2014. (DOI:10.1002/anie.201403929)(PubMed:24894900)
  11. X-ray crystallographic structure of RNase Po1 that exhibits antitumor activity. Kobayashi, H., Katsutani, T., Hara, Y., Motoyoshi, N., Itagaki, T., Akita, F., Higashiura, A., Yamada, Y., Inokuchi, N., Suzuki, M. Biol. Pharm. Bull., 37, 968-978, 2014. (DOI:10.1248/bpb.b13-00929)(PubMed:24882409)
  12. The phosphorylation of HIV-1 Gag by atypical protein kinase C facilitates viral infectivity by promoting Vpr incorporation into virions. Kudoh, A., Takahama, S., Sawasaki, T., Ode, H., Yokoyama, M., Okayama, A., Ishikawa, A., Miyakawa, K., Matsunaga, S., Kimura, H., Sugiura, W., Sato, H., Hirano, H., Ohno, S., Yamamoto, N., Ryo, A. Retrovirology, 11, e9, 2014. (DOI:10.1186/1742-4690-11-9)(PubMed:24447338)
  13. Suppression of LUBAC-mediated linear ubiquitination by a specific interaction between LUBAC and the deubiquitinases CYLD and OTULIN. Takiuchi, T., Nakagawa, T., Tamiya, H., Fujita, H., Sasaki, Y., Saeki, Y., Takeda, H., Sawasaki, T., Buchberger, A., Kimura, T., Iwai, K. Genes Cells, 19, 254-272, 2014. (DOI:10.1111/gtc.12128)(PubMed:24461064)
  14. Involvement of Hepatitis C virus NS5A hyperphosphorylation mediated by casein kinase I-α in infectious virus production. Masaki, T., Matsunaga, S., Takahashi, H., Nakashima, K., Kimura, Y., Ito, M., Matsuda, M., Murayama, A., Kato, T., Hirano, H., Endo, Y., Lemon, S.M., Wakita, T., Sawasaki, T., Suzuki, T. J Virol., 88, 7541-7555, 2014. (DOI:10.1128/JVI.03170-13)(PubMed:24760886)
  15. Retroviral vectors for homologous recombination provide efficient cloning and expression in mammalian cells. Kobayashi, E., Kishi, H., Ozawa, T., Horii, M., Hamana, H., Nagai, T., Muraguchi, A. Biochem. Bioph. Res. Co., 444, 319-324, 2014. (DOI:10.1016/j.bbrc.2014.01.049)(PubMed:24462869)
  16. Structural basis for potent inhibition of SIRT2 deacetylase by a macrocyclic peptide inducing dynamic structural change. Yamagata, K., Goto, Y., Nishimasu, H., Morimoto, J., Ishitani, R., Dohmae, N., Takeda, N., Nagai, R., Komuro, I., Suga, H., Nureki, O. Structure, 22, 345-352, 2014. (DOI:10.1016/j.str.2013.12.001)(PubMed:24389023)
  17. Structural basis for gating mechanisms of a eukaryotic P-glycoprotein homolog. Kodan, A., Yamaguchi, T., Nakatsu, T., Sakiyama, K., Hipolito, C.J., Fujioka, A., Hirokane, R., Ikeguchi, K., Watanabe, B., Hiratake, J., Kimura, Y., Suga, H., Ueda, K., Kato, H. Pro. Nat. Acad. Sci., 111, 4049-4054, 2014. (DOI:10.1073/pnas.1321562111)(PubMed:24591620)
  18. Protein cocrystallization molecules originating from in vitro selected macrocyclic peptides. Hipolito, C.J., Bashiruddin, N.K., Suga, H. Curr Opin Struct Biol., 26, 24-31, 2014. (DOI:10.1016/j.sbi.2014.03.001)(PubMed:24681557)
  19. PA tag: a versatile protein tagging system using a super high affinity antibody against a dodecapeptide derived from human podoplanin. Fujii, Y., Kaneko, M., Neyazaki, M., Nogi, T., Kato, Y., Takagi, J. Protein Exp. Pur., 95, 240-247, 2014. (DOI:10.1016/j.pep.2014.01.009)(PubMed:24480187)
  20. Lysosomal sorting of amyloid-β by the SORLA receptor is impaired by a familial Alzheimer's disease mutation. Caglayan, S., Takagi-Niidome, S., Liao, F., Carlo, A-S., Schmidt, V., Burgert, T., Kitago, Y., Fuchtbauer, E-M., Fuchtbauer, A., Holtzman, D.M., Takagi, J., Wilnow, T.E. Science Transl. Med., 6, e223ra20, 2014. (DOI:10.1126/scitranslmed.3007747)(PubMed:24523320)
  21. PA tag: a versatile protein tagging system using a super high affinity antibody against a dodecapeptide derived from human podoplanin. Fujii, Y., Kaneko, M., Neyazaki, M., Nogi, T., Kato, Y. and Takagi, J. Protein Exp. Pur., 95, 240-247, 2014. (DOI:10.1016/j.pep.2014.01.009)(PubMed:24480187)
  22. IDH2 mutation is frequently observed in giant cell tumor of bone. Kaneko, M., Liu, X., Oki, H., Ogasawara, S., Nakamura, T., Saidoh, N., Tsujimoto, Y., Matsuyama, Y., Uruno, A., Sugawara, M., Tsuchiya, T., Yamakawa, M., Yamamoto, M., Takagi, M., Kato, Y. Cancer Sci., 105, 744-748, 2014. (DOI:10.1111/cas.12413)(PubMed:24898068)
  23. PA tag: a versatile protein tagging system using a super high affinity antibody against a dodecapeptide derived from human podoplanin. Fujii, Y., Kaneko, M., Neyazaki, M., Nogi, T., Kato, Y., Takagi, J. Protein Exp. Pur., 95, 240-247, 2014. (DOI:10.1016/j.pep.2014.01.009)(PubMed:24480187)
  24. Distinct Features of the Histone Core Structure in Nucleosomes Containing the Histone H2A.B Variant. Sugiyama, M., Arimura, Y., Shirayama, K., Fujita, R., Oba, Y., Sato, N., Inoue, R., Oda, T., Sato, M., Heenan, R.K., Kurumizaka, H. Biophys. J., 106, 2206-2213, 2014. (DOI:10.1016/j.bpj.2014.04.007)(PubMed:24853749)
  25. Purification, crystallization and preliminary X-ray crystallographic analysis of a rice Rac/Rop GTPase, OsRac1. Kosami, K-I., Ohki, I., Hayashi, K., Tabata, R., Usugi, S., Kawasaki, T., Fujiwara, T., Nakagawa, A., Shimamoto, K., Kojima, C. Acta Cryst., F70, 113-115, 2014. (DOI:10.1107/S2053230X13033645)(PubMed:24419631)
  26. Active-site structure of thermophilic Foc subunit ring in membranes elucidated by solid-state NMR. Kang, S-J., Todokoro, Y., Yumen, I., Shen, B., Iwasaki, I., Suzuki, T., Miyagi, A., Yoshida, M., Fujiwara, T., Akutsu, H. Biophysical J., 106, 390-398, 2014. (DOI:10.1016/j.bpj.2013.12.005)(PubMed:24461014)
  27. 1H, 15N and 13C resonance assignments of the conserved region in the middle domain of S. pombe Sin1 protein. Kataoka, S., Furuita, K., Hattori, Y., Kobayashi, N., Ikegami, T., Shiozaki, K., Fujiwara, T., Kojima, C. Biomol. NMR Assign., 9, 89-92, 2014. (DOI:10.1007/s12104-014-9550-6)(PubMed:24610629)
  28. Cell-free expression of protein complexes for structural biology. Terada, T., Murata, T., Shirouzu, M., Yokoyama, S. Methods Mol. Biol. , 1091, 151-159, 2014. (DOI:10.1007/978-1-62703-691-7_10)(PubMed:24203330)
  29. Cell-free membrane protein expression. Kimura-Someya, T., Shirouzu, M., Yokoyama, S. Methods Mol. Biol., 1118 , 267-273, 2014. (DOI:10.1007/978-1-62703-782-2_18)(PubMed:24395423)
  30. Dimer-dimer interaction of the bacterial selenocysteine synthase SelA promotes functional active-site formation and catalytic specificity. Itoh, Y., Brocker, M.J., Sekine, S-I., Soll, D., Yokoyama, S. J. Mol. Biol., 8, 1723-1735, 2014. (DOI:10.1016/j.jmb.2014.01.003)(PubMed:24456689)
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2013
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  210. CoDP: predicting the impact of unclassified genetic variants in MSH6 by the combination of different properties of the protein. Terui, H., Akagi, K., Kawame, H., Yura, K. J. Biomed. Sci., 20, e25, 2013. (DOI:10.1186/1423-0127-20-25)(PubMed:23621914)
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2012
  1. Elongation factor G is a critical target during oxidative damage to the translation system of Escherichia coli. Nagano, T., Kojima, K., Hisabori, T., Hayashi. H., Morita, E.H., Kanamori, T., Miyagi, T., Ueda, T., Nishiyama, Y. J. Biol. Chem., 287, 28697-704, 2012. (DOI:10.1074/jbc.M112.378067)(PubMed:22773838)
  2. Structure and function of abscisic acid receptors. Miyakawa, T., Fujita, Y., Yamaguchi-Shinozaki, K., Tanokura, M. Trends Plant Sci., 18, 259-66, 2012. (DOI:10.1016/j.tplants.2012.11)(PubMed:23265948)
  3. Calaxin drives sperm chemotaxis by Ca2+-mediated direct modulation of a dynein motor. Mizuno, K., Shiba, K., Okai, M., Takahashi, Y., Shitaka, Y., Oiwa, K., Tanokura, M., Inaba, K. Pro. Nat. Acad. Sci., 109, 20497-502, 2012. (DOI:10.1073/pnas.1217018109)(PubMed:23169663)
  4. Novel approach to identifying autoantibodies in rheumatoid synovitis with a biotinylated human autoantigen library and the enzyme-labeled antigen method. Mizutani, Y., Matsuoka, K.,, Takeda, H., Shiogama, K., Inada, K., Hayakawa, K., Yamada, H., Miyazaki, T., Sawasaki, T., Endo, Y., Tsutsumi, Y. J. Immunol. Methods, 387, 57-70, 2012. (DOI:10.1016/j.jim.2012.09.011)(PubMed:23044167)
  5. Interferon-induced SCYL2 limits release of HIV-1 by triggering PP2A-mediated dephosphorylation of the viral protein Vpu. Miyakawa, K., Sawasaki, T., Matsunaga, S., Tokarev, A., Quinn, G., Kimura, H., Nomaguchi, M., Adachi, A., Yamamoto, N., Guatelli, J., Ryo, A. Sci. Signal., 5, era73, 2012. (DOI:10.1126/scisignal.2003212)(PubMed:23047923)
  6. A novel rabbit immunospot array assay on a chip allows for the rapid generation of rabbit monoclonal antibodies with high affinity. Ozawa, T., Piao, X., Kobayashi, E., Zhou, Y., Sakurai, H., Andoh, T., Jin, A., Kishi, H., Muraguchi, A. PLoS One, 7, e52383, 2012. (DOI:10.1371/journal.pone.0052383)(PubMed:23300658)
  7. Reduced Level of the BCL11B protein is associated with adult T-cell leukemia/lymphoma. Kurosawa, N., Fujimoto, R., Ozawa, T., Itoyama, T., Sadamori, N., Isobe, M. PLoS One, 8, e55147, 2012. (DOI:10.1371/journal.pone.0055147)(PubMed:23383087)
  8. Crystal structure of Enpp1, an extracellular glycoprotein involved in bone mineralization and insulin signaling. Kato, K., Nishimasu, H., Okudaira, S., Mihara, E., Ishitani, R., Takagi, J., Aoki, J., Nureki, O. Proc. Natl. Acad. Sci., 109, 16876-16881, 2012. (DOI:10.1073/pnas.1208017109)(PubMed:23027977)
  9. The structure of the deacetylase domain of E. coli PgaB, an enzyme required for biofilm formation. Nishiyama, T., Noguchi, H., Yoshida, H., Park, SY, Tame, J.R.H. Acta. Cryst. D., 69, 44-51, 2012. (DOI:10.1107/S0907444912042059)(PubMed:23275162)
  10. Crystal structure of penicillin-binding protein 3 (PBP3) from methicillin-resistant Staphylococcus aureus in the apo and cefotaxime-bound forms. Yoshida, H., Kawai, F., Obayashi, E., Akashi, S., Roper, D.I., Tame, J.R., Park, S.Y. J. Mol. Biol., 423, 351-64, 2012. (DOI:10.1016/j.jmb.2012.07.012)(PubMed:22846910)
  11. Intrinsic nucleic acid-binding activity of Chp1 chromodomain is required for heterochromatic gene silencing. Ishida, M., Shimojo, H., Hayashi, A., Kawaguchi, R., Ohtani, Y., Uegaki, K., Nishimura, Y., Nakayama, J. Mol. Cell, 47, 228-41, 2012. (DOI: 10.1016/j.molcel.2012.05.017)(PubMed:22727667)
  12. Function of homo- and hetero-oligomers of human nucleoplasmin/nucleophosmin family proteins NPM1, NPM2 and NPM3 during sperm chromatin remodeling. Okuwaki, M., Sumi, A., Hisaoka, M., Saotome-Nakamura, A., Akashi, S., Nishimura, Y., Nagata, K. Nucleic Acids Res., 40, 4861-78, 2012. (DOI:10.1093/nar/gks162.)(PubMed:22362753)
  13. An automated system designed for large scale NMR data deposition and annotation: application to over 600 assigned chemical shift data entries to the BioMagResBank from the Riken Structural Genomics/Proteomics Initiative internal database. Kobayashi, N., Harano, Y., Tochio, N., Nakatani, E., Kigawa, T., Yokoyama, S., Mading, S., Ulrich, E.L., Markley, J.L., Akutsu, H., Fujiwara, T. J. Biomol. NMR, 53, 311-320, 2012. (DOI:10.1007/s10858-012-9641-6)(PubMed:22689068)
  14. Helium-cooling and -spinning dynamic nuclear polarization for sensitivity-enhanced solid-state NMR at 14 T and 30 K. Matsuki, Y., Ueda, K., Idehara, T., Ikeda, R., Ogawa, I., Nakamura, S., Toda, M., Anai, T., Fujiwara, T. J. Magn. Reson., 225, 1-9, 2012. (DOI:10.1016/j.jmr.2012.09.008)(PubMed:23079589)
  15. Reconstitution of eukaryotic translation initiation factor 3 by co-expression of the subunits in a human cell-derived in vitro protein synthesis system. Masutani, M., Machida, K., Kobayashi, T., Yokoyama, S., Imataka, H. Protein Expr. Purif., 87, 5-10, 2012. (DOI:10.1016/j.pep.2012.10.001)(PubMed:23063735)
  16. A novel crystal form of pyrrolysyl-tRNA synthetase reveals the pre- and post-aminoacyl-tRNA synthesis conformational states of the adenylate and aminoacyl moieties and an asparagine residue in the catalytic site. Yanagisawa, T., Sumida, T., Ishii, R., Yokoyama, S. Acta Crystallogr. D Biol. Crystallogr., 69, 5-15, 2012. (DOI:10.1107/S0907444912039881)(PubMed:23275158)
  17. Tetrameric interaction of the ectoenzyme CD38 on the cell surface enables its catalytic and raft-Association activities. Hara-Yokoyama, M., Kukimoto-Niino, M., Terasawa, K., Harumiya, S., Podyma-Inoue, K.A., Hino, N., Sakamoto, K., Itoh, S., Hashii, N., Hiruta, Y., Kawasaki, N., Mishima-Tsumagari, C., Kaitsu, Y., Matsumoto, T., Wakiyama, M., Shirouzu, M., Kasama, T., Takayanagi, H., Utsunomiya-Tate, N., Takatsu, T., Katada, K., Hirabayashi, Y., Yokoyama, S., Yanagishita, M. Structure, 20, 1585-1595, 2012. (DOI:10.1016/j.str.2012.06.017)(PubMed:22863568)
  18. Crystallization and preliminary X-ray crystallographic analysis of Aquifex aeolicus SelA, a bacterial selenocysteine synthase. Itoh, Y., Sekine, S-I., Yokoyama, S. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun., 68, 1128-1133, 2012. (DOI:10.1107/S1744309112033519)(PubMed:22949212)
  19. Meningococcal PilV potentiates Neisseria meningitidis type IV pilus-mediated internalization into human endothelial and epithelial cells. Takahashi, H., Yanagisawa, T., Kim, K.S., Yokoyama, S., Ohnishi, M. Infect. Immun., 80, 4154-4166, 2012. (DOI:10.1128/IAI.00423-12)(PubMed:22988016)
  20. Insights from Pim1 structure for anti-cancer drug design. Ogawa, N., Yuki, H., Tanaka, A. Expert Opin. Drug Discov., 7, 1177-1192, 2012. (DOI:10.1517/17460441.2012.727394)(PubMed:23004574)
  21. Dimerization of DOCK2 is essential for DOCK2-mediated Rac activation and lymphocyte migration. Terasawa, M., Uruno, T., Mori, S., Kukimoto-Niino, M., Nishikimi, A., Sanematsu, F., Tanaka, Y., Yokoyama, S., Fukui, Y. PLoS ONE, 7, e46277, 2012. (DOI:10.1371/journal.pone.0046277)(PubMed:23050005)
  22. UTX and UTY demonstrate histone demethylase-independent function in mouse embryonic development. Shpargel, K.B., Sengoku, T., Yokoyama, S., Magnuson, T. PLoS Genet., 8, e1002964, 2012. (DOI:10.1371/journal.pgen)(PubMed:23028370)
  23. Characterization and structure of the Aquifex aeolicus protein DUF752: a bacterial tRNA-methyltransferase (MnmC2) functioning without the usually fused oxidase domain (MnmC1). Kitamura, A., Nishimoto, M., Sengoku, T., Shibata, R., Jager, G., Bjork, G.R., Grosjean, H., Yokoyama, S., Bessho, Y. J. Biol. Chem., 287, 43950-43960, 2012. (DOI:10.1074/jbc.M112.409300)(PubMed:23091054)
  24. Structural biology toward rational drug development in collaboration with molecular imaging. Umehara, T., Shirouzu, M., Yokoyama, S. Curr. Med. Imaging Rev., 8, 308-313, 2012. (DOI:10.2174/157340512803759794)
  25. Structure of the Rho-specific guanine nucleotide-exchange factor Xpln. Murayama, K., Kato-Murayama, M., Akasaka, R., Terada, T., Yokoyama, S., Shirouzu, M. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun., 68, 1455-1459, 2012. (DOI:10.1107/S1744309112045265)(PubMed:23192023)
  26. Molecular dynamics simulations of yeast F1-ATPase before and after 16° rotation of the γ subunit. Ito, Y., Yoshidome, T., Matubayasi, N., Kinoshita, M., Ikeguchi, M. J. Phys. Chem. B, 117, 3298-3307, 2012. (DOI:10.1021/jp312499u)(PubMed:23452086)
  27. MICAN: a protein structure alignment algorithm that can handle Multiple-chains, inverse alignments, Ca only models, Alternative alignments, and Non-sequential alignments. Minami, S., Sawada, K., Chikenji, G. BMC Bioinformatics, 18,14-24, 2012. (DOI:10.1186/1471-2105-14-24)(PubMed:23331634)
  28. Substrate-shielding and hydrolytic reaction in hydrolases. Kanematsu, Y., Koike, R., Amemiya, T., Ota, M. Proteins, 81, 926-932, 2012. (DOI:10.1002/prot.24253)(PubMed:23345013)
  29. A new method for evaluating the specificity of indirect readout in protein-DNA recognition. Yamasaki, S., Terada, T., Shimizu, K., Kono, H., Sarai, A. Nucleic Acids Res., 40, e129, 2012. (DOI:10.1093/nar/gks462)(PubMed:22618872)
  30. Blind prediction of quaternary structures of homo-oligomeric proteins from amino acid sequences based on templates. Morita, M., Kakuta, M., Shimizu, K., Nakamura, S. J. Proteome. Sci. Comput. Biol., 1, e, 2012. (DOI:10.7243/2050-2273-1-1)
  31. A normalization strategy for comparing tag count data. Kadota, K., Nishiyama, T., Shimizu, K. Algorithms. Mo.l Biol., 7, e5 , 2012. (PubMed:22475125)
  32. A new entropy model for RNA: part II, Persistence-related entropic contributions to RNA secondary structure free energy calculation. Dawson, W., Yamamoto,K., Shimizu, K., Kawai, G. J. Nucleic. Acids. Investig., 3, 4-18, 2012. (DOI:10.4081/jnai.2013.e2)
  33. Small-angle X-ray scattering constraints and local geometry like secondary structures can construtct a coarse-grained protein model at amino acid residue resolution. Morimoto, Y., Nakagawa, T., Kojima, M. Biochem. Biophys. Res. Commun., 431, 65-69, 2012. (DOI:10.1016/j.bbrc)(PubMed:23291239)
  34. Structure of the trypanosome cyanide-insensitive alternative oxidase. Shiba, T., Kido, Y., Sakamoto, K., Inaoka, D. K., Tsuge, C., Tatsumi, R., Takahashi, G., Balogun, E. O., Nara, T., Aoki, T., Honma, T., Tanaka, A., Inoue, M., Matsuoka, S., Saimoto, H., Moore, A. L., Harada, S., Kita, K. Proc. Natl. Acad. Sci., 110, 4580-4585, 2012. (DOI:10.1073/pnas.1218386110)(PubMed:23487766)
  35. Prediction of ligand-induced structural polymorphism of receptor interaction sites using machine learning. Takaya, D., Sato, T., Yuki, H., Sasaki, S., Tanaka, A., Yokoyama, S., Honma, T. J. Chem. Inf. Model., 53, 704-716, 2012. (DOI:10.1021/ci300458g)(PubMed:23351076)
  36. Protein loop modeling with optimized backbone potential functions. Liang, S., Zhang, C., Sarmiento, J., Standley, D.M. J. Chem. Theory Comput., 8, 1820-1827, 2012. (DOI:10.1021/ct300131p)
  37. The transcription factor Jdp2 controls bone homeostasis and antibacterial immunity by regulating osteoclast and neutrophil differentiation. Maruyama, K., Fukasaka, M., Vandenbon, A., Saitoh, T., Kawasaki, T., Kondo, T., Yokoyama, K.K., Kidoya, H., Takakura, N., Standley, D., Takeuchi, O., Akira, S. Immunity, 37, 1024-1036, 2012. (DOI:10.1016/j.immuni.2012.08.022)(PubMed:23200825)
  38. Rational evolution of a novel type of potent and selective proviral integration site in Moloney murine leukemia virus kinase 1 (PIM1) inhibitor from a screening-hit compound. Nakano, H., Saito, N., Parker, L, Tada, Y., Abe, M., Tsuganezawa, K., Yokoyama, S., Tanaka, A., Kojima, H., Okabe, T., Nagano, T. J. Med. Chem., 55, 5151-5164, 2012. (DOI:10.1021/jm3001289)(PubMed:22540945)
  39. Incorporation of rapid thermodynamic data in fragment-based drug discovery. Kobe, A., Caaveiro, J.M., Tashiro, S., Kajihara, D., Kikkawa, M., Mitani, T., Tsumoto, K. J. Med. Chem., 56, 2155-2159, 2012. (DOI:10.1021/jm301603n)(PubMed:23419007)
  40. Oxysterol-binding protein (OSBP) family I is the target of minor enviroxime-like compounds. Arita, M., Kojima, H., Nagano, T., Okabe, T., Wakita, T., Shimizu, H. J. Virol., 87, 4252-4260, 2012. (DOI:10.1128/JVI.03546-12)(PubMed:23365445)
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  50. Synthesis of pachastrissamine (jaspine B) and its derivatives by the late-stage introduction of the C-2 alkyl side-chains using olefin cross metathesis. Yoshimitsu, Y., Miyagaki, J., Oishi, S., Fujii, N., Ohno, H. Tetrahedron, 69, 4211-4220, 2012. (DOI:10.1016/j.tet.2013.03.091)
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