| Co-Investigator(Kenkyū-buntansha) |
KYO Masaharu Kagawa Univ., 農学部, 助教授 (70195395)
WATANABE Masao Tohoku Univ., 農学部, 助手 (90240522)
OKADA Kiyotaka Tokyo Univ., 理学部, 教授 (50101093)
KOMEDA Yoshifumi Hokkaido Univ., 理学部, 教授 (10124215)
中世古 幸信 京都大学, 理学部, 助手 (30231468)
KATO Koichi Tokyo Univ., 薬学部, 助手 (20211849)
MURAKAMI Yuji Japan Advanced Institute of Science and Technology Hokuriku, 助手 (70272995)
YOSHIDA Minoru Tokyo Univ., 農学部, 助手 (80191617)
ISOGAI Akira Japan Advenced Institute of Science and Technology Nara, 教授 (20011992)
KAMADA Hiroshi Tsukuba Univ., 生物科学系, 教授 (00169608)
WAKASUGI Hiro National Insti. Cancer Center, がん宿主免疫研, 室長 (10112632)
SASAZUKI Takehiko Kyushu Univ., 生体防御医学研究所, 教授 (50014121)
KISHIMOTO Tadamitsu Osaka Univ., 医学部, 教授 (10093402)
OKUMURA Ko Juntendo Univ., 医学部, 教授 (50009700)
SHINOZAKI Kazuo The Institute of Physical and Chemical Research, ライフサイエンス筑波研究センター, 研究員 (20124216)
FUJII Tadashi Tsukuba Univ., 生物科学系, 教授 (20011611)
YAMADA Tetsuji Okayama Univ., 農学部, 教授 (00191320)
DOKE Noriyuki Nagoya Univ., 農学部, 教授 (80023472)
TANAKA Keiji Tokushima Univ., 酵素科学研究センター, 助教授 (10108871)
SAKAI Shingo Tsukuba Univ., 生物科学系, 助教授 (60033388)
マリセン B. CNRS, ラサンテ医研・マルセイユルミニー免疫センター, センター長
バーリング R. GSF, 遺伝研, 教授
マティス D. CNRS, 免疫学研究所, 室長
ベノワ C. CNRS, 免疫学研究所, 室長
クーパー J.A. フレッドハッチンソンがん研, 研究員
ハーガン I.M. マンチェスター大, がん研, 研究員
ラジャウスキー K. ケルン大, 科学, 教授
シラー F.W. ポツダム大, バイオ化学研, 教授
URANO Naoto Tokyo Univ. of Fisheries, 食品生産学科, 助教授 (90262336)
SHIMADA Kazuo Tokyo Univ., 薬学部, 教授 (70196476)
HORINOUCHI Sueharu Tokyo Univ., 農業生命科学研究所, 教授 (80143410)
SHIMURA Yoshiro Kyoto Univ. Faculty of Science professor, 理学部, 教授 (60025426)
MATSUBARA Ken-ichi Osaka Univ. Institute of Molecular and Cellular Siology, Professor, 細胞生体工学センター, 教授 (20037394)
YAMADA Yasuyuki Japan Advanced Institute of Science and Technology Nara, 農学部, 教授 (50026415)
KARUBE Isao Tokyo Univ. Research Center for Advanced Science and Technology, Professor, 先端科学技術研究センター, 教授 (50089827)
BEPPU Teruhiko Nippon Univ. Faculty of Agriculture and Veterinary Medicin Professor, 獣医学部, 教授 (80011873)
KIKUTANI Hitoshi Osaka Univ., 細胞生体工学センター, 助教授 (80161412)
KOSEKI Haruhiko Chiba Univ. School of Medicine Assistant, 医学部, 助手 (40225446)
SAITO Takashi Chiba Univ., 医学部, 教授 (50205655)
WATANABE Takeshi Kyushu Univ. Medical Institute of Bioregulation, Professo, 生体防御医学研究所, 教授 (40028684)
デュマ C. リヨン高等専門学校, 教授
ツジイ F.I. カリフォルニア大, スクリプト研, 教授
ロバーツ G.C.K. ライセスター大, 生物研, 教授
デルセニー M. ペルピニョン大学, 教授
フォルセン K.S. ランド大, 工, 教授
TSUJI Federick California Univ., USA
FORSEN Karl Lund Univ., Sweden
COOPER Jonathan Fred Huchinson Cancer Res. Ctr, USA
HAGAN Iain Manchester Univ., England
ROBERTS Gordon Leicester Univ., England
NAKASEKO Nobuyuki Kyoto Univ.
DUMAS C. Ecole Normale Surperieure de Lyon, France
SCHELLER Frieder Potsdam Univ.
DELSENY Michel Univ. de Perpignan, France
MATHIS Diane CNRS,France
BENOIST Christophe CNRS,France
MALISSEN Bernard CNRS,France
BALLING Rudolf GSF,Germany
RAJEWSKY Klaus Kologne Univ., Germany
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| Research Abstract |
Following results were obtained :
1. We isolated several homologues of Vp-1 or Abi 3 genes which are essential for ABA-mediated signal transduction in the regulation of higher plant morphogenesis.
2. By using gene targeting, we investigated function of several genes, including mel-18 which is a negative regulatory transcription factor and controls the expression of homeobox genes. Mel-18 knock-outs showed posterior transformation of skeletal bones, suggesting their equivalent functions to those of Drosophila.
3. By NMR,molecular interactions between IgG and protein-A,-G,and -L,were analyzed. It was revealed that 1) the IgG-binding domains of protein-A and -G have quite different three-dimensional structures, but bind to sites on the Fc that overlap extensively, 2) protein G employs two quite different regions of its surface to bind to the Fab and the Fc regions, and 3) the fold of the IgG-binding domain of protein L is similar to that of protein G,but they bind to a different domain in the Fab.
4. By indirect immunofluorescence microscopy, we analyzed location and morphological change of chromatin region and microtuble especially during mitosis in the fission yeast S.pombe cells.
5. For development of high sensitive biosensor, some devices with the chamber packing beads immobilized with microorganisms were fabricated by micromachine and CCD camera system. The system gave current response proportional to glucose concentration. Distribution of the luminescendce gave theoretical decrease as a function of low-rate and activity of immobilized enzyme. The system has ability to be highly sensitive due to chemical amplification by the enzyme induced by analyte.
6. We discussed future collaborations on France-Japan Immunology, particularly on T-B collaboration, regulation lymphocyte development, and immune diseases. Collaboration includes exchange of information, materials, and young scientists.
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