神田 大輔

J-GLOBALへ         更新日: 18/10/23 15:59
 
アバター
研究者氏名
神田 大輔
URL
http://www.bioreg.kyushu-u.ac.jp/vsb/index.html
所属
九州大学
部署
生体防御医学研究所構造生物学分野
職名
教授
学位
理学博士(東京大学), 理学修士(東京大学)
その他の所属
九州大学

研究分野

 
 

経歴

 
1986年4月
 - 
1995年12月
東京都臨床医学総合研究所,研究員
 
1994年7月
 - 
1995年7月
日本学術振興会特定国派遣研究者
 
1994年7月
 - 
1995年7月
イギリス・オックスフォード大学・生物化学部の客員研究員
 
1996年1月
 - 
2000年3月
(株)生物分子工学研究所,主任研究員
 
2000年4月
 - 
2001年12月
(株)生物分子工学研究所,主席研究員
 
2002年1月
 - 
2002年3月
(技術研究組合)生物分子工学研究所,主席研究員
 
2002年4月
 - 
現在
九州大学生体防御医学研究所,教授
 
2014年9月
 - 
現在
九州大学,主幹教授
 

学歴

 
1977年4月
 - 
1981年3月
東京大学 理I 
 
1979年4月
 - 
1981年3月
東京大学 理学部 生物化学科
 
1981年4月
 - 
1986年3月
東京大学大学院 理学系研究科 生物化学専攻
 

委員歴

 
2019年1月
 - 
現在
日本糖鎖科学コンソーシアム  JCGG幹事
 
2017年7月
 - 
現在
日本糖質学会  評議員
 
2017年4月
 - 
現在
日本生化学  代議員,理事
 
2017年4月
 - 
現在
九州大学生体防御医学研究所技術室  技術室長
 
2014年4月
 - 
現在
大阪大学蛋白質研究所共同利用・共同研究委員会  蛋白質立体構造データベース専門部会委員
 
2015年4月
 - 
2019年3月
wwPDB  Advisory Committee
 
2010年4月
 - 
2016年3月
九州大学生体多階層システム研究  センター長
 
2008年4月
 - 
2010年3月
九州大学生体防御医学研究所  副所長
 
2005年4月
 - 
2007年3月
九州大学感染防御研究センター  センター長
 
2005年
   
 
日本蛋白質科学会  理事
 
2004年
   
 
日本核磁気共鳴学会  評議員,理事
 

論文

 
Hashiguchi T, Fukuda Y, Matsuoka R, Kuroda D, Kubota M, Shirogane Y, Watanabe S, Tsumoto K, Kohda D, Plemper RK, Yanagi Y
Proceedings of the National Academy of Sciences of the United States of America   115(10) 2496-2501   2018年3月   [査読有り]
Fujinami D, -Mahin AA, Elsayed KM, Islam MR, Nagao JI, Roy U, Momin S, Zendo T, Kohda D, Sonomoto K
Communications biology   1 150   2018年   [査読有り]
Abe Y, Shioi S, Kita S, Nakata H, Maenaka K, Kohda D, Katayama T, Ueda T
FEBS letters   591(22) 3805-3816   2017年11月   [査読有り]
Ogino H, Ishino S, Kohda D, Ishino Y
The Journal of biological chemistry   292(19) 7921-7931   2017年5月   [査読有り]
Fujinami D, Taguchi Y, Kohda D
Glycobiology   27(8) 701-712   2017年5月   [査読有り]
Matsumoto S, Taguchi Y, Shimada A, Igura M, Kohda D
Biochemistry   56(4) 602-611   2017年1月   [査読有り]
Kubota M, Takeuchi K, Watanabe S, Ohno S, Matsuoka R, Kohda D, Nakakita SI, Hiramatsu H, Suzuki Y, Nakayama T, Terada T, Shimizu K, Shimizu N, Shiroishi M, Yanagi Y, Hashiguchi T
Proceedings of the National Academy of Sciences of the United States of America   113(41) 11579-11584   2016年10月   [査読有り]
Taguchi Y, Fujinami D, Kohda D
The Journal of biological chemistry   291(21) 11042-11054   2016年5月   [査読有り]
Matsuoka R, Shimada A, Komuro Y, Sugita Y, Kohda D
Protein science : a publication of the Protein Society   25(3) 754-768   2016年3月   [査読有り]
Shimada A, Yamaguchi A, Kohda D
Scientific reports   6 19565   2016年1月   [査読有り]
Fujinami D, Nyirenda J, Matsumoto S, Kohda D
Carbohydrate research   413 55-62   2015年9月   [査読有り]
Ishiwata A, Taguchi Y, Lee YJ, Watanabe T, Kohda D, Ito Y
Chembiochem : a European journal of chemical biology   16(5) 731-737   2015年3月   [査読有り]
Ogino H, Ishino S, Oyama T, Kohda D, Ishino Y
Bioscience, biotechnology, and biochemistry   79(3) 432-438   2015年3月   [査読有り]
Hashiguchi T, Fusco ML, Bornholdt ZA, Lee JE, Flyak AI, Matsuoka R, Kohda D, Yanagi Y, Hammel M, Crowe JE Jr, Saphire EO
Cell   160(5) 904-912   2015年2月   [査読有り]
Esaki K, Yoshinaga S, Tsuji T, Toda E, Terashima Y, Saitoh T, Kohda D, Kohno T, Osawa M, Ueda T, Shimada I, Matsushima K, Terasawa H
The FEBS journal   281(24) 5552-5566   2014年12月   [査読有り]
Ogino H, Ishino S, Haugland GT, Birkeland NK, Kohda D, Ishino Y
Extremophiles : life under extreme conditions   18(5) 915-924   2014年9月   [査読有り]
Takahashi N, Hamada-Nakahara S, Itoh Y, Takemura K, Shimada A, Ueda Y, Kitamata M, Matsuoka R, Hanawa-Suetsugu K, Senju Y, Mori MX, Kiyonaka S, Kohda D, Kitao A, Mori Y, Suetsugu S
Nature communications   5 4994   2014年9月   [査読有り]
Fujinami D, Matsumoto M, Noguchi T, Sonomoto K, Kohda D
Carbohydrate research   387 30-36   2014年3月   [査読有り]
Iwamoto C, Takenaka K, Urata S, Yamauchi T, Shima T, Kuriyama T, Daitoku S, Saito Y, Miyamoto T, Iwasaki H, Kitabayashi I, Itoh K, Kishimoto J, Kohda D, Matozaki T, Akashi K
Experimental hematology   42(3) 163-171.e1   2014年3月   [査読有り]
BALB/c- Specific L29V Polymorphism In SIRPA Determines The Efficient Engraftment Of Human Hematopoiesis In Xenogeneic Model
Iwamoto Chika, Takenaka Katsuto, Urata Shingo, Shima Takahiro, Yamauchi Takuji, Kuriyama Takuro, Daitoku Shinya, Saito Yasuyuki, Itoh Katsuhiko, Kishimoto Junji, Kohda Daisuke, Matozaki Takashi, Akashi Koichi
BLOOD   122(21)    2013年11月   [査読有り]
Matsumoto S, Shimada A, Nyirenda J, Igura M, Kawano Y, Kohda D
Proceedings of the National Academy of Sciences of the United States of America   110(44) 17868-17873   2013年10月   [査読有り]
Matsumoto S, Shimada A, Kohda D
BMC structural biology   13 11   2013年7月   [査読有り]
Inoue M, Yasuda K, Uemura H, Yasaka N, Schnaufer A, Yano M, Kido H, Kohda D, Doi H, Fukuma T, Tsuji A, Horikoshi N
Journal of biochemistry   153(5) 431-439   2013年5月   [査読有り]
Komuro Y, Miyashita N, Mori T, Muneyuki E, Saitoh T, Kohda D, Sugita Y
The journal of physical chemistry. B   117(10) 2864-2871   2013年3月   [査読有り]
Komuro Yasuaki, Miyashita Naoyuki, Mori Takaharu, Muneyuki Eiro, Saitoh Takashi, Kohda Daisuke, Sugita Yuji
BIOPHYSICAL JOURNAL   104(2) 665A   2013年1月   [査読有り]
Nyirenda J, Matsumoto S, Saitoh T, Maita N, Noda NN, Inagaki F, Kohda D
Structure (London, England : 1993)   21(1) 32-41   2013年1月   [査読有り]
Matsumoto S, Igura M, Nyirenda J, Matsumoto M, Yuzawa S, Noda N, Inagaki F, Kohda D
Biochemistry   51(20) 4157-4166   2012年5月   [査読有り]
Nishikimi A, Uruno T, Duan X, Cao Q, Okamura Y, Saitoh T, Saito N, Sakaoka S, Du Y, Suenaga A, Kukimoto-Niino M, Miyano K, Gotoh K, Okabe T, Sanematsu F, Tanaka Y, Sumimoto H, Honma T, Yokoyama S, Nagano T, Kohda D, Kanai M, Fukui Y
Chemistry & biology   19(4) 488-497   2012年4月   [査読有り]
Islam MR, Nishie M, Nagao J, Zendo T, Keller S, Nakayama J, Kohda D, Sahl HG, Sonomoto K
Journal of the American Chemical Society   134(8) 3687-3690   2012年2月   [査読有り]
Hanawa-Suetsugu K, Kukimoto-Niino M, Mishima-Tsumagari C, Akasaka R, Ohsawa N, Sekine S, Ito T, Tochio N, Koshiba S, Kigawa T, Terada T, Shirouzu M, Nishikimi A, Uruno T, Katakai T, Kinashi T, Kohda D, Fukui Y, Yokoyama S
Proceedings of the National Academy of Sciences of the United States of America   109(9) 3305-3310   2012年2月   [査読有り]
Hiroaki H, Umetsu Y, Nabeshima Y, Hoshi M, Kohda D
Journal of structural and functional genomics   12(3) 167-174   2011年9月   [査読有り]
Saitoh T, Igura M, Miyazaki Y, Ose T, Maita N, Kohda D
Biochemistry   50(24) 5487-5496   2011年6月   [査読有り]
Igura M, Kohda D
Glycobiology   21(5) 575-583   2011年5月   [査読有り]
Igura M, Kohda D
The Journal of biological chemistry   286(15) 13255-13260   2011年4月   [査読有り]
Mayanagi K, Kiyonari S, Nishida H, Saito M, Kohda D, Ishino Y, Shirai T, Morikawa K
Proceedings of the National Academy of Sciences of the United States of America   108(5) 1845-1849   2011年2月   [査読有り]
Yamamoto H, Itoh N, Kawano S, Yatsukawa Y, Momose T, Makio T, Matsunaga M, Yokota M, Esaki M, Shodai T, Kohda D, Hobbs AE, Jensen RE, Endo T
Proceedings of the National Academy of Sciences of the United States of America   108(1) 91-96   2011年1月   [査読有り]
Suetsugu N, Takano A, Kohda D, Wada M
Plant signaling & behavior   5(12) 1602-1606   2010年12月   [査読有り]
Ichikawa S, Takai T, Yashiki T, Takahashi S, Okumura K, Ogawa H, Kohda D, Hatanaka H
Genes to cells : devoted to molecular & cellular mechanisms   14(9) 1055-1065   2009年9月   [査読有り]
Fukao M, Obita T, Yoneyama F, Kohda D, Zendo T, Nakayama J, Sonomoto K
Bioscience, biotechnology, and biochemistry   72(7) 1750-1755   2008年7月   [査読有り]
Tabata S, Kuroki K, Wang J, Kajikawa M, Shiratori I, Kohda D, Arase H, Maenaka K
The Journal of biological chemistry   283(14) 8893-8901   2008年4月   [査読有り]
Aoki N, Sakiyama A, Kuroki K, Maenaka K, Kohda D, Deshimaru M, Terada S
Biochimica et biophysica acta   1784(4) 621-628   2008年4月   [査読有り]
Hashiguchi T, Kajikawa M, Maita N, Takeda M, Kuroki K, Sasaki K, Kohda D, Yanagi Y, Maenaka K
Journal of virological methods   149(1) 171-174   2008年4月   [査読有り]
Takada A, Yoshida S, Kajikawa M, Miyatake Y, Tomaru U, Sakai M, Chiba H, Maenaka K, Kohda D, Fugo K, Kasahara M
Journal of immunology (Baltimore, Md. : 1950)   180(3) 1678-1685   2008年2月   [査読有り]
Tabata S, Kuroki K, Maita N, Wang J, Shiratori I, Arase H, Kohda D, Maenaka K
Acta crystallographica. Section F, Structural biology and crystallization communications   64(Pt 1) 44-46   2008年1月   [査読有り]
Hashiguchi T, Kajikawa M, Maita N, Takeda M, Kuroki K, Sasaki K, Kohda D, Yanagi Y, Maenaka K
Proceedings of the National Academy of Sciences of the United States of America   104(49) 19535-19540   2007年12月   [査読有り]
Ose T, Soler N, Rasubala L, Kuroki K, Kohda D, Fourmy D, Yoshizawa S, Maenaka K
Structure (London, England : 1993)   15(5) 577-586   2007年5月   [査読有り]
Kuroki K, Kobayashi S, Shiroishi M, Kajikawa M, Okamoto N, Kohda D, Maenaka K
Journal of immunological methods   320(1-2) 172-176   2007年3月   [査読有り]
Shiroishi M, Kuroki K, Rasubala L, Tsumoto K, Kumagai I, Kurimoto E, Kato K, Kohda D, Maenaka K
Proceedings of the National Academy of Sciences of the United States of America   103(44) 16412-16417   2006年10月   [査読有り]
Shiroishi M, Kajikawa M, Kuroki K, Ose T, Kohda D, Maenaka K
The Journal of biological chemistry   281(28) 19536-19544   2006年7月   [査読有り]
Shiroishi M, Kohda D, Maenaka K
Biochimica et biophysica acta   1764(5) 985-988   2006年5月   [査読有り]
Nobuhisa I, Takeya R, Ogura K, Ueno N, Kohda D, Inagaki F, Sumimoto H
The Biochemical journal   396(1) 183-192   2006年5月   [査読有り]
Shiroishi M, Kuroki K, Ose T, Rasubala L, Shiratori I, Arase H, Tsumoto K, Kumagai I, Kohda D, Maenaka K
The Journal of biological chemistry   281(15) 10439-10447   2006年4月   [査読有り]
Shiroishi M, Kuroki K, Tsumoto K, Yokota A, Sasaki T, Amano K, Shimojima T, Shirakihara Y, Rasubala L, van der Merwe PA, Kumagai I, Kohda D, Maenaka K
Journal of molecular biology   355(2) 237-248   2006年1月   [査読有り]
Mizuki K, Takeya R, Kuribayashi F, Nobuhisa I, Kohda D, Nunoi H, Takeshige K, Sumimoto H
Archives of biochemistry and biophysics   444(2) 185-194   2005年12月   [査読有り]
Kuroki K, Tsuchiya N, Shiroishi M, Rasubala L, Yamashita Y, Matsuta K, Fukazawa T, Kusaoi M, Murakami Y, Takiguchi M, Juji T, Hashimoto H, Kohda D, Maenaka K, Tokunaga K
Human molecular genetics   14(16) 2469-2480   2005年8月   [査読有り]
Rasubala L, Fourmy D, Ose T, Kohda D, Maenaka K, Yoshizawa S
Acta crystallographica. Section F, Structural biology and crystallization communications   61(Pt 3) 296-298   2005年3月   [査読有り]
Yoshizawa S, Rasubala L, Ose T, Kohda D, Fourmy D, Maenaka K
Nature structural & molecular biology   12(2) 198-203   2005年2月   [査読有り]
Shioi S, Ose T, Maenaka K, Shiroishi M, Abe Y, Kohda D, Katayama T, Ueda T
Biochemical and biophysical research communications   326(4) 766-776   2005年1月   [査読有り]
Kamura T, Maenaka K, Kotoshiba S, Matsumoto M, Kohda D, Conaway RC, Conaway JW, Nakayama KI
Genes & development   18(24) 3055-3065   2004年12月   [査読有り]
Urata H, Shimizu H, Hiroaki H, Kohda D, Akagi M
Biochemical and biophysical research communications   309(1) 79-83   2003年9月   [査読有り]
1H, 13C and 15N backbone resonance assignments of the N-terminal domain of Drosophila GCM protein.
Shimizu M, Hiroaki H, Kohda D, Hayato Morita E, Hotta S, Morikawa K
Journal of biomolecular NMR   26(3) 277-278   2003年7月   [査読有り]
Ago T, Kuribayashi F, Hiroaki H, Takeya R, Ito T, Kohda D, Sumimoto H
Proceedings of the National Academy of Sciences of the United States of America   100(8) 4474-4479   2003年4月   [査読有り]
NMR and ICP spectroscopic analysis of the DNA-binding domain of the Drosophila GCM protein reveals a novel Zn2+ -binding motif.
Shimizu M, Hiroaki H, Kohda D, Hosoya T, Akiyama-Oda Y, Hotta Y, Morita EH, Morikawa K
Protein engineering   16(4) 247-254   2003年4月   [査読有り]
Tanaka T, Mizukoshi T, Taniyama C, Kohda D, Arai K, Masai H
The Journal of biological chemistry   277(41) 38062-38071   2002年10月   [査読有り]

Misc

 
Takano A, Suetsugu N, Wada M, Kohda D.
Plant Cell Physiol.   51(8) 1372-1376   2010年8月
An auxilin-like J-domain-containing protein, JAC1, is necessary for chloroplast movement in Arabidopsis thaliana, to capture photosynthetic light efficiently under weak light conditions. Here, we performed crystallographic and functional analyses ...
Yuya Taguchi, Daisuke Fujinami, Daisuke Kohda
Trends in Glycoscience and Glycotechnology   30    2018年1月
© 2018 FCCA (Forum: Carbohydrates Coming of Age). The glycosylation on asparagine residues is one of the ubiquitous protein modifications occurring in the three domains of life. An oligosaccharide chain is preassembled on a lipid-phospho carrier, ...
Masai H, Tanaka T, Kohda D.
Bioessays   32(8) 687-697   2010年8月
In bacteria, PriA protein, a conserved DEXH-type DNA helicase, plays a central role in replication restart at stalled replication forks. Its unique DNA-binding property allows it to recognize and stabilize stalled forks and the structures derived ...
Hidekazu Hiroaki, Daisuke Kohda
Experimental Approaches of NMR Spectroscopy: Methodology and Application to Life Science and Materials Science   579-600   2017年11月
© Springer Nature Singapore Pte Ltd. 2018. All rights reserved. Various solution NMR experiments for studying protein-ligand interactions have become indispensable techniques in both academia and industry. In general, solution NMR is superior to o...
Maita N, Nyirenda, J, Igura M, Kamishikiryo J, Kohda D
J. Biol. Chem.   285(7) 4941-4950   2010年2月
Oligosaccharyltransferase (OST) catalyzes the transfer of an oligosaccharide from a lipid donor to an asparagine residue in nascent polypeptide chains. In the bacterium Campylobacter jejuni, a single-subunit membrane protein, PglB, catalyzes N-gly...
Shunsuke Matsumoto, James Nyirenda, Daisuke Kohda
Glycoscience: Biology and Medicine   437-445   2015年1月
© Springer Japan 2015. Asparagine-linked glycosylation of proteins is widespread not only in eukaryotes but also in archaea and some eubacteria. The oligosaccharyl transfer reaction is catalyzed by a membrane-bound enzyme, oligosaccharyltransferas...
M. Igura, N. Maita, J. Kamishikiryo, M. Yamada, T. Obita, K. Maenaka, D. Kohda
EMBO J   27(1) 234-243   2008年1月
Asn-glycosylation is widespread not only in eukaryotes but also in archaea and some eubacteria. Oligosaccharyltransferase (OST) catalyzes the co-translational transfer of an oligosaccharide from a lipid donor to an asparagine residue in nascent po...
T. Saitoh, M. Igura, T. Obita, T. Ose, R. Kojima, K. Maenaka, T. Endo, and D. Kohda
EMBO J   26(22) 4777-4787   2007年11月
Most mitochondrial proteins are synthesized in the cytosol and imported into mitochondria. The N-terminal presequences of mitochondrial-precursor proteins contain a diverse consensus motif (φχχφφ, φ is hydrophobic and χ is any amino acid), which i...
K. Sasaki, T. Ose, N. Okamoto, K. Maenaka, T. Tanaka, H. Masai, M. Saito, T. Shirai, and D. Kohda
EMBO J   26(10) 2584-2593   2007年5月
In eubacteria, PriA helicase detects the stalled DNA replication forks. This critical role of PriA is ascribed to its ability to bind to the 3′ end of a nascent leading DNA strand in the stalled replication forks. The crystal structures in complex...
T. Tanaka, T. Mizukoshi, K. Sasaki, D. Kohda, and H. Masai
J Biol Chem   282(27) 19917-19927   2007年7月
Escherichia coli PriA protein plays crucial roles in processing of arrested replication forks. PriA serves as a sensor/stabilizer for an arrested replication fork and eventually promotes restart of DNA replication through assembly of a primosome. ...
D. Kohda*, M. Yamada, M. Igura, J. Kamishikiryo, and K. Maenaka
Glycobiology   17(11) 1175-1182   2007年11月
We developed a new in vitro assay for oligosaccharyltransferase (OST), which catalyzes the transfer of preassembled oligosaccharides on lipid carriers onto asparagine residues in polypeptide chains. The asparagine residues reside in the sequon, As...
Daisuke Kohda
Seikagaku   80 888-896   2008年12月
M. Igura, N. Maita, T. Obita, J. Kamishikiryo, K. Maenaka, and D. Kohda
Acta Crystallogr.   F63 798-801   2007年8月
Oligosaccharyltransferase catalyzes the transfer of preassembled oligosaccharides onto asparagine residues in nascent polypeptide chains. The STT3 subunit is thought to bear the catalytic site. The C-terminal domain of the STT3 protein of Pyrococc...
Sasaki, K., Ose, T., Tanaka, T., Mizukoshi, T., Ishigaki, T., Maenaka, K., Masai, H., and Kohda, D.
Biochim Biophys Acta   1764 157-160   2006年1月
PriA, a DEXH-type DNA helicase, binds specifically to the 3′ end of DNA through its N-terminal domain, and is a candidate sensor protein that recognizes arrested DNA replication forks in bacteria. We crystallized an N-terminal fragment of PriA in ...
Igura, M., Ose, T., Obita, T., Sato, C., Maenaka, K., Endo, T., and Kohda, D.
Acta Crystallogr   F61 514-517   2005年12月
Most mitochondrial proteins are synthesized in the cytosol and must be imported into the mitochondria. Many mitochondrial precursor proteins have an extra leader sequence at their N-terminus called a presequence. Presequences are recognized by the...
Takayuki Obita, Takayuki Obita, Takanori Muto, Toshiya Endo, Daisuke Kohda, Daisuke Kohda
J. Mol. Biol.   328, 495-504 495-504   2003年4月
Many mitochondrial matrix and inner-membrane proteins are synthesized in the cytosol as precursor proteins with an N-terminal presequence, and are imported into the mitochondria. Although no distinct sequence homology has been found among mitochon...
Toshimi Mizukoshi, Toshimi Mizukoshi, Taku Tanaka, Ken Ichi Arai, Daisuke Kohda, Daisuke Kohda, Hisao Masai, Hisao Masai
J. Biol. Chem.   278, 42234-42239 42234-42239   2003年10月
Arrest of replication forks by various internal and external threats evokes a myriad of cellular reactions, collectively known as DNA replication checkpoint responses. In bacteria, PriA is essential for restoration of stalled replication forks and...
Toshiya Endo, Daisuke Kohda
Biochim Biopys Acta   1592, 3-14 3-14   2002年9月
Most mitochondrial proteins are synthesized in the cytosol as precursor proteins and are imported into mitochondria. The targeting signals for mitochondria are encoded in the presequences or in the mature parts of the precursor proteins, and are d...
Keiichiro Kami, Keiichiro Kami, Ryu Takeya, Hideki Sumimoto, Daisuke Kohda, Daisuke Kohda
Embo J   21, 4268-76 4268-4276   2002年8月
The basic function of the Src homology 3 (SH3) domain is considered to be binding to proline-rich sequences containing a PxxP motif. Recently, many SH3 domains, including those from Grb2 and Pex13p, were reported to bind sequences lacking a PxxP m...
Hidekazu Hiroaki, Tetsuro Ago, Takashi Ito, Hideki Sumimoto, Daisuke Kohda
Nature Struct Biol   8, 526-30 526-530   2001年6月
The phox homology (PX) domain is a novel protein module containing a conserved proline-rich motif. We have shown that the PX domain isolated from the human p47phoxprotein, a soluble subunit of phagocyte NADPH oxidase, binds specifically to the C-t...
Takanori Muto, Takayuki Obita, Yoshito Abe, Toshihiro Shodai, Toshiya Endo, Daisuke Kohda
J Mol Biol   306, 137-43 137-143   2001年2月
Many mitochondrial proteins are synthesized in the cytosol as precursors with N-terminal presequences, and are imported into mitochondria with the aid of translocator protein complexes containing presequence-binding proteins. Tom20, a receptor pro...
Daisuke Kohda
Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme   50 1303-1310   2005年1月
Yoshito Abe, Toshihiro Shodai, Takanori Muto, Katsuyoshi Mihara, Hisayoshi Torii, Shuh ichi Nishikawa, Toshiya Endo, Daisuke Kohda
Cell   100, 551-60 551-560   2000年3月
Most mitochondrial proteins are synthesized in the cytosol as precursor proteins with a cleavable N-terminal presequence and are imported into mitochondria. We report here the NMR structure of a general import receptor, rat Tom20, in a complex wit...
Chiaki Sato, Jae Hoon Kim, Yoshito Abe, Kazuki Saito, Shigeyuki Yokoyama, Daisuke Kohda
J Biochem (Tokyo)   127, 65-72 65-72   2000年1月
The extracellular domain of human EGF receptor (sEGFR) produced by CHO cells has been used in various biophysical studies to elucidate the molecular mechanism of EGF-induced receptor activation. We have found that the CHO sEGFR contains one oligos...
Yoshito Abe, Masafumi Odaka, Masafumi Odaka, Fuyuhiko Inagaki, Irit Lax, Joseph Schlessinger, Daisuke Kohda, Daisuke Kohda
J Biol Chem   273, 11150-7 11150-11157   1998年5月
The extracellular domain of the human epidermal growth factor receptor (sEGFR) consists of 621 amino acid residues, including 50 cysteines. The connections of the 25 disulfide bonds in the recombinant sEGFR protein, obtained from Chinese hamster o...
Daisuke Kohda
Seikagaku. The Journal of Japanese Biochemical Society   74 1244-1250   2002年10月
Daisuke Kohda, Daisuke Kohda, Craig J. Morton, Ashfaq A. Parkar, Hideki Hatanaka, Fuyuhiko M. Inagaki, Iain D. Campbell, Iain D. Campbell, Anthony J. Day
Cell   86, 767-75 767-775   1996年9月
Link modules are hyaluronan-binding domains found in proteins involved in the assembly of extracellular matrix, cell adhesion, and migration. The solution structure of the Link module from human TSG-6 was determined and found to consist of two α h...
Kaori Wakamatsu, Masanao Oya, Daisuke Kohda, Hideki Hatanaka, Jean Marc Lancelin, Fuyuhiko Inagaki, Yukisato Ishida, Kazuki Sato, Hideshi Nakamura
Biochemistry   31 12577-12584   1992年2月
A synthetic replacement study of the amino acid residues of µ-conotoxin GIIIA, a peptide blocker for muscle sodium channels, has recently shown that the conformation formed by three disulfide bridges and the molecular basicity, especially the one ...
Daisuke Kohda, Fuyuhiko Inagaki
Biochemistry   31, 677-85 677-685   1992年2月
The interaction of mouse epidermal growth factor (mEGF) with micelles of a phospholipid analogue, perdeuterated dodecylphosphocholine (DPC), was investigated by two-dimensional 1H NMR. Sequence-specific resonance assignments of the micelle-bound m...
Daisuke Kohda, Fuyuhiko Inagaki
Biochemistry   31, 11928-39 11928-11939   1992年2月
The three-dimensional structures of epidermal growth factors (EGF) previously reported were all in acidic solutions (pH 2.0-3.2), at which pHs EGF cannot bind to the receptor. Here we studied the structure of mouse EGF at pH 6.8, where EGF is phys...
Lidong Liu, Lidong Liu, Kayoko Komori, Sonoko Ishino, Arnaud A. Bocquier, Arnaud A. Bocquier, Isaac K O Cann, Isaac K O Cann, Daisuke Kohda, Yoshizumi Ishino, Yoshizumi Ishino
Journal of Biological Chemistry   276 45484-45490   2001年11月
We characterized the primase complex of the hyperthermophilic archaeon, Pyrococcus furiosus. The two proteins, Pfup41 and Pfup46, have similar sequences to the p48 and p58 subunits, respectively, of the eukaryotic DNA polymerase α-primase complex....
Daisuke Kohda, Toshie Sawada, Fuyuhiko Inagaki
Biochemistry   30, 4896-900 4896-4900   1991年5月
The pH titration shifts for all the nonlabile proton resonances in a 53-residue protein (mouse epidermal growth factor) were measured in the p2H range 1.5-9 with two-dimensional (2D)1H NMR. The 2D NMR pH titration experiment made it possible to de...
Tetsuro Ago, Tetsuro Ago, Ryu Takeya, Ryu Takeya, Hidekazu Hiroaki, Futoshi Kuribayashi, Futoshi Kuribayashi, Takashi Ito, Daisuke Kohda, Hideki Sumimoto, Hideki Sumimoto
Biochemical and Biophysical Research Communications   287 733-738   2001年9月
The phox (phagocyte oxidase) homology (PX) domain occurs in the mammalian phox proteins p40phoxand p47phox, the polarity establishment protein Bem1p in budding yeast, and a variety of proteins involved in membrane trafficking. Here we show that th...
F. Inagaki, I. Shimada, D. Kohda, A. Suzuki, A. Bax
Journal of Magnetic Resonance (1969)   81 186-190   1989年1月
Daisuke Kohda, Ichio Shimada, Tetsuo Miyake, Toru Fuwa, Fuyuhiko Inagaki
Biochemistry   28, 953-8 953-958   1989年1月
The 1H NMR spectrum of human transforming growth factor α (TGF-α) was analyzed almost completely by the sequential assignment method using two-dimensional NMR techniques. On the basis of the nearly complete sequence-specific resonance assignment, ...
D. Kohda, C. Kodama, R. Kase, H. Nomoto, K. Hayashi, F. Inagaki
Biochem. International   16, 647-54 647-654   1988年4月
The three-dimensional structure of the mouse epidermal growth factor (EGF) in solution was studied by comparison of the 1H NMR spectra of alpha EGF (1-53) and beta EGF (2-53, des-asparaginyl 1 form). Using pH dependence of chemical shifts and a tw...
Arnaud A. Bocquier, Lidong Liu, Isaac K.O. Cann, Kayoko Komori, Daisuke Kohda, Yoshizumi Ishino
Current Biology   11 452-456   2001年3月
In the evolution of life, DNA replication is a fundamental process, by which species transfer their genetic information to their offspring. DNA polymerases, including bacterial and eukaryotic replicases, are incapable of de novo DNA synthesis. DNA...
D. Kohda, S. Yokoyama, T. Miyazawa
J Biol Chem   262, 558-63 558-563   1987年1月
Methionyl-tRNA synthetase (MetRS, 2 x 75 kDa) was purified to homogeneity from an extreme thermophile, Thermus thermophilus HB8. The polypeptide chain of MetRS was cleaved by limited digestion with trypsin into four domains: T1 (29 kDa), T2 (23 kD...
H. Urata, H. Shimizu, H. Hiroaki, D. Kohda, M. Akagi
Nucleic acids research. Supplement (2001)   243-244   2001年1月
In order to investigate the duplex structure of DNA and RNA containing an L-nucleotide residue, we carried out the UV-melting and CD experiments. Although the introduction of an L-nucleotide into DNA/DNA, DNA/RNA and RNA/RNA duplexes reduced their...
Daisuke Kohda, Gota Kawai, Shigeyuki Yokoyama, Tatsuo Miyazawa, Daisuke Kohda, Makoto Kawakami, Shoji Mizushima
Biochemistry   26, 6531-8 6531-6538   1987年1月
The 400-MHz1H NMR spectra of L-isoleucine and L-valine were measured in the presence of Escherichia coli isoleucyl-tRNA synthetase (IleRS). Because of chemical exchange of L-isoleucine or L-valine between the free state and the IleRS-bound state, ...
D. Kohda, H. Sumimoto, F. Inagaki
Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme   46 1726-1731   2001年1月
Daisuke Kohda, Shigeyuki Yokoyama, Tatsuo Miyazawa
FEBS Lett   21. 174, 20-3 20-23   1984年8月
Thermostable valyl-tRNA, isoleucyl-tRNA and methionyl-tRNA synthetases have been purified from an extreme thermophile, Thermus thermophilus HB8. Valyl-tRNA and isoleucyl-tRNA synthetases are found to be monomer proteins (Mr108000 and 129000, respe...
D. Kohda
Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme   46 240-246   2001年1月
Ayumi Kashiwada, Hidekazu Hiroaki, Daisuke Kohda, Mamoru Nango, Toshiki Tanaka
Journal of the American Chemical Society   122 212-215   2000年1月
We previously prepared the de novo designed peptide, [YGG(IEKKIEA)4], which forms a parallel triple-stranded coiled coil. To prepare an AAB-type heterotrimeric α-helical bundle, two variants, where the Ile15 residue in the hydrophobic position was...
Xiangqun Li, Kazuo Suzuki, Kenji Kanaori, Kunihiko Tajima, Ayumi Kashiwada, Hidekazu Hiroaki, Daisuke Kohda, Toshiki Tanaka, Toshiki Tanaka
Protein Science   9 1327-1333   2000年1月
We previously reported the de novo design of an amphiphilic peptide (YGG(IEKKIEA)4) that forms a native-like, parallel triple-stranded coiled coil. Starting from this peptide, we sought to regulate the assembly of the peptide by a metal ion. The r...
D. Kohda
Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme   44 338-346   1999年1月
Susan E. Tsutakawa, Takanori Muto, Tomohiko Kawate, Hisato Jingami, Naoki Kunishima, Mariko Ariyoshi, Daisuke Kohda, Masako Nakagawa, Kosuke Morikawa, Kosuke Morikawa
Molecular Cell   3 621-628   1999年1月
Vsr endonuclease plays a crucial role in the repair of TG mismatched base pairs, which are generated by the spontaneous degradation of methylated cytidines; Vsr recognizes the mismatched base pair and cleaves the phosphate backbone 5' to the thymi...
Kazuo Suzuki, Hidekazu Hiroaki, Daisuke Kohda, Haruki Nakamura, Toshiki Tanaka
Journal of the American Chemical Society   120 13008-13015   1998年12月
Coiled coils, which mediate the associations and regulate the functions of various proteins, have a representative amino acid sequence of (defgabc)(n) heptad repeats and usually have hydrophobic residues at the a and d positions. We have designed ...
Kazuo Suzuki, Hidekazu Hiroaki, Daisuke Kohda, Toshiki Tanaka
Protein Engineering   11 1051-1055   1998年11月
Recent studies in the field of de novo protein design have focused on the construction of native-like structures. Here we describe the design and characterization of an isoleucine zipper peptide intended to form a parallel triple-stranded coiled c...
Masafumi Odaka, Masafumi Odaka, Daisuke Kohda, Daisuke Kohda, Irit Lax, Joseph Schlessinger, Fuyuhiko Inagaki
Journal of Biochemistry   122 116-121   1997年1月
We studied the dimerization of the recombinant soluble extracellular domain of the epidermal growth factor receptor (sEGFR) in response to EGF-binding using multi-angle laser light scattering with size exclusion chromatography (SEC-MALLS). In the ...
Koji Nagata, Koji Nagata, Hideki Hatanaka, Daisuke Kohda, Hiroshi Kataoka, Hiromichi Nagasawa, Hiromichi Nagasawa, Akira Isogai, Hironori Ishizaki, Akinori Suzuki, Fuyuhiko Inagaki
Journal of Molecular Biology   253 749-758   1995年11月
The three-dimensional solution structure of bombyxin-II, an insulin-like two-chain peptide produced by the brain of the silkwormBombyx morihas been determined by simulated annealing calculations based on 535 distance constraints and 24 torsion-ang...
Koji Nagata, Koji Nagata, Hideki Hatanaka, Daisuke Kohda, Hiroshi Kataoka, Hiromichi Nagasawa, Hiromichi Nagasawa, Akira Isogai, Hironori Ishizaki, Akinori Suzuki, Fuyuhiko Inagaki
Journal of Molecular Biology   253 759-770   1995年11月
Bombyxin-II, a brain-secretory peptide of the silkmothBombyx mori, shares 40% sequence identity and the characteristics core structure with human insulin. In spite of the structural similarity, no cross-activity is observed between them. To locali...
Daisuke Kohda, Fuyuhiko Inagaki
Journal of Biomolecular NMR   5 357-361   1995年6月
NMR as well as X-ray crystallography are used to determine the three-dimensional structures of macromolecules at atomic resolution. Structure calculation generates coordinates that are compatible with NMR data from randomly generated initial struc...
Hiroaki Terasawa, Hiroaki Terasawa, Daisuke Kohda, Hideki Hatanaka, Koji Nagata, Nobuyuki Higashihashi, Hiroyuki Fujiwara, Katsu Ichi Sakano, Fuyuhiko Inagaki
EMBO Journal   13 5590-5597   1994年12月
The three-dimensional structure of human insulin-like growth factor II was determined at high resolution in aqueous solution by NMR and simulated annealing based calculations. The structure is quite similar to those of insulin and insulin-like gro...
Hideki Hatanaka, Miyuki Oka, Daisuke Kohda, Shin Ichi Tate, Akiko Suda, Nobuo Tamiya, Fuyuhiko Inagaki
Journal of Molecular Biology   240 155-166   1994年7月
The three-dimensional structure of erabutoxin b, a short-chain neurotoxic peptide purified from the venom of the sea snake Laticauda semifasciata, was determined in aqueous solution by two-dimensional proton nuclear magnetic resonance and simulate...
K. Nagata, D. Kohda, H. Hatanaka, S. Ichikawa, S. Matsuda, T. Yamamoto, A. Suzuki, F. Inagaki
EMBO Journal   13 3517-3523   1994年1月
p185(erB-2) and p180(erB-4) are epidermal growth factor (EGF) receptor-like tyrosine kinases, whose co-expression is observed in many breast carcinomas. Heregulins (HRGs), which contain an immunoglobulin unit and an EGF-like domain, bind to p180(e...
Daisuke Kohda, Hiroaki Terasawa, Saori Ichikawa, Kenji Ogura, Hideki Hatanaka, Valsan Mandiyan, Axel Ullrich, Joseph Schlessinger, Fuyuhiko Inagaki
Structure   2 1029-1040   1994年1月
Background: Growth factor receptor-bound protein 2 (GRB2) is an adaptor protein with three Src homology (SH) domains in the order SH3- SH2-SH3. Both SH3 domains of GRB2 are necessary for interaction with the protein Son of sevenless (Sos), which a...
Hiroaki Terasawa, Hiroaki Terasawa, Daisuke Kohda, Hideki Hatanaka, Shigeo Tsuchiya, Kenji Ogura, Koji Nagata, Shunsuke Ishii, Valsan Mandiyan, Axel Ullrich, Joseph Schlessinger, Fuyuhiko Inagaki, Fuyuhiko Inagaki
Nature Structural Biology   1 891-997   1994年1月
Src-homology 3 (SH3) domains mediate signal transduction by binding to proline- rich motifs in target proteins. We have determined the high-resolution NMR structure of the complex between the amino-terminal SH3 domain of GRB2 and a ten amino acid ...
Hirokazu Tamamura, Masataka Kuroda, Masao Masuda, Akira Otaka, Susumu Funakoshi, Hideki Nakashima, Naoki Yamamoto, Michinori Waki, Akiyoshi Matsumoto, Jean M. Lancelin, Daisuke Kohda, Shinichi Tate, Fuyuhiko Inagaki, Nobutaka Fujii
Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular   1163 209-216   1993年5月
The solution structure of tachyplesin I, which was isolated from membrane acid extracts of the hemocytes from the Japanese horseshoe crab (Tachypleus tridentatus), was determined by nuclear magnetic resonance (NMR) and distance geometry calculatio...
D. Kohda, H. Hatanaka, M. Odaka, V. Mandiyan, A. Ullrich, J. Schlessinger, F. Inagaki
Cell   72 953-960   1993年3月
SH3 (Src homology 3) domains are found in many signaling proteins and appear to function as binding modules for cytoplasmic target proteins. The solution structure of the SH3 domain of human phospholipase C-γ (PLC-γ) was determined by two-dimensio...
Teikichi Ikura, Nobuhiro Gō, Daisuke Kohda, Fuyuhiko Inagaki, Hiroshi Yanagawa, Masuyo Kawabata, Shun‐ichiro ‐i Kawabata, Sadaaki Iwanaga, Tosiyuki Noguti, Mitiko Gō
Proteins: Structure, Function, and Bioinformatics   16 341-356   1993年1月
Proteins consist of structural units such as globular domains, secondary structures, and modules. Modules were originally defined by partitioning a globular domain into compact regions, each of which is a contiguous polypeptide segment having a co...
D. Kohda, M. Odaka, I. Lax, H. Kawasaki, K. Suzuki, A. Ullrich, J. Schlessinger, F. Inagaki
Journal of Biological Chemistry   268 1976-1981   1993年1月
Elucidation of the three-dimensional structure of the complex of the epidermal growth factor (EGF) and its receptor is essential for understanding the molecular mechanisms of the EGF-receptor interaction and EGF-induced receptor-receptor interacti...
Solution structure and ligand-binding site of the carboxy-terminal SH3 domain of GRB2
Structure   72, 953-60    1993年
Hiroshi Koide, Yutaka Muto, Hidefumi Kasai, Kaoru Kohri, Kaoru Kohri, Kumiko Hoshi, Kumiko Hoshi, Seizo Takahashi, Ken ichi Tsukumo, Tetsuyuki Sasaki, Takanori Oka, Tetsuo Miyake, Tohru Fuwa, Daisuke Kohda, Fuyuhiko Inagaki, Tatsuo Miyazawa, Shigeyuki Yokoyama
Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular   1120 257-261   1992年4月
The isoleucine-23 residue of human epidermal growth factor (hEGF) was substituted by a variety of amino acid residues and the receptor-binding activities of variant hEGFs were determined by the use of human KB cell. Tight receptor binding was foun...
Kazuki Sato, Kazuki Sato, Yukisato Ishida, Kaori Wakamatsu, Rika Kato, Hiromi Honda, Yasushi Ohizumi, Hideshi Nakamura, Masanao Ohya, Jean Marc Lancelin, Daisuke Kohda, Fuyuhiko Inagaki
Journal of Biological Chemistry   266 16989-16991   1991年9月
The amino acid sequence of μ-conotoxin GIIIA (otherwise called geographutoxin I), a peptide having 22 amino acid residues with three disulfide bridges, was modified by replacing each residue with Ala or Lys to elucidate its active center for block...
O. Nureki, T. Muramatsu, K. Suzuki, D. Kohda, H. Matsuzawa, T. Ohta, T. Miyazawa, S. Yokoyama
Journal of Biological Chemistry   266 3268-3277   1991年7月
The gene for the methionyl-tRNA synthetase (MetRS) from an extreme thermophile, Thermus thermophilus HB8, was cloned and sequenced. By expression of the T. thermophilus MetRS gene in Escherichia coli cells, thermostable MetRS was overproduced and ...
Jean Marc Lancelin, Daisuke Kohda, Shin ichi Tate, Fuyuhiko Inagaki, Yuchio Yanagawa, Teruo Abe, Mei Satake
Biochemistry   30 6908-6916   1991年7月
The three-dimensional structure of conotoxin GIIIA, an important constituent of the venom from the marine hunting snail Conus geographus L., was determined in aqueous solution by two-dimensional proton nuclear magnetic resonance and simulated anne...
Daisuke Kohda, Fuyuhiko Inagaki
Analytical Sciences   7 853-856   1991年1月
The 3D structures of epidermal growth factor (EGF from mouse and human) and type a transforming growth factor (TGFα from human) in solution were studied by two-dimensional proton NMR spectroscopy. The pH of the samples were pH 2-3 for EGF and pH 4...
Hiroyuki Hanzawa, Ichio Shimada, Takashi Kuzuhara, Hiroto Komano, Daisuke Kohda, Fuyuhiko Inagaki, Shunji Natori, Yoji Arata
FEBS Letters   269 413-420   1990年9月
The solution conformation of an antibacterial protein sapecin has been determined by1H nuclear magnetic resonance (NMR) and dynamical simulated annealing calculations. It has been shown that the polypeptide fold consists of one flexible loop (resi...
T. Kohno, D. Kohda, M. Haruki, S. Yokoyama, T. Miyazawa
Journal of Biological Chemistry   265 6931-6935   1990年5月
Nonprotein amino acid furanomycin was found to bind with Escherichia coli isoleucyl-tRNA synthetase (IleRS) almost as tightly as the substrate L-isoleucine. The conformation of furanomycin bound to the enzyme was determined by NMR analyses includi...
Robert M. COOKE, Michael J. TAPPIN, Iain D. CAMPBELL, Daisuke KOHDA, Tetsuo MIYAKE, Toru FUWA, Tatsuo MIYAZAWA, Fuyuhiko INAGAKI
European Journal of Biochemistry   193 807-815   1990年1月
The1H‐NMR spectra of native human epidermal growth factor (EGF) and a derivative lacking the final five residues have been assigned by two‐dimensional methods, enabling their structures to be compared. The same structural features are observed for...
D. Kohda, F. Inagaki
Seikagaku. The Journal of Japanese Biochemical Society   61 698-704   1989年8月
Daisuke Kohda, Nobuhiro Go, Kyozo Hayashi, Fuyuhiko Inagaki
Journal of Biochemistry   103 741-743   1988年1月
The tertiary structure of mouse epidermal growth factor (EGF) in solution (28°C, pH 2.0) was studied by two-dimensional NMR spectroscopy. Proton-proton distance constraints derived from NOESY spectra were used to construct a mechanical molecular m...
Daisuke Kohda, Fuyuhiko Inagaki
Journal of Biochemistry   103 554-571   1988年1月
The1H NMR spectrum of the mouse epidermal growth factor (53 residues) was analyzed with the use of two-dimensional NMR techniques. All the observable 296 proton resonances were completely assigned in a sequential manner. For the spin system identi...
Complete sequence-specific 1H nuclear magnetic resonance assignments for mouse epidermal growth factor
J Biochem (Tokyo)   103, 554-71    1988年
Tertiary structure of mouse epidermal growth factor determined by two-dimensional 1H NMR
J Biochem (Tokyo)   103, 741-3    1988年
F. Inagaki, D. Kohda, C. Kodama, A. Suzuki
FEBS Letters   212 91-97   1987年2月
We applied multiple relayed COSY and 2D homonuclear Hartman-Hahn spectroscopy to globoside, a glycolipid purified from human red blood cells. The subspectra corresponding to individual sugar components were extracted even from overlapping proton r...
Shigeyuki Yokoyama, Daisuke Kohda, Tatsuo Miyazawa
Nippon Kagaku Kaishi   1987 402-404   1987年1月
The 400-MHz1H-NMR spectra of L-isoleucine were measured in the presence of Escherichia coli isoleucyl-tRNA synthetase (IleRS). Because of chemical exchange of L-isoleucine between the free state and the IleRS-bound state, transferred nuclear Overh...
D. Kohda, M. Hara, S. Yokoyama, T. Miyazawa
Nucleic acids symposium series   153-154   1983年12月
Thermostable aminoacyl-tRNA synthetases specific to Val, Ile, Met and Glu were purified from an extreme thermophile, Thermus thermophilus HB8. As for the subunit compositions and molecular weights, these four aminoacyl-tRNA synthetases are similar...

書籍等出版物

 
新生化学実験講座1 タンパク質III 高次構造 
東京化学同人   1990年   
Marusen Advanced Technology 生物工学編 タンパク質-基礎と応用- 
丸善    1992年   
分子生物学
神田大輔 (担当:分担執筆, 範囲:構造生物学の意義と役割)
東京化学同人   1999年   
分子生物学 第2版
神田大輔 (担当:分担執筆, 範囲:構造生物学の意義と役割)
東京化学同人   2009年   
いきなりはじめる構造生物学
神田大輔
秀潤社   2011年   
ISBN978-4-7809-0842-8 C3045 \3600E

担当経験のある科目

 
 

Works

 
プロテインデータバンク(PDB)への登録
1BOM, 1BON, 1EPG, 1EPH, 1EPI, 1EPJ, 1ERA, 1FRA, 1GD5, 1GFC, 1GFD, 1HRE, 1HRF, 1HSQ, 1K4U, 1L4V, 1OM2, 1TCG, 1TCH, 1TCJ, 1TCK, 1UFU, 1UGN, 1VDG, 1VSR, 1WOC, 1WSU, 2D31, 2D3V, 2D7E, 2D7G, 2D7H, 2DWL, 2DWM, 2DWN, 2DYP, 2HSP, 2MLO, 2MLQ, 2UWM, 2V1S, 2...

特許

 
「タンパク質の構造座標およびNMR化学シフト並びにそれらの使用
特願平11-346193

その他

 
2008年12月   日本生物物理学会年会 実行委員長
第46回年会 実行委員長 福岡国際会議場
2009年11月   NMR討論会 運営委員長
第48回NMR討論会 (日本核磁気共鳴学会年会)
運営委員長 九州大学病院百年講堂
2016年6月   日本蛋白質科学会 年会年会長
第16回日本蛋白質科学会 年会年会長 福岡国際会議場
2017年10月   糖鎖科学コンソーシアム シンポジウム世話人
第15回糖鎖科学コンソーシアム(JCGG)シンポジウム 世話人 九州大学病院百年講堂