村上 一馬

Last Update: 2018/10/07 17:05:03

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Name(Kanji/Kana/Abecedarium Latinum)
村上 一馬/ムラカミ カズマ/Kazuma Murakami
Primary department(Org1/Job title)
Graduate Schools Agriculture/Associate Professor
Faculty
Org1 Job title
農学部
Contact address
Type Address(Japanese) Address(English)
Office 606-8502 京都市左京区北白川追分町 Kitashirakawa Oiwake-cho, Sakyo-ku, Kyoto 606-8502, Japan
Phone
Type Number
Office 075-753-6282
E-mail address
メールアドレス
alzkazu @ kais.kyoto-u.ac.jp
Affiliated academic organization(s) (Japanese)
Organization name(Japanese) Organization name(English)
日本農芸化学会 Japan Society for Bioscience, Biotechnology, Agrochemistry
日本認知症学会 Japan Society for Dementia Research
日本ペプチド学会 The Japanese Peptide Society
日本ケミカルバイオロジー学会 Japan Society for Chemical Biology
Affiliated academic organization(s) (overseas)
Organization name Country
American Chemical Society USA
Academic degree
Field(Japanese) Field(English) University(Japanese) University(English) Method
修士(農学) 京都大学
博士(農学) 京都大学
Graduate school
University(Japanese) University(English) Faculty(Japanese) Faculty(English) Major(Japanese) Major(English) Degree
京都大学 大学院農学研究科博士後期課程食品生物科学専攻 修了
京都大学 大学院農学研究科修士課程食品生物科学専攻 修了
University
University(Japanese) University(English) Faculty(Japanese) Faculty(English) Major(s)(Japanese) Major(s)(English) Degree
京都大学 農学部生物機能科学科 卒業
Highschool
Highschool Kana
清風高等学校
Work Experience
Period Organization(Japanese) Organization(English) Job title(Japanese) Job title(English)
2004/04/01-2007/03/31 京都大学農学研究科 Graduate School of Agriculture, Kyoto University 日本学術振興会特別研究員DC1 Research Fellow of the Japan Society for the Promotion DC1
2007/04/01-2009/09/30 東京都老人総合研究所 Tokyo Metroplitan Institute of Gerontology 日本学術振興会特別研究員SPD Research Fellow of the Japan Society for the Promotion SPD
2009/10/01-2013/06/30 京都大学農学研究科 Graduate School of Agriculture, Kyoto University 助教 Assistant Professor
2013/07/01- 京都大学農学研究科 Graduate School of Agriculture, Kyoto University 准教授 Associate Professor
Personal website address
URL
http://www.orgchem.kais.kyoto-u.ac.jp/
ORCID ID
orcid.org/0000-0003-3152-1784
Research Topics
(Japanese)
1. アミロイドβの毒性オリゴマーの細胞内標的探索、2. 食品・漢方薬に含まれるアミロイドβのオリゴマー化抑制化合物の探索とそれをシードにした特異的阻害剤の開発、3. アミロイドβの毒性オリゴマーに対する核酸アプタマーの開発、4. インスリン分泌ホルモン・アミリンを標的とした糖尿病治療薬の開発、5. アンチセンス核酸の活性化アナログの開発とその構造機能解析
Overview of your research
(Japanese)
アルツハイマー病因物質であるアミロイドβの毒性オリゴマーの細胞内標的タンパク質を探索している。また、毒性オリゴマー形成の阻害剤を食品・漢方薬より探索し、その阻害機構を核磁気共鳴および質量分析法を駆使しながら解析している。さらに、毒性オリゴマーを特異的に検知する核酸アプタマーを作製し、血液を用いた超高感度診断プラットフォームへの応用を目指している。一方で、アルツハイマー病の最大リスク因子である2型糖尿病にも着目し、原因物質の一つであるアミリンペプチドによるインスリン分泌を調節する化合物を開発する。具体的には、アミリンの分子内スルフィド形成阻害剤、ペプチド核酸アナログを開発し、その作用機序を複数の高度機器分析を利活用することで明らかにする。以上の研究テーマを推進することで、大多数の国民が苦しむ生活習慣病の健康予防ならびに早期診断に貢献したい。
Fields of research (key words)
Key words(Japanese) Key words(English)
生物有機化学 bioorganic organic chemistry
ケミカルバイオロジー chemical biology
天然物化学 chemistry of natural products
抗体 antibody
アルツハイマー病 Alzheimer's disease
核酸生物化学
糖尿病
Fields of research (kaken code)
Kaken code
Biological production chemistry/biological organic chemistry
Living organism molecular science
Published Papers
Author Author(Japanese) Author(English) Title Title(Japanese) Title(English) Bibliography Bibliography(Japanese) Bibliography(English) Publication date Refereed paper Language Publishing type Disclose
†Murakami, K., Yoshioka, T., Horii, S., Hanaki, M., Midorikawa, S., Taniwaki, S., Gunji, H., Akagi, K., Kawase, T., Hirose, K., and *Irie, K. †Murakami, K., Yoshioka, T., Horii, S., Hanaki, M., Midorikawa, S., Taniwaki, S., Gunji, H., Akagi, K., Kawase, T., Hirose, K., and *Irie, K. †Murakami, K., Yoshioka, T., Horii, S., Hanaki, M., Midorikawa, S., Taniwaki, S., Gunji, H., Akagi, K., Kawase, T., Hirose, K., and *Irie, K. Role of carboxy groups of triterpenoids in their inhibition of the nucleation of amyloid β42 required for forming toxic oligomers Role of carboxy groups of triterpenoids in their inhibition of the nucleation of amyloid β42 required for forming toxic oligomers Role of carboxy groups of triterpenoids in their inhibition of the nucleation of amyloid β42 required for forming toxic oligomers Chem. Commun.,54,49,6272-6275 Chem. Commun.,54,49,6272-6275 Chem. Commun.,54,49,6272-6275 2018/07 Refereed English Research paper(scientific journal) Disclose to all
†Hanaki, M., Murakami, K., Katayama, S., Akagi, K., and *Irie, K. †Hanaki, M., Murakami, K., Katayama, S., Akagi, K., and *Irie, K. †Hanaki, M., Murakami, K., Katayama, S., Akagi, K., and *Irie, K. Mechanistic analyses of the suppression of amyloid β42 aggregation by apomorphine Mechanistic analyses of the suppression of amyloid β42 aggregation by apomorphine Mechanistic analyses of the suppression of amyloid β42 aggregation by apomorphine Bioorg. Med. Chem.,26,8,1538-1546 Bioorg. Med. Chem.,26,8,1538-1546 Bioorg. Med. Chem.,26,8,1538-1546 2018/05 Refereed English Research paper(scientific journal) Disclose to all
†Izuo, N., Kasahara, C., Murakami, K., Kume, T., Maeda, M., Irie, K., Yokote, K., and *Shimizu, T. †Izuo, N., Kasahara, C., Murakami, K., Kume, T., Maeda, M., Irie, K., Yokote, K., and *Shimizu, T. †Izuo, N., Kasahara, C., Murakami, K., Kume, T., Maeda, M., Irie, K., Yokote, K., and *Shimizu, T. A toxic conformer of Aβ42 with a turn at 22-23 is a novel therapeutic target for Alzheimer’s disease A toxic conformer of Aβ42 with a turn at 22-23 is a novel therapeutic target for Alzheimer’s disease A toxic conformer of Aβ42 with a turn at 22-23 is a novel therapeutic target for Alzheimer’s disease Sci. Rep.,7,1,11811 Sci. Rep.,7,1,11811 Sci. Rep.,7,1,11811 2017/09 Refereed English Research paper(scientific journal) Disclose to all
Oku Y, Murakami K, Irie K, Hoseki J, Sakai Y Oku Y, Murakami K, Irie K, Hoseki J, Sakai Y Oku Y, Murakami K, Irie K, Hoseki J, Sakai Y Synthesized Aβ42 Caused Intracellular Oxidative Damage, Leading to Cell Death, via Lysosome Rupture. Synthesized Aβ42 Caused Intracellular Oxidative Damage, Leading to Cell Death, via Lysosome Rupture. Synthesized Aβ42 Caused Intracellular Oxidative Damage, Leading to Cell Death, via Lysosome Rupture. Cell structure and function,42,1,71-79 Cell structure and function,42,1,71-79 Cell structure and function,42,1,71-79 2017/05 Refereed Disclose to all
Irie Y, Murakami K, Hanaki M, Hanaki Y, Suzuki T, Monobe Y, Takai T, Akagi KI, Kawase T, Hirose K, Irie K Irie Y, Murakami K, Hanaki M, Hanaki Y, Suzuki T, Monobe Y, Takai T, Akagi KI, Kawase T, Hirose K, Irie K Irie Y, Murakami K, Hanaki M, Hanaki Y, Suzuki T, Monobe Y, Takai T, Akagi KI, Kawase T, Hirose K, Irie K Synthetic Models of Quasi-Stable Amyloid β40 Oligomers with Significant Neurotoxicity. Synthetic Models of Quasi-Stable Amyloid β40 Oligomers with Significant Neurotoxicity. Synthetic Models of Quasi-Stable Amyloid β40 Oligomers with Significant Neurotoxicity. ACS chemical neuroscience,8,4,807-816 ACS chemical neuroscience,8,4,807-816 ACS chemical neuroscience,8,4,807-816 2017/04 Refereed Disclose to all
Ben Hmidene A, Hanaki M, Murakami K, Irie K, Isoda H, Shigemori H Ben Hmidene A, Hanaki M, Murakami K, Irie K, Isoda H, Shigemori H Ben Hmidene A, Hanaki M, Murakami K, Irie K, Isoda H, Shigemori H Inhibitory Activities of Antioxidant Flavonoids from Tamarix gallica on Amyloid Aggregation Related to Alzheimer's and Type 2 Diabetes Diseases. Inhibitory Activities of Antioxidant Flavonoids from Tamarix gallica on Amyloid Aggregation Related to Alzheimer's and Type 2 Diabetes Diseases. Inhibitory Activities of Antioxidant Flavonoids from Tamarix gallica on Amyloid Aggregation Related to Alzheimer's and Type 2 Diabetes Diseases. Biological & pharmaceutical bulletin,40,2,238-241 Biological & pharmaceutical bulletin,40,2,238-241 Biological & pharmaceutical bulletin,40,2,238-241 2017 Refereed Disclose to all
Y. Aihara, A. Kawaguchi, M. Hanaki, K. Murakami, K. Irie and H. Shigemori* Y. Aihara, A. Kawaguchi, M. Hanaki, K. Murakami, K. Irie and H. Shigemori* Y. Aihara, A. Kawaguchi, M. Hanaki, K. Murakami, K. Irie and H. Shigemori* Inhibitory activity of hispidin derivatives isolated from Inonotus obliquus on amyloid β aggregation Inhibitory activity of hispidin derivatives isolated from Inonotus obliquus on amyloid β aggregation Inhibitory activity of hispidin derivatives isolated from Inonotus obliquus on amyloid β aggregation Heterocycles,94,7,1280-1287 Heterocycles,94,7,1280-1287 Heterocycles,94,7,1280-1287 2017 Refereed English Research paper(scientific journal) Disclose to all
Yoshioka T, Murakami K, Ido K, Hanaki M, Yamaguchi K, Midorikawa S, Taniwaki S, Gunji H, Irie K Yoshioka T, Murakami K, Ido K, Hanaki M, Yamaguchi K, Midorikawa S, Taniwaki S, Gunji H, Irie K Yoshioka T, Murakami K, Ido K, Hanaki M, Yamaguchi K, Midorikawa S, Taniwaki S, Gunji H, Irie K Semisynthesis and Structure-Activity Studies of Uncarinic Acid C Isolated from Uncaria rhynchophylla as a Specific Inhibitor of the Nucleation Phase in Amyloid β42 Aggregation. Semisynthesis and Structure-Activity Studies of Uncarinic Acid C Isolated from Uncaria rhynchophylla as a Specific Inhibitor of the Nucleation Phase in Amyloid β42 Aggregation. Semisynthesis and Structure-Activity Studies of Uncarinic Acid C Isolated from Uncaria rhynchophylla as a Specific Inhibitor of the Nucleation Phase in Amyloid β42 Aggregation. Journal of natural products,79,10,2521-2529 Journal of natural products,79,10,2521-2529 Journal of natural products,79,10,2521-2529 2016/10 Refereed Disclose to all
Murakami K, Tokuda M, Suzuki T, Irie Y, Hanaki M, Izuo N, Monobe Y, Akagi K, Ishii R, Tatebe H, Tokuda T, Maeda M, Kume T, Shimizu T, *Irie K Murakami K, Tokuda M, Suzuki T, Irie Y, Hanaki M, Izuo N, Monobe Y, Akagi K, Ishii R, Tatebe H, Tokuda T, Maeda M, Kume T, Shimizu T, *Irie K Murakami K, Tokuda M, Suzuki T, Irie Y, Hanaki M, Izuo N, Monobe Y, Akagi K, Ishii R, Tatebe H, Tokuda T, Maeda M, Kume T, Shimizu T, *Irie K Monoclonal antibody with conformational specificity for a toxic conformer of amyloid β42 and its application toward the Alzheimer's disease diagnosis. Monoclonal antibody with conformational specificity for a toxic conformer of amyloid β42 and its application toward the Alzheimer's disease diagnosis. Monoclonal antibody with conformational specificity for a toxic conformer of amyloid β42 and its application toward the Alzheimer's disease diagnosis. Scientific Reports,6,29038 Scientific Reports,6,29038 Scientific Reports,6,29038 2016/07 Refereed English Research paper(scientific journal) Disclose to all
Hanaki, M., Murakami, K., Akagi, K., and *Irie, K. Hanaki, M., Murakami, K., Akagi, K., and *Irie, K. Hanaki, M., Murakami, K., Akagi, K., and *Irie, K. Structural insights into mechanism for inhibiting amyloid β42 aggregation by non-catechol-type flavonoids Structural insights into mechanism for inhibiting amyloid β42 aggregation by non-catechol-type flavonoids Structural insights into mechanism for inhibiting amyloid β42 aggregation by non-catechol-type flavonoids Bioorg. Med. Chem.,24,2,304-313 Bioorg. Med. Chem.,24,2,304-313 Bioorg. Med. Chem.,24,2,304-313 2016/01 Refereed English Research paper(scientific journal) Disclose to all
Hanaki M, Murakami K, Akagi K, Irie K Hanaki M, Murakami K, Akagi K, Irie K Hanaki M, Murakami K, Akagi K, Irie K Structural insights into mechanisms for inhibiting amyloid β42 aggregation by non-catechol-type flavonoids. Structural insights into mechanisms for inhibiting amyloid β42 aggregation by non-catechol-type flavonoids. Structural insights into mechanisms for inhibiting amyloid β42 aggregation by non-catechol-type flavonoids. Bioorganic & medicinal chemistry,24,2,304-313 Bioorganic & medicinal chemistry,24,2,304-313 Bioorganic & medicinal chemistry,24,2,304-313 2016/01 Refereed Disclose to all
E. Kidachi, M. Kurisu, Y. Miyamae, M. Hanaki, K. Murakami, K. Irie and H. Shigemori* E. Kidachi, M. Kurisu, Y. Miyamae, M. Hanaki, K. Murakami, K. Irie and H. Shigemori* E. Kidachi, M. Kurisu, Y. Miyamae, M. Hanaki, K. Murakami, K. Irie and H. Shigemori* Structure-activity relationship of phenylethanoid glycosides on the inhibition of amyloid β aggregation Structure-activity relationship of phenylethanoid glycosides on the inhibition of amyloid β aggregation Structure-activity relationship of phenylethanoid glycosides on the inhibition of amyloid β aggregation Heterocycles,92,11,1976-1982 Heterocycles,92,11,1976-1982 Heterocycles,92,11,1976-1982 2016 Refereed English Research paper(scientific journal) Disclose to all
Murakami, K., Suzuki, T., Hanaki, M., Monobe, Y., Akagi, K., and *Irie, K. Murakami, K., Suzuki, T., Hanaki, M., Monobe, Y., Akagi, K., and *Irie, K. Murakami, K., Suzuki, T., Hanaki, M., Monobe, Y., Akagi, K., and *Irie, K. Synthesis and characterization of the amyloid β40 dimer model with a linker at position 30 adjacent to the intermolecular β-sheet region Synthesis and characterization of the amyloid β40 dimer model with a linker at position 30 adjacent to the intermolecular β-sheet region Synthesis and characterization of the amyloid β40 dimer model with a linker at position 30 adjacent to the intermolecular β-sheet region Biochem. Biophys. Res. Commun.,466,3,463-467 Biochem. Biophys. Res. Commun.,466,3,463-467 Biochem. Biophys. Res. Commun.,466,3,463-467 2015/10 Refereed English Research paper(scientific journal) Disclose to all
泉尾直孝*,村上一馬,久米利明,前田雅弘,入江一浩,清水孝彦 泉尾直孝*,村上一馬,久米利明,前田雅弘,入江一浩,清水孝彦 アルツハイマー病様神経毒性におけるアミロイドβコンホマーの役割 アルツハイマー病様神経毒性におけるアミロイドβコンホマーの役割 基礎老化研究,39,3,29-34 基礎老化研究,39,3,29-34 ,39,3,29-34 2015 Japanese Research paper(scientific journal) Disclose to all
*Kazuma Murakami *Kazuma Murakami *Kazuma Murakami Conformation-specific antibodies to target amyloid β oligomers and their application to immunotherapy for Alzheimer’s disease. Conformation-specific antibodies to target amyloid β oligomers and their application to immunotherapy for Alzheimer’s disease. Conformation-specific antibodies to target amyloid β oligomers and their application to immunotherapy for Alzheimer’s disease. Biosci. Biotechnol. Biochem.,78,8,1293-1305 Biosci. Biotechnol. Biochem.,78,8,1293-1305 Biosci. Biotechnol. Biochem.,78,8,1293-1305 2014/08 Refereed English Research paper(scientific journal) Disclose to all
Murakami K, Keene AC Murakami K, Keene AC Murakami K, Keene AC Development: better sleep on it, children. Development: better sleep on it, children. Development: better sleep on it, children. Current biology : CB,24,12,R569-71 Current biology : CB,24,12,R569-71 Current biology : CB,24,12,R569-71 2014/06 Refereed Disclose to all
Sato M, Murakami K, Uno M, Nakagawa Y, Katayama S, Akagi K, Masuda Y, Takegoshi K, Irie K Sato M, Murakami K, Uno M, Nakagawa Y, Katayama S, Akagi K, Masuda Y, Takegoshi K, Irie K Sato M, Murakami K, Uno M, Nakagawa Y, Katayama S, Akagi K, Masuda Y, Takegoshi K, Irie K Site-specific inhibitory mechanism for amyloid β42 aggregation by catechol-type flavonoids targeting the Lys residues. Site-specific inhibitory mechanism for amyloid β42 aggregation by catechol-type flavonoids targeting the Lys residues. Site-specific inhibitory mechanism for amyloid β42 aggregation by catechol-type flavonoids targeting the Lys residues. The Journal of biological chemistry,288,32,23212-23224 The Journal of biological chemistry,288,32,23212-23224 The Journal of biological chemistry,288,32,23212-23224 2013/08 Refereed Disclose to all
Izuo N, Murakami K, Sato M, Iwasaki M, Izumi Y, Shimizu T, Akaike A, Irie K, Kume T Izuo N, Murakami K, Sato M, Iwasaki M, Izumi Y, Shimizu T, Akaike A, Irie K, Kume T Izuo N, Murakami K, Sato M, Iwasaki M, Izumi Y, Shimizu T, Akaike A, Irie K, Kume T Non-toxic conformer of amyloid β may suppress amyloid β-induced toxicity in rat primary neurons: implications for a novel therapeutic strategy for Alzheimer's disease. Non-toxic conformer of amyloid β may suppress amyloid β-induced toxicity in rat primary neurons: implications for a novel therapeutic strategy for Alzheimer's disease. Non-toxic conformer of amyloid β may suppress amyloid β-induced toxicity in rat primary neurons: implications for a novel therapeutic strategy for Alzheimer's disease. Biochemical and biophysical research communications,438,1,1-5 Biochemical and biophysical research communications,438,1,1-5 Biochemical and biophysical research communications,438,1,1-5 2013/08 Refereed Disclose to all
Kamachi, H., Tanaka, K., Yanagita, R. C., Murakami, A., Murakami, K., Tokuda, H., Suzki, N., Nakagawa, Y., and *Irie, K. Kamachi, H., Tanaka, K., Yanagita, R. C., Murakami, A., Murakami, K., Tokuda, H., Suzki, N., Nakagawa, Y., and *Irie, K. Kamachi, H., Tanaka, K., Yanagita, R. C., Murakami, A., Murakami, K., Tokuda, H., Suzki, N., Nakagawa, Y., and *Irie, K. Structure-activity studies on the side chain of a simplified analog of aplysiatoxin (aplog-1) with anti-proliferative activity Structure-activity studies on the side chain of a simplified analog of aplysiatoxin (aplog-1) with anti-proliferative activity Structure-activity studies on the side chain of a simplified analog of aplysiatoxin (aplog-1) with anti-proliferative activity Bioorg. Med. Chem. 21 (10), 2695-2702 (2013).,21,10,2695-2702 Bioorg. Med. Chem. 21 (10), 2695-2702 (2013).,21,10,2695-2702 Bioorg. Med. Chem. 21 (10), 2695-2702 (2013).,21,10,2695-2702 2013/05 Refereed English Research paper(scientific journal) Disclose to all
Kondo T, Asai M, Tsukita K, Kutoku Y, Ohsawa Y, Sunada Y, Imamura K, Egawa N, Yahata N, Okita K, Takahashi K, Asaka I, Aoi T, Watanabe A, Watanabe K, Kadoya C, Nakano R, Watanabe D, Maruyama K, Hori O, Hibino S, Choshi T, Nakahata T, Hioki H, Kaneko T, Naitoh M, Yoshikawa K, Yamawaki S, Suzuki S, Hata R, Ueno S, Seki T, Kobayashi K, Toda T, Murakami K, Irie K, Klein WL, Mori H, Asada T, Takahashi R, Iwata N, Yamanaka S, Inoue H Kondo, T., Asai, M., Tsukita, K., Kutoku, Y., Ohsawa, Y., Sunada, Y., Imamura, K., Egawa, N., Yahata, N., Okita, K., Takahashi, K., Asaka, I., Aoi, T., Watanabe, A., Watanabe, K., Kadoya, C., Nakano, R., Watanabe, D., Maruyama, K., Hori, O., Hibino, S., Choshi, T., Nakahata, T., Hioki, H., Kaneko, T., Naitoh, M., Yoshikawa, S., Yamawaki, S., Suzuki, S., Hata, R., Ueno, S., Seki, T., Kobayashi, K., Toda, T., Murakami, K., Irie, K., Klein, W. L., Mori, H., Asada, T., Takahashi, R., *Iwata, N., Yamanaka, S., and *Inoue, H. Kondo T, Asai M, Tsukita K, Kutoku Y, Ohsawa Y, Sunada Y, Imamura K, Egawa N, Yahata N, Okita K, Takahashi K, Asaka I, Aoi T, Watanabe A, Watanabe K, Kadoya C, Nakano R, Watanabe D, Maruyama K, Hori O, Hibino S, Choshi T, Nakahata T, Hioki H, Kaneko T, Naitoh M, Yoshikawa K, Yamawaki S, Suzuki S, Hata R, Ueno S, Seki T, Kobayashi K, Toda T, Murakami K, Irie K, Klein WL, Mori H, Asada T, Takahashi R, Iwata N, Yamanaka S, Inoue H Modeling Alzheimer's disease with iPSCs reveals stress phenotypes associated with intracellular Aβ and differential drug responsiveness. Modeling Alzheimer’s disease with iPSCs reveals stress phenotypes associated with intracellular Aβ and differential drug responsiveness. Modeling Alzheimer's disease with iPSCs reveals stress phenotypes associated with intracellular Aβ and differential drug responsiveness. Cell stem cell,12,4,487-496 Cell Stem Cell 12 (4), 487-496 (2013).,12,4,487-496 Cell stem cell,12,4,487-496 2013/04 Refereed Japanese Research paper(scientific journal) Disclose to all
Kenche VB, Hung LW, Perez K, Volitakes I, Ciccotosto G, Kwok J, Critch N, Sherratt N, Cortes M, Lal V, Masters CL, Murakami K, Cappai R, Adlard PA, Barnham KJ Kenche, V. B., Hung, L. W., Perez, K., Volitakes, I., Ciccotosto, G., Kwok, J., Critch, N., Sherratt, N., Cortes, M., Lal, V., Masters, C. L., Murakami, K., Cappai, R., Adlard, P. A., and *Barnham, K. J. Kenche VB, Hung LW, Perez K, Volitakes I, Ciccotosto G, Kwok J, Critch N, Sherratt N, Cortes M, Lal V, Masters CL, Murakami K, Cappai R, Adlard PA, Barnham KJ Development of a platinum complex as an anti-amyloid agent for the therapy of Alzheimer's disease. Development of a platinum complex as an anti-amyloid agent for the therapy of Alzheimer’s disease. Development of a platinum complex as an anti-amyloid agent for the therapy of Alzheimer's disease. Angewandte Chemie (International ed. in English),52,12,3374-3378 Angew. Chem. Int. Ed. 52 (12), 3374-3378 (2013).,52,12,3374-3378 Angewandte Chemie (International ed. in English),52,12,3374-3378 2013/03 Refereed Japanese Research paper(scientific journal) Disclose to all
Soejima, N., *Ohyagi, Y., Nakamura, N., Himeno, E., Iimura, K. M., Sakae, N., Yamasaki, R., Tabira, T., Murakami, K., Irie, K., Kinoshita, N., LaFerla, F. M., Kiyohara, Y., Iwaki, T., and Kira, J. Soejima, N., *Ohyagi, Y., Nakamura, N., Himeno, E., Iimura, K. M., Sakae, N., Yamasaki, R., Tabira, T., Murakami, K., Irie, K., Kinoshita, N., LaFerla, F. M., Kiyohara, Y., Iwaki, T., and Kira, J. Soejima, N., *Ohyagi, Y., Nakamura, N., Himeno, E., Iimura, K. M., Sakae, N., Yamasaki, R., Tabira, T., Murakami, K., Irie, K., Kinoshita, N., LaFerla, F. M., Kiyohara, Y., Iwaki, T., and Kira, J. Intracellular accumulation of toxic turn amyloid-β is associated with endoplasmic reticulum stress in Alzheimer's disease. Intracellular accumulation of toxic turn amyloid-β is associated with endoplasmic reticulum stress in Alzheimer's disease. Intracellular accumulation of toxic turn amyloid-β is associated with endoplasmic reticulum stress in Alzheimer's disease. Curr. Alzheimer Res.,10,1,11-20 Curr. Alzheimer Res.,10,1,11-20 Curr. Alzheimer Res.,10,1,11-20 2013/01 Refereed English Research paper(scientific journal) Disclose to all
Sato, M., Murakami, K., Uno, M., Ikubo, H., Nakagawa, Y., Katayama, S., Akagi, K., and *Irie, K. Sato, M., Murakami, K., Uno, M., Ikubo, H., Nakagawa, Y., Katayama, S., Akagi, K., and *Irie, K. Identification of (+)-taxifolin from silymarin as inhibitor of amyloid β aggregation and evaluation of its structure-activity relationship. Identification of (+)-taxifolin from silymarin as inhibitor of amyloid β aggregation and evaluation of its structure-activity relationship. Biosci. Biotechnol. Biochem. 77 (5), 1100-1103 (2013). Biosci. Biotechnol. Biochem. 77 (5), 1100-1103 (2013). 2013 Refereed Japanese Research paper(scientific journal) Disclose to all
Kurisu, M., Miyamae, Y., Murakami, K., Han, J., Isoda, H., Irie, K., and *Shigemori, H. Kurisu, M., Miyamae, Y., Murakami, K., Han, J., Isoda, H., Irie, K., and *Shigemori, H. Acteoside, a phenylethanoid glycoside, inhibits amyloid β aggregation. Acteoside, a phenylethanoid glycoside, inhibits amyloid β aggregation. Biosci. Biotechnol. Biochem. 77 (6), 1329-1332 (2013). Biosci. Biotechnol. Biochem. 77 (6), 1329-1332 (2013). 2013 Refereed Japanese Research paper(scientific journal) Disclose to all
Izuo, N., Murakami, K., Sato, M., Iwasaki, M., Izumi, Y., Kinoshita, N., Akaike, A., *Irie, K., and *Kume, T. Izuo, N., Murakami, K., Sato, M., Iwasaki, M., Izumi, Y., Kinoshita, N., Akaike, A., *Irie, K., and *Kume, T. Izuo, N., Murakami, K., Sato, M., Iwasaki, M., Izumi, Y., Kinoshita, N., Akaike, A., *Irie, K., and *Kume, T. Non-toxic conformer of Aβ42 may suppress Aβ42-induced toxicity in rat primary neurons: implications for a novel therapeutic strategy of Alzheimer’s disease. Non-toxic conformer of Aβ42 may suppress Aβ42-induced toxicity in rat primary neurons: implications for a novel therapeutic strategy of Alzheimer’s disease. Non-toxic conformer of Aβ42 may suppress Aβ42-induced toxicity in rat primary neurons: implications for a novel therapeutic strategy of Alzheimer’s disease. Biochem. Biophys. Res. Commun.,438,1,1-5 Biochem. Biophys. Res. Commun.,438,1,1-5 Biochem. Biophys. Res. Commun.,438,1,1-5 2013 Refereed English Research paper(scientific journal) Disclose to all
Sato, M., Murakami, K., Uno, M., Nakagawa, Y., Katayama, S., Akagi, K., Masuda, Y., Takegoshi, K., and *Irie, K. Sato, M., Murakami, K., Uno, M., Nakagawa, Y., Katayama, S., Akagi, K., Masuda, Y., Takegoshi, K., and *Irie, K. Sato, M., Murakami, K., Uno, M., Nakagawa, Y., Katayama, S., Akagi, K., Masuda, Y., Takegoshi, K., and *Irie, K. Site-specific inhibitory mechanism of amyloid-β42 aggregation by catechol-type flavonoids targeting the Lys residues. Site-specific inhibitory mechanism of amyloid-β42 aggregation by catechol-type flavonoids targeting the Lys residues. Site-specific inhibitory mechanism of amyloid-β42 aggregation by catechol-type flavonoids targeting the Lys residues. J. Biol. Chem.,288,32,23212-23224 J. Biol. Chem.,288,32,23212-23224 J. Biol. Chem.,288,32,23212-23224 2013 Refereed English Research paper(scientific journal) Disclose to all
Kurisu M, Miyamae Y, Murakami K, Han J, Isoda H, Irie K, Shigemori H Kurisu M, Miyamae Y, Murakami K, Han J, Isoda H, Irie K, Shigemori H Kurisu M, Miyamae Y, Murakami K, Han J, Isoda H, Irie K, Shigemori H Inhibition of amyloid β aggregation by acteoside, a phenylethanoid glycoside. Inhibition of amyloid β aggregation by acteoside, a phenylethanoid glycoside. Inhibition of amyloid β aggregation by acteoside, a phenylethanoid glycoside. Bioscience, biotechnology, and biochemistry,77,6,1329-1332 Bioscience, biotechnology, and biochemistry,77,6,1329-1332 Bioscience, biotechnology, and biochemistry,77,6,1329-1332 2013 Refereed Disclose to all
Sato M, Murakami K, Uno M, Ikubo H, Nakagawa Y, Katayama S, Akagi K, Irie K Sato M, Murakami K, Uno M, Ikubo H, Nakagawa Y, Katayama S, Akagi K, Irie K Sato M, Murakami K, Uno M, Ikubo H, Nakagawa Y, Katayama S, Akagi K, Irie K Structure-activity relationship for (+)-taxifolin isolated from silymarin as an inhibitor of amyloid β aggregation. Structure-activity relationship for (+)-taxifolin isolated from silymarin as an inhibitor of amyloid β aggregation. Structure-activity relationship for (+)-taxifolin isolated from silymarin as an inhibitor of amyloid β aggregation. Bioscience, biotechnology, and biochemistry,77,5,1100-1103 Bioscience, biotechnology, and biochemistry,77,5,1100-1103 Bioscience, biotechnology, and biochemistry,77,5,1100-1103 2013 Refereed Disclose to all
Miyamae Y, Kurisu M, Murakami K, Han J, Isoda H, Irie K, Shigemori H Miyamae Y, Kurisu M, Murakami K, Han J, Isoda H, Irie K, Shigemori H Miyamae Y, Kurisu M, Murakami K, Han J, Isoda H, Irie K, Shigemori H Protective effects of caffeoylquinic acids on the aggregation and neurotoxicity of the 42-residue amyloid β-protein. Protective effects of caffeoylquinic acids on the aggregation and neurotoxicity of the 42-residue amyloid β-protein. Protective effects of caffeoylquinic acids on the aggregation and neurotoxicity of the 42-residue amyloid β-protein. Bioorganic & medicinal chemistry,20,19,5844-5849 Bioorganic & medicinal chemistry,20,19,5844-5849 Bioorganic & medicinal chemistry,20,19,5844-5849 2012/10 Refereed Disclose to all
Izuo N, Kume T, Sato M, Murakami K, Irie K, Izumi Y, Akaike A Izuo N, Kume T, Sato M, Murakami K, Irie K, Izumi Y, Akaike A Izuo N, Kume T, Sato M, Murakami K, Irie K, Izumi Y, Akaike A Toxicity in rat primary neurons through the cellular oxidative stress induced by the turn formation at positions 22 and 23 of Aβ42. Toxicity in rat primary neurons through the cellular oxidative stress induced by the turn formation at positions 22 and 23 of Aβ42. Toxicity in rat primary neurons through the cellular oxidative stress induced by the turn formation at positions 22 and 23 of Aβ42. ACS chemical neuroscience,3,9,674-681 ACS chemical neuroscience,3,9,674-681 ACS chemical neuroscience,3,9,674-681 2012/09 Refereed Disclose to all
Murakami K, Shimizu T Murakami K, Shimizu T Murakami K, Shimizu T Cytoplasmic superoxide radical: a possible contributing factor to intracellular Aβ oligomerization in Alzheimer disease. Cytoplasmic superoxide radical: a possible contributing factor to intracellular Aβ oligomerization in Alzheimer disease. Cytoplasmic superoxide radical: a possible contributing factor to intracellular Aβ oligomerization in Alzheimer disease. Communicative & integrative biology,5,3,255-258 Communicative & integrative biology,5,3,255-258 Communicative & integrative biology,5,3,255-258 2012/05 Refereed Disclose to all
Tsuji, F., Ishihara, A., Kurata, K., Nakagawa, A., Okada, M., Kitamura, S., Kanamaru, K., Masuda, Y., Murakami, K., Irie, K., and *Sakagami, Y.: Tsuji, F., Ishihara, A., Kurata, K., Nakagawa, A., Okada, M., Kitamura, S., Kanamaru, K., Masuda, Y., Murakami, K., Irie, K., and *Sakagami, Y.: Tsuji, F., Ishihara, A., Kurata, K., Nakagawa, A., Okada, M., Kitamura, S., Kanamaru, K., Masuda, Y., Murakami, K., Irie, K., and *Sakagami, Y.: Geranyl modification on the tryptophan residue of ComXRO-E-2 pheromone by a cell-free system. Geranyl modification on the tryptophan residue of ComXRO-E-2 pheromone by a cell-free system. Geranyl modification on the tryptophan residue of ComXRO-E-2 pheromone by a cell-free system. FEBS Lett. 586 (2), 174-179 (2012).,586,2,174-179 FEBS Lett. 586 (2), 174-179 (2012).,586,2,174-179 FEBS Lett. 586 (2), 174-179 (2012).,586,2,174-179 2012/01 Refereed English Research paper(scientific journal) Disclose to all
Tsuji F, Ishihara A, Nakagawa A, Okada M, Kitamura S, Kanamaru K, Masuda Y, Murakami K, Irie K, Sakagami Y Tsuji F, Ishihara A, Nakagawa A, Okada M, Kitamura S, Kanamaru K, Masuda Y, Murakami K, Irie K, Sakagami Y Tsuji F, Ishihara A, Nakagawa A, Okada M, Kitamura S, Kanamaru K, Masuda Y, Murakami K, Irie K, Sakagami Y Lack of the consensus sequence necessary for tryptophan prenylation in the ComX pheromone precursor. Lack of the consensus sequence necessary for tryptophan prenylation in the ComX pheromone precursor. Lack of the consensus sequence necessary for tryptophan prenylation in the ComX pheromone precursor. Bioscience, biotechnology, and biochemistry,76,8,1492-1496 Bioscience, biotechnology, and biochemistry,76,8,1492-1496 Bioscience, biotechnology, and biochemistry,76,8,1492-1496 2012 Refereed Disclose to all
Ueno S, Yanagita RC, Murakami K, Murakami A, Tokuda H, Suzuki N, Fujiwara T, Irie K Ueno S, Yanagita RC, Murakami K, Murakami A, Tokuda H, Suzuki N, Fujiwara T, Irie K Ueno S, Yanagita RC, Murakami K, Murakami A, Tokuda H, Suzuki N, Fujiwara T, Irie K Identification and biological activities of bryostatins from Japanese bryozoan. Identification and biological activities of bryostatins from Japanese bryozoan. Identification and biological activities of bryostatins from Japanese bryozoan. Bioscience, biotechnology, and biochemistry,76,5,1041-1043 Bioscience, biotechnology, and biochemistry,76,5,1041-1043 Bioscience, biotechnology, and biochemistry,76,5,1041-1043 2012 Refereed Disclose to all
村上一馬,佐藤瑞穂,鈴木啓之,泉尾直孝,久米利明,赤池昭紀,永田 徹,西崎知之,富山貴美,森 啓,入江一浩* 村上一馬,佐藤瑞穂,鈴木啓之,泉尾直孝,久米利明,赤池昭紀,永田 徹,西崎知之,富山貴美,森 啓,入江一浩* アミロイドβの「毒性コンホマー」形成とGlu22位における遺伝性変異 アミロイドβの「毒性コンホマー」形成とGlu22位における遺伝性変異 アミロイドβの「毒性コンホマー」形成とGlu22位における遺伝性変異 Dementia Japan,,26,3,311-318 Dementia Japan,26,3,311-318 Dementia Japan,,26,3,311-318 2012 Japanese Research paper(scientific journal) Disclose to all
村上一馬,入江一浩* 村上一馬,入江一浩* Aβの毒性ターン構造を認識する抗体 Aβの毒性ターン構造を認識する抗体 神経内科,77,179-184 神経内科,77,179-184 ,77,179-184 2012 Japanese Research paper(scientific journal) Disclose to all
Rosensweig, C. Ono, K., Murakami, K., Lowenstein, D., Bitan, G., and *Teplow, D. B. Rosensweig, C. Ono, K., Murakami, K., Lowenstein, D., Bitan, G., and *Teplow, D. B. Rosensweig, C. Ono, K., Murakami, K., Lowenstein, D., Bitan, G., and *Teplow, D. B. Preparation of stable amyloid β-protein oligomers of defined assembly order. Preparation of stable amyloid β-protein oligomers of defined assembly order. Preparation of stable amyloid β-protein oligomers of defined assembly order. Methods. Mol. Biol. 849, 23-31 (2012).,849,23-31 Methods. Mol. Biol. 849, 23-31 (2012).,849,23-31 Methods. Mol. Biol. 849, 23-31 (2012).,849,23-31 2012 Refereed English Research paper(scientific journal) Disclose to all
Ueno, S., Yanagita, R. C., Murakami, K., Murakami, A., Tokuda, H., Suzuki, N., Fujiwara, T., and *Irie, K. Ueno, S., Yanagita, R. C., Murakami, K., Murakami, A., Tokuda, H., Suzuki, N., Fujiwara, T., and *Irie, K. Ueno, S., Yanagita, R. C., Murakami, K., Murakami, A., Tokuda, H., Suzuki, N., Fujiwara, T., and *Irie, K. Identification and biological activities of bryostatins isolated from Japanese bryozoan Identification and biological activities of bryostatins isolated from Japanese bryozoan Identification and biological activities of bryostatins isolated from Japanese bryozoan Biosci. Biotechnol. Biochem. 76 (5), 1041-1043 (2012). Biosci. Biotechnol. Biochem. 76 (5), 1041-1043 (2012). Biosci. Biotechnol. Biochem. 76 (5), 1041-1043 (2012). 2012 Refereed English Research paper(scientific journal) Disclose to all
Murakami, K., Murata, N., Noda, Y., Irie, K., Shirasawa, T., and *Shimizu, T. Murakami, K., Murata, N., Noda, Y., Irie, K., Shirasawa, T., and *Shimizu, T. Murakami, K., Murata, N., Noda, Y., Irie, K., Shirasawa, T., and *Shimizu, T. Stimulation of the amyloidogenic pathway by cytoplasmic superoxide radicals in an Alzheimer’s disease mouse model Stimulation of the amyloidogenic pathway by cytoplasmic superoxide radicals in an Alzheimer’s disease mouse model Stimulation of the amyloidogenic pathway by cytoplasmic superoxide radicals in an Alzheimer’s disease mouse model Biosci. Biotechnol. Biochem. 76 (6), 1098-1103 (2012).,76,6,1098-1103 Biosci. Biotechnol. Biochem. 76 (6), 1098-1103 (2012).,76,6,1098-1103 Biosci. Biotechnol. Biochem. 76 (6), 1098-1103 (2012).,76,6,1098-1103 2012 Refereed English Research paper(scientific journal) Disclose to all
Tsuji, F., Ishihara, A., Kurata, K., Nakagawa, A., Okada, M., Kitamura, S., Kanamaru, K., Masuda, Y., Murakami, K., Irie, K., and Sakagami, Y. Tsuji, F., Ishihara, A., Kurata, K., Nakagawa, A., Okada, M., Kitamura, S., Kanamaru, K., Masuda, Y., Murakami, K., Irie, K., and Sakagami, Y. Tsuji, F., Ishihara, A., Kurata, K., Nakagawa, A., Okada, M., Kitamura, S., Kanamaru, K., Masuda, Y., Murakami, K., Irie, K., and Sakagami, Y. ComX pheromone precursor contains no consensus sequence necessary for tryptophan prenylation. ComX pheromone precursor contains no consensus sequence necessary for tryptophan prenylation. ComX pheromone precursor contains no consensus sequence necessary for tryptophan prenylation. Biosci. Biotechnol. Biochem. 76 (8), 1492-1496 (2012). Biosci. Biotechnol. Biochem. 76 (8), 1492-1496 (2012). Biosci. Biotechnol. Biochem. 76 (8), 1492-1496 (2012). 2012 Refereed English Research paper(scientific journal) Disclose to all
Izuo, N., Kume, T., Sato, M., Murakami, K., *Irie, K., Izumi Y., and *Akaike, A. Izuo, N., Kume, T., Sato, M., Murakami, K., *Irie, K., Izumi Y., and *Akaike, A. Izuo, N., Kume, T., Sato, M., Murakami, K., *Irie, K., Izumi Y., and *Akaike, A. Toxicity in rat primary neuron through the cellular oxidative stress induced by the turn formation 22 and 23 of Aβ42. Toxicity in rat primary neuron through the cellular oxidative stress induced by the turn formation 22 and 23 of Aβ42. Toxicity in rat primary neuron through the cellular oxidative stress induced by the turn formation 22 and 23 of Aβ42. ACS Chem. Neurosci. 3 (9), 674-681 (2012). ACS Chem. Neurosci. 3 (9), 674-681 (2012). ACS Chem. Neurosci. 3 (9), 674-681 (2012). 2012 Refereed English Research paper(scientific journal) Disclose to all
Miyamae, Y., Kurisu, M., Murakami, K., Han, J., Isoda, H., Irie, K., and *Shigemori, H. Miyamae, Y., Kurisu, M., Murakami, K., Han, J., Isoda, H., Irie, K., and *Shigemori, H. Miyamae, Y., Kurisu, M., Murakami, K., Han, J., Isoda, H., Irie, K., and *Shigemori, H. Caffeoylquinic acids inhibit amyloid β fibril formation and cellular toxicity. Caffeoylquinic acids inhibit amyloid β fibril formation and cellular toxicity. Caffeoylquinic acids inhibit amyloid β fibril formation and cellular toxicity. Bioorg. Med. Chem. 19 (1), 5844-5849 (2012). Bioorg. Med. Chem. 19 (1), 5844-5849 (2012). Bioorg. Med. Chem. 19 (1), 5844-5849 (2012). 2012 Refereed English Research paper(scientific journal) Disclose to all
*Kulic, L., McAfoose, J., Welt, T., Tackenberg, C., Spani, C., Wirth, F., Finder, V., Konietzko, U., Giese, M., Eckert, A., Kinoshita, N., Shimizu, T., Murakami, K., Irie, K., Rasool, S., Glabe, C., Hock, C., and Nitsch, R. *Kulic, L., McAfoose, J., Welt, T., Tackenberg, C., Spani, C., Wirth, F., Finder, V., Konietzko, U., Giese, M., Eckert, A., Kinoshita, N., Shimizu, T., Murakami, K., Irie, K., Rasool, S., Glabe, C., Hock, C., and Nitsch, R. *Kulic, L., McAfoose, J., Welt, T., Tackenberg, C., Spani, C., Wirth, F., Finder, V., Konietzko, U., Giese, M., Eckert, A., Kinoshita, N., Shimizu, T., Murakami, K., Irie, K., Rasool, S., Glabe, C., Hock, C., and Nitsch, R. Early accumulation of intracellular finrillar oligomers and late congophilic amyloid angiopathy in mice overexpressing the Osaka intra-Aβ APP mutation. Early accumulation of intracellular finrillar oligomers and late congophilic amyloid angiopathy in mice overexpressing the Osaka intra-Aβ APP mutation. Early accumulation of intracellular finrillar oligomers and late congophilic amyloid angiopathy in mice overexpressing the Osaka intra-Aβ APP mutation. Transl. Psychiatry 2012, 2, e183 (2012). Transl. Psychiatry 2012, 2, e183 (2012). Transl. Psychiatry 2012, 2, e183 (2012). 2012 Refereed English Research paper(scientific journal) Disclose to all
Murakami K, Murata N, Noda Y, Tahara S, Kaneko T, Kinoshita N, Hatsuta H, Murayama S, Barnham KJ, Irie K, Shirasawa T, Shimizu T Murakami K, Murata N, Noda Y, Tahara S, Kaneko T, Kinoshita N, Hatsuta H, Murayama S, Barnham KJ, Irie K, Shirasawa T, Shimizu T Murakami K, Murata N, Noda Y, Tahara S, Kaneko T, Kinoshita N, Hatsuta H, Murayama S, Barnham KJ, Irie K, Shirasawa T, Shimizu T SOD1 (copper/zinc superoxide dismutase) deficiency drives amyloid β protein oligomerization and memory loss in mouse model of Alzheimer disease. SOD1 (copper/zinc superoxide dismutase) deficiency drives amyloid β protein oligomerization and memory loss in mouse model of Alzheimer disease. SOD1 (copper/zinc superoxide dismutase) deficiency drives amyloid β protein oligomerization and memory loss in mouse model of Alzheimer disease. The Journal of biological chemistry,286,52,44557-44568 The Journal of biological chemistry,286,52,44557-44568 The Journal of biological chemistry,286,52,44557-44568 2011/12 Refereed Disclose to all
Irie K, Murakami K, Masuda Y, Murata N, Noda Y, Hatsuta H, Murayama S, Shimizu T, Horikoshi Y, Kinoshita N, Shirasawa T Irie K, Murakami K, Masuda Y, Murata N, Noda Y, Hatsuta H, Murayama S, Shimizu T, Horikoshi Y, Kinoshita N, Shirasawa T Irie K, Murakami K, Masuda Y, Murata N, Noda Y, Hatsuta H, Murayama S, Shimizu T, Horikoshi Y, Kinoshita N, Shirasawa T [Monoclonal antibody against the turn of the 42-residue amyloid β-protein at positions 22 and 23]. [Monoclonal antibody against the turn of the 42-residue amyloid β-protein at positions 22 and 23]. [Monoclonal antibody against the turn of the 42-residue amyloid β-protein at positions 22 and 23]. Rinsho shinkeigaku = Clinical neurology,51,11,890-891 Rinsho shinkeigaku = Clinical neurology,51,11,890-891 Rinsho shinkeigaku = Clinical neurology,51,11,890-891 2011/11 Refereed Disclose to all
Murakami, K., Yokoyama, S., Murata, N., Ozawa, Y., Irie, K., Shirasawa, T., and *Shimizu, T. Murakami, K., Yokoyama, S., Murata, N., Ozawa, Y., Irie, K., Shirasawa, T., and *Shimizu, T. Murakami, K., Yokoyama, S., Murata, N., Ozawa, Y., Irie, K., Shirasawa, T., and *Shimizu, T. Insulin receptor mutation results in insulin resistance and hyperinsulinemia but does not exacerbate Alzheimer's-like phenotypes in mice. Insulin receptor mutation results in insulin resistance and hyperinsulinemia but does not exacerbate Alzheimer's-like phenotypes in mice. Insulin receptor mutation results in insulin resistance and hyperinsulinemia but does not exacerbate Alzheimer's-like phenotypes in mice. Biochem. Biophys. Res. Commun. 409 (1), 34-39 (2011).,409,1,34-39 Biochem. Biophys. Res. Commun. 409 (1), 34-39 (2011).,409,1,34-39 Biochem. Biophys. Res. Commun. 409 (1), 34-39 (2011).,409,1,34-39 2011/05 Refereed English Research paper(scientific journal) Disclose to all
Murakami K, Shimizu T, Irie K Murakami K, Shimizu T, Irie K Murakami K, Shimizu T, Irie K Formation of the 42-mer Amyloid β Radical and the Therapeutic Role of Superoxide Dismutase in Alzheimer's Disease. Formation of the 42-mer Amyloid β Radical and the Therapeutic Role of Superoxide Dismutase in Alzheimer's Disease. Formation of the 42-mer Amyloid β Radical and the Therapeutic Role of Superoxide Dismutase in Alzheimer's Disease. Journal of amino acids,2011,654207 Journal of amino acids,2011,654207 Journal of amino acids,2011,654207 2011 Refereed Disclose to all
Suzuki, T., Murakami, K., Izuo, N., Kume, T., Akaike, A., Nagata, T., Nishizaki, T., Tomiyama, T., Takuma, H., Mori, H., and *Irie, K. Suzuki, T., Murakami, K., Izuo, N., Kume, T., Akaike, A., Nagata, T., Nishizaki, T., Tomiyama, T., Takuma, H., Mori, H., and *Irie, K. Suzuki, T., Murakami, K., Izuo, N., Kume, T., Akaike, A., Nagata, T., Nishizaki, T., Tomiyama, T., Takuma, H., Mori, H., and *Irie, K. E22Δ mutation in amyloid β-protein promotes β-sheet transformation, radical production, and synaptotoxicity, but not neurotoxicity. E22Δ mutation in amyloid β-protein promotes β-sheet transformation, radical production, and synaptotoxicity, but not neurotoxicity. E22Δ mutation in amyloid β-protein promotes β-sheet transformation, radical production, and synaptotoxicity, but not neurotoxicity. Int. J. Alzheimers Dis. 2011, doi:10.4061/2011/431320 (2011). Int. J. Alzheimers Dis. 2011, doi:10.4061/2011/431320 (2011). Int. J. Alzheimers Dis. 2011, doi:10.4061/2011/431320 (2011). 2011 Refereed English Research paper(scientific journal) Disclose to all
Murakami, K., Murata, N., Ozawa, Y., Kinoshita, N., Irie, K., Shirasawa, T., *Shimizu, T. Murakami, K., Murata, N., Ozawa, Y., Kinoshita, N., Irie, K., Shirasawa, T., *Shimizu, T. Murakami, K., Murata, N., Ozawa, Y., Kinoshita, N., Irie, K., Shirasawa, T., *Shimizu, T. Vitamin C restores behavioral deficits and amyloid-β oligomerization without affecting plaque formation in a mouse model of Alzheimer's disease. Vitamin C restores behavioral deficits and amyloid-β oligomerization without affecting plaque formation in a mouse model of Alzheimer's disease. Vitamin C restores behavioral deficits and amyloid-β oligomerization without affecting plaque formation in a mouse model of Alzheimer's disease. J. Alzheimers Dis. 26 (1), 7-18 (2011).,26,1,7-18 J. Alzheimers Dis. 26 (1), 7-18 (2011).,26,1,7-18 J. Alzheimers Dis. 26 (1), 7-18 (2011).,26,1,7-18 2011 Refereed English Research paper(scientific journal) Disclose to all
Murakami, K., Murata, N., Noda, Y., Tahara, S., Kaneko, T., Kinoshita, N., Hatsuta, H., Murayama, S., Barnham, K. J., Irie, K., Shirasawa, T., and *Shimizu, T. Murakami, K., Murata, N., Noda, Y., Tahara, S., Kaneko, T., Kinoshita, N., Hatsuta, H., Murayama, S., Barnham, K. J., Irie, K., Shirasawa, T., and *Shimizu, T. Murakami, K., Murata, N., Noda, Y., Tahara, S., Kaneko, T., Kinoshita, N., Hatsuta, H., Murayama, S., Barnham, K. J., Irie, K., Shirasawa, T., and *Shimizu, T. SOD1 deficiency drives amyloid-β oligomerization and memory loss in a mouse model of Alzheimer's disease. SOD1 deficiency drives amyloid-β oligomerization and memory loss in a mouse model of Alzheimer's disease. SOD1 deficiency drives amyloid-β oligomerization and memory loss in a mouse model of Alzheimer's disease. J. Biol. Chem. 286 (52), 44557-44568 (2011). J. Biol. Chem. 286 (52), 44557-44568 (2011). J. Biol. Chem. 286 (52), 44557-44568 (2011). 2011 Refereed English Research paper(scientific journal) Disclose to all
Suzuki T, Murakami K, Izuo N, Kume T, Akaike A, Nagata T, Nishizaki T, Tomiyama T, Takuma H, Mori H, Irie K Suzuki T, Murakami K, Izuo N, Kume T, Akaike A, Nagata T, Nishizaki T, Tomiyama T, Takuma H, Mori H, Irie K Suzuki T, Murakami K, Izuo N, Kume T, Akaike A, Nagata T, Nishizaki T, Tomiyama T, Takuma H, Mori H, Irie K E22Δ Mutation in Amyloid β-Protein Promotes β-Sheet Transformation, Radical Production, and Synaptotoxicity, But Not Neurotoxicity. E22Δ Mutation in Amyloid β-Protein Promotes β-Sheet Transformation, Radical Production, and Synaptotoxicity, But Not Neurotoxicity. E22Δ Mutation in Amyloid β-Protein Promotes β-Sheet Transformation, Radical Production, and Synaptotoxicity, But Not Neurotoxicity. International journal of Alzheimer's disease,2011,431320 International journal of Alzheimer's disease,2011,431320 International journal of Alzheimer's disease,2011,431320 2010/12 Refereed Disclose to all
Murakami, K., Horikoshi-Sakuraba, Y., Murata, N., Noda, Y. Masuda, Y., Kinoshita, N., Hatsuta, H., Murayama, S., Shirasawa, T., *Shimizu, T., and *Irie, K. Murakami, K., Horikoshi-Sakuraba, Y., Murata, N., Noda, Y. Masuda, Y., Kinoshita, N., Hatsuta, H., Murayama, S., Shirasawa, T., *Shimizu, T., and *Irie, K. Murakami, K., Horikoshi-Sakuraba, Y., Murata, N., Noda, Y. Masuda, Y., Kinoshita, N., Hatsuta, H., Murayama, S., Shirasawa, T., *Shimizu, T., and *Irie, K. Monoclonal antibody against the turn of the 42-residue amyloid β-protein at positions 22 and 23. Monoclonal antibody against the turn of the 42-residue amyloid β-protein at positions 22 and 23. Monoclonal antibody against the turn of the 42-residue amyloid β-protein at positions 22 and 23. ACS Chem. Neurosci. 1 (11), 747-756 (2010).,1,11,747-756 ACS Chem. Neurosci. 1 (11), 747-756 (2010).,1,11,747-756 ACS Chem. Neurosci. 1 (11), 747-756 (2010).,1,11,747-756 2010/11 Refereed English Research paper(scientific journal) Disclose to all
Murakami K, Masuda Y, Shirasawa T, Shimizu T, Irie K Murakami K, Masuda Y, Shirasawa T, Shimizu T, Irie K Murakami K, Masuda Y, Shirasawa T, Shimizu T, Irie K The turn formation at positions 22 and 23 in the 42-mer amyloid beta peptide: the emerging role in the pathogenesis of Alzheimer's disease. The turn formation at positions 22 and 23 in the 42-mer amyloid beta peptide: the emerging role in the pathogenesis of Alzheimer's disease. The turn formation at positions 22 and 23 in the 42-mer amyloid beta peptide: the emerging role in the pathogenesis of Alzheimer's disease. Geriatrics & gerontology international,10 Suppl 1,S169-79 Geriatrics & gerontology international,10 Suppl 1,S169-79 Geriatrics & gerontology international,10 Suppl 1,S169-79 2010/07 Refereed Disclose to all
Murata N, Murakami K, Ozawa Y, Kinoshita N, Irie K, Shirasawa T, Shimizu T Murata N, Murakami K, Ozawa Y, Kinoshita N, Irie K, Shirasawa T, Shimizu T Murata N, Murakami K, Ozawa Y, Kinoshita N, Irie K, Shirasawa T, Shimizu T Silymarin attenuated the amyloid β plaque burden and improved behavioral abnormalities in an Alzheimer's disease mouse model. Silymarin attenuated the amyloid β plaque burden and improved behavioral abnormalities in an Alzheimer's disease mouse model. Silymarin attenuated the amyloid β plaque burden and improved behavioral abnormalities in an Alzheimer's disease mouse model. Bioscience, biotechnology, and biochemistry,74,11,2299-2306 Bioscience, biotechnology, and biochemistry,74,11,2299-2306 Bioscience, biotechnology, and biochemistry,74,11,2299-2306 2010 Refereed Disclose to all
Murata, N., Murakami, K., Ozawa, Y., Kinoshita, N., Irie, K., Shirasawa, T., and *Shimizu, T. Murata, N., Murakami, K., Ozawa, Y., Kinoshita, N., Irie, K., Shirasawa, T., and *Shimizu, T. Murata, N., Murakami, K., Ozawa, Y., Kinoshita, N., Irie, K., Shirasawa, T., and *Shimizu, T. Silymarin attenuates the amyloid β plaque burden and rescues behavioral abnormalities in an Alzheimer’s disease mouse model. Silymarin attenuates the amyloid β plaque burden and rescues behavioral abnormalities in an Alzheimer’s disease mouse model. Silymarin attenuates the amyloid β plaque burden and rescues behavioral abnormalities in an Alzheimer’s disease mouse model. Biosci. Biotechnol. Biochem. 74 (11), 2299-2306 (2010). Biosci. Biotechnol. Biochem. 74 (11), 2299-2306 (2010). Biosci. Biotechnol. Biochem. 74 (11), 2299-2306 (2010). 2010 Refereed English Research paper(scientific journal) Disclose to all
Rahimi F, Murakami K, Summers JL, Chen CH, Bitan G Rahimi F, Murakami K, Summers JL, Chen CH, Bitan G Rahimi F, Murakami K, Summers JL, Chen CH, Bitan G RNA aptamers generated against oligomeric Abeta40 recognize common amyloid aptatopes with low specificity but high sensitivity. RNA aptamers generated against oligomeric Abeta40 recognize common amyloid aptatopes with low specificity but high sensitivity. RNA aptamers generated against oligomeric Abeta40 recognize common amyloid aptatopes with low specificity but high sensitivity. PloS one,4,11,e7694 PloS one,4,11,e7694 PloS one,4,11,e7694 2009/11 Refereed Disclose to all
Murakami, K., Inagaki, J., Saito, M., Ikeda, Y., Tsuda, C., Noda, Y., Kawakami, S., Shirasawa, T., and *T. Shimizu. Murakami, K., Inagaki, J., Saito, M., Ikeda, Y., Tsuda, C., Noda, Y., Kawakami, S., Shirasawa, T., and *T. Shimizu. Murakami, K., Inagaki, J., Saito, M., Ikeda, Y., Tsuda, C., Noda, Y., Kawakami, S., Shirasawa, T., and *T. Shimizu. Skin atrophy in cytoplasmic SOD-deficient mice and its complete recovery using a vitamin C derivative. Skin atrophy in cytoplasmic SOD-deficient mice and its complete recovery using a vitamin C derivative. Skin atrophy in cytoplasmic SOD-deficient mice and its complete recovery using a vitamin C derivative. Biochem. Biophys. Res. Commun. 382 (2), 457-461 (2009).,382,2,457-461 Biochem. Biophys. Res. Commun. 382 (2), 457-461 (2009).,382,2,457-461 Biochem. Biophys. Res. Commun. 382 (2), 457-461 (2009).,382,2,457-461 2009/05 Refereed English Research paper(scientific journal) Disclose to all
Rahimi, F., Murakami, K., Summers, J. L., Chen, C. B., and *Bitan, G. Rahimi, F., Murakami, K., Summers, J. L., Chen, C. B., and *Bitan, G. Rahimi, F., Murakami, K., Summers, J. L., Chen, C. B., and *Bitan, G. RNA aptamers generated against oligomeric Aβ40 recognize common amyloid aptatopes with low specificity but high sensitivity. RNA aptamers generated against oligomeric Aβ40 recognize common amyloid aptatopes with low specificity but high sensitivity. RNA aptamers generated against oligomeric Aβ40 recognize common amyloid aptatopes with low specificity but high sensitivity. PLoS ONE 4 (11), e7694 (2009). PLoS ONE 4 (11), e7694 (2009). PLoS ONE 4 (11), e7694 (2009). 2009 Refereed English Research paper(scientific journal) Disclose to all
Murakami K, Uno M, Masuda Y, Shimizu T, Shirasawa T, Irie K Murakami K, Uno M, Masuda Y, Shimizu T, Shirasawa T, Irie K Murakami K, Uno M, Masuda Y, Shimizu T, Shirasawa T, Irie K Isomerization and/or racemization at Asp23 of Abeta42 do not increase its aggregative ability, neurotoxicity, and radical productivity in vitro. Isomerization and/or racemization at Asp23 of Abeta42 do not increase its aggregative ability, neurotoxicity, and radical productivity in vitro. Isomerization and/or racemization at Asp23 of Abeta42 do not increase its aggregative ability, neurotoxicity, and radical productivity in vitro. Biochemical and biophysical research communications,366,3,745-751 Biochemical and biophysical research communications,366,3,745-751 Biochemical and biophysical research communications,366,3,745-751 2008/02 Refereed Disclose to all
村上 一馬*, 清水 孝彦, 白澤 卓二, 入江 一浩 村上 一馬*, 清水 孝彦, 白澤 卓二, 入江 一浩 アミロイドβ (Aβ42) の毒性コンホメーションの提唱 アミロイドβ (Aβ42) の毒性コンホメーションの提唱 基礎老化研究,32,3,25-29 基礎老化研究,32,3,25-29 ,32,3,25-29 2008 Refereed Disclose to all
Murakami, K., Uno, M., Masuda, Y., Shimizu, T., Shirasawa, T., and *Irie, K. Murakami, K., Uno, M., Masuda, Y., Shimizu, T., Shirasawa, T., and *Irie, K. Murakami, K., Uno, M., Masuda, Y., Shimizu, T., Shirasawa, T., and *Irie, K. Isomerization and/or racemization at Asp23 of Aβ42 do not increase its aggregative ability, neurotoxicity, and radical productivity in vitro. Isomerization and/or racemization at Asp23 of Aβ42 do not increase its aggregative ability, neurotoxicity, and radical productivity in vitro. Isomerization and/or racemization at Asp23 of Aβ42 do not increase its aggregative ability, neurotoxicity, and radical productivity in vitro. Biochem. Biophys. Res. Commun. 366 (3), 745-751 (2008). Biochem. Biophys. Res. Commun. 366 (3), 745-751 (2008). Biochem. Biophys. Res. Commun. 366 (3), 745-751 (2008). 2008 Refereed English Research paper(scientific journal) Disclose to all
Murakami K, Hara H, Masuda Y, Ohigashi H, Irie K Murakami K, Hara H, Masuda Y, Ohigashi H, Irie K Murakami K, Hara H, Masuda Y, Ohigashi H, Irie K Distance measurement between Tyr10 and Met35 in amyloid beta by site-directed spin-labeling ESR spectroscopy: implications for the stronger neurotoxicity of Abeta42 than Abeta40. Distance measurement between Tyr10 and Met35 in amyloid beta by site-directed spin-labeling ESR spectroscopy: implications for the stronger neurotoxicity of Abeta42 than Abeta40. Distance measurement between Tyr10 and Met35 in amyloid beta by site-directed spin-labeling ESR spectroscopy: implications for the stronger neurotoxicity of Abeta42 than Abeta40. Chembiochem : a European journal of chemical biology,8,18,2308-2314 Chembiochem : a European journal of chemical biology,8,18,2308-2314 Chembiochem : a European journal of chemical biology,8,18,2308-2314 2007/12 Refereed Disclose to all
Murakami, K., Hara, H., Masuda, Y., Ohigashi, H., and *Irie, K. Murakami, K., Hara, H., Masuda, Y., Ohigashi, H., and *Irie, K. Murakami, K., Hara, H., Masuda, Y., Ohigashi, H., and *Irie, K. Distance measurement between Tyr10 and Met35 in amyloid β by site-directed spin-labeling ESR spectroscopy: implications for the stronger neurotoxicity of Aβ42 than Aβ40. Distance measurement between Tyr10 and Met35 in amyloid β by site-directed spin-labeling ESR spectroscopy: implications for the stronger neurotoxicity of Aβ42 than Aβ40. Distance measurement between Tyr10 and Met35 in amyloid β by site-directed spin-labeling ESR spectroscopy: implications for the stronger neurotoxicity of Aβ42 than Aβ40. ChemBioChem 8 (18), 2308-2314 (2007). ChemBioChem 8 (18), 2308-2314 (2007). ChemBioChem 8 (18), 2308-2314 (2007). 2007 Refereed English Research paper(scientific journal) Disclose to all
Masuda Y, Irie K, Murakami K, Ohigashi H, Ohashi R, Takegoshi K, Shimizu T, Shirasawa T Masuda Y, Irie K, Murakami K, Ohigashi H, Ohashi R, Takegoshi K, Shimizu T, Shirasawa T Masuda Y, Irie K, Murakami K, Ohigashi H, Ohashi R, Takegoshi K, Shimizu T, Shirasawa T Verification of the turn at positions 22 and 23 of the beta-amyloid fibrils with Italian mutation using solid-state NMR. Verification of the turn at positions 22 and 23 of the beta-amyloid fibrils with Italian mutation using solid-state NMR. Verification of the turn at positions 22 and 23 of the beta-amyloid fibrils with Italian mutation using solid-state NMR. Bioorganic & medicinal chemistry,13,24,6803-6809 Bioorganic & medicinal chemistry,13,24,6803-6809 Bioorganic & medicinal chemistry,13,24,6803-6809 2005/12 Refereed Disclose to all
Murakami K, Irie K, Ohigashi H, Hara H, Nagao M, Shimizu T, Shirasawa T Murakami K, Irie K, Ohigashi H, Hara H, Nagao M, Shimizu T, Shirasawa T Murakami K, Irie K, Ohigashi H, Hara H, Nagao M, Shimizu T, Shirasawa T Formation and stabilization model of the 42-mer Abeta radical: implications for the long-lasting oxidative stress in Alzheimer's disease. Formation and stabilization model of the 42-mer Abeta radical: implications for the long-lasting oxidative stress in Alzheimer's disease. Formation and stabilization model of the 42-mer Abeta radical: implications for the long-lasting oxidative stress in Alzheimer's disease. Journal of the American Chemical Society,127,43,15168-15174 Journal of the American Chemical Society,127,43,15168-15174 Journal of the American Chemical Society,127,43,15168-15174 2005/11 Refereed Disclose to all
Irie K, Murakami K, Masuda Y, Morimoto A, Ohigashi H, Ohashi R, Takegoshi K, Nagao M, Shimizu T, Shirasawa T Irie K, Murakami K, Masuda Y, Morimoto A, Ohigashi H, Ohashi R, Takegoshi K, Nagao M, Shimizu T, Shirasawa T Irie K, Murakami K, Masuda Y, Morimoto A, Ohigashi H, Ohashi R, Takegoshi K, Nagao M, Shimizu T, Shirasawa T Structure of beta-amyloid fibrils and its relevance to their neurotoxicity: implications for the pathogenesis of Alzheimer's disease. Structure of beta-amyloid fibrils and its relevance to their neurotoxicity: implications for the pathogenesis of Alzheimer's disease. Structure of beta-amyloid fibrils and its relevance to their neurotoxicity: implications for the pathogenesis of Alzheimer's disease. Journal of bioscience and bioengineering,99,5,437-447 Journal of bioscience and bioengineering,99,5,437-447 Journal of bioscience and bioengineering,99,5,437-447 2005/05 Refereed Disclose to all
Masuda, Y., *Irie, K., Murakami, K., Ohigashi, H., Ohashi, R., Takegoshi, K., Shimizu, T., and Shirasawa, T. Masuda, Y., *Irie, K., Murakami, K., Ohigashi, H., Ohashi, R., Takegoshi, K., Shimizu, T., and Shirasawa, T. Masuda, Y., *Irie, K., Murakami, K., Ohigashi, H., Ohashi, R., Takegoshi, K., Shimizu, T., and Shirasawa, T. Verification of the turn at positions 22 and 23 of the β-amyloid fibrils with Italian mutation using solid-state NMR. Verification of the turn at positions 22 and 23 of the β-amyloid fibrils with Italian mutation using solid-state NMR. Verification of the turn at positions 22 and 23 of the β-amyloid fibrils with Italian mutation using solid-state NMR. Bioorg. Med. Chem. 13 (24), 6803-6809 (2005). Bioorg. Med. Chem. 13 (24), 6803-6809 (2005). Bioorg. Med. Chem. 13 (24), 6803-6809 (2005). 2005 Refereed English Research paper(scientific journal) Disclose to all
Murakami, K., *Irie, K., Ohigashi, H., Hara, H., Nagao, M., Shimizu, T., and Shirasawa, T. Murakami, K., *Irie, K., Ohigashi, H., Hara, H., Nagao, M., Shimizu, T., and Shirasawa, T. Murakami, K., *Irie, K., Ohigashi, H., Hara, H., Nagao, M., Shimizu, T., and Shirasawa, T. Formation and stabilization model of the 42-mer Aβ radical: implications for the long-lasting oxidative stress in Alzheimer’s disease. Formation and stabilization model of the 42-mer Aβ radical: implications for the long-lasting oxidative stress in Alzheimer’s disease. Formation and stabilization model of the 42-mer Aβ radical: implications for the long-lasting oxidative stress in Alzheimer’s disease. J. Am. Chem. Soc. 127 (43), 15168-15174 (2005). J. Am. Chem. Soc. 127 (43), 15168-15174 (2005). J. Am. Chem. Soc. 127 (43), 15168-15174 (2005). 2005 Refereed English Research paper(scientific journal) Disclose to all
Morimoto A, Irie K, Murakami K, Masuda Y, Ohigashi H, Nagao M, Fukuda H, Shimizu T, Shirasawa T Morimoto A, Irie K, Murakami K, Masuda Y, Ohigashi H, Nagao M, Fukuda H, Shimizu T, Shirasawa T Morimoto A, Irie K, Murakami K, Masuda Y, Ohigashi H, Nagao M, Fukuda H, Shimizu T, Shirasawa T Analysis of the secondary structure of beta-amyloid (Abeta42) fibrils by systematic proline replacement. Analysis of the secondary structure of beta-amyloid (Abeta42) fibrils by systematic proline replacement. Analysis of the secondary structure of beta-amyloid (Abeta42) fibrils by systematic proline replacement. The Journal of biological chemistry,279,50,52781-52788 The Journal of biological chemistry,279,50,52781-52788 The Journal of biological chemistry,279,50,52781-52788 2004/12 Refereed Disclose to all
Morimoto, A., *Irie, K., Murakami, K., Masuda, Y., Ohigashi, H., Nagao, M., Fukuda, H., Shimizu, T., and Shirasawa, T. Morimoto, A., *Irie, K., Murakami, K., Masuda, Y., Ohigashi, H., Nagao, M., Fukuda, H., Shimizu, T., and Shirasawa, T. Morimoto, A., *Irie, K., Murakami, K., Masuda, Y., Ohigashi, H., Nagao, M., Fukuda, H., Shimizu, T., and Shirasawa, T. Analysis of the secondary structure of β-amyloid (Aβ42) fibrils by systematic proline replacement. Analysis of the secondary structure of β-amyloid (Aβ42) fibrils by systematic proline replacement. Analysis of the secondary structure of β-amyloid (Aβ42) fibrils by systematic proline replacement. J. Biol. Chem. 279 (50), 52781-52788 (2004). J. Biol. Chem. 279 (50), 52781-52788 (2004). J. Biol. Chem. 279 (50), 52781-52788 (2004). 2004 Refereed English Research paper(scientific journal) Disclose to all
Murakami K, Irie K, Morimoto A, Ohigashi H, Shindo M, Nagao M, Shimizu T, Shirasawa T Murakami K, Irie K, Morimoto A, Ohigashi H, Shindo M, Nagao M, Shimizu T, Shirasawa T Murakami K, Irie K, Morimoto A, Ohigashi H, Shindo M, Nagao M, Shimizu T, Shirasawa T Neurotoxicity and physicochemical properties of Abeta mutant peptides from cerebral amyloid angiopathy: implication for the pathogenesis of cerebral amyloid angiopathy and Alzheimer's disease. Neurotoxicity and physicochemical properties of Abeta mutant peptides from cerebral amyloid angiopathy: implication for the pathogenesis of cerebral amyloid angiopathy and Alzheimer's disease. Neurotoxicity and physicochemical properties of Abeta mutant peptides from cerebral amyloid angiopathy: implication for the pathogenesis of cerebral amyloid angiopathy and Alzheimer's disease. The Journal of biological chemistry,278,46,46179-46187 The Journal of biological chemistry,278,46,46179-46187 The Journal of biological chemistry,278,46,46179-46187 2003/11 Refereed Disclose to all
Murakami, K., *Irie, K., Morimoto, A., Ohigashi, H., Shindo, M., Nagao, M., Shimizu, T., and Shirasawa, T. Murakami, K., *Irie, K., Morimoto, A., Ohigashi, H., Shindo, M., Nagao, M., Shimizu, T., and Shirasawa, T. Murakami, K., *Irie, K., Morimoto, A., Ohigashi, H., Shindo, M., Nagao, M., Shimizu, T., and Shirasawa, T. Neurotoxicity and physicochemical properties of Aβ mutant peptides from cerebral amyloid angiopathy: implication for the pathogenesis of cerebral amyloid angiopathy and Alzheimer’s disease. Neurotoxicity and physicochemical properties of Aβ mutant peptides from cerebral amyloid angiopathy: implication for the pathogenesis of cerebral amyloid angiopathy and Alzheimer’s disease. Neurotoxicity and physicochemical properties of Aβ mutant peptides from cerebral amyloid angiopathy: implication for the pathogenesis of cerebral amyloid angiopathy and Alzheimer’s disease. J. Biol. Chem. 278 (46), 46179-46187 (2003). J. Biol. Chem. 278 (46), 46179-46187 (2003). J. Biol. Chem. 278 (46), 46179-46187 (2003). 2003 Refereed English Research paper(scientific journal) Disclose to all
Morimoto A, Irie K, Murakami K, Ohigashi H, Shindo M, Nagao M, Shimizu T, Shirasawa T Morimoto A, Irie K, Murakami K, Ohigashi H, Shindo M, Nagao M, Shimizu T, Shirasawa T Morimoto A, Irie K, Murakami K, Ohigashi H, Shindo M, Nagao M, Shimizu T, Shirasawa T Aggregation and neurotoxicity of mutant amyloid beta (A beta) peptides with proline replacement: importance of turn formation at positions 22 and 23. Aggregation and neurotoxicity of mutant amyloid beta (A beta) peptides with proline replacement: importance of turn formation at positions 22 and 23. Aggregation and neurotoxicity of mutant amyloid beta (A beta) peptides with proline replacement: importance of turn formation at positions 22 and 23. Biochemical and biophysical research communications,295,2,306-311 Biochemical and biophysical research communications,295,2,306-311 Biochemical and biophysical research communications,295,2,306-311 2002/07 Refereed Disclose to all
Murakami K, Irie K, Morimoto A, Ohigashi H, Shindo M, Nagao M, Shimizu T, Shirasawa T Murakami K, Irie K, Morimoto A, Ohigashi H, Shindo M, Nagao M, Shimizu T, Shirasawa T Murakami K, Irie K, Morimoto A, Ohigashi H, Shindo M, Nagao M, Shimizu T, Shirasawa T Synthesis, aggregation, neurotoxicity, and secondary structure of various A beta 1-42 mutants of familial Alzheimer's disease at positions 21-23. Synthesis, aggregation, neurotoxicity, and secondary structure of various A beta 1-42 mutants of familial Alzheimer's disease at positions 21-23. Synthesis, aggregation, neurotoxicity, and secondary structure of various A beta 1-42 mutants of familial Alzheimer's disease at positions 21-23. Biochemical and biophysical research communications,294,1,5-10 Biochemical and biophysical research communications,294,1,5-10 Biochemical and biophysical research communications,294,1,5-10 2002/05 Refereed Disclose to all
Murakami, K., *Irie, K., Morimoto, A., Ohigashi, H., Shindo, M., Nagao, M., Shimizu, T., and Shirasawa, T. Murakami, K., *Irie, K., Morimoto, A., Ohigashi, H., Shindo, M., Nagao, M., Shimizu, T., and Shirasawa, T. Murakami, K., *Irie, K., Morimoto, A., Ohigashi, H., Shindo, M., Nagao, M., Shimizu, T., and Shirasawa, T. Synthesis, aggregation, neurotoxicity, and secondary structure of various Aβ1-42 mutants of familial Alzheimer’s disease at positions 21-23. Synthesis, aggregation, neurotoxicity, and secondary structure of various Aβ1-42 mutants of familial Alzheimer’s disease at positions 21-23. Synthesis, aggregation, neurotoxicity, and secondary structure of various Aβ1-42 mutants of familial Alzheimer’s disease at positions 21-23. Biochem. Biophys. Res. Commun. 294 (1), 5-10 (2002). Biochem. Biophys. Res. Commun. 294 (1), 5-10 (2002). Biochem. Biophys. Res. Commun. 294 (1), 5-10 (2002). 2002 Refereed English Research paper(scientific journal) Disclose to all
Morimoto, A., *Irie, K., Murakami, K., Ohigashi, H., Shindo, M., Nagao, M., Shimizu, T., and Shirasawa, T. Morimoto, A., *Irie, K., Murakami, K., Ohigashi, H., Shindo, M., Nagao, M., Shimizu, T., and Shirasawa, T. Morimoto, A., *Irie, K., Murakami, K., Ohigashi, H., Shindo, M., Nagao, M., Shimizu, T., and Shirasawa, T. Aggregation and neurotoxicity of mutant amyloid β (Aβ) peptides with proline replacement: importance of turn formation at positions 22 and 23. Aggregation and neurotoxicity of mutant amyloid β (Aβ) peptides with proline replacement: importance of turn formation at positions 22 and 23. Aggregation and neurotoxicity of mutant amyloid β (Aβ) peptides with proline replacement: importance of turn formation at positions 22 and 23. Biochem. Biophys. Res. Commun. 295 (2), 306-311 (2002). Biochem. Biophys. Res. Commun. 295 (2), 306-311 (2002). Biochem. Biophys. Res. Commun. 295 (2), 306-311 (2002). 2002 Refereed English Research paper(scientific journal) Disclose to all

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村上一馬、佐藤瑞穂、井久保遥子、宇野真弓、中川 優、片山寿美枝、赤木謙一、増田裕一、竹腰清乃理、入江一浩 村上一馬、佐藤瑞穂、井久保遥子、宇野真弓、中川 優、片山寿美枝、赤木謙一、増田裕一、竹腰清乃理、入江一浩 カテコール系フラボノイド類によるアミロイド β の凝集抑制機構 カテコール系フラボノイド類によるアミロイド β の凝集抑制機構 第54回天然有機化合物討論会 第54回天然有機化合物討論会 2012/09 Refereed Japanese Disclose to all
Murakami, K., Murata, N., Noda, Y., Tahara, S., Kaneko, T., Kinoshita, N., Hatsuta, H., Murayama, S., Barnham, Kevin J., Irie, K., Shirasawa, T., and Shimizu, T. Murakami, K., Murata, N., Noda, Y., Tahara, S., Kaneko, T., Kinoshita, N., Hatsuta, H., Murayama, S., Barnham, Kevin J., Irie, K., Shirasawa, T., and Shimizu, T. Murakami, K., Murata, N., Noda, Y., Tahara, S., Kaneko, T., Kinoshita, N., Hatsuta, H., Murayama, S., Barnham, Kevin J., Irie, K., Shirasawa, T., and Shimizu, T. CuZn-SOD loss accelerates the formation of amyloid β oligomer and memory impairment in Tg2576 mice CuZn-SOD loss accelerates the formation of amyloid β oligomer and memory impairment in Tg2576 mice CuZn-SOD loss accelerates the formation of amyloid β oligomer and memory impairment in Tg2576 mice Alzheimer’s Association International Conference, Vancouver, Canada Alzheimer’s Association International Conference, Vancouver, Canada Alzheimer’s Association International Conference, Vancouver, Canada 2012/07 Refereed English Disclose to all
Irie, K., Murakami, K., Kinoshita, N., Shirasawa, T., Shimizu, T., and Tokuda, T. Irie, K., Murakami, K., Kinoshita, N., Shirasawa, T., Shimizu, T., and Tokuda, T. Irie, K., Murakami, K., Kinoshita, N., Shirasawa, T., Shimizu, T., and Tokuda, T. Monoclonal antibody against a toxic conformer of Aβ42 with a turn at E22-D23. Monoclonal antibody against a toxic conformer of Aβ42 with a turn at E22-D23. Monoclonal antibody against a toxic conformer of Aβ42 with a turn at E22-D23. Alzheimer’s Association International Conference 2012, Vancouver, Canada Alzheimer’s Association International Conference 2012, Vancouver, Canada Alzheimer’s Association International Conference 2012, Vancouver, Canada 2012/07 Refereed English Disclose to all
村上一馬 村上一馬 アミロイド β ペプチドの毒性ターン構造の同定とその構造特異抗体の開発 アミロイド β ペプチドの毒性ターン構造の同定とその構造特異抗体の開発 第47回天然物化学談話会, 熊本 第47回天然物化学談話会, 熊本 2012/07 Refereed Japanese Disclose to all
村上一馬,村田 央,野田義博,田原正一,金子孝夫,木下憲明,初田裕幸,村山繁雄,入江一浩,白澤卓二,清水孝彦 村上一馬,村田 央,野田義博,田原正一,金子孝夫,木下憲明,初田裕幸,村山繁雄,入江一浩,白澤卓二,清水孝彦 細胞質酸化ストレスによるアミロイド β オリゴマー形成能および記憶異常の促進 細胞質酸化ストレスによるアミロイド β オリゴマー形成能および記憶異常の促進 日本農芸化学会2012年度大会, 京都 日本農芸化学会2012年度大会, 京都 2012/03 Refereed Japanese Disclose to all
Shirasawa, T., Murakami, K., Yokoyama, S., Murata, N., Ozawa, Y., Irie, K., and Shimizu, T. Shirasawa, T., Murakami, K., Yokoyama, S., Murata, N., Ozawa, Y., Irie, K., and Shimizu, T. Shirasawa, T., Murakami, K., Yokoyama, S., Murata, N., Ozawa, Y., Irie, K., and Shimizu, T. Insulin receptor mutation results in insulin resistance and hyperinsulinemia but does not exacerbate Alzheimer’s-like phenotypes in mice. Insulin receptor mutation results in insulin resistance and hyperinsulinemia but does not exacerbate Alzheimer’s-like phenotypes in mice. Insulin receptor mutation results in insulin resistance and hyperinsulinemia but does not exacerbate Alzheimer’s-like phenotypes in mice. 41st Annual Meeting of Society for Neuroscience, Washington DC, USA 41st Annual Meeting of Society for Neuroscience, Washington DC, USA 41st Annual Meeting of Society for Neuroscience, Washington DC, USA 2011/11 Refereed English Disclose to all
Shimizu, T., Murakami, K., Murata, N., Ozawa, Y., Irie, K., and Shirasawa, T. Shimizu, T., Murakami, K., Murata, N., Ozawa, Y., Irie, K., and Shirasawa, T. Shimizu, T., Murakami, K., Murata, N., Ozawa, Y., Irie, K., and Shirasawa, T. Silymarin attenuated the amyloid β deposition and improved behavioral abnormalities in a mouse model of Alzheimer’s disease. Silymarin attenuated the amyloid β deposition and improved behavioral abnormalities in a mouse model of Alzheimer’s disease. Silymarin attenuated the amyloid β deposition and improved behavioral abnormalities in a mouse model of Alzheimer’s disease. 41st Annual Meeting of Society for Neuroscience, Washington DC, USA 41st Annual Meeting of Society for Neuroscience, Washington DC, USA 41st Annual Meeting of Society for Neuroscience, Washington DC, USA 2011/11 Refereed English Disclose to all
村上一馬,鈴木啓之,泉尾直孝,久米利明,赤池昭紀,永田 徹,西崎知之,富山貴美,森 啓,入江一浩 村上一馬,鈴木啓之,泉尾直孝,久米利明,赤池昭紀,永田 徹,西崎知之,富山貴美,森 啓,入江一浩 大阪変異によるアミロイド β の毒性コンホマー形成能の増大. 大阪変異によるアミロイド β の毒性コンホマー形成能の増大. 第30回日本認知症学会学術集会, 東京. 第30回日本認知症学会学術集会, 東京. 2011/11 Refereed Japanese Disclose to all
Murakami, K., Horikoshi-Sakuraba, Y., Kinoshita, N., Shirasawa, T., Shimizu, T., and Irie, K. Murakami, K., Horikoshi-Sakuraba, Y., Kinoshita, N., Shirasawa, T., Shimizu, T., and Irie, K. Murakami, K., Horikoshi-Sakuraba, Y., Kinoshita, N., Shirasawa, T., Shimizu, T., and Irie, K. Antibody against toxic conformer of Alzheimer β. Antibody against toxic conformer of Alzheimer β. Antibody against toxic conformer of Alzheimer β. 22nd French-Japanese Symposium on Medicinal and Fine Chemistry, Rouen, France 22nd French-Japanese Symposium on Medicinal and Fine Chemistry, Rouen, France 22nd French-Japanese Symposium on Medicinal and Fine Chemistry, Rouen, France 2011/09 Refereed English Disclose to all
Murakami, K., Suzuki, T., Yamaguchi, T., Izuo, N., Kume, T., Akaike, A., Nagata, T., Nishizaki, T., Tomiyama, T., Takuma, H., Mori, H., and Irie, K. Murakami, K., Suzuki, T., Yamaguchi, T., Izuo, N., Kume, T., Akaike, A., Nagata, T., Nishizaki, T., Tomiyama, T., Takuma, H., Mori, H., and Irie, K. Murakami, K., Suzuki, T., Yamaguchi, T., Izuo, N., Kume, T., Akaike, A., Nagata, T., Nishizaki, T., Tomiyama, T., Takuma, H., Mori, H., and Irie, K. E22Δ mutation promotes the oformation of toxic conformer in Alzheimer’s peptide, Aβ42. E22Δ mutation promotes the oformation of toxic conformer in Alzheimer’s peptide, Aβ42. E22Δ mutation promotes the oformation of toxic conformer in Alzheimer’s peptide, Aβ42. 27th International Symposium on the Chemistry of Natural Products (ISCNP27)/7th International Conference on Biodiversity (ICOB7), Brisbane, Australia 27th International Symposium on the Chemistry of Natural Products (ISCNP27)/7th International Conference on Biodiversity (ICOB7), Brisbane, Australia 27th International Symposium on the Chemistry of Natural Products (ISCNP27)/7th International Conference on Biodiversity (ICOB7), Brisbane, Australia 2011/07 Refereed English Disclose to all
Sato, M., Murakami, K., Ikubo, H., Masuda, Y., Takegoshi, K., and Irie, K. Sato, M., Murakami, K., Ikubo, H., Masuda, Y., Takegoshi, K., and Irie, K. Sato, M., Murakami, K., Ikubo, H., Masuda, Y., Takegoshi, K., and Irie, K. Inhibitory mechanism of amyloid β aggregation by flavonoids. Inhibitory mechanism of amyloid β aggregation by flavonoids. Inhibitory mechanism of amyloid β aggregation by flavonoids. 27th International Symposium on the Chemistry of Natural Products (ISCNP27)/7th International Conference on Biodiversity (ICOB7), Brisbane, Australia 27th International Symposium on the Chemistry of Natural Products (ISCNP27)/7th International Conference on Biodiversity (ICOB7), Brisbane, Australia 27th International Symposium on the Chemistry of Natural Products (ISCNP27)/7th International Conference on Biodiversity (ICOB7), Brisbane, Australia 2011/07 Refereed English Disclose to all
村上一馬,鈴木啓之,泉尾直孝,久米利明,赤池昭紀,永田 徹,西崎知之,富山貴美,森 啓,入江一浩 村上一馬,鈴木啓之,泉尾直孝,久米利明,赤池昭紀,永田 徹,西崎知之,富山貴美,森 啓,入江一浩 アミロイド β のGlu22欠損による毒性コンホマー形成能の促進 アミロイド β のGlu22欠損による毒性コンホマー形成能の促進 日本農芸化学会2011年度大会, 京都 日本農芸化学会2011年度大会, 京都 2011/03 Refereed Japanese Disclose to all
Murakami, K., Horikoshi-Sakuraba, Y., Murata, N., Noda, Y., Masuda, Y., Kinoshita, N., Hatsuta, H., Murayama, S., Shirasawa, T., Shimizu, T., and Irie, K. Murakami, K., Horikoshi-Sakuraba, Y., Murata, N., Noda, Y., Masuda, Y., Kinoshita, N., Hatsuta, H., Murayama, S., Shirasawa, T., Shimizu, T., and Irie, K. Murakami, K., Horikoshi-Sakuraba, Y., Murata, N., Noda, Y., Masuda, Y., Kinoshita, N., Hatsuta, H., Murayama, S., Shirasawa, T., Shimizu, T., and Irie, K. Monoclonal antibody against the toxic turn structure of the 42-mer amyloid β peptide. Monoclonal antibody against the toxic turn structure of the 42-mer amyloid β peptide. Monoclonal antibody against the toxic turn structure of the 42-mer amyloid β peptide. The 2010 International Chemical Congress of Pacific Basin Societies, Honolulu HI, USA The 2010 International Chemical Congress of Pacific Basin Societies, Honolulu HI, USA The 2010 International Chemical Congress of Pacific Basin Societies, Honolulu HI, USA 2010/12 Refereed English Disclose to all
村上一馬,堀越優子,村田 央,野田義博,増田裕一,木下憲明,初田裕幸,村山繁雄,白澤卓二,清水孝彦,入江一浩 村上一馬,堀越優子,村田 央,野田義博,増田裕一,木下憲明,初田裕幸,村山繁雄,白澤卓二,清水孝彦,入江一浩 アミロイド β の毒性ターン構造特異的抗体. アミロイド β の毒性ターン構造特異的抗体. 第29回日本認知症学会学術集会, 名古屋 第29回日本認知症学会学術集会, 名古屋 2010/11 Refereed Japanese Disclose to all
村上一馬,村田 央,小澤裕介,木下憲明,入江一浩,白澤卓二,清水孝彦 村上一馬,村田 央,小澤裕介,木下憲明,入江一浩,白澤卓二,清水孝彦 SilymarinによるADモデルマウスの行動異常及びAβ オリゴマー形成の改善. SilymarinによるADモデルマウスの行動異常及びAβ オリゴマー形成の改善. 日本農芸化学会2010年度関西支部大会, 大阪 日本農芸化学会2010年度関西支部大会, 大阪 2010/10 Refereed Japanese Disclose to all
村上一馬,堀越優子,村田 央,野田義博,増田裕一,木下憲明,初田裕幸,村山繁雄,白澤卓二,清水孝彦,入江一浩 村上一馬,堀越優子,村田 央,野田義博,増田裕一,木下憲明,初田裕幸,村山繁雄,白澤卓二,清水孝彦,入江一浩 アミロイド β(Αβ42)の毒性コンホマー特異的抗体の作製 アミロイド β(Αβ42)の毒性コンホマー特異的抗体の作製 第52回天然有機化合物討論会, 静岡 第52回天然有機化合物討論会, 静岡 2010/09 Refereed Japanese Disclose to all
村上一馬,堀越優子,村田 央,野田義博,増田裕一,木下憲明,初田裕幸,村山繁雄,白澤卓二,清水孝彦,入江一浩 村上一馬,堀越優子,村田 央,野田義博,増田裕一,木下憲明,初田裕幸,村山繁雄,白澤卓二,清水孝彦,入江一浩 アミロイド β の毒性コンホマーを標的とした立体構造特異的抗体. アミロイド β の毒性コンホマーを標的とした立体構造特異的抗体. 日本農芸化学会2010年度大会, 東京 日本農芸化学会2010年度大会, 東京 2010/03 Refereed Japanese Disclose to all
村田 央、村上一馬、横山慎也、入江一浩、白澤卓二、清水孝彦 村田 央、村上一馬、横山慎也、入江一浩、白澤卓二、清水孝彦 Silyamarin inhibits neurotoxicity and aggregation of the 42-mer amyloid-β peptide. Silyamarin inhibits neurotoxicity and aggregation of the 42-mer amyloid-β peptide. 第32回日本分子生物学会年会, 横浜 第32回日本分子生物学会年会, 横浜 2009/12 Refereed Japanese Disclose to all
Rahimi, F., Murakami, K., Summers, J. L., Chen, C. B., and Bitan, G. Rahimi, F., Murakami, K., Summers, J. L., Chen, C. B., and Bitan, G. Aptamers generated against oligomeric Aβ40 recognize common amyloid aptatopes with high sensitivity. Aptamers generated against oligomeric Aβ40 recognize common amyloid aptatopes with high sensitivity. 39th Annual Meeting of Society for Neuroscience, Chicago, IL, USA 39th Annual Meeting of Society for Neuroscience, Chicago, IL, USA 2009/10 Refereed Japanese Disclose to all
清水孝彦、村上一馬、稲垣 潤、斎藤 充、池田泰隆、津田千鶴、野田義博、川上 哲、白澤卓二 清水孝彦、村上一馬、稲垣 潤、斎藤 充、池田泰隆、津田千鶴、野田義博、川上 哲、白澤卓二 CuZn-SOD欠損マウスにおける皮膚の菲薄化およびコラーゲン形成異常. CuZn-SOD欠損マウスにおける皮膚の菲薄化およびコラーゲン形成異常. 第32回日本基礎老化学会年会, 横浜 第32回日本基礎老化学会年会, 横浜 2009/06 Refereed Japanese Disclose to all
清水孝彦、村上一馬、稲垣 潤、斎藤 充、池田泰隆、津田千鶴、野田義博、川上 哲、白澤卓二 清水孝彦、村上一馬、稲垣 潤、斎藤 充、池田泰隆、津田千鶴、野田義博、川上 哲、白澤卓二 細胞質SOD欠損マウスにおける皮膚の菲薄化. 細胞質SOD欠損マウスにおける皮膚の菲薄化. 第9回日本抗加齢医学会総会 第9回日本抗加齢医学会総会 2009/05 Refereed Japanese Disclose to all
村上一馬、宇野真弓、増田裕一、清水孝彦、白澤卓二、入江一浩 村上一馬、宇野真弓、増田裕一、清水孝彦、白澤卓二、入江一浩 アミロイドβのAsp23における異性化あるいはラセミ化が凝集能および神経細胞毒性に及ぼす影響 アミロイドβのAsp23における異性化あるいはラセミ化が凝集能および神経細胞毒性に及ぼす影響 日本農芸化学会年2009年度大会, 福岡 日本農芸化学会年2009年度大会, 福岡 2009/03 Refereed Japanese Disclose to all
Murakami, K., Uno, M., Masuda, Y., Shimizu, T., Shirasawa, T., and Irie, K. Murakami, K., Uno, M., Masuda, Y., Shimizu, T., Shirasawa, T., and Irie, K. Murakami, K., Uno, M., Masuda, Y., Shimizu, T., Shirasawa, T., and Irie, K. Isomerization and/or racemization at Asp23 of Aβ42 do not enhance its aggregation, neurotoxicity, and radical productivity in vitro. Isomerization and/or racemization at Asp23 of Aβ42 do not enhance its aggregation, neurotoxicity, and radical productivity in vitro. Isomerization and/or racemization at Asp23 of Aβ42 do not enhance its aggregation, neurotoxicity, and radical productivity in vitro. 38th Annual Meeting of Society for Neuroscience, Washington D. C., USA 38th Annual Meeting of Society for Neuroscience, Washington D. C., USA 38th Annual Meeting of Society for Neuroscience, Washington D. C., USA 2008/11 Refereed English Disclose to all
入江一浩、村上一馬、増田裕一、上村諭子、原 英之、中西 梓、大橋竜太郎、竹腰清乃理 入江一浩、村上一馬、増田裕一、上村諭子、原 英之、中西 梓、大橋竜太郎、竹腰清乃理 β アミロイドの毒性コンホメーションのESRならびに固体NMRによる検証. β アミロイドの毒性コンホメーションのESRならびに固体NMRによる検証. 第27回日本認知症学会, 前橋 第27回日本認知症学会, 前橋 2008/10 Refereed Japanese Disclose to all
Summers, J. L., Rahimi, F, Murakami, K., and Bitan, G. Summers, J. L., Rahimi, F, Murakami, K., and Bitan, G. Aptamers selected against monomeric Aβ40 recognize other amyloid proteins. Aptamers selected against monomeric Aβ40 recognize other amyloid proteins. 22nd Annual Symposium of the Protein Society, San Diego, USA 22nd Annual Symposium of the Protein Society, San Diego, USA 2008/07 Refereed Japanese Disclose to all
村上一馬、増田裕一、森本 晃、宇野真弓、原 英之、清水孝彦、白澤卓二、入江一浩 村上一馬、増田裕一、森本 晃、宇野真弓、原 英之、清水孝彦、白澤卓二、入江一浩 アミロイド β ペプチド (Aβ42) の病的コンホメーションの提唱 アミロイド β ペプチド (Aβ42) の病的コンホメーションの提唱 第31回日本基礎老化学会, 松本 第31回日本基礎老化学会, 松本 2008/06 Refereed Japanese Disclose to all
清水孝彦、村上一馬、宇野真弓、入江一浩、白澤卓二: 清水孝彦、村上一馬、宇野真弓、入江一浩、白澤卓二: アミロイドβペプチドのターン構造形成とアスパラギン酸残基修飾 アミロイドβペプチドのターン構造形成とアスパラギン酸残基修飾 第80回日本生化学会大会ワークショップ 第80回日本生化学会大会ワークショップ 2007/12 Refereed Japanese Disclose to all
Murakami, K., Hara, H., and Irie, K. Murakami, K., Hara, H., and Irie, K. Murakami, K., Hara, H., and Irie, K. Distance analysis between Tyr-10 and Met-35 in amyloid β using site-directed spin labeling ESR: implications for the stronger neurotoxicity of Aβ42 than Aβ40. Distance analysis between Tyr-10 and Met-35 in amyloid β using site-directed spin labeling ESR: implications for the stronger neurotoxicity of Aβ42 than Aβ40. Distance analysis between Tyr-10 and Met-35 in amyloid β using site-directed spin labeling ESR: implications for the stronger neurotoxicity of Aβ42 than Aβ40. 37th Annual Meeting of Society for Neuroscience, San Diego, CA, USA 37th Annual Meeting of Society for Neuroscience, San Diego, CA, USA 37th Annual Meeting of Society for Neuroscience, San Diego, CA, USA 2007/11 Refereed English Disclose to all
入江一浩、○増田裕一、村上一馬、上村諭子、原 英之、大橋竜太郎、中西 梓、竹腰清乃理 入江一浩、○増田裕一、村上一馬、上村諭子、原 英之、大橋竜太郎、中西 梓、竹腰清乃理 固体NMRならびにESRによるアミロイド β (Aβ42) の毒性コンホメーションの解析. 固体NMRならびにESRによるアミロイド β (Aβ42) の毒性コンホメーションの解析. 第 49回天然有機化合物討論会, 北海道 第 49回天然有機化合物討論会, 北海道 2007/09 Refereed Japanese Disclose to all
村上一馬 他 村上一馬 他 ラジカル産生を介した β アミロイドの神経細胞毒性発現機構. ラジカル産生を介した β アミロイドの神経細胞毒性発現機構. 日本農芸化学会 2007年度大会, 東京 日本農芸化学会 2007年度大会, 東京 2007/03 Refereed Japanese Disclose to all
Murakami, K., Irie, K., Ohigashi, H., Hara, H., Nagao, M., Shimizu, T., and Shirasawa, T. Murakami, K., Irie, K., Ohigashi, H., Hara, H., Nagao, M., Shimizu, T., and Shirasawa, T. Murakami, K., Irie, K., Ohigashi, H., Hara, H., Nagao, M., Shimizu, T., and Shirasawa, T. ‘Malignant’ conformation of Alzheimer’s β peptides (Aβ42) through radical formation. ‘Malignant’ conformation of Alzheimer’s β peptides (Aβ42) through radical formation. ‘Malignant’ conformation of Alzheimer’s β peptides (Aβ42) through radical formation. International Conference of 43rd Japanese Peptide Symposium, Yokohama, Japan International Conference of 43rd Japanese Peptide Symposium, Yokohama, Japan International Conference of 43rd Japanese Peptide Symposium, Yokohama, Japan 2006/11 Refereed English Disclose to all
Murakami, K., Irie, K., Ohigashi, H., Hara, H., Nagao, M., Shimizu, T., and Shirasawa, T.: Murakami, K., Irie, K., Ohigashi, H., Hara, H., Nagao, M., Shimizu, T., and Shirasawa, T.: Murakami, K., Irie, K., Ohigashi, H., Hara, H., Nagao, M., Shimizu, T., and Shirasawa, T.: Formation and stabilization mechanism of the β-amyloid radical. Formation and stabilization mechanism of the β-amyloid radical. Formation and stabilization mechanism of the β-amyloid radical. ICOB-5 & ISCNP-25 IUPAC International Conference on Biodiversity and Natural Products ICOB-5 & ISCNP-25 IUPAC International Conference on Biodiversity and Natural Products ICOB-5 & ISCNP-25 IUPAC International Conference on Biodiversity and Natural Products 2006/07 Refereed English Disclose to all
Masuda, Y., Irie, K., Murakami, K., Ohigashi, H., Ohashi, R., Takegoshi, K. Masuda, Y., Irie, K., Murakami, K., Ohigashi, H., Ohashi, R., Takegoshi, K. Masuda, Y., Irie, K., Murakami, K., Ohigashi, H., Ohashi, R., Takegoshi, K. Elucidation of the ‘malignant’ conformation of β-amyloid with Italian mutation (E22K-Aβ42) using solid-state NMR. Elucidation of the ‘malignant’ conformation of β-amyloid with Italian mutation (E22K-Aβ42) using solid-state NMR. Elucidation of the ‘malignant’ conformation of β-amyloid with Italian mutation (E22K-Aβ42) using solid-state NMR. ICOB-5 & ISCNP-25 IUPAC International Conference on Biodiversity and Natural Products, Kyoto, Japan ICOB-5 & ISCNP-25 IUPAC International Conference on Biodiversity and Natural Products, Kyoto, Japan ICOB-5 & ISCNP-25 IUPAC International Conference on Biodiversity and Natural Products, Kyoto, Japan 2006/07 Refereed English Disclose to all
Masuda, Y., Irie, K., Murakami, K., Ohigashi, H., Ohashi, R., ○Takegoshi, K. Masuda, Y., Irie, K., Murakami, K., Ohigashi, H., Ohashi, R., ○Takegoshi, K. Masuda, Y., Irie, K., Murakami, K., Ohigashi, H., Ohashi, R., ○Takegoshi, K. Application of dipolar-assisted rotational resonance (DARR) to β-amyloid. Application of dipolar-assisted rotational resonance (DARR) to β-amyloid. Application of dipolar-assisted rotational resonance (DARR) to β-amyloid. The 2005 International Chemical Congress of Pacific Basin Societies, Honolulu, USA The 2005 International Chemical Congress of Pacific Basin Societies, Honolulu, USA The 2005 International Chemical Congress of Pacific Basin Societies, Honolulu, USA 2005/12 Refereed English Disclose to all
Murakami, K., Irie, K., Ohigashi, H., Hara, H., Nagao, M., Shimizu, T., and Shirasawa, T. Murakami, K., Irie, K., Ohigashi, H., Hara, H., Nagao, M., Shimizu, T., and Shirasawa, T. Murakami, K., Irie, K., Ohigashi, H., Hara, H., Nagao, M., Shimizu, T., and Shirasawa, T. Alzheimer’s 42-mer β peptide-specific mechanism of neurotoxicity through radical formation. Alzheimer’s 42-mer β peptide-specific mechanism of neurotoxicity through radical formation. Alzheimer’s 42-mer β peptide-specific mechanism of neurotoxicity through radical formation. 35th Annual Meeting of Society for Neuroscience, Washington DC, USA 35th Annual Meeting of Society for Neuroscience, Washington DC, USA 35th Annual Meeting of Society for Neuroscience, Washington DC, USA 2005/11 Refereed English Disclose to all
Irie, K., Murakami, K., Masuda, Y., Morimoto, A., Ohigashi, H., Hara, H., Nagao, M., Shimizu, T., and Shirasawa, T. Irie, K., Murakami, K., Masuda, Y., Morimoto, A., Ohigashi, H., Hara, H., Nagao, M., Shimizu, T., and Shirasawa, T. Irie, K., Murakami, K., Masuda, Y., Morimoto, A., Ohigashi, H., Hara, H., Nagao, M., Shimizu, T., and Shirasawa, T. New aggregation model of 42-mer amyloid β by the systematic proline replacement. New aggregation model of 42-mer amyloid β by the systematic proline replacement. New aggregation model of 42-mer amyloid β by the systematic proline replacement. 35th Annual Meeting of Society for Neuroscience, Washington DC, USA 35th Annual Meeting of Society for Neuroscience, Washington DC, USA 35th Annual Meeting of Society for Neuroscience, Washington DC, USA 2005/11 Refereed English Disclose to all
Masuda, Y., Irie, K., Murakami, K., Ohigashi, H., Ohashi, R., Takegoshi, K., Shimizu, T., and Shirasawa, T. Masuda, Y., Irie, K., Murakami, K., Ohigashi, H., Ohashi, R., Takegoshi, K., Shimizu, T., and Shirasawa, T. Masuda, Y., Irie, K., Murakami, K., Ohigashi, H., Ohashi, R., Takegoshi, K., Shimizu, T., and Shirasawa, T. Elucidation of the ‘malignant’ conformation of β-amyloid with Italian mutation (E22K-Aβ42) using solid-state NMR: implications for the pathogenesis of cerebral amyloid angiopathy and Alzheimer’s disease. Elucidation of the ‘malignant’ conformation of β-amyloid with Italian mutation (E22K-Aβ42) using solid-state NMR: implications for the pathogenesis of cerebral amyloid angiopathy and Alzheimer’s disease. Elucidation of the ‘malignant’ conformation of β-amyloid with Italian mutation (E22K-Aβ42) using solid-state NMR: implications for the pathogenesis of cerebral amyloid angiopathy and Alzheimer’s disease. 35th Annual Meeting of Society for Neuroscience, Washington DC, USA 35th Annual Meeting of Society for Neuroscience, Washington DC, USA 35th Annual Meeting of Society for Neuroscience, Washington DC, USA 2005/11 Refereed English Disclose to all
村上一馬、入江一浩、森本 晃、増田裕一、大東 肇、永尾雅哉、清水孝彦、白澤卓二 村上一馬、入江一浩、森本 晃、増田裕一、大東 肇、永尾雅哉、清水孝彦、白澤卓二 β アミロイドの新しい凝集モデルに基づく神経細胞毒性発現機構. β アミロイドの新しい凝集モデルに基づく神経細胞毒性発現機構. 第 47回天然有機化合物討論会, 徳島 第 47回天然有機化合物討論会, 徳島 2005/10 Refereed Japanese Disclose to all
村上一馬 他 村上一馬 他 Aβ42 ラジカルの生成と神経細胞毒性発現機構. Aβ42 ラジカルの生成と神経細胞毒性発現機構. 第 24 回日本認知症学会, 大阪 第 24 回日本認知症学会, 大阪 2005/09 Refereed Japanese Disclose to all
村上一馬 他 村上一馬 他 系統的プロリン置換による β アミロイドフィブリルの2次構造解析 系統的プロリン置換による β アミロイドフィブリルの2次構造解析 日本農芸化学会 2005 年度大会, 札幌 日本農芸化学会 2005 年度大会, 札幌 2005/03 Refereed Japanese Disclose to all
Ohashi, R., Takegoshi, K., Terao, T., Masuda, Y., Murakami, K., Irie, K. Ohashi, R., Takegoshi, K., Terao, T., Masuda, Y., Murakami, K., Irie, K. Ohashi, R., Takegoshi, K., Terao, T., Masuda, Y., Murakami, K., Irie, K. Structural analysis of amyloid β. Structural analysis of amyloid β. Structural analysis of amyloid β. XXI International Conference on Magnetic Resonance in Biological Systems, (Hyderabad, Andhra Pradesh, India), XXI International Conference on Magnetic Resonance in Biological Systems, (Hyderabad, Andhra Pradesh, India), XXI International Conference on Magnetic Resonance in Biological Systems, (Hyderabad, Andhra Pradesh, India), 2005/01 English Disclose to all
Murakami, K., Irie, K., Morimoto, A., Masuda, Y., Ohigashi, H., Nagao, M., Fukuda, H., Shimizu, T., and Shirasawa, T. Murakami, K., Irie, K., Morimoto, A., Masuda, Y., Ohigashi, H., Nagao, M., Fukuda, H., Shimizu, T., and Shirasawa, T. Murakami, K., Irie, K., Morimoto, A., Masuda, Y., Ohigashi, H., Nagao, M., Fukuda, H., Shimizu, T., and Shirasawa, T. New aggregation model of amyloid β by the systematic proline replacement. New aggregation model of amyloid β by the systematic proline replacement. New aggregation model of amyloid β by the systematic proline replacement. 1st Asia-Pacific International Peptide Symposium, 41st Japanese Peptide Symposium, Fukuoka, Japan 1st Asia-Pacific International Peptide Symposium, 41st Japanese Peptide Symposium, Fukuoka, Japan 1st Asia-Pacific International Peptide Symposium, 41st Japanese Peptide Symposium, Fukuoka, Japan 2004/11 Refereed English Disclose to all
村上一馬 村上一馬 β アミロイド (Aβ42) の新しい凝集モデル β アミロイド (Aβ42) の新しい凝集モデル 第 37 回若手ペプチド夏の勉強会, 京都 第 37 回若手ペプチド夏の勉強会, 京都 2004/08 Refereed Japanese Disclose to all
村上一馬 他 村上一馬 他 プロリン置換による Aβ42 凝集体の立体構造解析. プロリン置換による Aβ42 凝集体の立体構造解析. 日本農芸化学会 2004 年度大会, 広島 日本農芸化学会 2004 年度大会, 広島 2004/03 Refereed Japanese Disclose to all
村上一馬 他 村上一馬 他 β アミロイドの新しい凝集モデル β アミロイドの新しい凝集モデル 第 22 回日本認知症学会 第 22 回日本認知症学会 2003/10 Refereed Japanese Disclose to all
村上一馬 他 村上一馬 他 β アミロイドの新しい凝集仮説. β アミロイドの新しい凝集仮説. 第 38 回天然物化学談話会, 福岡 第 38 回天然物化学談話会, 福岡 2003/07 Refereed Japanese Disclose to all
村上一馬 他 村上一馬 他 家族性アルツハイマー病因 β アミロイドの凝集活性および神経細胞毒性. 家族性アルツハイマー病因 β アミロイドの凝集活性および神経細胞毒性. 日本農芸化学会 2003 年度大会, 東京 日本農芸化学会 2003 年度大会, 東京 2003/04 Refereed Japanese Disclose to all
Murakami, K., Irie, K., Morimoto, A., Ohigashi, H., Shindo, M., Nagao, M., Shimizu, T., and Shirasawa, T. Murakami, K., Irie, K., Morimoto, A., Ohigashi, H., Shindo, M., Nagao, M., Shimizu, T., and Shirasawa, T. Murakami, K., Irie, K., Morimoto, A., Ohigashi, H., Shindo, M., Nagao, M., Shimizu, T., and Shirasawa, T. Synthesis, aggregation, neurotoxicity, and secondary structure of various Aβ1-40 and Aβ1-42 mutants of familial Alzheimer’s disease at positions 21-23. Synthesis, aggregation, neurotoxicity, and secondary structure of various Aβ1-40 and Aβ1-42 mutants of familial Alzheimer’s disease at positions 21-23. Synthesis, aggregation, neurotoxicity, and secondary structure of various Aβ1-40 and Aβ1-42 mutants of familial Alzheimer’s disease at positions 21-23. Japan-Korea Young Scientists Meeting on Bioorganic and Natural Products Chemistry, Hiroshima, Japan Japan-Korea Young Scientists Meeting on Bioorganic and Natural Products Chemistry, Hiroshima, Japan Japan-Korea Young Scientists Meeting on Bioorganic and Natural Products Chemistry, Hiroshima, Japan 2002/09 Refereed English Disclose to all
村上一馬 他 村上一馬 他 家族性アルツハイマー病因ペプチドの化学合成、凝集活性および神経細胞毒性 家族性アルツハイマー病因ペプチドの化学合成、凝集活性および神経細胞毒性 第 37 回天然物化学談話会, 京都 第 37 回天然物化学談話会, 京都 2002/07 Refereed Japanese Disclose to all
村上一馬 他 村上一馬 他 家族性アルツハイマー β ペプチドの合成、凝集活性および神経細胞毒性. 家族性アルツハイマー β ペプチドの合成、凝集活性および神経細胞毒性. 日本農芸化学会 2002 年度大会, 仙台 日本農芸化学会 2002 年度大会, 仙台 2002/03 Refereed Japanese Disclose to all

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Title language:
Conference Activities & Talks
Title Title(Japanese) Title(English) Conference Conference(Japanese) Conference(English) Promotor Promotor(Japanese) Promotor(English) Date Language Assortment Disclose
抗酸化ストレスに着目したアルツハイマー病予防の可能性 抗酸化ストレスに着目したアルツハイマー病予防の可能性 京都大学原子炉実験所専門研究会「タンパク質の異常凝集とフォールディング病」 京都大学原子炉実験所専門研究会「タンパク質の異常凝集とフォールディング病」 京都大学原子炉実験所 京都大学原子炉実験所 2011/11/10 Japanese Oral presentation(invited, special) Disclose to all
アミロイドβ異常凝集における「折れ曲がり」の役割 アミロイドβ異常凝集における「折れ曲がり」の役割 京都大学原子炉実験所専門研究会 「タンパク質の異常凝集とフォールディング病」 京都大学原子炉実験所専門研究会 「タンパク質の異常凝集とフォールディング病」 京都大学原子炉実験所(大阪) 京都大学原子炉実験所(大阪) 2010/11/12 Japanese Oral presentation(invited, special) Disclose to all
アルツハイマー病と機能性食品因子 (Alzheimer’s disease and functional foods) アルツハイマー病と機能性食品因子 (Alzheimer’s disease and functional foods) Invited Lecturer in Gwangju University Invited Lecturer in Gwangju University Gwangju大学 (Gwangju, 韓国) Gwangju大学 (Gwangju, 韓国) 2010/10/13 Japanese Oral presentation(invited, special) Disclose to all
Structural analysis of toxic conformer of 42-mer amyloid β peptide using ESR spectrometry Structural analysis of toxic conformer of 42-mer amyloid β peptide using ESR spectrometry Structural analysis of toxic conformer of 42-mer amyloid β peptide using ESR spectrometry 7th Asia-Pacific EPR/ESR Symposium 7th Asia-Pacific EPR/ESR Symposium 7th Asia-Pacific EPR/ESR Symposium Convention Center (Jeju, 韓国) Convention Center (Jeju, 韓国) 2010/10/12 English Oral presentation(invited, special) Disclose to all
‘Toxic’ turn formation at positions 22 and 23 in Aβ42 and its relevance to oxidative stress in AD ‘Toxic’ turn formation at positions 22 and 23 in Aβ42 and its relevance to oxidative stress in AD ‘Toxic’ turn formation at positions 22 and 23 in Aβ42 and its relevance to oxidative stress in AD Neurodegeneration Research Meeting Neurodegeneration Research Meeting Neurodegeneration Research Meeting Melbourne大学 (Melbourne, Australia) Melbourne大学 (Melbourne, Australia) 2009/08/14 English Oral presentation(invited, special) Disclose to all
Title language:
Books etc
Author Author(Japanese) Author(English) Title Title(Japanese) Title(English) Publisher Publisher(Japanese) Publisher(English) Publication date Language Type Disclose
村上一馬,増田裕一,入江一浩 村上一馬,増田裕一,入江一浩 固体NMRおよびESRによるアミロイド β の立体構造解析と毒性ターン構造特異抗体の開発. 固体NMRおよびESRによるアミロイド β の立体構造解析と毒性ターン構造特異抗体の開発. 遺伝子医学MOOK「最新ペプチド合成技術とその創薬研究への応用」 21, 211-216 (2012) 遺伝子医学MOOK「最新ペプチド合成技術とその創薬研究への応用」 21, 211-216 (2012) 2012 Japanese Single Work Disclose to all
Murakami, K. and *Shimizu, T. Murakami, K. and *Shimizu, T. Cytoplasmic superoxide radicals as contributing factors to intracellular Aβ oligomerization in Alzheimer’s disease Cytoplasmic superoxide radicals as contributing factors to intracellular Aβ oligomerization in Alzheimer’s disease Commun. Integr. Biol. 5 (3), 255-258 (2012). Commun. Integr. Biol. 5 (3), 255-258 (2012). 2012 Japanese Single Work Disclose to all
村上一馬,*入江一浩 村上一馬,*入江一浩 アミロイド β の毒性ターン構造を認識する抗体の開発 アミロイド β の毒性ターン構造を認識する抗体の開発 神経内科 77 (2), 179-184 (2012). 神経内科 77 (2), 179-184 (2012). 2012 Japanese Single Work Disclose to all
村上一馬,佐藤瑞穂,鈴木啓之,泉尾直孝,久米利明,赤池昭紀,永田 徹,西崎知之,富山貴美,森 啓,*入江一浩 村上一馬,佐藤瑞穂,鈴木啓之,泉尾直孝,久米利明,赤池昭紀,永田 徹,西崎知之,富山貴美,森 啓,*入江一浩 アミロイドβの「毒性コンホマー」形成とGlu22における遺伝性変異. アミロイドβの「毒性コンホマー」形成とGlu22における遺伝性変異. Dementia Japan 26 (3), 311-318 (2012). Dementia Japan 26 (3), 311-318 (2012). 2012 Japanese Single Work Disclose to all
*Murakami, K., Shimizu, T., and Irie, K. *Murakami, K., Shimizu, T., and Irie, K. *Murakami, K., Shimizu, T., and Irie, K. Formation of the 42-mer amyloid β radical and the therapeutic role of superoxide dismutase in Alzheimer’s disease. Formation of the 42-mer amyloid β radical and the therapeutic role of superoxide dismutase in Alzheimer’s disease. Formation of the 42-mer amyloid β radical and the therapeutic role of superoxide dismutase in Alzheimer’s disease. J. Amino Acids 2011, doi: 10.4061/2011/654207 (2011). J. Amino Acids 2011, doi: 10.4061/2011/654207 (2011). J. Amino Acids 2011, doi: 10.4061/2011/654207 (2011). 2011 English Single Work Disclose to all
*入江一浩,村上一馬,増田裕一,村田 央,野田義博,初田裕幸,村山繁雄,清水孝彦,堀越優子,木下憲明,白澤卓二 *入江一浩,村上一馬,増田裕一,村田 央,野田義博,初田裕幸,村山繁雄,清水孝彦,堀越優子,木下憲明,白澤卓二 アミロイド β の毒性ターン構造を認識する抗体の開発. アミロイド β の毒性ターン構造を認識する抗体の開発. 臨床神経 51 (3), 25-29 (2011). 臨床神経 51 (3), 25-29 (2011). 2011 Japanese Single Work Disclose to all
*村上一馬,入江一浩,清水孝彦 *村上一馬,入江一浩,清水孝彦 抗酸化ストレスに着目したアルツハイマー病予防の可能性. 抗酸化ストレスに着目したアルツハイマー病予防の可能性. タンパク質の異常凝集とその防御・修復機構に関する研究会報告, 4, 10-14 (2011). タンパク質の異常凝集とその防御・修復機構に関する研究会報告, 4, 10-14 (2011). 2011 Japanese Single Work Disclose to all
Murakami, K., Masuda, Y. Shirasawa, T. *Shimizu, T., and *Irie, K. Murakami, K., Masuda, Y. Shirasawa, T. *Shimizu, T., and *Irie, K. Murakami, K., Masuda, Y. Shirasawa, T. *Shimizu, T., and *Irie, K. The turn formation at positions 22 and 23 in the 42-mer amyloid β peptide: the merging role in the pathogenesis of Alzheimer’s disease. The turn formation at positions 22 and 23 in the 42-mer amyloid β peptide: the merging role in the pathogenesis of Alzheimer’s disease. The turn formation at positions 22 and 23 in the 42-mer amyloid β peptide: the merging role in the pathogenesis of Alzheimer’s disease. Geriatr. Gerontol. Int. 10 (Suppl. 1), S169-S179 (2010). Geriatr. Gerontol. Int. 10 (Suppl. 1), S169-S179 (2010). Geriatr. Gerontol. Int. 10 (Suppl. 1), S169-S179 (2010). 2010 English Single Work Disclose to all
村上一馬,入江一浩 村上一馬,入江一浩 アミロイドβ異常凝集における「折れ曲がり」の役割 アミロイドβ異常凝集における「折れ曲がり」の役割 タンパク質の異常凝集とその防御・修復機構に関する研究会報告(III) タンパク質の異常凝集とその防御・修復機構に関する研究会報告(III) 2010 Japanese Single Work Disclose to all
Li, H., Rahimi, F., Sinha, S., Maiti, P., *Bitan, G., Murakami, K. Li, H., Rahimi, F., Sinha, S., Maiti, P., *Bitan, G., Murakami, K. Li, H., Rahimi, F., Sinha, S., Maiti, P., *Bitan, G., Murakami, K. Amyloids and protein aggregation – analytical methods. Amyloids and protein aggregation – analytical methods. Amyloids and protein aggregation – analytical methods. Encyclopedia Anal. Chem. doi: 10.1002/9780470027318.a9038 (2009). Encyclopedia Anal. Chem. doi: 10.1002/9780470027318.a9038 (2009). Encyclopedia Anal. Chem. doi: 10.1002/9780470027318.a9038 (2009). 2009 English Single Work Disclose to all
*村上一馬,清水孝彦,白澤卓二,入江一浩 *村上一馬,清水孝彦,白澤卓二,入江一浩 アミロイド β (Aβ42) の毒性コンホメーションの提唱. アミロイド β (Aβ42) の毒性コンホメーションの提唱. 基礎老化研究 32 (3), 25-29 (2008). 基礎老化研究 32 (3), 25-29 (2008). 2008 Japanese Single Work Disclose to all
*村上一馬 *村上一馬 Young investigator’s competition in Yokohama ~‘Malignant conformation of Aβ42 peptide’. Young investigator’s competition in Yokohama ~‘Malignant conformation of Aβ42 peptide’. PEPTIDE NEWSLETTER JAPAN 63 (1), 5-8 (2007). PEPTIDE NEWSLETTER JAPAN 63 (1), 5-8 (2007). 2007 Japanese Single Work Disclose to all
*Irie, K, Murakami, K., Masuda, Y., Morimoto, A., Ohigashi, H., Hara, H., Ohashi, R., Takegoshi K., Fukuda, H., Nagao, M., Shimizu, T., and Shirasawa, T. *Irie, K, Murakami, K., Masuda, Y., Morimoto, A., Ohigashi, H., Hara, H., Ohashi, R., Takegoshi K., Fukuda, H., Nagao, M., Shimizu, T., and Shirasawa, T. *Irie, K, Murakami, K., Masuda, Y., Morimoto, A., Ohigashi, H., Hara, H., Ohashi, R., Takegoshi K., Fukuda, H., Nagao, M., Shimizu, T., and Shirasawa, T. The toxic conformation of the 42-residue amyloid β peptide and its relevance to oxidative stress in Alzheimer’s disease. The toxic conformation of the 42-residue amyloid β peptide and its relevance to oxidative stress in Alzheimer’s disease. The toxic conformation of the 42-residue amyloid β peptide and its relevance to oxidative stress in Alzheimer’s disease. Mini-Rev. Med. Chem. 7 (10), 1001-1008 (2007). Mini-Rev. Med. Chem. 7 (10), 1001-1008 (2007). Mini-Rev. Med. Chem. 7 (10), 1001-1008 (2007). 2007 English Single Work Disclose to all
Murakami, K., *Irie, K., Ohigashi, H., Hara, H., Nagao, M., Shimizu, T., and Shirasawa, T. Murakami, K., *Irie, K., Ohigashi, H., Hara, H., Nagao, M., Shimizu, T., and Shirasawa, T. Murakami, K., *Irie, K., Ohigashi, H., Hara, H., Nagao, M., Shimizu, T., and Shirasawa, T. ‘Malignant’ conformation of Alzheimer’s β peptides (Aβ42) through radical formation. ‘Malignant’ conformation of Alzheimer’s β peptides (Aβ42) through radical formation. ‘Malignant’ conformation of Alzheimer’s β peptides (Aβ42) through radical formation. In Peptide Science 2006, eds. Ishida, H. & Mihara, H., The Japanese Peptide Society, 19-20 (2006). In Peptide Science 2006, eds. Ishida, H. & Mihara, H., The Japanese Peptide Society, 19-20 (2006). In Peptide Science 2006, eds. Ishida, H. & Mihara, H., The Japanese Peptide Society, 19-20 (2006). 2006 English Single Work Disclose to all
Murakami, K., *Irie, K., Morimoto, A., Masuda, Y., Ohigashi, H., Nagao, M., Fukuda, H., Shimizu, T., and Shirasawa, T. Murakami, K., *Irie, K., Morimoto, A., Masuda, Y., Ohigashi, H., Nagao, M., Fukuda, H., Shimizu, T., and Shirasawa, T. Murakami, K., *Irie, K., Morimoto, A., Masuda, Y., Ohigashi, H., Nagao, M., Fukuda, H., Shimizu, T., and Shirasawa, T. New aggregation model of amyloid β by the systematic proline replacement. New aggregation model of amyloid β by the systematic proline replacement. New aggregation model of amyloid β by the systematic proline replacement. In Peptide Science 2004, ed. Shimohigashi, Y., The Japanese Peptide Society, 179-182 (2005). In Peptide Science 2004, ed. Shimohigashi, Y., The Japanese Peptide Society, 179-182 (2005). In Peptide Science 2004, ed. Shimohigashi, Y., The Japanese Peptide Society, 179-182 (2005). 2005 English Single Work Disclose to all
*Irie, K., Murakami, K., Masuda, Y., Morimoto, A., Ohigashi, H., Ohashi, R., Takegoshi, K., Nagao, M., Shimizu, T., and Shirasawa, T. *Irie, K., Murakami, K., Masuda, Y., Morimoto, A., Ohigashi, H., Ohashi, R., Takegoshi, K., Nagao, M., Shimizu, T., and Shirasawa, T. *Irie, K., Murakami, K., Masuda, Y., Morimoto, A., Ohigashi, H., Ohashi, R., Takegoshi, K., Nagao, M., Shimizu, T., and Shirasawa, T. Structure of β-amyloid fibrils and its relevance to their neurotoxicity: implications for the pathogenesis of Alzheimer’s disease. Structure of β-amyloid fibrils and its relevance to their neurotoxicity: implications for the pathogenesis of Alzheimer’s disease. Structure of β-amyloid fibrils and its relevance to their neurotoxicity: implications for the pathogenesis of Alzheimer’s disease. J. Biosci. Bioeng. 99 (5), 437-447 (2005). J. Biosci. Bioeng. 99 (5), 437-447 (2005). J. Biosci. Bioeng. 99 (5), 437-447 (2005). 2005 English Single Work Disclose to all

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Title language:
Patents
Inventor(s) Inventor(s) (Japanese) Inventor(s) (English) Title Title(Japanese) Title(English) Stage Patent number Date Disclose
Irie, K., Murakami, K., Masuda, Y., Shimizu, T., Shirasawa, T., Seito, T. Irie, K., Murakami, K., Masuda, Y., Shimizu, T., Shirasawa, T., Seito, T. Irie, K., Murakami, K., Masuda, Y., Shimizu, T., Shirasawa, T., Seito, T. Antibody recognizing turn structure in amyloid β Antibody recognizing turn structure in amyloid β Antibody recognizing turn structure in amyloid β 特許登録 特許US 8,710,193; CN ZL201080046483.9 2014/04/29 Disclose to all
入江一浩,村上一馬,清水孝彦,泉尾直孝,清藤 勉 入江一浩,村上一馬,清水孝彦,泉尾直孝,清藤 勉 アミロイドβの22位及び23位のターン構造を極めて特異的に認識する抗体 アミロイドβの22位及び23位のターン構造を極めて特異的に認識する抗体 特許出願 特願2014−251898,2015−104411 2015/05/22 Disclose to all
入江一浩、村上一馬、増田裕一、清水孝彦、白澤卓二、清藤 勉 入江一浩、村上一馬、増田裕一、清水孝彦、白澤卓二、清藤 勉 アミロイドβのターン構造を認識する抗体 アミロイドβのターン構造を認識する抗体 特許出願 特願2009−239542 2009/10/16 Disclose to all
Title language:
Awards
Title(Japanese) Title(English) Organization name(Japanese) Organization name(English) Date
第47回天然有機化合物討論会奨励賞 2005/10/
IUPAC天然物化学国際会議ICOB-5&ISCNP-25 poster prize 2006/07/
第43回ペプチド討論会&第4回ペプチド工学国際会議若手奨励賞 日本ペプチド学会 The Japanese Peptide Society 2006/11/
第31回日本基礎老化学会奨励賞 日本基礎老化学会 Japan Society for Biomedical Gerontology 2008/06/
2010年度日本農芸化学会大会トピックス賞 日本農芸化学 Japan Society for Bioscience, Biotechnology, Agrochemistry 2010/03/
第52回天然有機化合物討論会奨励賞 2010/09/
第12回天然物談話会奨励賞 2012/07/
2013年度農芸化学奨励賞 日本農芸化学会 Japan Society for Bioscience, Biotechnology, Agrochemistry 2013/03/
2012年Biosci. Biotechnol. Biochem.論文賞 日本農芸化学会 Japan Society for Bioscience, Biotechnology, Agrochemistry 2013/03/
2013年度日本農芸化学会大会トピックス賞 日本農芸化学会 Japan Society for Bioscience, Biotechnology, Agrochemistry 2013/03/
2018年度日本農芸化学会大会トピックス賞 日本農芸化学会 Japan Society for Bioscience, Biotechnology, Agrochemistry 2018/03/

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External funds, competitive funds and Grants-in-Aid for Scientific Research(kaken)
Type Position Title(Japanese) Title(English) Period
特別研究員奨励費DC1 Representative βアミロイドの凝集機構に関する有機化学的研究 The new aggregation model of the 42-mer amyloid β peptides (Aβ42). 2004/04/01-2007/03/31
特別研究員奨励費SPD Representative βアミロイドの病的コンホメーションを標的としたアルツハイマー病治療薬の設計 Development of therapeutic agents for Alzheimer’s disease based on the toxic conformation of Aβ42 and their estimation using novel disease-model mice. 2007/04/01-2010/03/31
基盤研究(C) Representative アミロイドβの毒性オリゴマー特異的なRNAアプタマーの開発 2010/04/01-2013/03/31
基盤研究(A) Assignment アミロイドβの毒性オリゴマーの構造解析に基づいた抗アルツハイマー病薬の開発 2010/04/01-2014/03/31
若手研究(B) Representative 伝統生薬チョウトウコウに含まれるアミロイドβオリゴマー化抑制物質の同定と作用機構 2013/04/01-2015/03/31
基盤研究(A) Assignment アミロイドβの毒性配座理論に基づいたアルツハイマー病の新規診断法の開発 2014/04/01-2014/05/30
基盤研究(S) Assignment アミロイドβの毒性配座理論を基盤としたアルツハイマー病の新しい予防戦略 2014/05/30-2019/03/31
挑戦的萌芽 Representative 細胞内アミロイドβの新しい標的分子の探索 2015/04/01-2017/03/31
若手研究(A) Representative アミロイドβオリゴマーの形成阻害機構に関する構造有機化学的研究 2016/04/01-2020/03/31
Non-external, competitive funds or grants other than grants-in-aid for Scientific research (kaken)
System Main person Title(Japanese) Title(English) Period
加藤記念バイオサイエンス振興財団 村上一馬 光親和性標識法及び固体NMR法を用いたアミロイドβ凝集阻害機構の解明 2011/04/01-2013/03/30
上原記念生命科学財団研究奨励金 村上一馬 Aβ毒性コンホマーの細胞内標的タンパク質 2013/04/01-2014/03/31
Teaching subject(s)
Name(Japanese) Name(English) Term Department Period
有機化学実験及び実験法 前期 農学部 2011/04-2012/03
生命有機化学 前期 農学部 2011/04-2012/03
食品有機化学III 後期 農学部 2011/04-2012/03
生命有機化学専攻実験 農学研究科 2011/04-2012/03
生命有機化学専攻演習 農学研究科 2011/04-2012/03
生命有機化学 Organic Chemistry in Life Science 前期 農学部 2012/04-2013/03
食品有機化学III Organic Chemistry in Food Science III 後期 農学部 2012/04-2013/03
食品有機化学実験及び実験法 Laboratory Course in Organic Chemistry in Food Science 前期 農学部 2012/04-2013/03
食品有機化学III Organic Chemistry in Food Science III 後期 農学部 2013/04-2014/03
生命有機化学 Organic Chemistry in Life Science 前期 農学部 2013/04-2014/03
食品有機化学実験及び実験法 Laboratory Course in Organic Chemistry in Food Science 前期 農学部 2013/04-2014/03
生命有機化学専攻演習 Seminar of Organic Chemistry in Life Science 通年 農学研究科 2013/04-2014/03
生命有機化学専攻実験 Experimental Course of Organic Chemistry in Life Science 通年 農学研究科 2013/04-2014/03
生命有機化学 Organic Chemistry in Life Science 前期 農学部 2014/04-2015/03
食品有機化学実験及び実験法 Laboratory Course in Organic Chemistry in Food Science 前期 農学部 2014/04-2015/03
食品分析化学 Analytical Chemistry in Food Science 後期 農学部 2014/04-2015/03
生体反応有機化学 Organic Chemistry in Life Science 前期集中 農学研究科 2014/04-2015/03
生命有機化学専攻演習 Seminar of Organic Chemistry in Life Science 通年 農学研究科 2014/04-2015/03
生命有機化学専攻実験 Experimental Course of Organic Chemistry in Life Science 通年 農学研究科 2014/04-2015/03
生命有機化学 Organic Chemistry in Life Science 前期 農学部 2015/04-2016/03
生命有機化学専攻実験1 Experimental Course of Organic Chemistry in Life Science1 通年 農学研究科 2015/04-2016/03
生命有機化学専攻実験 Experimental Course of Organic Chemistry in Life Science 通年 農学研究科 2015/04-2016/03
生命有機化学専攻演習1 Seminar of Organic Chemistry in Life Science1 通年 農学研究科 2015/04-2016/03
生命有機化学専攻演習 Seminar of Organic Chemistry in Life Science 通年 農学研究科 2015/04-2016/03
食品分析化学 Analytical Chemistry in Food Science 後期 農学部 2015/04-2016/03
食品有機化学実験及び実験法 Laboratory Course in Organic Chemistry in Food Science 前期 農学部 2015/04-2016/03
基礎有機化学I Basic Organic Chemistry I 前期 全学共通科目 2016/04-2017/03
天然物化学 Natural Products Chemistry 前期 農学部 2016/04-2017/03
生体反応有機化学 Organic Chemistry in Life Science 前期集中 農学研究科 2016/04-2017/03
生命有機化学専攻実験1 Experimental Course of Organic Chemistry in Life Science1 通年 農学研究科 2016/04-2017/03
生命有機化学専攻実験2 Experimental Course of Organic Chemistry in Life Science2 通年 農学研究科 2016/04-2017/03
生命有機化学専攻実験 Experimental Course of Organic Chemistry in Life Science 通年 農学研究科 2016/04-2017/03
生命有機化学専攻演習1 Seminar of Organic Chemistry in Life Science1 通年 農学研究科 2016/04-2017/03
生命有機化学専攻演習2 Seminar of Organic Chemistry in Life Science2 通年 農学研究科 2016/04-2017/03
生命有機化学専攻演習 Seminar of Organic Chemistry in Life Science 通年 農学研究科 2016/04-2017/03
食品分析化学 Analytical Chemistry in Food Science 後期 農学部 2016/04-2017/03
食品有機化学実験及び実験法 Laboratory Course in Organic Chemistry in Food Science 前期 農学部 2016/04-2017/03
基礎有機化学I Basic Organic Chemistry I 前期 全学共通科目 2017/04-2018/03
天然物化学 Natural Products Chemistry 前期 農学部 2017/04-2018/03
生命有機化学専攻実験1 Experimental Course of Organic Chemistry in Life Science1 通年 農学研究科 2017/04-2018/03
生命有機化学専攻実験2 Experimental Course of Organic Chemistry in Life Science2 通年 農学研究科 2017/04-2018/03
生命有機化学専攻演習1 Seminar of Organic Chemistry in Life Science1 通年 農学研究科 2017/04-2018/03
生命有機化学専攻演習2 Seminar of Organic Chemistry in Life Science2 通年 農学研究科 2017/04-2018/03
生物有機化学特論 Advanced Course of Bioorganic Chemistry 前期集中 農学研究科 2017/04-2018/03
食品分析化学 Analytical Chemistry in Food Science 後期 農学部 2017/04-2018/03
食品有機化学実験及び実験法 Laboratory Course in Organic Chemistry in Food Science 前期 農学部 2017/04-2018/03
基礎有機化学I Basic Organic Chemistry I 前期 全学共通科目 2018/04-2019/03
天然物化学 Natural Products Chemistry 前期 農学部 2018/04-2019/03
天然物化学特論 Advanced Course of Natural Products Chemistry 前期集中 農学研究科 2018/04-2019/03
生命有機化学専攻実験1 Experimental Course of Organic Chemistry in Life Science1 通年 農学研究科 2018/04-2019/03
生命有機化学専攻実験2 Experimental Course of Organic Chemistry in Life Science2 通年 農学研究科 2018/04-2019/03
生命有機化学専攻演習1 Seminar of Organic Chemistry in Life Science1 通年 農学研究科 2018/04-2019/03
生命有機化学専攻演習2 Seminar of Organic Chemistry in Life Science2 通年 農学研究科 2018/04-2019/03
生理化学概論 Outline of Physiological Chemistry 後期集中 全学共通科目 2018/04-2019/03
食品分析化学 Analytical Chemistry in Food Science 後期 農学部 2018/04-2019/03
食品有機化学実験及び実験法 Laboratory Course in Organic Chemistry in Food Science 前期 農学部 2018/04-2019/03

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School management (title, position)
Title Period
環境管理専門委員会有機廃液情報管理小委員会 委員 2017/04/01-2019/03/31
放射線障害予防小委員会 委員 2015/04/01-2019/03/31
Faculty management (title, position)
Title Period
放射線取扱主任者(農学研究科) 2010/10/1-
エックス線作業主任者(農学研究科) -
広報委員会 委員 2014/04/01-2016/03/31
研究活動推進委員会 委員 2014/04/01-2016/03/31
動物実験委員会 委員 2015/04/01-2019/03/31
環境・安全・衛生委員会 委員 2016/04/01-2018/03/31
放射線障害防止委員会 委員 2015/04/01-2019/03/31
広報委員会 委員 2018/04/01-2020/03/31
Academic organizations (administrative title, position)
Organization name(Japanese) Organization name(English) Title(Japanese) Title(English) Period
天然物化学談話会世話人会メンバー 世話人 2009-
Other activities (awards)
Award name Organization name Date
平成28年度科研費 審査委員表彰 日本学術振興会 2016/09/30
History of staying abroad
Organization Department Research theme Country Period
米国UCLA 神経学科 Aβオリゴマー特異的なRNAアプタマーの開発 米国 2007/06/-2008/03/
豪州メルボルン大学 病理学科 高分解能NMRを用いたAβオリゴマーの立体構造解析 豪州 2009/06/-2009/08/