Study on functions generated by suppressing diffusive motion of proteins by interaction with intracellular structures
| Project/Area Number |
16K14704
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| Research Category |
Grant-in-Aid for Challenging Exploratory Research
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| Allocation Type | Multi-year Fund |
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| Research Field |
Biophysics
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| Research Institution | Muroran Institute of Technology |
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Principal Investigator |
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| Project Period (FY) |
2016-04-01 – 2018-03-31
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| Project Status |
Completed (Fiscal Year 2017)
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| Budget Amount *help |
¥3,640,000 (Direct Cost: ¥2,800,000、Indirect Cost: ¥840,000)
Fiscal Year 2017: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2016: ¥2,340,000 (Direct Cost: ¥1,800,000、Indirect Cost: ¥540,000)
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| Keywords | タンパク質 / 拡散運動 / 自己集合 / 細胞骨格 / 微小管 / アクチン / 細胞膜 / アミロイド / 拡散 / 自己組織化 |
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| Outline of Final Research Achievements |
In this study, we analyzed how proteins interact with each other and express their functions under conditions where the diffusive motion of protein molecules is spatially restricted as in vivo. Microtubule assembly-promoting activity of MAP2 and MAP4 with high affinity for F-actin was enhanced in the presence of F-actin, but tau with low affinity for F-actin was not. Besides, when aggregation of amyloid β was real-time imaged using quantum dots, it was observed that aggregation was promoted in the presence of cultured cells. These results suggested that suppression of diffusion of protein molecules by interaction with F-actin and cell membrane greatly affects expression of the protein functions.
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Report
(3 results)
Research Products
(18 results)
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[Journal Article] Structure-activity relations of rosmarinic acid derivatives for the amyloid beta aggregation inhibition and antioxidant properties2017
Author(s)
Taguchi Riho, Hatayama Koki, Takahashi Tomohito, Hayashi Takafumi, Sato Yuki, Sato Daisuke, Ohta Kiminori, Nakano Hiroto, Seki Chigusa, Endo Yasuyuki, Tokuraku Kiyotaka, Uwai Koji
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Journal Title
EUROPEAN JOURNAL OF MEDICINAL CHEMISTRY
Volume: 138
Pages: 1066-1075
DOI
Related Report
Peer Reviewed
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[Journal Article] Mutually exclusive cooperative binding of myosin and cofilin to actin filaments involves cooperative conformational changes of actin.2016
Author(s)
Ngo KX, Umeki N, Kijima ST, Kodera N, Ueno H, Furutani-Umezu N, Nakajima J, Noguchi TQP, Nagasaki A, Tokuraku K, Uyeda TQP
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Journal Title
Scientific Reports
Volume: 6
Issue: 1
Pages: 35449-35449
DOI
Related Report
Peer Reviewed / Open Access / Acknowledgement Compliant
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