| Project/Area Number |
16K13101
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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 |
Chemical biology
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| Research Institution | Osaka University |
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Principal Investigator |
Kato Nobuo 大阪大学, 産業科学研究所, 教授 (50150537)
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| Project Period (FY) |
2016-04-01 – 2017-03-31
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| Project Status |
Completed (Fiscal Year 2016)
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| Budget Amount *help |
¥3,510,000 (Direct Cost: ¥2,700,000、Indirect Cost: ¥810,000)
Fiscal Year 2016: ¥3,510,000 (Direct Cost: ¥2,700,000、Indirect Cost: ¥810,000)
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| Keywords | タンパク質間相互作用 / 14-3-3タンパク質 / フシコクシン / コチレニン / 生体分子 / 生体機能利用 / シグナル伝達 / 生理活性 / 蛋白質 |
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| Outline of Final Research Achievements |
14-3-3 proteins regulate intracellular signal transductions by associating with phosphorylated proteins. This study aimed to elucidate the functions of seven isoforms of human 14-3-3 protein by using their point mutants and small molecule chemical tools. The ζ isoform was used for wild type 14-3-3, and several point mutants on its Lys 120 were obtained. In any cases, the binding affinities of the point mutants toward model peptides were attenuated as compared with that of the wild type, but the association ability was partly recovered by derivatives of diterpene glycoside, fusicoccin (FC). Thus, phenotypic analysis using 14-3-3 point mutants and FC derivatives can be a useful method for functional analysis of 14-3-3 isoforms.
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