Functional analysis of RIG-I and its medical application
| Project/Area Number |
23770113
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Multi-year Fund |
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| Research Field |
Structural biochemistry
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| Research Institution | Kyoto University |
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Principal Investigator |
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| Project Period (FY) |
2011 – 2012
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| Project Status |
Completed (Fiscal Year 2012)
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| Budget Amount *help |
¥4,550,000 (Direct Cost: ¥3,500,000、Indirect Cost: ¥1,050,000)
Fiscal Year 2012: ¥2,340,000 (Direct Cost: ¥1,800,000、Indirect Cost: ¥540,000)
Fiscal Year 2011: ¥2,210,000 (Direct Cost: ¥1,700,000、Indirect Cost: ¥510,000)
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| Keywords | 自然免疫 / RIG-I / インターフェロン / 構造解析 / I型インターフェロン |
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| Research Abstract |
RIG-I is a sensor protein that specifically recognize viral RNA and induce early immunity . In the absence of virus RIG-I forms resting form not to induce antiviral activities. Because, those activities are also toxic for our body. I performed functional analysis of sensor protein RIG-I and identified suppression domain of RIG-I that controls RIG-I activation. From this result I suggested the mechanism that how RIG-I is self-controlled its activity .
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Report
(3 results)
Research Products
(7 results)
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[Journal Article] 55 Amino acid linker between helicase and carboxyl terminal domains of RIG-I functions as a critical repression domain and determines inter-domain conformation2011
Author(s)
Kageyama, M., Takahasi, K., Narita, R., Hirai, R., Yoneyama, M., Kato, H., Fujita, T.
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Journal Title
Biochem. Biophys. Res. Commun
Volume: 415 (1)
Pages: 75-81
Related Report
Peer Reviewed
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