Molecular basis of polyglutamine disease using yeast
Project/Area Number |
19680017
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Research Category |
Grant-in-Aid for Young Scientists (A)
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Allocation Type | Single-year Grants |
Research Field |
Neuroscience in general
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Research Institution | The Institute of Physical and Chemical Research |
Principal Investigator |
TANAKA Motomasa The Institute of Physical and Chemical Research, 田中研究ユニット, ユニットリーダー (40321781)
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Project Period (FY) |
2007 – 2009
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Project Status |
Completed (Fiscal Year 2009)
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Budget Amount *help |
¥20,930,000 (Direct Cost: ¥16,100,000、Indirect Cost: ¥4,830,000)
Fiscal Year 2009: ¥4,030,000 (Direct Cost: ¥3,100,000、Indirect Cost: ¥930,000)
Fiscal Year 2008: ¥5,850,000 (Direct Cost: ¥4,500,000、Indirect Cost: ¥1,350,000)
Fiscal Year 2007: ¥11,050,000 (Direct Cost: ¥8,500,000、Indirect Cost: ¥2,550,000)
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Keywords | ポリグルタミン / アミロイド / プリオン / 酵母 / 凝集体 / ハンチントン病 / ミスフォールディング / 酵母プリオン / 神経変性疾患 |
Research Abstract |
We observed structural polymorphism in the aggregates of huntingtin, a protein responsible for Huntington disease, both in vitro and in vivo. Among distinct conformations of huntingtin amyloids derived from a variety of brain regions, those in striatum showed the highest cytotoxicity. Therefore, amyloid conformation may be a critical determinant of regional specificity in Huntington disease. In addition, a genetic screening system that can detect cross-seeding between a certain protein and polyglutamine aggregates allows us to identify a novel yeast prion protein that lacks a Gln/Asn-rich domain.
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Report
(4 results)
Research Products
(30 results)
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[Journal Article] Distinct conformations of in vitro and in vivo amyloids of huntingtin-exon1 show different cytotoxicity.2009
Author(s)
Nekooki-Machida, Y., Kurosawa, M., Nukina, N., Ito, K., Oda, T., Tanaka, M.
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Journal Title
Proc. Natl. Acad. Sci. U.S.A. 106
Pages: 9679-9684
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