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- KAGAWA Yasuo
- Department of Biochemistry, Jichi Medical School Department of Medical Chemistry, Kagawa Nutrition University
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抄録
ATP synthase (FoF1) consists of an ATP-driven motor (F1) and a H+-driven motor (Fo), which rotate in opposite directions. FoF1 reconstituted into a lipid membrane is capable of ATP synthesis driven by H+ flux. As the basic structures of F1 (α3β3γδε) and Fo (ab2c10) are ubiquitous, stable thermophilic FoF1 (TFoF1) has been used to elucidate molecular mechanisms, while human F1Fo (HF1Fo) has been used to study biomedical significance. Among F1s, only thermophilic F1 (TF1) can be analyzed simultaneously by reconstitution, crystallography, mutagenesis and nanotechnology for torque-driven ATP synthesis using elastic coupling mechanisms. In contrast to the single operon of TFoF1, HFoF1 is encoded by both nuclear DNA with introns and mitochondrial DNA. The regulatory mechanism, tissue specificity and physiopathology of HFoF1 were elucidated by proteomics, RNA interference, cytoplasts and transgenic mice. The ATP synthesized daily by HFoF1 is in the order of tens of kilograms, and is primarily controlled by the brain in response to fluctuations in activity.<BR><BR>(Communicated by Fumio OOSAWA, M.J.A.)
収録刊行物
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- Proceedings of the Japan Academy. Ser. B: Physical and Biological Sciences
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Proceedings of the Japan Academy. Ser. B: Physical and Biological Sciences 86 (7), 667-693, 2010
日本学士院
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詳細情報 詳細情報について
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- CRID
- 1390282679124154496
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- NII論文ID
- 130000309237
- 40017237075
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- NII書誌ID
- AA00785485
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- COI
- 1:STN:280:DC%2BC3cjivFCjsQ%3D%3D
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- ISSN
- 13492896
- 03862208
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- NDL書誌ID
- 10779674
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- PubMed
- 20689227
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- 本文言語コード
- en
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- データソース種別
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- JaLC
- NDL
- Crossref
- PubMed
- CiNii Articles
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- 抄録ライセンスフラグ
- 使用不可