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the 6th letter of the Roman alphabet (同)f

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1. 酸関連疾患治療のためのプロトンポンプ阻害剤の概要および比較 overview and comparison of the proton pump inhibitors for the treatment of acid related disorders
2. 腎尿細管性アシドーシスの概要と病態生理、およびカリウムバランスへの影響 overview and pathophysiology of renal tubular acidosis and the effect on potassium balance
3. 赤血球水分量の制御 control of red blood cell hydration
4. 拡張能障害の細胞学的機序 cellular mechanisms of diastolic dysfunction
5. ウィルソン病：疫学および病因 wilson disease epidemiology and pathogenesis

English Journal

Complementation of the Fo c Subunit of Escherichia coli with That of Streptococcus mutans and Properties of the Hybrid FoF1 ATP Synthase.

Araki M, Hoshi K, Fujiwara M, Sasaki Y, Yonezawa H, Senpuku H, Iwamoto-Kihara A, Maeda M.SourceDepartment of Molecular Biology, School of Pharmacy, Iwate Medical University, Nishitokuta, Yahaba, Shiwa-gun, Iwate, Japan.
Journal of bacteriology.J Bacteriol.2013 Nov;195(21):4873-8. doi: 10.1128/JB.00542-13. Epub 2013 Aug 23.
The c subunit of Streptococcus mutans ATP synthase (FoF1) is functionally exchangeable with that of Escherichia coli, since E. coli with a hybrid FoF1 is able to grow on minimum succinate medium through oxidative phosphorylation. E. coli F1 bound to the hybrid Fo with the S. mutans c subunit showed
PMID 23974030

The mitochondrial F1FO-ATPase desensitization to oligomycin by tributyltin is due to thiol oxidation.

Nesci S, Ventrella V, Trombetti F, Pirini M, Pagliarani A.SourceDepartment of Veterinary Medical Sciences, University of Bologna, Via Tolara di Sopra 50, 40064 Ozzano Emilia, Bologna, Italy.
Biochimie.Biochimie.2013 Oct 11. pii: S0300-9084(13)00351-9. doi: 10.1016/j.biochi.2013.10.002. [Epub ahead of print]
The antibiotic oligomycin is known to inhibit mitochondrial F-type ATP synthases. The antibiotic inhibits both ATP synthesis and hydrolysis by blocking the H+ translocation through FO which is coupled to the catalytic activity of F1. The amphiphilic organotin tributyltin (TBT), a known mitochondrial
PMID 24125699

Phosphate release coupled to rotary motion of F1-ATPase.

Okazaki K, Hummer G.SourceDepartment of Theoretical Biophysics, Max Planck Institute of Biophysics, 60438 Frankfurt am Main, Germany.
Proceedings of the National Academy of Sciences of the United States of America.Proc Natl Acad Sci U S A.2013 Oct 8;110(41):16468-73. doi: 10.1073/pnas.1305497110. Epub 2013 Sep 23.
F1-ATPase, the catalytic domain of ATP synthase, synthesizes most of the ATP in living organisms. Running in reverse powered by ATP hydrolysis, this hexameric ring-shaped molecular motor formed by three αβ-dimers creates torque on its central γ-subunit. This reverse operation enables detailed exp
PMID 24062450

Japanese Journal

Implications of the gene for F1-ATPase β subunit (AtpB) for the grain quality of rice matured in a high-temperature environment

Plant biotechnology 33(3), 169-175, 2016-09
NAID 40020996799

アミノ酸レベルの構造が生体分子モーター：F1-ATPaseのエネルギー論に与える影響

大学院研究年報　理工学研究科篇 (第46号/2016), 2016-08-01
NAID 120005851976

22aPS-107 回転軸の長さを半分にしたF1-ATPaseの回転とATP加水分解素過程との連動

日本物理学会講演概要集 71(1), 3317, 2016-03-19
NAID 110010059229

Related Pictures

fof1 atp synthase Fo-F1 ATPase The resulting movie after ATP addition is 403 Forbidden Figure 2: Schematic view of F1-ATPase. The f0f1 atpase by F1-ATPase single molecules : Nature of atp binding affinity of f1 atpase

★リンクテーブル★

リンク元	「proton-translocating ATPase」「H+-ATPase」「F1F0-ATPase」「F1-ATPアーゼ」
拡張検索	「F0F1-ATPase」「mitochondrial F0F1-ATPase」
関連記事	「ATPase」「F」