Cryo-EM studies of the rotary H+-ATPase/synthase from Thermus thermophilus
Author:
Affiliation:
1. Department of Molecular Biosciences, Kyoto Sangyo University
2. Research Center for Ultra-High Voltage Electron Microscopy, Osaka University
Publisher
Biophysical Society of Japan
Subject
General Medicine
Link
https://www.jstage.jst.go.jp/article/biophysico/16/0/16_140/_pdf
Reference22 articles.
1. [1] Yoshida, M., Muneyuki, E. & Hisabori, T. ATP synthase—a marvellous rotary engine of the cell. Nat. Rev. Mol. Cell Biol. 2, 669–677 (2001).
2. [2] Forgac, M. Vacuolar ATPases: rotary proton pumps in physiology and pathophysiology. Nat. Rev. Mol. Cell Biol. 8, 917–929 (2007).
3. [3] Yokoyama, K. & Imamura, H. Rotation, structure, and classification of prokaryotic V-ATPase. J. Bioenerg. Biomembr. 37, 405–410 (2005).
4. [4] Imamura, H., Nakano, M., Noji, H., Muneyuki, E., Ohkuma, S., Yoshida, M., et al. Evidence for rotation of V1-ATPase. Proc. Natl. Acad. Sci. USA 100, 2312–2315 (2003).
5. [7] Kobayashi, H. A proton-translocating ATPase regulates pH of the bacterial cytoplasm. J. Biol. Chem. 260, 72–76 (1985).
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