Electron cryomicroscopy observation of rotational states in a eukaryotic V-ATPase
Author:
Publisher
Springer Science and Business Media LLC
Subject
Multidisciplinary
Link
http://www.nature.com/articles/nature14365.pdf
Reference51 articles.
1. Sumner, J. P. et al. Regulation of plasma membrane V-ATPase activity by dissociation of peripheral subunits. J. Biol. Chem. 270, 5649–5653 (1995)
2. Kane, P. M. Disassembly and reassembly of the yeast vacuolar H+-ATPase in vivo. J. Biol. Chem. 270, 17025–17032 (1995)
3. Pänke, O., Cherepanov, D. A., Gumbiowski, K., Engelbrecht, S. & Junge, W. Viscoelastic dynamics of actin filaments coupled to rotary F-ATPase: angular torque profile of the enzyme. Biophys. J. 81, 1220–1233 (2001)
4. Stewart, A. G., Lee, L. K., Donohoe, M., Chaston, J. J. & Stock, D. The dynamic stator stalk of rotary ATPases. Nature Commun. 3, 687 (2012)
5. Zhou, M. et al. Ion mobility–mass spectrometry of a rotary ATPase reveals ATP-induced reduction in conformational flexibility. Nature Chem. 6, 208–215 (2014)
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