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Single-molecule analysis of inhibitory pausing states of V1-ATPase.
Uner NE, Nishikawa Y, Okuno D, Nakano M, Yokoyama K, Noji H. Uner NE, et al. Among authors: yokoyama k. J Biol Chem. 2012 Aug 17;287(34):28327-35. doi: 10.1074/jbc.M112.381194. Epub 2012 Jun 26. J Biol Chem. 2012. PMID: 22736762 Free PMC article.
Evidence for rotation of V1-ATPase.
Imamura H, Nakano M, Noji H, Muneyuki E, Ohkuma S, Yoshida M, Yokoyama K. Imamura H, et al. Among authors: yokoyama k. Proc Natl Acad Sci U S A. 2003 Mar 4;100(5):2312-5. doi: 10.1073/pnas.0436796100. Epub 2003 Feb 21. Proc Natl Acad Sci U S A. 2003. PMID: 12598655 Free PMC article.
Rotation of the proteolipid ring in the V-ATPase.
Yokoyama K, Nakano M, Imamura H, Yoshida M, Tamakoshi M. Yokoyama K, et al. J Biol Chem. 2003 Jul 4;278(27):24255-8. doi: 10.1074/jbc.M303104200. Epub 2003 Apr 21. J Biol Chem. 2003. PMID: 12707282 Free article.
We demonstrated recently the rotation of the central stalk subunits in V1, a catalytic sector of V0V1-ATPase (Imamura, H., Nakano, M., Noji, H., Muneyuki, E., Ohkuma, S., Yoshida, M., and Yokoyama, K. (2003) Proc. Natl. Acad. Sci. U. S. A. 100, 2312-2315), but the r …
We demonstrated recently the rotation of the central stalk subunits in V1, a catalytic sector of V0V1-ATPase (Imamura, H., Nakano, M., Noji, …
Subunit arrangement in V-ATPase from Thermus thermophilus.
Yokoyama K, Nagata K, Imamura H, Ohkuma S, Yoshida M, Tamakoshi M. Yokoyama K, et al. J Biol Chem. 2003 Oct 24;278(43):42686-91. doi: 10.1074/jbc.M305853200. Epub 2003 Aug 11. J Biol Chem. 2003. PMID: 12913005 Free article.
Based on these observations and our recent demonstration that D, F, and L subunits rotate relative to A3B3 (Imamura, H., Nakano, M., Noji, H., Muneyuki, E., Ohkuma, S., Yoshida, M., and Yokoyama, K. (2003) Proc. Natl. Acad. Sci. U. S. A. 100, 2312-2315; Yokoyama
Based on these observations and our recent demonstration that D, F, and L subunits rotate relative to A3B3 (Imamura, H., Nakano, M., Noji, H …
Leu309 plays a critical role in the encapsulation of substrate protein into the internal cavity of GroEL.
Koike-Takeshita A, Shimamura T, Yokoyama K, Yoshida M, Taguchi H. Koike-Takeshita A, et al. Among authors: yokoyama k. J Biol Chem. 2006 Jan 13;281(2):962-7. doi: 10.1074/jbc.M506298200. Epub 2005 Oct 20. J Biol Chem. 2006. PMID: 16239229 Free article.
The side chain of Leu, in the GXXLE region, forms a hydrophobic cluster with residues of the H helix (Shimamura, T., Koike-Takeshita, A., Yokoyama, K., Masui, R., Murai, N., Yoshida, M., Taguchi, H., and Iwata, S. (2004) Structure (Camb.) 12, 1471-1480). ...
The side chain of Leu, in the GXXLE region, forms a hydrophobic cluster with residues of the H helix (Shimamura, T., Koike-Takeshita, A., …
3,411 results