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Solution structure of the epsilon subunit of the F1-ATPase from Escherichia coli and interactions of this subunit with beta subunits in the complex.
Wilkens S, Capaldi RA. Wilkens S, et al. J Biol Chem. 1998 Oct 9;273(41):26645-51. doi: 10.1074/jbc.273.41.26645. J Biol Chem. 1998. PMID: 9756905 Free article.
This subunit has a two-domain structure with an N-terminal 10-stranded beta sandwich and a C-terminal antiparallel two alpha-helix hairpin, as described previously (Wilkens, S., Dahlquist, F. W., McIntosh, L. P., Donaldson, L. W., and Capaldi, R. ...
This subunit has a two-domain structure with an N-terminal 10-stranded beta sandwich and a C-terminal antiparallel two alpha-helix hairpin, …
Localization of subunit C (Vma5p) in the yeast vacuolar ATPase by immuno electron microscopy.
Zhang Z, Inoue T, Forgac M, Wilkens S. Zhang Z, et al. Among authors: wilkens s. FEBS Lett. 2006 Apr 3;580(8):2006-10. doi: 10.1016/j.febslet.2006.03.001. Epub 2006 Mar 10. FEBS Lett. 2006. PMID: 16546180 Free article.
The data show that subunit C is binding at the interface of the ATPase and proton channel, opposite from another stalk density previously identified as subunit H [Wilkens S., Inoue T., and Forgac M. (2004) Three-dimensional structure of the vacuolar ATPase - Localiz …
The data show that subunit C is binding at the interface of the ATPase and proton channel, opposite from another stalk density previously id …
Structure of the yeast vacuolar ATPase.
Zhang Z, Zheng Y, Mazon H, Milgrom E, Kitagawa N, Kish-Trier E, Heck AJ, Kane PM, Wilkens S. Zhang Z, et al. Among authors: wilkens s. J Biol Chem. 2008 Dec 19;283(51):35983-95. doi: 10.1074/jbc.M805345200. Epub 2008 Oct 27. J Biol Chem. 2008. PMID: 18955482 Free PMC article.
Domain architecture of the stator complex of the A1A0-ATP synthase from Thermoplasma acidophilum.
Kish-Trier E, Wilkens S. Kish-Trier E, et al. Among authors: wilkens s. J Biol Chem. 2009 May 1;284(18):12031-40. doi: 10.1074/jbc.M808962200. Epub 2009 Feb 20. J Biol Chem. 2009. PMID: 19234304 Free PMC article.
Previously, we have characterized the peripheral stalk forming subunits E and H of the A-ATPase from Thermoplasma acidophilum and demonstrated that the two polypeptides interact to form a stable heterodimer with 1:1 stoichiometry (Kish-Trier, E., Briere, L. K., Dunn, S. D. …
Previously, we have characterized the peripheral stalk forming subunits E and H of the A-ATPase from Thermoplasma acidophilum and demonstrat …
144 results