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Murata, T., Yamamoto, I., Kakinuma, Y., Leslie, A. G. & Walker, J. E. Structure of the rotor of the V-type Na-ATPase from Enterococcus hirae. Science 308, 654-659 (2005). The first high-resolution structure of an A-ATPase subcomplex (namely the proteolipid ring from E. hirae).
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Wang, Y., Inoue, T. & Forgac, M. TM2 but not TM4 of subunit c″ interacts with TM7 of subunit a of the yeast V-ATPase as defined by disulfide-mediated cross-linking. J. Biol. Chem. 279, 44628-44638 (2004).
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Wang, Y., Inoue, T. & Forgac, M. TM2 but not TM4 of subunit c″ interacts with TM7 of subunit a of the yeast V-ATPase as defined by disulfide-mediated cross-linking. J. Biol. Chem. 279, 44628-44638 (2004).
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22
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Localization of subunits D, E and G in the yeast V-ATPase complex using cysteine-mediated crosslinking to subunit B
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Wilkens, S., Inoue, T. & Forgac, M. Three-dimensional structure of the vacuolar ATPase - localization of subunit H by difference imaging and chemical cross-linking. J. Biol. Chem. 279, 41942-41949 (2004). Describes the first use of a combination of EM image analysis and photoactivated cross-linking to localize a subunit in the V-ATPase.
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Wilkens, S., Inoue, T. & Forgac, M. Three-dimensional structure of the vacuolar ATPase - localization of subunit H by difference imaging and chemical cross-linking. J. Biol. Chem. 279, 41942-41949 (2004). Describes the first use of a combination of EM image analysis and photoactivated cross-linking to localize a subunit in the V-ATPase.
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25
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Localization of subunit C (Vma5p) in the yeast vacuolar ATPase by immunoelectron microscopy
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Curtis, K. K. & Kane, P. M. Novel V-ATPase complexes resulting from overproduction of Vma5p and Vma13p. J. Biol. Chem. 277, 2716-2724 (2002). This study provided important insight into the function of two regulatory subunits.
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The amino-terminal domain of the V-ATPase a subunit controls targeting and in vivo dissociation and the carboxyl-terminal domain affects coupling of proton transport and ATP hydrolysis
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Kawasaki-Nishi, S., Bowers, K., Nishi, T., Forgac, M. & Stevens, T. H The amino-terminal domain of the V-ATPase a subunit controls targeting and in vivo dissociation and the carboxyl-terminal domain affects coupling of proton transport and ATP hydrolysis. J. Biol. Chem. 276, 47411-47420 (2001).
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46
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Yeast V-ATPase complexes containing different isoforms of the 100-kDa a-subunit differ in coupling efficiency and in vivo dissociation
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This study provided an important insight into the functional differences between isoforms of subunit a
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Kawasaki-Nishi, S., Nishi, T. & Forgac, M. Yeast V-ATPase complexes containing different isoforms of the 100-kDa a-subunit differ in coupling efficiency and in vivo dissociation. J. Biol. Chem. 276, 17941-17948 (2001). This study provided an important insight into the functional differences between isoforms of subunit a.
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+-ATPase with the a3 isoform during osteoclast differentiation. J. Biol. Chem. 278, 22023-22030 (2003). This study indicated that V-ATPase localization that is directed by isoforms of subunit a is not necessarily static.
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+-ATPase with the a3 isoform during osteoclast differentiation. J. Biol. Chem. 278, 22023-22030 (2003). This study indicated that V-ATPase localization that is directed by isoforms of subunit a is not necessarily static.
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49
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Distinct expression patterns of different subunit isoforms of the V-ATPase in the rat epididymis
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+ATPase a subunit to nerve terminals where it associates with both synaptic vesicles and the presynaptic plasma membrane
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+ATPase a subunit to nerve terminals where it associates with both synaptic vesicles and the presynaptic plasma membrane. J. Cell Sci. 116, 4751-4762 (2003).
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Hurtado-Lorenzo, A. et al. V-ATPase interacts with ARNO and Arf6 in early endosomes and regulates the protein degradative pathway. Nature Cell Biol. 8, 124-136 (2006). This finding suggests that V-ATPase subunits interact with other parts of the trafficking machinery in a pH-dependent manner.
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Hurtado-Lorenzo, A. et al. V-ATPase interacts with ARNO and Arf6 in early endosomes and regulates the protein degradative pathway. Nature Cell Biol. 8, 124-136 (2006). This finding suggests that V-ATPase subunits interact with other parts of the trafficking machinery in a pH-dependent manner.
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52
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Sun-Wada, G. H., Yoshimizu, T., Imai-Senga, Y., Wada, Y. & Futai, M. Diversity of mouse proton-translocating ATPase: presence of multiple isoforms of the C, d and G subunits. Gene 302, 147-153 (2003).
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