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1 ification of synaptic vesicles relies on the vacuolar-type ATPase (V-ATPase) and provides the electro
2 , we demonstrate that inhibition of the H(+) vacuolar-type ATPase (V-ATPase) caused drastic cell swel
4 the antitumor activity of inhibitors of the vacuolar-type ATPase (V-ATPase), a heteromultimeric prot
8 Based upon the precedent of the subunit c in vacuolar-type ATPases, which are composed of four transm
11 etreatment of oocytes with bafilomycin A1, a vacuolar type H+-ATPase inhibitor, abolished the increas
12 afficking of soluble proteins, requires both vacuolar-type H(+) ATPase-dependent acidification as wel
13 ies have suggested that the V0 domain of the vacuolar-type H(+)-adenosine triphosphatase (V-ATPase) i
18 clone encoding the c ("16 kDa') subunit of a vacuolar-type H(+)-ATPase (V-ATPase) from Kalanchoe daig
19 fication of endomembrane compartments by the vacuolar-type H(+)-ATPase (V-ATPase) is central to many
20 y and polarity-dependent localization of the vacuolar-type H(+)-ATPase (V-ATPase) mediate the impact
21 by 25 microm bafilomycin-A1, an inhibitor of vacuolar-type H(+)-ATPase (v-ATPase), which actively pum
24 ctor binds to the conserved Vo domain of the vacuolar-type H(+)-ATPase and causes deacidification of
26 ltaneously, MDMs increased the expression of vacuolar-type H(+)-ATPase components, acidified the peri
27 ng of phagosomal acidification by inhibiting vacuolar-type H(+)-ATPase enabled macrophages to elicit
28 ake in vesicles, because bafilomycin A(1), a vacuolar-type H(+)-ATPase inhibitor, reduced glutamate r
29 din B is structurally similar to more potent vacuolar-type H(+)-ATPase inhibitors, which all inhibite
31 CO2 Bafilomycin A1, a specific inhibitor of vacuolar-type H(+)-ATPase that blocks lysosomal degradat
32 et membranes dictate its preference for host vacuolar-type H(+)-ATPase-containing membranes, indicati
35 ication of intracellular compartments by the vacuolar-type H(+)-ATPases (VHA) is known to energize io
36 e isolation and characterization of a type I vacuolar-type H(+)-pyrophosphatase (V-PPase), TgVP1, fro
37 determinant of acidic pH at the Golgi is the vacuolar-type H(+)-translocating ATPase (V-ATPase), whos
45 ept those with deletions of YCK3, encoding a vacuolar type I casein kinase; SVP26, encoding an endopl
48 ribution of the conserved residues among the vacuolar-type proteolipids suggest a zipper-type interac
50 era raised against a peptide sequence of the vacuolar type proton pyrophosphatase (H(+)-PPase) of Ara
55 r assembly with the catalytic sector (V1) of vacuolar-type proton translocating ATPase (V-ATPase) and
56 idic calcium store in trypanosomatids with a vacuolar-type proton-pumping pyrophosphatase (V-H(+)-PPa
61 (Baf), a potent and specific blocker of the vacuolar-type (V-type) ATPase, which eliminates the driv
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