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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
3                                          The vacuolar-type ATPase (V-ATPase) is a proton pump compose
4  the antitumor activity of inhibitors of the vacuolar-type ATPase (V-ATPase), a heteromultimeric prot
5                Instead, an H+ translocating, vacuolar-type ATPase generates a voltage of approximatel
6                                              Vacuolar-type ATPases (V-ATPases) are ATP-powered proton
7                                              Vacuolar-type ATPases (V-ATPases) exist in various cellu
8 Based upon the precedent of the subunit c in vacuolar-type ATPases, which are composed of four transm
9                                         This vacuolar-type Ca(2+)-ATPase could play an important role
10 ipropylamine and stained weakly positive for vacuolar type H+ ATPase.
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
14       Without actin, lysosomes never recycle vacuolar-type H(+)-adenosine triphosphatase (V-ATPase) o
15                    We show that the neuronal vacuolar-type H(+)-adenosine triphosphatase V0 subunit a
16 at the regulation occurs on the level of the vacuolar-type H(+)-adenosine triphosphatase.
17  and expression of the proton pumping enzyme vacuolar-type H(+)-adenosine triphosphatase.
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
22 rom inhibition of proton pumping activity of vacuolar-type H(+)-ATPase (v-ATPase).
23 but is not dependent on Na(+)-H+ exchange or vacuolar-type H(+)-ATPase activity.
24 ctor binds to the conserved Vo domain of the vacuolar-type H(+)-ATPase and causes deacidification of
25                             Mutations in the vacuolar-type H(+)-ATPase B1 subunit gene ATP6V1B1 cause
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
30                        Proton pumping of the vacuolar-type H(+)-ATPase into the lumen of the central
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
33 e electrochemical gradient maintained by the vacuolar-type H(+)-ATPase.
34                                              Vacuolar-type H(+)-ATPases (V-H(+)-ATPases) are the majo
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
38                             The multisubunit vacuolar-type H(+)ATPases mediate acidification of vario
39                                              Vacuolar-type H+-ATPase (V-ATPase) and calcineurin (Cn)
40                                              Vacuolar-type H+-ATPase was not colocalized with HGE age
41                                              Vacuolar-type H+-translocating ATPases (V-ATPases or V-p
42                                          The vacuolar-type H+-transporting ATPase (V-ATPase), rather
43                          The presence of the vacuolar-type (H+) ATPase (V-ATPase) within the Coxiella
44 filomycin, consistent with a major role of a vacuolar-type (H+)-ATPase in this process.
45 ept those with deletions of YCK3, encoding a vacuolar type I casein kinase; SVP26, encoding an endopl
46                        Secreted A1AT carried vacuolar-type paucimannosidic N-glycans generated by the
47                        The gene encoding the vacuolar-type proteolipid of the V-ATPase from Giardia l
48 ribution of the conserved residues among the vacuolar-type proteolipids suggest a zipper-type interac
49                                          The vacuolar type proton pump of clathrin-coated vesicles ha
50 era raised against a peptide sequence of the vacuolar type proton pyrophosphatase (H(+)-PPase) of Ara
51                                          The vacuolar type proton-translocating ATPase of clathrin-co
52                          However, it affects vacuolar-type proton ATPase (V-ATPase) activity, thereby
53                                          The vacuolar-type proton pump of clathrin-coated vesicles is
54 oton gradient maintained by an ATP-dependent vacuolar-type proton pump.
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
57                             The multisubunit vacuolar-type proton-translocating ATPases (H(+)-ATPases
58                                          The vacuolar-type proton-translocating pyrophosphatase (V-H+
59                                          The vacuolar-type, proton-translocating ATPase (V-ATPase) is
60                       Subunit a of the yeast vacuolar-type, proton-translocating ATPase enzyme comple
61  (Baf), a potent and specific blocker of the vacuolar-type (V-type) ATPase, which eliminates the driv
62             The membrane rotor ring from the vacuolar-type (V-type) sodium ion-pumping adenosine trip

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