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1 n in the MTATP6 subunit of the mitochondrial F1F0-ATPase.
2 s dependent on the activity of mitochondrial F1F0-ATPase.
3 T8993G mutation results in loss of assembled F1F0-ATPase.
4  transporter, or by direct inhibition of the F1F0-ATPase.
5 ose genes encode the various subunits of the F1F0-ATPase.
6 carbodiimide (DCCD), a specific inhibitor of F1F0-ATPase.
7 ollowing ATP hydrolysis by the mitochondrial F1F0-ATPase.
8 opy models of either V-ATPase or the related F1F0-ATPase.
9 term or long-term acid survival capacity and F1F0 ATPase activity remained unaffected in the mutants.
10 ntibodies to the beta- and gamma-subunits of F1F0-ATPase (anti-beta, anti-gamma) occur.
11 lta psi m is maintained by the mitochondrial F1F0-ATPase at the expense of ATP reserves.
12 . subtilis deleted in atp genes encoding the F1F0-ATPase (BD99-A), glucose energized Na+ exclusion in
13 clone the gene (atpD) encoding the H. pylori F1F0-ATPase beta subunit.
14      The deduced amino acid sequences of the F1F0-ATPase beta subunits from H. pylori and Wolinella s
15 chia coli mutants in the beta subunit of the F1F0-ATPase can be complemented with the beta subunit fr
16 ADH-ubiquinone oxidoreductase (complex I) or F1F0-ATPase (complex V) also precipitated a 45-kDa prote
17 cassette and sought to construct an isogenic F1F0-ATPase H. pylori mutant by natural transformation a
18             A mutant of the Escherichia coli F1F0-ATPase has been generated (alphaQ2C) in which the g
19  that more c subunits are assembled into the F1F0 ATPase in cells grown on glucose than in cells grow
20  characterize a potential functional role of F1F0-ATPase in H. pylori, H. pylori or Escherichia coli
21 potential energy and the formation of ATP by F1F0-ATPase in heart and skeletal muscle mitochondria.
22 ole of IF1 (the natural inhibitor protein of F1F0-ATPase) in cancer cell metabolism is still uncertai
23 lipoprotein (SmpA), and the C subunit of the F1F0 ATPase indicated that the lowest-density membrane f
24    In the presence of oligomycin (Oligo), an F1F0-ATPase inhibitor, the decrease in pH(i) was attenua
25 dle, which is different from all other known F1F0-ATPase inhibitors.
26                     The proton-translocating F1F0-ATPase is an important enzyme for regulating intrac
27 odiazepine derivate blocks the mitochondrial F1F0-ATPase, leads to a surplus production of mitochondr
28         Furthermore, we demonstrate that the F1F0-ATPase monomers present in su e null mutant mitocho
29 ly been demonstrated that the binding of the F1F0-ATPase natural inhibitor protein to purified bovine
30 ntibodies to the beta- and gamma-subunits of F1F0-ATPase occur in anti-M2 positive and -negative PBC
31 e structural data suggest a new mechanism of F1F0-ATPase regulation in alpha-proteobacteria.
32 re recently discovered alpha-proteobacterial F1F0-ATPase-regulatory proteins representing a Pfam prot
33 ate primers derived from conserved bacterial F1F0-ATPase sequences to PCR amplify and clone the gene
34 mechanisms to cope with acidic environments (F1F0-ATPase system, fatty acid biosynthesis, branched ch
35 cessing of only one, the beta subunit of the F1F0 ATPase, was dramatically affected.

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