In this review we discuss the role of ATP synthase as a molecular drug target for natural and
synthetic antimicrobial/antitumor peptides. We start with an introduction of the universal …

The F 1-ATPase is the catalytic portion of the F o F 1 ATP synthase and acts as a rotary
molecular motor when it hydrolyzes ATP. Two decades have passed since the single …

The aim of this study was to determine if the dietary benefits of bioflavonoids are linked to
the inhibition of ATP synthase. We studied the inhibitory effect of 17 bioflavonoid compounds …

The crystal structure of yeast mitochondrial F1 ATPase contains three independent copies of
the complex, two of which have similar conformations while the third differs in the position of …

We have studied the inhibitory effect of five polyphenols namely, resveratrol, piceatannol,
quercetin, quercetrin, and quercetin-3-β-d glucoside on Escherichia coli ATP synthase …

In this review we discuss the inhibitory effects of dietary polyphenols and amphibian
antimicrobial/antitumor peptides on ATP synthase. In the beginning general structural …

Previously melittin, the α-helical basic honey bee venom peptide, was shown to inhibit F1-
ATPase by binding at the β-subunit DELSEED motif of F1Fo-ATP synthase. Herein, we …

Pentatricopeptide repeat (PPR) proteins are involved in the C-to-U RNA editing of organellar
transcripts. The maize genome contains over 600 PPR proteins and few have been found to …

Insect venom peptides (IVPs) eumenitin, lasiocepsin, lycosin1, mastoparanB, panurgine1,
and protonectin possess antibacterial properties, and the ubiquitous enzyme ATP synthase …

In this paper we present the inhibitory effect of a variety of structurally modulated/modified
polyphenolic compounds on purified F1 or membrane bound F1FoEscherichia coli ATP …