The F1F0–ATP synthase exists as a dimer in mitochondria, where it is essential for the
biogenesis of the inner membrane cristae. How two ATP synthase complexes dimerize to …

The effect of increased expression or reconstitution of the mitochondrial inhibitor protein
(IF1) on the dimer/monomer ratio (D/M) of the rat liver and bovine heart F1F0-ATP synthase …

Solubilization of heavy bovine heart mitochondria with Triton X-100 leads to the selective
extraction of F0F1ATP synthase monomer and dimer in a 2: 1 ratio, as revealed by blue …

Inhibition of the yeast F0F1-ATP synthase by the regulatory peptides IF1 and STF1 was
studied using intact mitochondria and submitochondrial particles from wild-type cells or from …

IF1, an inhibitor protein of mitochondrial ATP synthase, suppresses ATP hydrolytic activity of
F1. One of the unique features of IF1 is the selective inhibition in mitochondrial F1 (MF1); it …

Cross-linking experiments showed that the supernumerary subunit i is close to the interface
between two ATP synthases. These data were used to demonstrate the presence of ATP …

The ATPase inhibitor protein (IP) of mitochondria was detected in the plasma membrane of
living endothelial cells by flow cytometry, competition assays, and confocal microscopy of …

The inhibitor protein IF 1 is a basic protein of 84 residues which inhibits the ATPase activity
of the mitochondrial F o F 1-ATP synthase complex without having any effect on ATP …

The location of the endogenous inhibitor protein (IF 1) in the rotor/stator architecture of the
bovine mitochondrial ATP synthase was studied by reversible cross-linking with dithiobis …

Human placenta maintains pregnancy. The mitochondria of this tissue synthesize
pregnenolone (P5) from cholesterol through a transport chain formed by adrenodoxin …