Probing the interaction of the diarylquinoline TMC207 with its target mycobacterial ATP synthase.
Haagsma, Anna C; Podasca, Ioana; Koul, Anil; Andries, Koen; Guillemont, Jerome; Lill, Holger; Bald, Dirk.
; 6(8): e23575, 2011.
Artigo em Inglês | MEDLINE | ID: mdl-21858172
Nonequilibrium fluctuations of lipid membranes by the rotating motor protein F<sub>1</sub>F<sub>0</sub>-ATP synthase.
Analysis of an N-terminal deletion in subunit a of the Escherichia coli ATP synthase.
The c-ring ion binding site of the ATP synthase from Bacillus pseudofirmusâ OF4 is adapted to alkaliphilic lifestyle.
Microbial Siderophore Enterobactin Promotes Mitochondrial Iron Uptake and Development of the Host via Interaction with ATP Synthase.
Fo-driven Rotation in the ATP Synthase Direction against the Force of F1 ATPase in the FoF1 ATP Synthase.
Remarkable stability of the proton translocating F1FO-ATP synthase from the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1.
Reversible control of F(1)-ATPase rotational motion using a photochromic ATP analog at the single molecule level.
Tracking protons from respiratory chain complexes to ATP synthase c-subunit: The critical role of serine and threonine residues.
Half channels mediating H(+) transport and the mechanism of gating in the Fo sector of Escherichia coli F1Fo ATP synthase.
Structural biology: Toward the ATP synthase mechanism.