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
The c-ring ion binding site of the ATP synthase from Bacillus pseudofirmusâ OF4 is adapted to alkaliphilic lifestyle.
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.
Fo-driven Rotation in the ATP Synthase Direction against the Force of F1 ATPase in the FoF1 ATP Synthase.
Thermodynamic analyses of nucleotide binding to an isolated monomeric ß subunit and the α3ß3Î³ subcomplex of F1-ATPase.
Remarkable stability of the proton translocating F1FO-ATP synthase from the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1.
Obstruction of transmembrane helical movements in subunit a blocks proton pumping by F1Fo ATP synthase.
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.
Conformational transitions of subunit epsilon in ATP synthase from thermophilic Bacillus PS3.