Selectivity of TMC207 towards mycobacterial ATP synthase compared with that towards the eukaryotic homologue.
Haagsma, Anna C; Abdillahi-Ibrahim, Rooda; Wagner, Marijke J; Krab, Klaas; Vergauwen, Karen; Guillemont, Jerome; Andries, Koen; Lill, Holger; Koul, Anil; Bald, Dirk.
Antimicrob Agents Chemother
; 53(3): 1290-2, 2009 Mar.
Artigo em Inglês | MEDLINE | ID: mdl-19075053
Assembly of the membrane domain of ATP synthase in human mitochondria.
Budowa, biogeneza i mechanizm dzialania kompleksu mitochondrialnej syntazy ATP.
Interacting cytoplasmic loops of subunits a and c of Escherichia coli F1F0 ATP synthase gate H+ transport to the cytoplasm.
ATP synthase from <i>Trypanosoma brucei</i> has an elaborated canonical F<sub>1</sub>-domain and conventional catalytic sites.
Organization of Subunits in the Membrane Domain of the Bovine F-ATPase Revealed by Covalent Cross-linking.
The region from phenylalanine-28 to lysine-50 of a yeast mitochondrial ATPase inhibitor (IF1) forms an α-helix in solution.
Mitochondrial permeability transition involves dissociation of F<sub>1</sub>F<sub>O</sub> ATP synthase dimers and C-ring conformation.
The structure of the membrane extrinsic region of bovine ATP synthase.
Regulation of Aerobic Energy Metabolism in Podospora anserina by Two Paralogous Genes Encoding Structurally Different c-Subunits of ATP Synthase.
Rate of hydrolysis in ATP synthase is fine-tuned by α-subunit motif controlling active site conformation.