H
Holger Lill
Researcher at VU University Amsterdam
Publications - 68
Citations - 3128
Holger Lill is an academic researcher from VU University Amsterdam. The author has contributed to research in topics: ATP synthase & Protein subunit. The author has an hindex of 28, co-authored 63 publications receiving 2828 citations. Previous affiliations of Holger Lill include University of Western Ontario & University of Amsterdam.
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Journal ArticleDOI
ATP synthase: an electrochemical transducer with rotatory mechanics.
TL;DR: How ion flow through the membrane-intrinsic portion, F0, may generate torque and how this might be transmitted between stator and rotor to finally expel spontaneously formed ATP from F1 into water is discussed.
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Diarylquinolines target subunit c of mycobacterial ATP synthase.
Anil Koul,Najoua Dendouga,Karen Vergauwen,Brenda Molenberghs,Luc Vranckx,Rudy Edmond Willebrords,Zorica Ristic,Holger Lill,Ismet Dorange,Jerome Guillemont,Dirk Bald,Koen Andries +11 more
TL;DR: It is established by genetic, biochemical and binding assays that the oligomeric subunit c (AtpE) of ATP synthase is the target of R207910, and targeting energy metabolism is a new, promising approach for antibacterial drug discovery.
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Selectivity of TMC207 towards Mycobacterial ATP Synthase Compared with That towards the Eukaryotic Homologue
Anna C. Haagsma,Rooda Abdillahi-Ibrahim,Marijke J. Wagner,Klaas Krab,Karen Vergauwen,Jerome Emile Georges Guillemont,Koen Andries,Holger Lill,Anil Koul,Dirk Bald +9 more
TL;DR: Results suggest that TMC207 may not elicit ATP synthesis-related toxicity in mammalian cells, and ATP synthase, although highly conserved between prokaryotes and eukaryotes, may still qualify as an attractive antibiotic target.
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Probing the interaction of the diarylquinoline TMC207 with its target mycobacterial ATP synthase.
Anna C. Haagsma,Anna C. Haagsma,Ioana Podasca,Ioana Podasca,Anil Koul,Koen Andries,Jerome Guillemont,Holger Lill,Holger Lill,Dirk Bald,Dirk Bald +10 more
TL;DR: The results are consistent with previous docking studies and provide experimental support for a predicted function of TMC207 in mimicking key residues in the proton transfer chain and blocking rotary movement of subunit c during catalysis.
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Transport of cytochrome c derivatives by the bacterial Tat protein translocation system.
TL;DR: It is concluded that, in addition to the nature of the specific signal peptide, the folding state of a particular protein also governs its acceptance by a given transport system.