Claus Spitzfaden

TL;DR: This work provides new insights into the mechanism of topoisomerase action and a platform for structure-based drug design of a new class of antibacterial agents against a clinically proven, but conformationally flexible, enzyme class.

TL;DR: There is a close correlation between the activity of the benzofurans as inhibitors of fibril formation and their ability to bind to beta-amyloid, as identified by scintillation proximity binding assay and NMR studies.

TL;DR: The first co-crystal structures of the antibacterial QPT-1 and the anticancer drug etoposide with Staphylococcus aureus DNA gyrase are reported, showing binding at the same sites in the cleaved DNA as the fluoroquinolone moxifloxacin.

TL;DR: X-ray crystallographic studies were used to provide insight into the structural basis for the difference in antibacterial potency between enantiomers and advanced studies were reported on compound 1 which demonstrates good PK and in vivo efficacy properties.

TL;DR: A mechanochemical scheme to explain how ATP hydrolysis is coupled to domain motion is proposed that could be applicable not only to GHKL phosphotransferases, but also to unrelated ATPases and GTPases such as Ras.