Daniel R. Gentry

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: The sigB gene of Staphylococcus aureus, coding for the alternate sigma factor B, has been deleted by allelic replacement mutagenesis and the mutant grew as well as the parent in vitro, although it was deficient in clumping factor, coagulase, and pigment.

TL;DR: The availability of purified and characterized S. pneumoniae FabH will greatly aid in structural studies of this class of essential bacterial enzymes and facilitate the identification of small molecule inhibitors of type II fatty acid synthase with the potential to be novel and potent antibacterial agents active against pathogenic bacteria.

TL;DR: Optimized compounds show excellent antibacterial activity against staphylococcal and enterococcal pathogens, including strains resistant to clinical antibiotics, and demonstrated in vivo efficacy in an S. aureus rat abscess infection model.

TL;DR: It is likely that target-specific resistance to retapamulin will be slow to emerge due to the need for three mutations for a significant effect on activity and the fitness cost of each mutational step, and mutations in rplC that lead to pleuromutilin resistance have a direct, negative effect on fitness.