Andrew P. Fosberry

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: A crystal structure of moxifloxacin in complex with Acinetobacter baumannii topoisomerase IV now shows the wedge-shaped quinolone stacking between base pairs at the DNA cleavage site and binding conserved residues in theDNA cleavage domain through chelation of a noncatalytic magnesium ion.

TL;DR: Results show that compound 4 is representative of a new, totally synthetic series of antibacterial agents that has the potential to provide novel alternatives for the treatment of S. aureus infections that are resistant to the present armory of antibiotics.

TL;DR: Although the expression of Sema7A was demonstrated in lymphoid and myeloid cells, no stimulation of cytokine production or proliferation was evident in B or T cells, and Sema 7A is an extremely potent monocyte activator, stimulating chemotaxis at 0.1 pm and inflammatory cytokineproduction and superoxide release at 1–10‰pm.

TL;DR: Crystal structures of this class of potent and specific inhibitors of bacterial tyrosyl‐tRNA synthetases may contribute to the understanding of the catalytic mechanism and provide the structural basis for designing novel antimicrobial agents.