Joseph W. Becker

TL;DR: Platensimycin demonstrates strong, broad-spectrum Gram-positive antibacterial activity by selectively inhibiting cellular lipid biosynthesis through the selective targeting of β-ketoacyl-(acyl-carrier-protein (ACP) in the synthetic pathway of fatty acids.

TL;DR: The three-dimensional structure of a complex of the human CED-3 homologue CPP32/apopain with a potent tetrapeptide-aldehyde inhibitor is determined, finding that the protein resembles ICE in overall structure, but its S4 subsite is strikingly different in size and chemical composition.

TL;DR: Comparison of the active site of stromelysin with that of thermolysin reveals that most of the residues proposed to play significant roles in the enzymatic mechanism of temperaturesolysin have equivalents in stromlysin, but that three residues implicated in the catalytic mechanism of Thermolysin are not represented in stamelysin.

TL;DR: The preferred sequence for ICE (WEHD) differs significantly from that found in human pro-interleukin-1beta (YVHD), which suggests that this protease may have additional endogenous substrates, consistent with evidence linking it to apoptosis and IL-1alpha production.

TL;DR: The structures show that inhibitors bind in membrane-embedded pockets of FLAP, which suggests how these inhibitors prevent arachidonic acid from binding to FLAP and subsequently being transferred to 5-lipoxygenase, thereby preventing leukotriene biosynthesis.