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Inside Cover: Tailoring Small Molecules for an Allosteric Site on Procaspase‐6 (ChemMedChem 1/2014)
ChemMedChem2013Vol. 9(1), pp. 2–2
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Jeremy Murray, Anthony M. Giannetti, Micah Steffek, Paul Gibbons, Brian R. Hearn, Frederick Cohen, Christine Tam, Christine D. Pozniak, Brandon Bravo, Joe Lewcock, Priyadarshini Jaishankar, Cuong Q. Ly, Xianrui Zhao, Yinyan Tang, Preeti Chugha, Michelle R. Arkin, John A. Flygare, Adam R. Renslo
Abstract
The inside cover picture shows small molecules tailored for an allosteric site in procaspase-6. The combination of biophysical fragment screening, structure- and computation-aided design, and chemical synthesis enabled the discovery of multiple nanomolar-affinity ligands for this new site. The compounds significantly stabilize the protein, suggesting new avenues for controlling caspase activity and/or activation by allosteric mechanisms. For more details, see the Communication by Jeremy Murray, Adam R. Renslo et al. on p. 73 ff.
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