M. Joanne Lemieux

TL;DR: This work reports the 3.3 angstrom resolution structure of a member of the major facilitator superfamily, GlpT, which transports glycerol-3-phosphate into the cytoplasm and inorganic phosphate into the periplasm and proposes that it operates by a single–binding site, alternating-access mechanism through a rocker-switch type of movement.

TL;DR: The main protease, Mpro (or 3CLpro) in SARS-CoV-2 is a viable drug target because of its essential role in the cleavage of the virus polypeptide and NMR analysis reveals that inhibition proceeds via reversible formation of a hemithioacetal.

TL;DR: NGT, a mechanism-based inhibitor, has been shown to act as a chemical chaperone that prevents misfolding of a Hex A mutant associated with adult onset Tay Sachs disease and, as a result, increases the residual activity of Hex A to a level above the critical threshold for disease.

TL;DR: The structural results on these rhomboid peptidases have allowed us to speculate on the catalytic mechanism of substrate cleavage in a membranous environment and to identify the relative disposition of the nucleophilic serine to the general base/acid function of the conserved histidine.

TL;DR: GC373 and GC376 are potent inhibitors of SARS-CoV-2 in cell culture, with EC50 values near one micromolar and little to no toxicity and the framework for their use in human trials for the treatment of COVID-19 is laid.