Mark Bartlam

TL;DR: Using intense synchrotron sources, it is observed that six different ex vivo amyloid fibrils and two synthetic fibril preparations all gave similar high-resolution X-ray fibre diffraction patterns, consistent with a helical array of beta-sheets parallel to the fibre long axis, with the strands perpendicular to this axis, which confirms that amyloidsfibrils comprise a structural superfamily and share a common protofilament substructure.

TL;DR: This series of crystal structures, which is the first, to the authors' knowledge, of any protein from the SARS virus, reveal substantial pH-dependent conformational changes, and an unexpected mode of inhibitor binding, providing a structural basis for rational drug design.

TL;DR: The structure correlates the protein environments around prosthetic groups with their unique midpoint redox potentials and provides a bona fide model for study of the mitochondrial respiratory system and human mitochondrial diseases related to mutations in this complex.

TL;DR: A structure-assisted optimization program has yielded compounds with fast in vitro inactivation of multiple CoV Mpros, potent antiviral activity, and extremely low cellular toxicity in cell-based assays.

TL;DR: Structural comparisons and mutagenesis analysis of the motif identified in PAN provide further evidence that PAN holds an endonuclease active site and has critical roles in end onuclease activity of the influenza virus polymerase, rather than PB1.