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Structure of the NS2B-NS3 protease from Zika virus after self-cleavage
The structural and functional insights of the ZikV protease presented here should advance the current understanding of flavivirus replication and accelerate structure-based antiviral drug discovery against ZIKV.
Crystal structure of unlinked NS2B-NS3 protease from Zika virus
High-resolution crystal structures of the ZIKV NS2B-NS3 protease reveal that, unlike in other flaviviruses, the protease adopts a closed conformation, in whichNS2B engages NS3 to form an empty substrate-binding site, making it an attractive antiviral drug target.
Structure of the Cyclic Nucleotide-Binding Homology Domain of the hERG Channel and Its Insight into Type 2 Long QT Syndrome
The structural study reveals that the CNBHD adopts a similar fold to other KCNH channels, and it is self-liganded and it contains a short β-strand that blocks the nucleotide-binding pocket in the β-roll.
Structural Dynamics of Zika Virus NS2B-NS3 Protease Binding to Dipeptide Inhibitors.
Membrane topology of NS2B of dengue virus revealed by NMR spectroscopy.
Solution NMR Spectroscopy in Target-Based Drug Discovery
The possible roles of NMR spectroscopy in drug discovery are described and several examples demonstrating the roles are included such as hit identification, ranking ligand binding affinities, and mapping the ligandbinding site are included.
Structural Insights into the Inhibition of Zika Virus NS2B-NS3 Protease by a Small-Molecule Inhibitor.
Secondary Structure and Membrane Topology of the Full-Length Dengue Virus NS4B in Micelles.
Atomic level information for an important drug target to control flavivirus infections is provided and backbone resonance assignment of NS4B was obtained using conventional solution NMR experiments.
Secondary structure and membrane topology of dengue virus NS4A protein in micelles.
Targeting the Bacterial Epitranscriptome for Antibiotic Development: Discovery of Novel tRNA-(N1G37) Methyltransferase (TrmD) Inhibitors.
A widely applicable, radioactivity-free, bioluminescence-based high-throughput screen (HTS) against 116350 compounds from structurally diverse small-molecule libraries to identify inhibitors of Pseudomonas aeruginosa TrmD ( PaTrmD), expanding the repertoire of Trmd-inhibiting molecular scaffolds that show promise for antibiotic development.