Drug targeting Nsp1-ribosome interaction shows rescue of Nsp1-mediated translation inhibition and has antiviral activity against SARS-CoV-2.

When antiviral compounds target oligomeric assemblages, the formation of chimeric oligomers within cells can negate selection for naturally occurring drug-resistant variants.

High-throughput and ultra-stable magnetic tweezers reveal that Remdesivir induces a long-lived backtrack pause upon incorporation by the coronavirus polymerase, and SARS-CoV-2 is able to evade interferon-induced antiviral ddhCTP.

Interactions between viral genomes within the same cells can impact the selection of drug-resistant variants and this has been finessed by hepatitis C virus.

Studies of the substrate selectivity of concentrative nucleoside transporters provide proof of principle for structure-based improvement of drug delivery by these transporters.

Shortened hepatitis C therapy, with retreatment if needed, can reduce antiviral drug use in patients with mild liver disease, but day 2 viral load is not an adequate predictor of outcome.

Exploiting virus-encoded ion channels as drug targets drove a multi-faceted approach to deriving potent small molecules targeting HCV p7, simultaneously providing new insights into its fundamental biology.

High-resolution structures of HIV-1 RT in complex with two newly developed non-nucleoside inhibitors explain how they retain antiviral activities against drug-resistant RT mutants with considerably reduced susceptibility to rilpivirine.

Favipiravir, a novel nucleoside analogue, can clear a persistent norovirus infection in vivo through lethal mutagenesis.

GRL-142 is an HIV protease inhibitor with a unique structure and atto-to-picomolar potency against a wide range of HIV strains.