Highly pathogenic influenza virus strains currently in circulation pose a significant risk of a
global pandemic. Following the reported crystal structure of the endonuclease domain from …

Influenza A viruses are highly pathogenic and pose an unpredictable public health danger
to humans. An attractive target for developing new antiviral drugs is the PA N-terminal …

The influenza A polymerase is a heterotrimer which transcribes viral mRNAs and replicates
the viral genome. To initiate synthesis of mRNA, the polymerase binds a host pre-mRNA and …

Influenza virus polymerase initiates the biosynthesis of its own mRNAs with capped 10-to 13-
nucleotide fragments cleaved from cellular (pre-) mRNAs. Two activities are required for this …

Influenza virus uses a unique cap-snatching mechanism characterized by hijacking and
cleavage of host capped pre-mRNAs, resulting in short capped RNAs, which are used as …

The endonuclease activity within the influenza virus cap-snatching process is a proven
therapeutic target. The anti-influenza drug baloxavir is highly effective, but is associated with …

Emerging influenza viruses are a serious threat to human health because of their pandemic
potential. A promising target for the development of novel anti-influenza therapeutics is the …

Influenza viruses cause seasonal epidemics and pandemic outbreaks associated with
significant morbidity and mortality, and a huge cost. Since resistance to the existing anti …

The structure of the ribonucleoprotein complexes is crucial to viral transcription and
replication of influenza virus, but association of the nucleoprotein (NP) with the polymerase …

The influenza virus polymerase, a heterotrimer composed of three subunits, PA, PB1 and
PB2, is responsible for replication and transcription of the eight separate segments of the …