Ives, J.A.L., Carr, J.A., Mendel, D.B., Tai, C.Y., Lambkin, R., Kelly, L., Oxford, J.S., Hayden, F.G. and Roberts, N.A. (2002) The H274Y Mutation in the Influenza A/H1N1 Neuraminidase Active Site Following Oseltamivir Phosphate Treatment Leave Virus Severely Compromised both in Vitro and in Vivo. Antiviral Research, 55, 307-317.
http://dx.doi.org/10.1016/S0166-3542(02)00053-0

has been cited by the following article:

• TITLE: Evaluation of Benzamide Derivatives as New Influenza A Nucleoprotein Inhibitors

  AUTHORS: Jinxi Liao, Huimin Cheng, Junting Wan, Panyu Chen, Yingjun Li, Ke Ding, Micky D. Tortorella, Zhengchao Tu, Yanmei Zhang

  KEYWORDS: Benzamides, Nucleoprotein, Anti-Influenza, NP Inhibitors, Nucleozin

  JOURNAL NAME: Open Journal of Medicinal Chemistry, Vol.6 No.3, July 18, 2016

  ABSTRACT: Virus nucleoprotein (NP) is an emerging target for drug development for Influenza. We designed benzamide derivatives as new inhibitors of NP that demonstrate good potency in blocking influenza A. Screening revealed that compound 39 was the most potent molecule in the series, exhibiting IC50 values of 0.46 and 0.27 μM in blocking the replication of H3N2 (A/HK/8/68) and (A/WSN/33) influenza A viral strains. The observed inhibition of viral replication correlated well with cytopathic protection. Furthermore, based on computational analysis and fluorescence microscopy, it was determined that compound 39 inhibited nuclear accumulation by targeting influenza A viral nucleoproteins. Finally, the rodent pharmacokinetic profile of compound 32 displayed half-life of greater than 4 hours and bioavailability greater than 20%, suggesting this class of molecules had drug-like properties.