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Collins, P.J., Haire, L.F., Lin, Y.P., Liu, J., Russell, R.J., Walker, P.A., Skehel, J.J., Martin, S.R., Hay, A.J. and Gamblin, S.J. (2008) Crystal structures of oseltamivir- resistant influenza virus neuraminidase mutants, Nature, 453, 1258-1261. doi:10.1038/nature06956

has been cited by the following article:

• TITLE: Molecular docking investigation for Indonesian H274Y mutant neuraminidase type 1 with neuraminidase inhibitors

  AUTHORS: Sigit Jaya Herlambang, Rosari Saleh

  KEYWORDS: Molecular Docking; Neuraminidase; Inhibitor; Resistance

  JOURNAL NAME: American Journal of Molecular Biology, Vol.2 No.1, December 30, 2011

  ABSTRACT: The aim of this study is to get insight the interaction between Indonesian H274Y mutant neuraminidase with four inhibitors. Not only to seek preferable inhibitor to be used, but also to investigate the interaction occurred, especially hydrogen bonds formed. Hydrogen bonds analysis and its interaction energies calculation showed that zanamivir is the most preferable inhibitor with 13 hydrogen bonds formed and –439.96 kcal/mol. Laninamivir would be an alternative inhibitor since it has 10 hydrogen bonds and –307.19 kcal/mol. The investigation of ΔSAS showed almost all active site residues buried when interacted with inhibitors. Only a few residues have an increases ΔSAS. Lipinski rule analysis showed that zanamivir and laninamivir would be best taken by injection or inhalation.