The Mechanism by which 146-N-Glycan Affects the Active Site of Neuraminidase

Discovery of N-Substituted Oseltamivir Derivatives as Potent and Selective Inhibitors of H5N1 Influenza Neuraminidase

(2014) Yuanchao Xie et al.   JOURNAL OF MEDICINAL CHEMISTRY

Plasticity of 150-Loop in Influenza Neuraminidase Explored by Hamiltonian Replica Exchange Molecular Dynamics Simulations

(2013) Nanyu Han et al.   PLoS One

Structural basis for a class of nanomolar influenza A neuraminidase inhibitors

(2013) Philip S. Kerry et al.   Scientific Reports

MM/GBSA Binding Energy Prediction on the PDBbind Data Set: Successes, Failures, and Directions for Further Improvement

(2012) Paulette A. Greenidge et al.   Journal of Chemical Information and Modeling

Influenza neuraminidase: A druggable target for natural products

(2011) Ulrike Grienke et al.   NATURAL PRODUCT REPORTS

Glycosylation Site Alteration in the Evolution of Influenza A (H1N1) Viruses

(2011) Shisheng Sun et al.   PLoS One

Mechanism of 150-cavity formation in influenza neuraminidase

(2011) Rommie E. Amaro et al.   Nature Communications

Carbocycles Related to Oseltamivir as Influenza Virus Group-1-Specific Neuraminidase Inhibitors. Binding to N1 Enzymes in the Context of Virus-like Particles

(2010) Sankar Mohan et al.   JOURNAL OF MEDICINAL CHEMISTRY

POVME: An algorithm for measuring binding-pocket volumes

(2010) Jacob D. Durrant et al.   JOURNAL OF MOLECULAR GRAPHICS & MODELLING

The 2009 pandemic H1N1 neuraminidase N1 lacks the 150-cavity in its active site

(2010) Qing Li et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Active 1918 pandemic flu viral neuraminidase has distinct N -glycan profile and is resistant to trypsin digestion

(2009) Zhengliang L. Wu et al.   BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS

Structural Characterization of the 1918 Influenza Virus H1N1 Neuraminidase

(2008) X. Xu et al.   JOURNAL OF VIROLOGY