@article{(Open Science Index):https://publications.waset.org/pdf/5452,
	  title     = {Source of Oseltamivir Resistance Due to R152K Mutation of Influenza B Virus Neuraminidase: Molecular Modeling},
	  author    = {J. Tengrang and  T. Rungrotmongkol and  S. Hannongbua},
	  country	= {},
	  institution	= {},
	  abstract     = {Every 2-3 years the influenza B virus serves
epidemics. Neuraminidase (NA) is an important target for influenza
drug design. Although, oseltamivir, an oral neuraminidase drug, has
been shown good inhibitory efficiency against wild-type of influenza
B virus, the lower susceptibility to the R152K mutation has been
reported. Better understanding of oseltamivir efficiency and
resistance toward the influenza B NA wild-type and R152K mutant,
respectively, could be useful for rational drug design. Here, two
complex systems of wild-type and R152K NAs with oseltamivir
bound were studied using molecular dynamics (MD) simulations.
Based on 5-ns MD simulation, the loss of notable hydrogen bond and
decrease in per-residue decomposition energy from the mutated
residue K152 contributed to drug compared to those of R152 in wildtype
were found to be a primary source of high-level of oseltamivir
resistance due to the R152K mutation.},
	    journal   = {International Journal of Biotechnology and Bioengineering},
	  volume    = {6},
	  number    = {6},
	  year      = {2012},
	  pages     = {326 - 329},
	  ee        = {https://publications.waset.org/pdf/5452},
	  url   	= {https://publications.waset.org/vol/66},
	  bibsource = {https://publications.waset.org/},
	  issn  	= {eISSN: 1307-6892},
	  publisher = {World Academy of Science, Engineering and Technology},
	  index 	= {Open Science Index 66, 2012},
	}