Molecular prediction of oseltamivir efficiency against probable influenza A (H1N1-2009) mutants: molecular modeling approach
暂无分享,去创建一个
Thanyada Rungrotmongkol | Supot Hannongbua | Nadtanet Nunthaboot | Maturos Malaisree | Pornthep Sompornpisut | T. Rungrotmongkol | S. Hannongbua | Nadtanet Nunthaboot | M. Malaisree | P. Sompornpisut
[1] Thanyada Rungrotmongkol,et al. Susceptibility of antiviral drugs against 2009 influenza A (H1N1) virus. , 2009, Biochemical and biophysical research communications.
[2] Dominik Gront,et al. The crystal structure of the AF2331 protein from Archaeoglobus fulgidus DSM 4304 forms an unusual interdigitated dimer with a new type of α + β fold , 2009, Protein science : a publication of the Protein Society.
[3] Vasiliy P. Mishin,et al. Susceptibilities of Antiviral-Resistant Influenza Viruses to Novel Neuraminidase Inhibitors , 2005, Antimicrobial Agents and Chemotherapy.
[4] Guy Boivin,et al. Susceptibility of recent Canadian influenza A and B virus isolates to different neuraminidase inhibitors. , 2002, Antiviral research.
[5] Thanyada Rungrotmongkol,et al. Source of oseltamivir resistance in avian influenza H5N1 virus with the H274Y mutation , 2009, Amino Acids.
[6] Arieh Warshel,et al. A surface constrained all‐atom solvent model for effective simulations of polar solutions , 1989 .
[7] J. Aqvist,et al. A new method for predicting binding affinity in computer-aided drug design. , 1994, Protein engineering.
[8] Thanyada Rungrotmongkol,et al. How does each substituent functional group of oseltamivir lose its activity against virulent H5N1 influenza mutants? , 2009, Biophysical chemistry.
[9] Ling-Yun Wu,et al. Prediction of palmitoylation sites using the composition of k-spaced amino acid pairs. , 2009, Protein engineering, design & selection : PEDS.
[10] R. Webster,et al. Neuraminidase Inhibitor-Resistant Recombinant A/Vietnam/1203/04 (H5N1) Influenza Viruses Retain Their Replication Efficiency and Pathogenicity In Vitro and In Vivo , 2007, Journal of Virology.
[11] Jie J. Zheng,et al. Computational studies of H5N1 influenza virus resistance to oseltamivir , 2009, Protein science : a publication of the Protein Society.
[12] B. Lina,et al. Mutations of neuraminidase implicated in neuraminidase inhibitors resistance. , 2008, Journal of clinical virology : the official publication of the Pan American Society for Clinical Virology.
[13] Janet Daly,et al. Mutations conferring zanamivir resistance in human influenza virus N2 neuraminidases compromise virus fitness and are not stably maintained in vitro. , 2006, The Journal of antimicrobial chemotherapy.
[14] G. Ciccotti,et al. Numerical Integration of the Cartesian Equations of Motion of a System with Constraints: Molecular Dynamics of n-Alkanes , 1977 .
[15] Thanyada Rungrotmongkol,et al. Understanding of known drug‐target interactions in the catalytic pocket of neuraminidase subtype N1 , 2008, Proteins.
[16] G. Boivin,et al. Activity of the neuraminidase inhibitor A-315675 against oseltamivir-resistant influenza neuraminidases of N1 and N2 subtypes. , 2008, Antiviral research.
[17] Alan J. Hay,et al. Crystal structures of oseltamivir-resistant influenza virus neuraminidase mutants , 2008, Nature.
[18] Johan Åqvist,et al. Ligand binding affinity prediction by linear interaction energy methods , 1998, J. Comput. Aided Mol. Des..
[19] M G Ford,et al. Binding constants of neuraminidase inhibitors: An investigation of the linear interaction energy method. , 1999, Journal of medicinal chemistry.
[20] J. Åqvist,et al. Q: a molecular dynamics program for free energy calculations and empirical valence bond simulations in biomolecular systems. , 1998, Journal of molecular graphics & modelling.
[21] R. Webster,et al. Neuraminidase Inhibitor-Resistant Influenza Viruses May Differ Substantially in Fitness and Transmissibility , 2005, Antimicrobial Agents and Chemotherapy.
[22] Ricky Chachra,et al. Origins of Resistance Conferred by the R292K Neuraminidase Mutation via Molecular Dynamics and Free Energy Calculations. , 2008, Journal of chemical theory and computation.