References
- Colpitts TM, Conway MJ, Montgomery RR, Fikrig E. West Nile virus: biology, transmission, and human infection. Clin Microbiol Rev 2012;25:635–48
- Solomon T. Flavivirus encephalitis. N Engl J Med 2004;351:370–8
- Johnson RT. West Nile virus in the US and abroad. Curr Clin Top Infect Dis 2002;22:52–60
- Gould LH, Fikrig E. West Nile virus: a growing concern? J Clin Invest 2004;113:1102–7
- Kramer LD, Li J, Shi PY. West Nile virus. Lancet Neurol 2007;6:171–81
- Gray TJ, Webb CE. A review of the epidemiological and clinical aspects of West Nile virus. Int J Gen Med 2014;7:193–203
- www.cdc.gov/ncidod/dvbid/westnile/index.htm
- Kaiser J. Public health. Outbreak pattern stymies vaccine work. Science 2012;337:1030
- Diamond MS. Progress on the development of therapeutics against West Nile virus. Antiviral Res 2009;83:214–27
- Mukhopadhyay S, Kuhn RJ, Rossmann MG. A structural perspective of the flavivirus life cycle. Nat Rev Microbiol 2005;3:13–22
- Chappell KJ, Stoermer MJ, Fairlie DP, Young PR. Insights to substrate binding and processing by West Nile virus NS3 protease through combined modeling, protease mutagenesis and kinetic studies. J Biol Chem 2006;281:38448–58
- Chappell KJ, Stoermer MJ, Fairlie DP, Young PR. West Nile virus NS2B/NS3 protease as an antiviral target. Curr Med Chem 2008;15:2771–84
- Radichev I, Shiryaev SA, Aleshin AE, et al. Structure-based mutagenesis identifies important novel determinants of the NS2B cofactor of the West Nile virus two-component NS2B-NS3 proteinase. J Gen Virol 2008;89:636–41
- Poulsen A, Kang C, Keller TH. Drug design for Flavivirus proteases: what are we missing? Curr Pharm Des 2014;20:3422–7
- Kunitz M, Northrup J. Isolation from beef pancreas of crystalline trypsinogen, trypsin, a trypsin inhibitor, and an inhibitor-trypsin compound. J Gen Physiol 1936;19:991–1007
- Kassell B, Radicevic M, Ansfield MJ, Laskowski M. The basic trypsin inhibitor of bovine pancreas. IV. The linear sequence of the 58 amino acids. Biochem Biophys Res Commun 1965;18:255–8
- Ascenzi P, Bocedi A, Bolognesi M, et al. The bovine basic pancreatic trypsin inhibitor (Kunitz inhibitor): a milestone protein. Curr Protein Pept Sci 2003;4:231–51
- Robin G, Chappell K, Stoermer MJ, et al. Structure of West Nile virus NS3 protease: ligand stabilization of the catalytic conformation. J Mol Biol 2009;385:1568–77
- Aleshin AE, Shiryaev SA, Strongin AY, Liddington RC. Structural evidence for regulation and specificity of flaviviral proteases and evolution of the Flaviviridae fold. Protein Sci 2007;16:795–806
- Nall TA, Chappell KJ, Stoermer MJ, et al. Enzymatic characterization and homology model of a catalytically active recombinant West Nile virus NS3 protease. J Biol Chem 2004;279:48535–42
- Kaminski GA, Friesner RA, Tirado-Rives J, Jorgensen WL. Evaluation and reparametrization of the OPLS-AA force field for proteins via comparison with accurate quantum chemical calculations on peptides. J Phys Chem B 2001;105:6474–87
- Polak E, Ribière G. Rev. Francaise Informat Recherche Opérationelle, Série Rouge. Note sur la Convergence de Directions Conjuguée 1969;16:35–43
- Hasel W, Hendrickson TF, Still WC. A rapid approximation to the solvent accessible surface areas of atoms. Tetrahedron Comput Methodol 1988;1:103–16
- Chang CA, Chen W, Gilson MK. Ligand configurational entropy and protein binding. Proc Natl Acad Sci USA 2007;104:1534–9
- Zhirnov OP, Klenk HD, Wright PF. Aprotinin and similar protease inhibitors as drugs against influenza. Antiviral Res 2011;92:27–36
- Takeda-Shitaka M, Kamiya K, Miyata T, et al. Structural studies of the interactions of normal and abnormal human plasmins with bovine basic pancreatic trypsin inhibitor. Chem Pharm Bull 1999;47:322–8
- Chen Z, Bode W. Refined 2.5 Å X-ray crystal structure of the complex formed by porcine kallikrein A and the bovine pancreatic trypsin inhibitor. J Mol Biol 1983;164:283–311
- www.fda.gov/downloads/Drugs/DrugSafety/PostmarketDrugSafetyInformationforPatientsandProviders/UCM142741.pdf