All Outputs (2)

All three domains of the Hepatitis C virus nonstructural NS5A protein contribute to RNA binding (2010)
Journal Article
Foster, T. L., Belyaeva, T., Stonehouse, N. J., Pearson, A. R., & Harris, M. (2010). All three domains of the Hepatitis C virus nonstructural NS5A protein contribute to RNA binding. Journal of Virology, 84(18), 9267-9277. doi:10.1128/jvi.00616-10

The hepatitis C virus (HCV) nonstructural protein NS5A is critical for viral genome replication and is thought to interact directly with both the RNA-dependent RNA polymerase, NS5B, and viral RNA. NS5A consists of three domains which have, as yet, un... Read More about All three domains of the Hepatitis C virus nonstructural NS5A protein contribute to RNA binding.

Direct visualization of the small hydrophobic protein of human respiratory syncytial virus reveals the structural basis for membrane permeability (2010)
Journal Article
Carter, S. D., Dent, K. C., Atkins, E., Foster, T. L., Verow, M., Gorny, P., …Barr, J. N. (2010). Direct visualization of the small hydrophobic protein of human respiratory syncytial virus reveals the structural basis for membrane permeability. FEBS Letters, 584(13), 2786-2790. https://doi.org/10.1016/j.febslet.2010.05.006

Human respiratory syncytial virus (HRSV) is the leading cause of lower respiratory tract disease in infants. The HRSV small hydrophobic (SH) protein plays an important role in HRSV pathogenesis, although its mode of action is unclear. Analysis of the... Read More about Direct visualization of the small hydrophobic protein of human respiratory syncytial virus reveals the structural basis for membrane permeability.