Conformational Preferences of a Peptide Corresponding to the Major Antigenic Determinant of Foot-and- Mouth Disease Virus: Implications for Peptide-Vaccine Approaches

This publication has 45 references indexed in Scilit:

• Systematic Replacement of Amino Acid Residues within an Arg-Gly-Asp-containing Loop of Foot-and-Mouth Disease Virus and Effect on Cell Recognition
  Journal of Biological Chemistry, 1996
• Structural comparison of two strains of foot-and-mouth disease virus subtype O1 and a laboratory antigenic variant, G67
  Structure, 1995
• NMR structure of a biologically active peptide containing the RNA-binding domain of human immunodeficiency virus type 1 Tat.
  Proceedings of the National Academy of Sciences, 1994
• Structure of a major immunogenic site on foot-and-mouth disease virus
  Nature, 1993
• Defining Solution Conformations of Small Linear Peptides
  Annual Review of Biophysics, 1991
• Conformation of a T cell stimulating peptide in aqueous solution
  FEBS Letters, 1989
• The Cell Attachment Site on Foot-and-Mouth Disease Virus Includes the Amino Acid Sequence RGD (Arginine-Glycine-Aspartic Acid)
  Journal of General Virology, 1989
• The three-dimensional structure of foot-and-mouth disease virus at 2.9 Å resolution
  Nature, 1989
• The immunodominant site of a synthetic immunogen has a conformational preference in water for a type-II reverse turn
  Nature, 1985
• Location and Characterization of the Antigenic Portion of the FMDV Immunizing Protein
  Journal of General Virology, 1982